entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
| function
stringlengths 7
11k
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B1X6B7
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HCHA_ECODH
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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B1XJV9
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CRTE_SYNP2
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Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPS) (EC 2.5.1.29) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
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MVVADAHTQGFSLAQYLQEQKTIVETALDQSLVITEPVTIYEAMRYSLLAGGKRLRPILCLAACEMLGGTAAMAMNTACALEMIHTMSLIHDDLPAMDNDDLRRGKPTNHKVYGEDIAILAGDALLSYAFEYVARTPDVPAERLLQVIVRLGQAVGAEGLVGGQVVDLESEGKTDVAVETLNFIHTHKTGALLEVCVTAGAILAGAKPEEVQLLSRYAQNIGLAFQIVDDILDITATAEELGKTAGKDLEAQKVTYPSLWGIEKSQAEAQKLVAEAIASLEPYGEKANPLKALAEYIVNRKN
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Catalyzes the sequential condensation of three molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to yield geranylgeranyl diphosphate (GGPP). Thereby, is a key enzyme for the biosynthesis of terpenenoids.
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B1YAL1
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FBPAP_PYRNV
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Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13)
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MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNVGDDISLLMTHTKGEDNKDIHGLAWETFKEVTDQIAKRFKLYGAGQDLLKDAFSGNIRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAGLVIDPSMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRYIIRKVFRRADGAPAAANSVERLSLIAGRYVGKDDPVLLVRAQSGLPAVGEVLEAFAHPHLVHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPPKVGALGFQLHEGYLEGGVDLFDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTALPKILAKVKPYPADQYEKDRKKYIEAVVKGAKVEESQHD
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Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P).
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B2AXJ5
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HETQ1_PODAN
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Gasdermin-like protein het-Q1 (Heterokaryon incompatibility protein Q1) [Cleaved into: Gasdermin-like protein het-Q1, N-terminal]
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MPTKTSQHAFAGSERWVVPRYSSKPGTLIRLGSVLTDPEDLESSLNLDSIPPIPPHLLRDATPEVRMSVQTELSKSDSTLAKAAPALEGILTLGGGVEASRSQGVSSSLNISGTVKATVFRADKSYMDVLLKDKNVISYAKRGLGKPMFVVVGVATAGRVEMKETRHVTRKAGVSGKVGVEVIGEGEVGLERERSDKSCNEVRGEGGLDFAYRVREFGYSRVRGTVKDKGDWTGKVLFAGGKGPVVEKGGEVVPVFKEFKEGEVKLRATGSFDVAAKA
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[Gasdermin-like protein het-Q1]: Gasdermin-like protein involved in heterokaryon incompatibility, a process that ensures that during spontaneous vegetative cell fusion, only compatible cells from the same colony survive (non-self-recognition). In P.anserina, the het-q locus exists as 2 incompatible alleles, het-Q1 (this entry) and het-Q2 (AC P0DW09). This form constitutes the precursor of the pore-forming protein: during the allorecognition process, it is cleaved by het-Q2, releasing the N-terminal moiety (Gasdermin-like protein het-Q1, N-terminal) that binds to membranes and forms pores, triggering cell death. [Gasdermin-like protein het-Q1, N-terminal]: Pore-forming protein that causes membrane permeabilization and cell death. Released upon cleavage and maturation by het-Q2 and binds to membrane inner leaflet lipids. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering cell death (By similarity).
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B2B223
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ARO1_PODAN
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MTSSTGSGPTRISILGKDDIIVDHGIWLDFVTHDLLQNIPSSTYVLITDTNLHDTYVPAFQEVFERAAGQDARLLTYTIPPGEYSKGRETKAEIEDWMLSHQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLAFLETLPVREFINGMAEVIKTAAIWNETEFTALEDNAPAILEAIRSKPTGTGARLAPIRDILKRIVLGSAGVKAEVVSADEREGGLRNLLNFGHSIGHAYEAILTPQVLHGECVAIGMVREAELARFLGVLPPGAVARLTKCIASYELPTSLHDKRIVKLTAGKECPVDVLLQKMGVDKKNDGRKKKVVLLSAIGKTYEPKATVVEDRAIRIVLSPSVRVTPGVPKGLNVSVTPPGSKSISNRALVLAAMGEGTTRIKGLLHSDDTHYMLTAIAQLQGATYTWEEAGEVLVVKGRGGKLLASNEPLYLGNAGTASRFLTSVVALCSPTDTTTSTVLTGNARMKVRPIGPLVDALRSNGVAVKYLEKENSLPVQVDAVSGFAGGVIELAATISSQYVSSILMAAPYARQPVVLKLVGGKPISQFYIDMTIAMMASFGVKVERDAEDPNTYHIPQGSYKNPEEYVVESDASSATYPLAVAAITGTTCTIPNIGRTSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPPVGALKAIPHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIKAMKDELAKFGVHCSELEDGIEVTGKPYKELANPEPIYCYDDHRVAMSFSVLSVLAPHKVLILERECTAKTWPGWWDILSQKFNVHLEGEEDPTKKCTAKSSRPSTDRSIFIVGMRGAGKSTAGRWMSDILKRPLIDLDVELEKREKATIPEIIRSERGWEGFRKAELELLEDMIKNNSKGHVFSCGGGLVETEAARKLLISYQKNGGSVLLVHRDTDQVVEYLMRDKTRPAYSENIREVYYRRKPWFEEVSNFQYHSPHHNGSEEAPEDFSRFLSVISGSSTHFEDVLAKKHSFFVSLTVPNVAKALDIIPKVVVGSDAVELRVDLLESLNPEFVATQVALLRSAAKIPIVYTIRTISQGGKFPDDDYKRALELYQIGLRTGVEYLDLEMTMPEDVLQTVTETKGFTHIIASHHDPENKLSWKNGGWIPFYNKALQYGDVIKLVGMAREVSDNFDLTNFKMRMLEAHKKPIIALNMGTAGKLSRVLNGFLTPVSHPALPSKAAPGQLSAAEIRQALSLVGELEPKSFYLFGKPISSSRSPALHNGLFAQTGLPHQYSLFETDVAADVKDIIRSADFGGASVTIPLKLDIIPLLDEVSDAATAIGAVNTVIPVSPEGSDKTILRGDNTDWMGMVFSLRQAGIAPRTKTNPGAGMVVGSGGTTRAAVYALHDLGYSPIHIVARSPDRVKAIADSFPEDYNIQTLSTPEEVKAATDALPTVVISSIPADKPIDQSMREVLVASLRHPAKSEKEPRVLLEMAYTPRHTPLMQLAEDAGWKTIPGLEVLAAQGWYQFQLWTGVTPLYADARAAVMGDSE
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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B2B3C0
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MANA_PODAN
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Mannan endo-1,4-beta-mannosidase A (EC 3.2.1.78) (Endo-beta-1,4-mannanase A) (Man5A)
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MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA
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Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose. Also has transglycosylation activity.
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B2C4D0
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TS23B_MAIZE
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(E)-beta-caryophyllene synthase (EC 4.2.3.57) (Terpene synthase 23)
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MAADEARSVSRLHSEEDMHGKHHSTLWGDFFLHHVPCRPGQYLIMKDNVEIMKEEVKKMLLDVGSSDLSHKLDCIDTLERLGLDYHYTKEIDELMCNVFEARDQDLDLTTTSQLFYLLRKHGYHISSDVFLKFRDDKGDIVTNDARCLLRMYEAAHVRVNGEEILDNILIHTKRQLQCIVDDLEPTLQEEVRYALETPLFRRLNRVQARQFISTYEKSTTRINMLLEFSKLDFNILLTLYCEELKDLTLWWKEFQAQANTTIYARDRMVEMHFWMMGVFFEPQYSYSRKMLTQLFMIVSVLDDLYDSHCTTEEGNAFTAALQRWDEEGVEQCPTYLRTLYTNIRATIKAIEEDLNFQNNKHAKLVKGLIIDMAMCYNAETEWRDKKYVPATVDEHLKISARSSGCMHLVSQGFISMGDVATSEALEWASTYPKIVRAVCIIARLANDIMSYKREASNNTMVSTVQTCAKEYGTTTVEQAIEKIRELIEEAWMDITHECLRQPQPKALLERAVNLARTMDFLYKDADGYTDSRSIKGILDSLYVHLID
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Component of the volatile terpenes biosynthesis pathways. Sesquiterpene synthase that converts farnesyl diphosphate to (E)-beta-caryophyllene. Involved in indirect defense by producing volatile signals that attract natural enemies of leaf herbivores such as Chilo partellus and root herbivores like the western corn rootworm (WCR, Diabrotica virgifera) and fall armyworm (Spodoptera littoralis and Spodoptera frugiperda). Deters leaf herbivores by triggering (E)-beta-caryophyllene production upon insect (stemborer C.partellus) egg deposition (E)-beta-caryophyllene attracts the parasitic wasp Cotesia sesamiae which lays eggs on the larvae of C.partellus, which is ultimately fatal.
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B2C4J0
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GLYC_CHAVB
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Pre-glycoprotein polyprotein GP complex (Pre-GP-C) [Cleaved into: Stable signal peptide (SSP); Glycoprotein G1 (GP1); Glycoprotein G2 (GP2)]
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MGQLVSFFQEIPNIIQEAINIALIAVSLIAILKGLVNLWKSGLFQLLVFLILAGRSCSFKIGRSTELQNITINMLKVFEDHPISCTVNKTLYYIRESENATWCVEIAALDMSVLLSPHDPRVMGNLSNCVHPDIKHRSELLGLLEWILRALKYDFLNYPPLLCEKVTSSVNETRIQINVSDSAGSHDFKETMLQRLAILFGTKLMFDKTPKQFIVIRNQTWVNQCKSNHVNTLHLMMANAGHAVKLRRLQGVFTWTITDAAGNDMPGGYCLERWMLVTSDLKCFGNTALAKCNLNHDSEFCDMLKLFEFNKKAIESLNDNTKNKVNLLTHSINALISDNLLMKNRLKELLDTPYCNYTKFWYVNHTITGEHSLPRCWMVKNNSYLNESEFRNDWILESDHLLSEMLNKEYFDRQGKTPITLVDICFWSTLFFTTTLFLHLVGFPTHRHIQGEPCPLPHKLNSNGGCRCGRYPELKKPTTWHRKH
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[Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084}. Glycoprotein G1: Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor leading to virus endocytosis. {ECO:0000255|HAMAP-Rule:MF_04084}. [Glycoprotein G2]: Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification. {ECO:0000255|HAMAP-Rule:MF_04084}.
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B2D6K9
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PPH6R_CAEEL
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Serine/threonine-protein phosphatase 6 regulatory subunit
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MFWAKEEEENSLMRLLKTDNFTLEDVLLNEFVVQESRYGKAELVQYITSRENMKALLELSLNPKINTDLPMKQQYRLSFIASEILTIRGTDVFQKQIVTTEETRKCLVDFLNDKTPLNHLVAGFFAKIMECLLSRHFDLFQTFSLLQETKFFDKCLRNINLGAIECLLENLVRIPTTSEGTRIVKEWMISENLFEKIVDRMRESETDDEKECLAEVYCEILRELRDKLYIMESKVDELHAKSMDETLIAKIADNLIVEEGCPAEELVKKSALISASAKILEAFIKTNFVSNAPAQQLEEIERNLIEERHYSYGLMRPCMDNDPYEHSYQPDPERIVEGILANRLPNILQTVLRDIEANGSVWQPLLRLIIELCNTNCMSTHEKIAVAFRSLPFINLIKAAKMLPRASVLHCLLVKVVILLLHSSFPCDELSPAAEYLLTEGGLIQNIYDTATSPNPGSSVACSGLRSFNQNLGDAINRAKKAGIPNQKLLAILSADNTWTELEDIIHLYNLKHRPQMQHDFNDSSVVSSIRNDSHGFNDSEEWTDASTKFAEMDATSSAKQAFSGFSSPFEPNMQRFSDFEGQFDDTPDEDEFRKLCSERANSSSCAGISFETSPIKWPGEAEKTSEKASEPPSVVASTYPQQTNGNQAFLEQEEGDGEWVWPTVPPLGETEVVTQTGHRPENNWVDETAPDFSHLDMAPPKEDDMWADFSSFPTISPTAAANSASSSSSDAWPGSDIHLQGEASDWPLNNSHESKASDPVMVGLAASISHPGDSSEA
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Regulatory subunit of protein phosphatase 6 (PP6) (Probable). In complex with pph-6, promotes actomyosin contractility during cytokinesis by regulating the organization of cortical non-muscle myosin II nmy-2 and thus contributing to correct spindle positioning. Also required for the proper generation of pulling forces on spindle poles during anaphase by regulating the cortical localization of gpr-1, gpr-2 and lin-5. Negatively regulates kinase air-1 localization at the cell cortex.
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B2D6M2
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LIN61_CAEEL
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Protein lin-61 (Abnormal cell lineage protein 61)
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MLKLVILCFALFYNTVSSTRFLFGVEVKCDFDEVFQLTVSHWEDDGNTFWDRDEDITGRMTMFARKKIFFYQDGHHGFEFGKLEPYGWFLHNCTKNGNFREYRHGLSSTSGSNGLEYIEYTMSEFLKIVRANKKSDRKLDKTYLWESYLHQFEKGKTSFIPVEAFNRNLTVNFNECVKEGVIFETVVHDYDKNCDSIQVRWFARIEKVCGYRVLAQFIGADTKFWLNILSDDMFGLANAAMSDPNMDKIVYAPPLAINEEYQNDMVNYVNNCIDGEIVGQTSLSPKFDEGKALLSKHRFKVGQRLELLNYSNSTEIRVARIQEICGRRMNVSITKKDFPESLPDADDDRQVFSSGSQYWIDEGSFFIFPVGFAAVNGYQLNAKKEYIEHTNKIAQAIKNGENPRYDSDDVTFDQLAKDPIDPMIWRKVKVGQKFELIDPLAQQFNNLHVASILKFCKTEGYLIVGMDGPDALEDSFPIHINNTFMFPVGYAEKYNLELVPPDEFKGTFRWDEYLEKESAETLPLDLFKPMPSQERLDKFKVGLRLEAADMCENQFICPATVKSVHGRLINVNFDGWDEEFDELYDVDSHDILPIGWCEAHSYVLQPPKKYNY
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Synthetic multivulva class B (synMuvB) protein required to repress the induction of vulval development by Ras signaling. Unlike other synMuv proteins it does not associate with the multiprotein DRM complex and the NuRD-like complex. Interaction with methylated histone H3 is essential for vulva development. It has a role in maintaining genome stability.
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B2D6P4
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TBPL1_CAEEL
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TATA box-binding protein-like 1 (TBP-like) (TBP-like factor) (CeTLF)
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MQMGDHQMMGNQRYYRTYVQKVMPAQAGGAVSQNATYVQTAGIRTVHHDGNGQQRIVQLPPGVRQIQQNGVGPAYVRQVPGGQPMQVNFGHPGTIAGRNVAVGVQMRPVQGHNVQQGYQRQQVANQIQQQNRAVFMAQNQQGQQQISYAQAQHRQQQQNQQQHHQQPQHFNHPSQQNQMIMQHRQPQMHHNQQHQMVQPQMTRHQMAQHHAQQPHPQIYVPRDMNLAVPLREPSPEPIPVKIEVPDVPPEGTSAANEEPMPDDGDIDIQIRNVVCNYTLPLHIDLRKLAMNTHNVTYEREKGVMMKQKRSPGCYIKVYSSGKVYIVGCRSEADCKRAARSIARHVQRVMGKTKERVSIRNYRVNNVLATCRLPFGIKIEEVAAKYPSESTYEPELSVGLVWRSVTPKATLRIHTTGSITVTGAQSEADVLEVLSKIYPIVLEFRCLERAKGNVAAQKKRKRKAPVNRGPPIKRERFDDSNYRNSGVINNQVYFSDEDEDLYDELDLEE
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May be a general transcription factor. Plays an essential role for RNA polymerase II/ama-1 transcription in early embryos whereby it activates a subset of RNA polymerase II promoters and facilitates the reestablishment of transcription after mitosis.
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B2DBE9
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GGS4_PHOAM
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Geranylgeranyl pyrophosphate synthase D (GGPP synthase D) (GGPPSase) ((2E,6E)-farnesyl diphosphate synthase D) (Dimethylallyltranstransferase D) (EC 2.5.1.1) (Farnesyl diphosphate synthase D) (Farnesyltranstransferase D) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase D) (Geranyltranstransferase D) (EC 2.5.1.10)
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MDFPIRSQARLYPAQCVTFCLYVRVPPLSEWNFLKMQTDARPSATWPSVPKVHKRNRSTSLSDQQTAKKAHANHARLHLPQPIEPVYESQNGSVSQSEEKSSAVEINNSAAGDPQRFAVADLNFSWAEEEEKVVLAPYDYVASNSGKEFRTLILNAFNAWFRVPPESLTIICDVVRMLHTSSLLIDDIQDNSLLRRGRPVAHSIYGVAQTINTGNYVYFLAAKELNKLRNAASALEVFTAEMLNLHRGQGQELYWRDTLKCPTEDEYLKMVSNKTGGLFRMAVKLMQAESPAGPMAPVCDKLVQLLGLVYQIADDYKNLTAVEYTTSKGFCEDLTEGKFSFPVVHSIQSRPEDRRLYQILAQKTTEVEVKKYAVSYIESTGSLEYTKQVVRVLVQRARDELSRIDQGRERNQEMHALLGKMALE
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Catalyzes the trans-addition of the 3 molecules of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranylgeranyl pyrophosphate (GGDP).
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B2DCZ9
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ARHG2_PIG
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Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1)
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MKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTTRERPSSAIYPSDSFRQSLLGSRRGRSPLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNMRNRTLSVESLIDEGAEVIYNELMSDFEMGEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELQLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSPRNFVIHRLGDLLITQFSGPSADQMRKTYSEFCSRHTKALKLYKELYARDKRFQQFIRKVTRSAVLKRHGVQECILLVTQRITKYPVLISRILQHTHGIEEERQDLTTALGLVKELLSNVDQDVHELEKGARLQEIYNRMDPRAQTPVPGKGPFGREELLRRKLIHDGCLLWKTAAGRFKDVLMLLMTDVLVFLQEKDQKYIFPALDKPSVVSLQNLIVRDIANQEKGMFLISAAPPEMYEVHTASRDDRSTWIRVIQQSVRVCPSREDFPLIETEDEAYLRRIKMELQQKDRALVELLQEKVGLFAEMTHFQVEEDGGGGMPLPTLPRGLFRSESLESPRGERLLQDAIREVEGLKDLLVGPGVELLLTSREPALPVETDSGGNTSPGVTANGEARTFNGSIELCRADSDSSQKDRNGNQLRSPQEEALQRLVNLYGLLHGLQAAVAQQDTLMEARFPEGPERREKLTRANSRDGEAGRAGAAPVAPEKQATELALLQRQHALLQEELRRCRRLGEERATEAGSLEARLRESEQARALLEREVEEARRQLAALGHTEPLPAEAPWARRPLDPRRRSLPAGDALYLSFTPPQPSRGHDRLDLPVTIRSVHRPFEDRERQELGSPDERLQDSSDPDTGSEEEGSSSRLSPPHSPRDFTRMQDIPEETESRDGEPVASES
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Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability. Involved in neuronal progenitor cell division and differentiation. Involved in the migration of precerebellar neurons.
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B2DD29
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BRSK1_RAT
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Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B)
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MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGSGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGVGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSSGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGTPPRSLQPPPGRPDPDLSSSPRRGPSKDKKLLATNGTPLP
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Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C (By similarity). In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. {ECO:0000250, ECO:0000269|PubMed:16630837}.
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B2DEU7
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MSHMT_PARSX
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2-methylserine hydroxymethyltransferase (MSHMT) (EC 2.1.2.7) (Alpha-methylserine hydroxymethyltransferase) (D-alanine 2-hydroxymethyltransferase)
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MNELTRTFFNSSVHDTDPLIAQALDDERARQKNQIELIASENIVSQAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLVKPGDRILSLDLAAGGHLSHGMKGNLSGRWFEAHNYNVDPQNEVINYDEMERIAEEVKPKLLITGGSAYPRELDFARMAQIAKKVGAFFMVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQTAVFPGVQGSLHSNVLAAKAICLGEALRPEFRDYVAQVVKNAKVLAETLTSRGIRIVSGGTDTHIVLLDLSSKGLNGKQAEDALARANITSNKNPIPNDSPRPAEWVGMRLGVSAATTRGMKEDEFRKLGNVVADLLEAESAGNGPEAAEKAKVTVRELTEAFPVYAH
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Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine. {ECO:0000269|Ref.1}.
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B2DFG5
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DTHAD_DELSH
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D-threo-3-hydroxyaspartate dehydratase (D-THA DH) (D-THA dehydratase) (EC 4.3.1.27) (Threo-3-hydroxy-D-aspartate ammonia-lyase)
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MQDTLLTLDTPAAVIDLDRMQRNIARMQQRMDAQGVRLRPHVKTSKSVPVAAAQRAAGASGITVSTLKEAEQFFAAGTTDILYAVSMAPHRLPQALQLRRRGCDLKLIVDSVAAAQAIAAFGREQGEAFEVWIEIDTDGHRSGVGADDTPLLLAIGRTLHDGGMRLGGVLTHAGSSYELDTPEALQALAERERAGCVQAAEALRAAGLPCPVVSVGSTPTALAASRLDGVTEVRAGVYVFFDLVMRNIGVCAAEDVALSVLATVIGHQADKGWAIVDAGWMAMSRDRGTARQKQDFGYGQVCDLQGRVMPGFVLTGANQEHGILARADGAAEADIATRFPLGTRLRILPNHACATGAQFPAYQALAADGSVQTWERLHGW
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Catalyzes the deamination of D-threo-3-hydroxyaspartate (D-THA). Also exhibits dehydratase activity towards L-threo-3-hydroxyaspartate (L-THA), L-erythro-3-hydroxyaspartate (L-EHA) and D-serine.
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B2FDA8
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SMC3_CAEEL
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Structural maintenance of chromosomes protein 3
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MKIKEVRITGFRSYKDNTNVSGFSPRSNVVVGRNGSGKSNFFHAIQFVLSDEYAHLKEEQRLGLLHESTGPKVAHARVEITFDNSEKRLMAFENSEVKIVRQVGKKKDQYYIDNKMVPRAEVVNLMESAGFSRSNPYYIVKQGKINELATSPDAYKLKLLREVAGTRVYDERKEESLKILKETKMKTEKIQGLLKYIDERLQTLENEKEDLKEYQKLDKTKRSVEYTMYDNTNKEAIKEKTKLDEQKVELNQKDNNVKSQLNDVIAEMAKLKTDKKKLESLGRGLREDKETLQAEETKMVEEKMTLKLEIDSLNEENTRERQGRQNAEHSLQGVGDEIFKNEEELDTIKPEYAKLLEEESRLKTDIRIDESRAKEILAKQGQRSQFSSVDDRDKFLRNEIRRISGLIADNKEREETIQKELADVEREDEKLNNEIQSISRTIDENRYEMDTFAAKSTSLKQEYDAAYVAQQTAAREEKAIRDKIGNTEQDISAANDQLRRIVARPVYNGITGVRKVIEEFKHDNRNGQHDDVINGYYGTVIELAEVPDMFRTAVEVIAQNRLFYHVVETDRIATKILRKFNEMQLPGEINFFPMNRVSAPRQRDLSNNSNARPMSDVIDYEVQYDKVFKSITANVIIVRTLDQAARDLRNEGFDVVSVDGDQMSKKGVMTGGFIDKKRSKLELHTQKDRFTKELAELQKSLAEAEKMVRERTQEAEKIRNRMQQHENQIGDFHRKHRELTEAKNAISQQFYMVTSTKEPKKDQLLGIKNHLRELLAQKENFEQEIGSNMSSQLTSDEEQTVKKLRKKVDEMTKQLATVSRRRMDLMHRKNAIENLLTKKLYKTKESLTARVDDISDNERRHKLENANAQLTSLLTRMESTRKQLATAISELQDYETKEKALQINIDNVLEQQRDLEKQQADFQLQYDKITAKEDEVKQKREDSLKKLILSRYSIKTRKNQFSYEISDSEEVGAKREPIEHRKLKISTFCLEYRAKLEKVHSNMRLLGALPTDTFSKWQNVKPRELEKKLLECVNELKKYENVNKKALDQYMTASSQKEELTKRMAEQKKSEDSIEELLKVLENRKYEAIDLTFKQVKKNFEQVFKQLVPHGRGKMQMRAREQRDDEEGINSVELYEGISVLVSFVSDDGDSETREMTQLSGGQKSLVALAIIFSIQKCDPAPFYLFDEIDAALDAQHRKSVADMIQSLSDQAQFVTTTFRPELLATAEKFYGVRFRNKVSHIDSVTREQAYDFVEDDTTHG
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Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in the repair of double strand breaks during mitosis and meiosis. Required for chromosome segregation during mitosis. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped (By similarity). At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity). Required for the localization of lab-1 to meiotic and mitotic chromosomes.
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B2FHL8
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PL_STRMK
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Polysaccharide lyase (PL) (EC 4.2.2.-) (Alginate lyase) (EC 4.2.2.3) (Endolytic polysaccharide lyase) (Hyaluronate lyase) (EC 4.2.2.1) (Multifunctional polysaccharide lyase) (Poly-beta-D-glucuronate lyase) (EC 4.2.2.14)
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MSLPLRLALLPTLLASASAFAACPAPPPGQPDIRAIGYYTDKAGSVIDPALQQQNKDATAPLDRYAADVARMSDDYLRNGDPAAAQCTLSWLGAWADDGAMLGQMIRVNNDQSFYMRQWMLDAVAMAYLKVHDQANPQQRARIDPWLQKLARANLAYWDNPKRRRNNHYYWGGLGVLATGLATDDDALWQAGHAAFQKGIDDIQDDGSLPLEMARGQRALHYHDYALAPLVMMAELARLRGQDWYASRNHAIDRLARRVIEGSRDPAWFNQHTGAAQLPLQASGWVEFYRLRSPDGGVFDAAHARGPFHSPRLGGDLTLMATHGIVRTPLR
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Polysaccharide lyase that catalyzes the depolymerization of several anionic polysaccharides via a beta-elimination mechanism. Exhibits broad substrate specificity, catalyzing the degradation of not only alginate and poly-beta-D-mannuronate (poly-ManA), but poly-beta-D-glucuronate (poly-GlcA or poly-GlcUA) and hyaluronate (HA) as well. The oligosaccharide products formed by enzymatic cleavage are comprised mainly of disaccharides, with a lower abundance of trimers and pentamers. Is not active on poly-D-galacturonate, heparin and heparin sulfate.
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B2FSW8
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EALGL_STRMK
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Alginate lyase (EC 4.2.2.26) (Exolytic alginate lyase) (Exolytic polysaccharide lyase)
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MRLQPLFVSLALAAPCALLPTASLSAAPAAAARQADTAPVLVTAAQWQQMASEGRRYPWFAKEQARTEATLKKMMKAGIDVPVPRDKGGGRTHEQHKRNYQALLAAGTLYRLTGDRAYVDYARDMLLQYAQLYPTLGPHPEGRGQIPGRVFWQVLNDSVWLVNAIQGYDAIRDALSAEDRNTIESKVFRPMAEFLVSEPKNYDQIHNHATWAVAATGMTGYVLRDQELVEKSLRGSQKDDKFGFLRQIDLLFSPDGYYEEGPYYQRYALAPFLLFANAIERNEPQRKIFARRDGVLLKAVDVLVQSSYGGLFFPINDAILDKGIDTEELVAGIGIAYARTGDDRLLSVAEQQKRLLLSPEGLQVAQALAANKAKPFDYHPMLLRDGPDGDRGGLAILRMNGERGQALVQKDTMQGMGHGHFDKLNWLFYDNGNPVVTDYGAARFLNVEAKRGGIYLAENRSWAKQTVAHNTLVVDEQSHFNGNWKRGEAHAPQVRFFQADADTQIASATMRDAYPGVAFTRTQALLRHPDLGLPVVLDLLQVHGDKAARYDLPLHFNGHIVTTGFEAEHFPSQRPVLGKDNGYQHLWLDARSKPGSEPRSLAWLLDGRFYTYRFGSSAPAQALLVESGANDPEFNLRREPALLQRVDGQKDVTFFSVLEPHGEYNGTAEYVHGADSRIREIVRTRGSDAEVIELRLASGARIALGVADNSATTSEHSVTVDGHVYRWNGSHARLDRSKGDGK
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Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Shows an exolytic mode of action, producing unsaturated monomers. Displays a very low activity against poly-beta-D-glucuronate (poly-GlcA), and is not active on poly-alpha-D-galacturonate, hyaluronan, heparin, heparan sulfate and chondroitin sulfate.
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B2G331
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VKT2B_HETCR
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TauPI-stichotoxin-Hcr2b (TauPI-SHTX-Hcr2b) (Analgesic polypeptide HC1) (APHC1)
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MKGTFLICLILIAGFSFKSTQAGSICLEPKVVGPCTAYFRRFYFDSETGKCTVFIYGGCEGNGNNFETLRACRAICRA
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This protease inhibitor shows two different activities, it inhibits both the capsaicin receptor TRPV1 and serine proteases. It partially (max 50%) and reversibly inhibits capsaicin-induced response of TRPV1 (IC(50)=54 nM), a receptor of the pain pathway. The second activity is a weak inhibition of trypsin and chymotrypsin activity (Ki=1 uM and Ki=5 uM, respectively). In vivo, it shows antinociceptive and analgesic activities. It significantly prolongs tail-flick latency and reduces capsaicin-induced acute pain. In vivo, unlike other TRPV1 antagonists whose activity is associated with hyperthermia, this protein has the remarkable feature of dropping core body temperature.
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B2GUB3
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TTLL3_XENTR
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Tubulin tyrosine ligase 3 (EC 6.3.2.-) (Tubulin--tyrosine ligase protein 3)
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MAHHTAVNPDRLKHAKALVEKAIKQKKIFAIHGPYPVIRSCLRSRGWVEKKFPKSGKAKQKKEKASDEDMEDDDGDGSSNDDDDGENSDEEENGDPDGTCDLMSRLLRNEDPNFFWTTKRDAVDCRFLKKDQMLNHYAKAGSFTTKVGLCLNLRNLHWFDDADPDSFFPRCYRLGAEDEKQSFKEDFWHTAARSILKRVANRRDICSPAATGGAKASHREPGANNGAQLLAKRGSRKRAESVPVQIILTALEACERYLNSLEHNDIDMETEATPAMTDTQWEEFLHGYYQVIHDGATIEHSEYYVDQCSEVLHKLEAVNPQLDIEGGRNIWIVKPGAKSRGRGIICMDRLEEILKLVDCDPMIVKDGKWVVQKYIERPLLIFGTKFDVRQWFLVTDWNPLTIWFYKECYVRFSSQPFSLENLDTSIHLCNNSIQKHYENSQSRHPLVPTDNMWSSRQLQVHLHKLGAPHAWEAVIVPGMKAAIIHAMQSAQDIVEYRKSSFELYGADFMFGENFHPWLIEINASPTMAASTTVTSRLCAEVQEDTLRIVLDRKLDRNCDIGAFELIYKQCAVDIPQYLGINLLVEGSMVKKPRQLQQPNPNGAFNLSIVQSNKRSVSLLNAKTSGSNPGVGSQDSVKVAVPTRTAPAVMGNDFWTSRTHGTIGRAKTTAAGKENKAAEGGQRNSVMVELVRLPSKRALEQSKEGTNPRQRLFPAPKSCTLEKPIRVRQPIRLKNGGFVDLKFTSLDSGQVQLLRNMKTGMTDPNKMPCLFCKGPSSLTGLHAMCSCSRAGKQAAKPTCLKLSKRIIIGKFHGSSAALSARGTAILTSLLP
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Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction. Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases. Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions. Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity).
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B2GUT4
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WNT11_XENTR
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Protein Wnt-11 (Protein Wnt-11-related)
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MKIYFLLGIFLTFLLHTRICQGIKWLALAKTPLSLALNQSQHCKQLEGLVSSQMQLCRSNLELMQTIIHAAKEVKKTCIKAFTDMRWNCSSIELAPTFHQDLERGTRESAFVYALSAAAISHTIARACTTGDIPGCSCAPIPGESPGPGYRWGGCADNLNYGILMGSKFSDAPMKMKKSGSQANKLMHLHNSEVGRQVLKASLEMKCKCHGVSGSCSIKTCWRGLQELREIALDLKTKYLSATKVVHRPMGTRKQLVPKDIDIRPVQETEMIYLQSSPDYCLKNEKMGSHGTHERQCNKTSNGSDSCDLMCCGRGYNPYMDKVVERCHCKYHWCCYVTCKKCERTVERYVCK
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Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Shares much functionality with wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N-terminal kinase (JNK) to regulate gastrulation movements. Acts in a non-cell-autonomous manner to control neural crest migration, probably acting as an extracellular signal from surrounding tissue, but is not required for neural crest induction. Acts redundantly with wnt11b during pronephros induction. Regulates cardiac morphogenesis through the activation of JNK, but is not required for cardiac differentiation. Essential for dorsal fin development required for an epithelial to mesenchymal transformation event prior to migration of cells into the fin, and ultimately for maintenance of fin structure. Mediates dorsal fin development through a non-canonical pathway mediated by Ca(2+) (By similarity).
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B2GUV7
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IF2P_RAT
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Eukaryotic translation initiation factor 5B (eIF-5B) (EC 3.6.5.3) (Annexin V-binding protein ABP-7) (Translation initiation factor IF-2)
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MGKKQKNKSEDSTKDDTDLGALAAEIEGAGAAKEQEPQKGKGKKKKEKKKQDFDENDILRELEELSLEAQGIGADRDAATVKPTENNEEESASKQDKKKKGQKGKKTSFDENDSEELEDKDSKSKKPARPNSEVLLSGSEDADDPNKLSKKGKKAQKSTKKRDGSEEDEDNSKRSKERSRVNSSGESGGESDEFLQSRKGQKKNQKNKSVPTIDSGNEDDDSSFKIKTVAQKKAEKKERERKKREEEKAKLRKVKEKEELEKGRKEQSKQREPQKRPDEEVLVLRGTPDAGAASEEKGDIAATLEDDNEGDKKKKDKKKKKTEKDDKEKEKKKGPSKSTVKAIQEALAKLREEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEVTLRHLQAQGVEVPSKDSLPKKRPVYEDKKKKKTPQQLESKEALETVEVSAPVEVVDQGVPEKEETPPSVDAEEDEETEDAGLDDWEAMASDEEREKEGNMIHIEVEENPEEEEEEEEDEDEEDSEDEEDEGDSEGSDGDEEDYKLSDEKDLGKAGDTKPNKDASSDSEYDSDDDRTKEERAYDKAKRRIEKRRLEHGKNVNTEKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKDDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNSRDPIVIGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMFGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII
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Plays a role in translation initiation. Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex. Is released after formation of the 80S initiation complex. Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes. In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit.
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B2GUY0
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MA1B1_RAT
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Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (ER mannosidase 1) (ERMan1) (Mannosidase alpha class 1B member 1)
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MYPPPPAPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLQVSDQWKALSGSRAEVEKMKLEVLPVLPAPQKESAEPEGFADILSQKRQRHLRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATEPPSKRAEASIKPLFLASRIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKEARKWVSENLDFQKNVDVNLFESTIRILGGLLSAYHLSGDSLFLSKAEDFGNRLMPAFTTPSKIPYSDVNIGTGFAHSPQWTSDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFTHPGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVRAIEGIKAHLLRQSQPRKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNMYPRADHKDVEVKPADRHNLLRPETVESLFYLYRVTKDRKYQDWGWEILQSFNKYTRVPSGGYSSINNVQNSHKPEPRDKMESFFVGETLKYLYLLFSDDLELLGLDTCVFNTEAHPLPIWSPA
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Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity).
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B2GUY1
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PLK4_RAT
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Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase Sak)
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MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSESEARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSTKSKDLGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRRLLVGQPLPNKITVFQKNKNSSDFSSGDGSNFCTQWGNPEQEANNRGRGRVIEDAEERPHSRYLRRAHSSDRSNPSNQSRAKTYSIERCHSVEMLSKPRRSSLDETKHSSNHHCLGKTPFPFADQTPQMEIVQQWFGNLQMNGETSEHNTISPNRDFQDYPDVQDTLRNTWTDTRASKNSDNSANVHPAKQLSTMKYMTAHHHKPEIMQQELAIHPHSEQNKSRSMESTLGYRKPTLRSITSPLVAHRLKPIRQKTKKAVVSILDSEEVCVELLKECTSEGHVKEVLQISSDGTTITVYYPNDGRGFPLADRPPLPTDNISRYSFDSLPEKYWRKYQYASRFIQLVRSKTPKITYFTRYAKCILMENSPGADFEVWFYDGAKIHKTEDVIHIIEKTGLSYTLKNENDFTSLKEEVKIYMDHANEGHRTCLALESVISEEEKRSRGSSFFPIIVGRKPGTTSSPKALSPPPVDPGYSKGEQASSSRLSANSAAFPTQTPVLSPSAVTVEGPGQTAATTGTSISSSLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPSFQ
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Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). Phosphorylates CEP131 and PCM1 which is essential for proper organization and integrity of centriolar satellites (By similarity).
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B2GUZ1
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UBP4_RAT
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Ubiquitin carboxyl-terminal hydrolase 4 (EC 3.4.19.12) (Deubiquitinating enzyme 4) (Ubiquitin thioesterase 4) (Ubiquitin-specific-processing protease 4)
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MAEGRGTHERPDVETQKTELGALMGTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTIQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSSKPSASPYSSMSASLIANGDSTNSSGMHNSGVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKPYLEPKDANGRPDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRIMEVFLVPADPHCRPIQYRVTVPLMGAISDLCEALSKLSGIAAENMVVTDVYNHRFHKIFQMDEGLSHITPRDDIFVYEICTTPMDGSEYITLPVYFREKKSRPSSTSSGAVLYGQPLLVSVPKHRLTLESLYQAVCERISRYIKQPLPEEFLSSPLEPGACNGSRGSYEGDEEEMDHQEEGKEQLSEVEESGEDSQGGDPTETTQKAKGPPRHKRLFTFSLVNSCGTADINSLATDGKLLKLNSRSTLAIDWDSETRSLYFDEQESEACEKHTSMSQPQKKKKAAIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIVTKAAYVLFYQRRDDECPSTSSPVSFPGSDGGAKLSSSQQDLGEEEAYTMDTN
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Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. Deubiquitinates HAS2. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER.
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B2GV06
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SCOT1_RAT
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Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (SCOT) (EC 2.8.3.5) (3-oxoacid CoA-transferase 1) (Somatic-type succinyl-CoA:3-oxoacid CoA-transferase) (SCOT-s) (Succinyl-CoA:3-oxoacid CoA transferase)
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MAALKLLSSGLRLCASARNSRGALHKGCACYFSVSTRHHTKFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFRGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEKYEKRIERLSLRKEGEGKAKSGKPGEDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASFFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKGVFDVDKKNGLTLIELWEGLTVDDIRKSTGCDFAVSPNLMPMQQIST
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Key enzyme for ketone body catabolism. Catalyzes the first, rate-limiting step of ketone body utilization in extrahepatic tissues, by transferring coenzyme A (CoA) from a donor thiolester species (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl-CoA thiolase into two acetyl-CoA molecules which enter the citric acid cycle for energy production (By similarity). Forms a dimeric enzyme where both of the subunits are able to form enzyme-CoA thiolester intermediates, but only one subunit is competent to transfer the CoA moiety to the acceptor carboxylate (3-oxo acid) and produce a new acyl-CoA. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity).
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B2GV17
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CBPC5_RAT
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Cytosolic carboxypeptidase-like protein 5 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein-like 5) (Protein deglutamylase CCP5)
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MELRCGGLLFSSRFDSGNLAHVEKVETVPSDGEGVGGAATAPTSGSASSPDYEFNVWTRPDCAETEYENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPSRPRWERIRERPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLSQLDQRFPENYSAHSSPLDSIYYHRELLCYSLDGLRVDLLTITSCHGLRDDREPRLEQLFPDVGTPRPFRFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHSRLNSKNPSNQQPSSLHLPPEVPLSDLEKANNLHNELHLGQSPDGENHDRWTETEPTEEKTDPVWIMPQPIPELEEPAPDAIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPTFPSRYTVELFEQVGRALAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRNSRGLTSTANVGLNKKRGSRTPPKSNNGLPVSCSENALSRARSFSTGTSTGGSSSQQNSPQMKNSPSFPFHGSRPAGLPGLGSSTQKVSHRVLGPVREPRCPDRRRRQQQQQQQQQQQQQQQQQPLNQRSTTSSLAPSPTLASASPTSSRNMGSCLLPNSLSLSGSSCPFSSSGDKPEAVMVIGKSLLGAGARIPCIRTRLQTCQRRVSARRGPGFPRLGPGWAGAHRRLAEG
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Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation.
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B2GV24
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UFL1_RAT
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E3 UFM1-protein ligase 1 (EC 2.3.2.-) (E3 UFM1-protein transferase 1) (Multiple alpha-helix protein located at ER) (Regulator of C53/LZAP and DDRGK1)
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MADAWEEIRRLAADFQRAQFAESTQRLSERNCIEIVNKLISQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLTHIENRVGDIIKSEKHVQMVLGQLVDENYLDRLSEEVNDKLQESGQVTVSELCKTYDLPGDFLTQALTQRLGRIINGHLDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLVSKYGFQEQLLYSVLEELVSTGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVNYIKKRYKNTPLLFLKATCVGQGLVDQVEASVEEAISSGTWVDVSPLLPSSLSVEDAAMLLQQVMRPFGKHASATVFSDTVVVSEKFINDCTKLFSERMHQKAEKEMKNNPVHLITEEDLKQISILESVNTNKKDKKDERRKKATEGSGSVRGGGGGNAREYKIKKVKKKGRKDEDSDDESQSSHAGKKKPDITFMFQDEIEGCLRKHIPDAPEEFISELAEHLIKPLNKMYLEVVRSVFMSSTSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKYFADDTQTALTKHLLKTVCTDITNLMFNFLASDLMMAVEDPATITSDMRKKILSKLTEETKVALTKLHNSLNEKSIEDFLSCLDSATEACDIMVKKGDKKRERQILFQHRQALADQLKVTEDPALILHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLHNKIPEDQHTLLVKYQGLVVKQLVSQNKKSGQGEDPSSDDLDKEQHDVTNTTRKELQELSLSIKDLVLKPRKSSVTEE
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E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. In response to endoplasmic reticulum stress, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets. Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha. Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (By similarity). Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor (By similarity). Mediates ufmylation of DDRGK1 and CDK5RAP3 the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (By similarity). Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition. Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4. Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (By similarity). Required for hematopoietic stem cell function and hematopoiesis. Required for cardiac homeostasis (By similarity).
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B2GV46
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FFAR3_RAT
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Free fatty acid receptor 3 (G-protein coupled receptor 41)
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MDTSFFPGNHWLFFSVDLLVFLVGLPLNVMALVVFVNKLRRRPVAVDLLLLNLTISDLLLLLFLPFRIVEAACGMKWILPFIFCPLSGFLFFTTIYLTSLFLMTVSIERFLSVAYPLWYKTRPRLAQAGLVSGICWFLASAHCSVIYVTEYWGNATYSQGTNGTCYLEFREDQLAILLPVRLEMAVVLFMVPLCITSYCYSRLVWILSQGASRRRRKRVMGLLVATLLIFFVCFGPYNMSHVVGYVRGESPTWRSYVLLLSTLNSCIDPLVFYFSSSKFQADFHQLLSRLIRACVPWTQEVSLELKVKNGEEPSKECPS
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G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells.
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B2GV50
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RFX2_RAT
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DNA-binding protein RFX2 (Regulatory factor X 2)
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MQNSEGGADSPATVALRPAAQPVPASPQRVLVQAAGSTPKGTPMQTLTLPRVQPVPPQVQHVYPAQVQYVEGGDAVYANGAIRAAYTYNPDPQLYAPSSAASYFETPGGAQVTVAASSPPAVPSHGMVGITMDVSGTPIVSGAGTYLIHGGMDSTRHSLAHTARSSPATLQWLLDNYETAEGVSLPRSSLYNHYLRHCQEHKLEPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGIRLKPDSPLNRLQEDTQYMAMRQQPTHQKPRYRPAQKSDSLGDGSAHSNMHSTPEQAMAAQGQHHQQYIDVSHVFPEFPAPDLGSTLLQESVTLHDVKALQLVYRRHCEATLDVVMNLQFQYIEKLWLSFWNCKATSSDGRASLPASDEEPEVTLLPKDKLISLCKCEPILQWMRSCDHILYQALVETLIPDVLRPVPSSLTQAIRNFAKSLEGWLINAMSGFPQQVIQTKVGVVSAFAQTLRRYTSLNHLAQAARAVLQNTSQINQMLSDLNRVDFANVQEQASWVCQCEESLVQRLEHDFKVTLQQQSSLDQWASWLDNVVTQVLKQHAGSPSFPKAARQFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMFYLVEHRVAQATGETPIAVMGEFNDLASLSLTLLDKEDIGDGHSSEADVDGRSLGEPLVKRERSDPSHPLQGI
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Transcription factor that acts as a key regulator of spermatogenesis (By similarity). Acts by regulating expression of genes required for the haploid phase during spermiogenesis, such as genes required for cilium assembly and function (By similarity). Recognizes and binds the X-box, a regulatory motif with DNA sequence 5'-GTNRCC(0-3N)RGYAAC-3' present on promoters. Probably activates transcription of the testis-specific histone gene H1-6.
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B2GV54
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NCEH1_RAT
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Neutral cholesterol ester hydrolase 1 (NCEH) (EC 3.1.1.-) (Acetylalkylglycerol acetylhydrolase) (2-acetyl MAGE hydrolase) (EC 3.1.1.71) (Arylacetamide deacetylase-like 1)
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MRSSCVLLAALLALVAYYVYIPLPSAVSDPWKLMLLDATFRGAQQVSNLIHSLGLSHHLITLNFIIISFGKKSARSSPRVKVTDTDFDGVEVRVFEGPPKPDEPLRRSVVYIHGGGWALASAKISYYDQLCTAMAEELNAVIVSIEYRLVPQVYFPEQIHDVIRATKYFLQPEVLDKYKVDPGRVGVSGDSAGGNLAAALGQQFTYVESLKNKLKLQALIYPVLQALDFNTPSYQQSMNTPILPRHVMVRYWVDYFKGNYDFVEAMIVNNHTSLDVERAAALRARLDWTSLLPSSIKKNYKPVLQTIGDARIVKEIPQLLDAAASPLIAEQEVLQALPKTYILTCEHDVLRDDGIMYAKRLESAGVNVTLDHFEDGFHGCMIFTSWPTNFSVGIRTRDSYFKWLDQNL
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Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-acetyl-sn-glycerol), the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). May be responsible for the hydrolysis of cholesterol esters (such as cholesteryl (9Z-octadecenoate)) in macrophages (By similarity). Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds (By similarity).
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B2GV72
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CRB3_RAT
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Carbonyl reductase [NADPH] 3 (EC 1.1.1.184) (Monomeric carbonyl reductase 3) (Quinone reductase CBR3) (EC 1.6.5.10)
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MSSCSRVALVTGANKGIGFAITRDLCRKFSGDVVLTARDEARGRAAVKQLQAEGLSPRFHQLDIDNPQSIRALRDFLRKEYGGLNVLVNNAGIAFRMDDPTPFDVQAEVTLKTNFFATRNVCTELLPIMKPHGRVVNVSSLQGLKALENCSEDLQERFRCDTLTEGDLVDLMKKFVEDTKNEVHEREGWPDSAYGVSKLGVTVLTRILARQLDEKRKADRILLNACCPGWVKTDMARDQGSRTVEEGAETPVYLALLPPDATEPHGQLVRDKVVQTW
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Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols. Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin. Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones. Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified (By similarity).
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B2GV87
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PTPRE_RAT
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Receptor-type tyrosine-protein phosphatase epsilon (Protein-tyrosine phosphatase epsilon) (R-PTP-epsilon) (EC 3.1.3.48)
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MEPFCPLLLASFSLSLATAGQGNDTTPTESNWTSTTAGPPDPGTSQPLLTWLLLPLLLLLFLLAAYFFRFRKQRKAVVNSNDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGDTELDVSSLERHLQTLHGTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIFSDYANFK
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Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity). Acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver. Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake (By similarity). Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca(2+).
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B2HIL7
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MSL7_MYCMM
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Phenolphthiocerol synthesis polyketide synthase type I Pks15/1 (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41)
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MTTSGESADQQNDKLFRYLKKVAVELDEARARLREYEQRATEPVAVVGIGCRFPGGADGPEGLWDLVSQGRDAVTEFPNDRGWDTEGLFDPDPDAEGKTYTRWGAFVENATNFDAGFFGIPPSEVLAMDPQQRLMLEVSWEALEHAGIDPMSLRGSSTGVFTGIFAPSYGGKDVGALQGYGLTGSPVSVASGRVAYVLGLEGPALSVDTACSSSLVAIHWAMASLRSGECDMALAGGVTVMGLPSIFVGFSRQRGLAADGRCKAFAAAADGTGWGEGAGVLVLERLSDAQRNGHNVLAVVRGSAINQDGASNGLTAPNGLAQQRVIQAALANCGLTSADVDVVEAHGTATTLGDPIEAEALLATYGQGRPTDQPLWVGSIKSNMGHTQAAAGVAGVIKMVQAMRHGLMPASLHVDEPSKRVDWESGAVSVLAEARDWPDAGRPRRAGVSSFGISGTNAHVILEEAPAPEAVPDSESNKGEPSLPVVPWVISARSAEALTAQAGRLLAHVQADPQSNPVDIGFSLAGRSAFEHRAVVVGADRQQLLTGLATLADGAPGAGVVTGQAGSVGKTAVVFPGQGSQRIGMARELHDQLPVFAEAFDAVADELDRHLRIPLREVMWGSDAALLDSTEFAQPALFAVEVALFAALQRWGLQPDFVMGHSVGELSAAYVAGVLTLADAAMLVVARGRLMQALPAGGAMVAVAAAEDEVLPSLTDGVGIAAINAPKSVVISGAEAAVTAISDQFAQQGRRVHRLAVSHAFHSPLMEPMLEEFARIAAQVEAREPQIALVSNVTGELASADGGFGSAQYWVEHVRRAVRFADSARQLHTLGVTHFVEVGPGSGLTGSIEQSLAPAEAVVVSMLGKDRPEVASVLTAFGQLFSTGMSVDWPAVFAGSGATRVDLPTYAFQRRRFWEVPGADGPADATGLGLGGAEHALLGAVVERPDSGGVVLTGRLALADQPWLADHVIGGVVLFPGAGFVELAIRAGDEVGCAVVEELVLAAPLVLHPGMGVQVQVIVGAADDSGNRALSVYSRGDQSEDWLLNAEGMLGVEAASSGADLSVWPPEGAESVDISDGYAQLADRGYAYGPGFQGLVGVWRRDSELFAEVVAPSGVAVDKMGMHPVVLDAVLHALGLTAEQNPDSDETKLPFCWRGVSLHAGGAGRVRARLTMSGPDSISVEIADAAGLPVLTVGALVTRAMSAAQLRAAVAAAGGGAPDQGPLDVIWSPIPLSGSGTNGSAQPAVVSWADFCAGGDGGAAGDAGVVVWEPNPAGEDVVGSVYAATHAALEVLQSWFDGDRAGTLVVLTHGAVAMPGENVSDLAGAAVWGIVRSAQAENPGRIVLVDADAAVEAAELVAVGEPQLVVRSGAAHAARLAPAAPLLAVPADESAWRLAAGGGGTLEDLVIEPCPEVQAPLAAGQVRVAVRAVGVNFRDVVAALGMYPGEAPPLGAEGAGVVLEVGPQVSGVAVGDSVMGFLGGAGPLSVVDQQLITRMPQGWSFAQAAAVPVVFLTALFGLQDLAKIQPGESVLIHAGTGGVGMAAVQLARHWGVEIFVTASRGKWDTLRAMGFDDDHIGDSRTLDFEEKFLAVTDGRGVDVVLDSLAGDFVDASLRLLVRGGRFLEMGKTDIRDADKIAANYPGVWYRAFDLSEAGPVRMQEMLAEVRELFDTAVLHRLPVTTWDVRCAPAAFRFMSQARHIGKVVLTMPSALADGLADATVLITGATGAVGAVLARHMLDAYGVRHLVLASRRGDRAEGAAELAAELSEAGANVQVVACDVADRDAVEAMLARLSGEYPPVRGVIHAAGVLDDAVISSLTPERIDTVLRAKVDAAWNLHEATLDLDLSMFVLCSSIAATVGSPGQGNYSAANSFLDGLAAHRQAAGLAGISVAWGLWEQSGGMAAHLSSRDLARMSRSGLAPMNPEQAVGLLDAVLAINHPLMVATLLDRPALEARAQAGGLPPLFAGVVRRPRRRQIEDTGDAAQSKSALAERLNGLSAGERQDALVGLVCLQAAAVLGRPSPEDIDPEAGFQDLGFDSLTAVELRNRLKSATGLTLPPTVIFDHPTPTAIAEYVGRQIPDSQATQAEEEKLPESDGEMVSVTA
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Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).
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B2HN69
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CAR_MYCMM
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Carboxylic acid reductase (CAR) (EC 1.2.1.-) (ATP/NADPH-dependent carboxylic acid reductase) (Fatty acid reductase)
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MSPITREERLERRIQDLYANDPQFAAAKPATAITAAIERPGLPLPQIIETVMTGYADRPALAQRSVEFVTDAGTGHTTLRLLPHFETISYGELWDRISALADVLSTEQTVKPGDRVCLLGFNSVDYATIDMTLARLGAVAVPLQTSAAITQLQPIVAETQPTMIAASVDALADATELALSGQTATRVLVFDHHRQVDAHRAAVESARERLAGSAVVETLAEAIARGDVPRGASAGSAPGTDVSDDSLALLIYTSGSTGAPKGAMYPRRNVATFWRKRTWFEGGYEPSITLNFMPMSHVMGRQILYGTLCNGGTAYFVAKSDLSTLFEDLALVRPTELTFVPRVWDMVFDEFQSEVDRRLVDGADRVALEAQVKAEIRNDVLGGRYTSALTGSAPISDEMKAWVEELLDMHLVEGYGSTEAGMILIDGAIRRPAVLDYKLVDVPDLGYFLTDRPHPRGELLVKTDSLFPGYYQRAEVTADVFDADGFYRTGDIMAEVGPEQFVYLDRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYIYGNSARAYLLAVIVPTQEALDAVPVEELKARLGDSLQEVAKAAGLQSYEIPRDFIIETTPWTLENGLLTGIRKLARPQLKKHYGELLEQIYTDLAHGQADELRSLRQSGADAPVLVTVCRAAAALLGGSASDVQPDAHFTDLGGDSLSALSFTNLLHEIFDIEVPVGVIVSPANDLQALADYVEAARKPGSSRPTFASVHGASNGQVTEVHAGDLSLDKFIDAATLAEAPRLPAANTQVRTVLLTGATGFLGRYLALEWLERMDLVDGKLICLVRAKSDTEARARLDKTFDSGDPELLAHYRALAGDHLEVLAGDKGEADLGLDRQTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNALGTAELLRLALTSKIKPYSYTSTIGVADQIPPSAFTEDADIRVISATRAVDDSYANGYSNSKWAGEVLLREAHDLCGLPVAVFRCDMILADTTWAGQLNVPDMFTRMILSLAATGIAPGSFYELAADGARQRAHYDGLPVEFIAEAISTLGAQSQDGFHTYHVMNPYDDGIGLDEFVDWLNESGCPIQRIADYGDWLQRFETALRALPDRQRHSSLLPLLHNYRQPERPVRGSIAPTDRFRAAVQEAKIGPDKDIPHVGAPIIVKYVSDLRLLGLL
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Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes. Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor.
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B2IZD3
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BDLP_NOSP7
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Bacterial dynamin-like protein (BDLP) (EC 3.6.5.5)
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MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLNTFLTRERAIAELRQVRTLARLACNHTREAVARRIPLLEQDVNELKKRIDSVEPEFNKLTGIRDEFQKEIINTRDTQARTISESFRSYVLNLGNTFENDFLRYQPELNLFDFLSSGKREAFNAALQKAFEQYITDKSAAWTLTAEKDINAAFKELSRSASQYGASYNQITDQITEKLTGKDVKVHTTTTAEEDNSPGWAKWAMGLLSLSKGNLAGFALAGAGFDWKNILLNYFTVIGIGGIITAVTGILLGPIGFALLGLGVGFLQADQARRELVKTAKKELVKHLPQVAHEQSQVVYNAVKECFDSYEREVSKRINDDIVSRKSELDNLVKQKQTREINRESEFNRLKNLQEDVIAQLQKIEAAYSNLLAYYS
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Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bilayer this does not stimulate subsequent GTPase activity. Does not bind lipids in the presence of GDP perhaps GTP hydrolysis disrupts membrane-binding.
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B2J528
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PAL_NOSP7
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Phenylalanine ammonia-lyase (EC 4.3.1.24)
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MNITSLQQNITRSWQIPFTNSSDSIVTVGDRNLTIDEVVNVARHGTQVRLTDNADVIRGVQASCDYINNAVETAQPIYGVTSGFGGMADVVISREQAAELQTNLIWFLKSGAGNKLSLADVRAAMLLRANSHLYGASGIRLELIQRIETFLNAGVTPHVYEFGSIGASGDLVPLSYITGALIGLDPSFTVDFDGKEMDAVTALSRLGLPKLQLQPKEGLAMMNGTSVMTGIAANCVYDAKVLLALTMGVHALAIQGLYGTNQSFHPFIHQCKPHPGQLWTADQMFSLLKDSSLVREELDGKHEYRGKDLIQDRYSLRCLAQFIGPIVDGVSEITKQIEVEMNSVTDNPLIDVENQVSYHGGNFLGQYVGVTMDRLRYYIGLLAKHIDVQIALLVSPEFSNGLPPSLVGNSDRKVNMGLKGLQISGNSIMPLLSFYGNSLADRFPTHAEQFNQNINSQGYISANLTRRSVDIFQNYMAIALMFGVQAVDLRTYKMKGHYDARTCLSPNTVQLYTAVCEVVGKPLTSVRPYIWNDNEQCLDEHIARISADIAGGGLIVQAVEHIFSSLKST
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Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway.
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B2KF05
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BRPF3_MOUSE
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Bromodomain and PHD finger-containing protein 3
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MRKPRRKSRQNAEGRRSPSPYSLKCSPTRETLTYAQAQRIVEVDIDGRLHRISIYDPLKIITEDELTAQDITECNSNKENSEQPQFPAKSKKPSSKGKRKESCSKHASGTSFHLPQPSFRVVDTGSQPEAPPLPAAYYRYIEKPPEDLDAEVEYDMDEEDIAWLDMVNEKRRADGHSSVSADTFELLVDRLEKESYLESRSSGAQQSLIDEDAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRPVDCVLCPNKGGAFKQTSDGHWAHVVCAIWIPEVCFANTVFLEPIEGIDNIPPARWKLTCYICKQKGLGAAIQCHKVNCYTAFHVTCAQRAGLFMKIEPMRETSLNGTTFTVRKTAYCEAHSPSVAVARRKGDSPRSLSEVGDEDGPKEGGGEEEQEEAEEEGQEGQGGVGSPLKGVSKKGKMSLKQKIKKEPEEAGREAPSITLPMVTVPQIPSYRLNKICSGLSFQRKTQFMQRLHNYWLLKRQARNGVPLIRRLHSHLQSQRNAEQREQDEKTSAVKEELKYWQKLRHDLERARLLIELIRKREKLKREQVKVQQAAMELELMPFTVLLRTTLDLLQEKDSAHIFAEPVSLSEVPDYLEFISKPMDFSTMRRKLESHLYHTLEEFEEDFNLIVTNCMKYNAKDTIFHRAAVRLRDLGGAILRHARRQAENIGYDPERGTHLPESPRLEDFYRFSWEDVDNILIPENRAHLSPEAQLKELLEKLDLVSTMRSSGARTRRVRMLRREINALRQKLAQPPPPQLLSLNKTVPNGELPAGSRGDTAVLEQAQQEEPEEEGDRDDSKLPAPPTLEPTGPAPSLSEQESPPDPPTLKPISDSKPSSRFLKSRKVEDEELLEKSALQLGSEPLQCLLSDNGIDRLSLTNPDSHPDTPLGTVGRRTSVLFKKAKNGVKLQRGPDGTLENGEDHGPEDDPASPASTEDEHYSRKRPRSRSCSDSEGERSPQQEEETGVTNGFGKHTESGSDSECSLGLSGGLAFEAGSGLTPPKRSRGKPALSRVPFLEGVNGDSDHSGSGRSLLMPFEDHGDLEPLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGERLFLVLFFDNKRTWQWLPRDKVLPLGVEDTVDKLKMLEGRKTSIRKSVQVAYDRAMIHLSRVRGSHAFVTSSYL
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Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity. Plays a role in DNA replication initiation by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby facilitating the activation of replication origins. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.
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B2KI42
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CADH2_RHIFE
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Cadherin-2 (Neural cadherin) (N-cadherin) (CD antigen CD325)
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MCRIVGAPRTLLPLLAALLQASVEASGGIALCKTGFPEDVYSAVLSQDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPNLPEDSVKESQEIEEIVFPRQLMKHNGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDDDDPNTLNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYMLIIQATDTEGSPTYGLSNTATAVITVTDVNDNPPEFTAMSFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMPQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVVPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRLDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD
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Calcium-dependent cell adhesion protein preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.
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B2KI64
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PI4KB_RHIFE
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Phosphatidylinositol 4-kinase beta (PI4K-beta) (PI4Kbeta) (PtdIns 4-kinase beta) (EC 2.7.1.67)
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MGDTVVAPAPLKPASESTPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLQKVKLSHGGVASSDRGTPLELVNGDGVDGEIRCLDDPPTGIREEDDETEATVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYVHMDEDVGDAIKPYIVHRCRQSVDFSLQCALLLGAYSSDMHISTQRHSRGTKLRRLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVESEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTSVPARIPENRIRSTRSVENLPECGISHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEMHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
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Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (By similarity). May play an important role in the inner ear development.
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B2KPN7
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COMA_CONMR
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Conomarphin-Mr3 (Conomarphin) (Marmophine) (Mr-1)
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MMSKLGVLLCIFLVLFPMATLQLDGDQTADRHADQRGQDLTEQQRNSKRVLKKRDWEYHAHPKPNSFWTLV
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May act as a neurotoxin.
|
B2KPR3
|
LAMT_CATRO
|
Loganic acid O-methyltransferase (CrLAMT) (EC 2.1.1.50)
|
MVATIDSIEMPALPTAVEAHPMKGGDDSHSYSQNSCYQKGVIDAAKAVIVEAVNEKLDLENNPIFDPIKPFRIADFGCSTGPNTFHAMQNIVESVETKYKSLQKTPEFHVFFNDHVNNDFNVLFRSLPPNREFFAAGVPGSFYTRVFPKNSIHFAHCSYALHWLSKVPKEIQDKNSLAYNKGRIHYTGTEKHVVKAYFGQFQRDFEGFLKARAQEIVVGGLMVIQIPGLPSGEVLFSRTGAGLLHFLLGTSLMELVNKGIINEESVDSFNLPQYHPSVEDLEMVIEMNDCFTIERVGTLPHPMKNLPFDVQRTSLQVRAIMECILTEHFGENILDPLFEIYTKNLQENFHVFDKEIRKDADLYLVLKRKGN
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Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine and ajmalicine) biosynthesis pathway. Catalyzes the methylation of loganic acid (6S,7R) to produce loganin. Weak activity with secologanic acid as substrate. Inactive on deoxyloganic, dehydrologanic, epiloganic and loganetic acid.
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B2LT61
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TLR2_BISBI
|
Toll-like receptor 2 (CD antigen CD282)
|
MPRALWTAWVWAXIILSTEGASDQASSLSCDSTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLXTLKVGNSNSFTEIHEKDFTGLTFLEELEISAQNLQIYVPKSLKSIQNISHLILHLKQPVLLVDILVDIVSSLDCLELRDTNLHTFHFSEASISEMSTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFRALSLDRIRHLGNVETLTIRKLHIPQFFLFHDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACKDAWPFLQTLVLRQNRLKSLEKTGELLLTLENLNSLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISRNIINTFSKEQLDSFQQLKTLEAGGNNFICSCDFLSFTQGQQALGRVLVDWPDDYRCDSPSHVRGQRVQDARLSLSECHRAAVVSAACCALFLVLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDICYDAFVSYSERDSYWVENLMVQELEQFNPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTIFVLSENFVXSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPVDETQQEGFWLNLRAAIRS
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Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity).
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B2LT62
|
TLR2_CAPIB
|
Toll-like receptor 2 (CD antigen CD282)
|
MPRALWTAWVWAVISAFTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSDNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTQIHEKDFTGLTFLEELEISAQNLQLYVPKSLKSIQNISHLILHLKQPVLLLDILIDIVSSLDYLELRDTNLHTFYFSEASISEINTSVKKLIFRNVQFTDESFVEVVKLFNYVSGILEVEFDDCTHDGIGDFTALTLNRIRYLGNVETLTIRKLHIPQFFLFYDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLRNSACEHAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFTQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHRAAVVSAVCCALFLLLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSEQDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSENFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKIMNTKTYLEWPTDETQQEAFWLNLRAAIRS
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Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity).
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B2LT64
|
TLR2_GIRCA
|
Toll-like receptor 2 (CD antigen CD282)
|
MPRALWTAWVWAVISLSTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTAGVKSLDLSNNEITHVGNRDLQSCVNLKTLRLGANEIHTVEEDSFFHLRSLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYRTLGETSLFSHLSNLRTLKVGNSNSFTEIHEKDFTGLTFLEELEISARNLQIYAPKSLKSIQNISHLILHLKQPVLLLDILVDIVSSLDYLELRDTNLHTFHFSEASISEMNTSVKKLIFRNVQFTDESFVEVVKLFNYVSGISEVEFDDCTHDGIGDFRALALERTRYLGNVETLTIRKLHIPQFFLFQDLSSIYSLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACEHAWPFLQTLVLRQNRLKSLEKTGELLLTLKNLTNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTHCLPQTLEILDVSSNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISRNIINTFSKEQLDSFQQLKTLEAGGNNFICSCDFLSFMQGQQALARVLADWPDDYWCDSPSHVRGQRVRDARLTLSECHRTAVVSAVCCALFLLLLLTGVLCHRLHGLWYMKMMWAWLQAKRKPRKAPRRDICYDAFVSYSERDSYWVENLMVRELEHFDPPFKLCLHKRDFIPGKWIIDNIIDSIEKSHKTIFVLSENFVKSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAIPQRFCKLRKVMNTKTYLEWPMDETQQEGFWLNLRAAVRS
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Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity).
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B2LT65
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TLR2_SHEEP
|
Toll-like receptor 2 (CD antigen CD282)
|
MPRALWTAWVWAVISVFTEGASDQASSLSCDPTGVCDGHSRSLNSIPSGLTASVKSLDLSDNEITYVGNRDLQRCVNLKTLRLGANEIHTVEEDSFFHLRNLEYLDLSYNRLSNLSSSWFRSLYVLKFLNLLGNLYKTLGETSLFSHLPNLRTLKVGNSNSFTQIHEKDFTGLTFLEELEISAQNLQLYVPKSLKSIQNISHLILHLRQPVLLLDILIDIVSSLDYLELRDTNLHTFYFSEASISEINTSVKKLTFRNVQFTDDSFVEVVKLFNYVSGILEVEFDDCTHDGVGDFTALTLNRIRYLGNVETLTIRKLHIPQFFLFYDLSSIYPLTGKVKRVTIENSKVFLVPCLLSQHLKSLEYLDLSENLMSEETLKNSACEHAWPVLQTLVLRQNRLKSLEKTGELLLTLKNLNNLDISKNNFLSMPETCQWPGKMKQLNLSSTRIHSLTQCLPQTLEILDVSNNNLDSFSLILPQLKELYISRNKLKTLPDASFLPVLSVMRISGNIINTFSKEQLDSFPQLKALEAGGNNFICSCDFLSFAQGQQALARVLVDWPDGYRCDAPSHVRGQRVQDARLSLSECHRAAVVSAVCCALFLLLLLTGVLCHRFHGLWYMKMMWAWLQAKRKPRKAPRRDLCYDAFVSYSERDSYWVENLMVQELEHFNPPFKLCLHKRDFVPGKWIIDNIIDSIEKSRKTIFVLSESFVRSEWCKYELDFSHFRLFDENNDAAILILLEPIDKKAVPQRFCKLRKIMNTRTYLEWPTDETHREAFWLNLRAAIRS
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Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (By similarity).
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B2MVY4
|
CDK4_SHEEP
|
Cyclin-dependent kinase 4 (EC 2.7.11.22) (Cell division protein kinase 4)
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MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGAGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATARTDRETKVTLVFEHVDQDLRTYLDKAPPPGLPVETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFSPRGPRPVQSVVPELEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKAEGDAE
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Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (By similarity).
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B2RH54
|
FIMA1_PORG3
|
Major fimbrium subunit FimA type-1 (Fimbrillin) (Fimbrilin) (Major fimbrial subunit protein type I)
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MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW
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Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity.
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B2RHG1
|
MFA1_PORG3
|
Minor fimbrium subunit Mfa1 (Pg-II fim a)
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MKLNKMFLVGALLSLGFASCSKEGNGPDPDNAAKSYMSMTLSMPMGSARAGDGQDQANPDYHYVGEWAGKDKIEKVSIYMVPQGGPGLVESAEDLDFGTYYENPTIDPATHNAILKPKKGIKVNSAVGKTVKVYVVLNDIAGKAKALLANVNAADFDAKFKEIIELSTQAQALGTVADGPNPATAAGKIAKKNGTTDETIMMTCLQPSDALTIEAAVSEANAIAGIKNQAKVTVERSVARAMVSTKAQSYEIKATTQIGEIAAGSVLATITDIRWVVAQGERRQYLSKKRGTVPENTWVTPGSGFVPTSSTFHTNATEYYDYAGLWEDHNTNEAVISGTQVPTLADYQLQDVTGELANALSGKFLLPNTHKSGANAASSDYKRGNTAYVLVRAKFTPKKEAFIDRGKTYSDNTAVPEYVAGEDFFVGENGQFYVSMKSVTDPKVGGVAGMKAHKYVKGKVLYYAWLNPSTTSPDSWWNSPVVRNNIYHIHIKSIKKLGFNWNPLVPDPDPSNPENPNNPDPNPDEPGTPVPTDPENPLPDQDTFMSVEVTVLPWKVHSYEVDL
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Structural subunit of the minor fimbriae. These filamentous pili are attached to the cell surface they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Mfa1 orthologs from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable).
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B2RHG2
|
MFA2_PORG3
|
Minor fimbrium anchoring subunit Mfa2 (Minor fimbrial antigen 2)
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MNKRKHMDIRRLIISLPAIMALWGGLASCDKMIYDNYDDCPRGVYVNFYSQTECAENPSYPAEVARLNVYAFDKDGILRSANVFEDVQLSAAKEWLIPLEKDGLYTIFAWGNIDDHYNIGEIKIGETTKQQVLMRLKQDGKWATNIDGTTLWYATSPVVELKNMEDGADQYIHTRANLREYTNRVTVSVDSLPHPENYEIKLASSNGSYRFDGTVAKADSTYYPGETKVVGDSTCRAFFTTLKLESGHENTLSVTHKPTGREIFRTDLVGAILSSQYAQNINLRCINDFDIRLVAHHCNCPDDTYVVVQIWINGWLIHSYEIEL
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Anchoring subunit of the minor fimbriae. Regulates fimbrial length. These filamentous pili are attached to the cell surface they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis are major virulence factors (Probable).
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B2RHG4
|
MFA4_PORG3
|
Minor fimbrium tip subunit MfA4 (Immunoreactive 32 kDa antigen)
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MKKYLLYASLLTSVLLFSCSKNNPSEPVEDRSIEISIRVDDFTKTGETVRYERNQGSAAERLITNLYLLLFDQSGANPAKYYIAGNTFSGGIWLPDDMKVKLDMTQSEAGERKVYVVANVDNAVKTALDAVANESDLQTVKRTTAMPWSTDIASPFLMSGNKTHDFLANRLLDNVPLVRAIAKVELNISLSEKFQIVPIIVNGSLSEFKFRYVNFDKETYVVKPTTKPDNLISSANGVWPQITDWTVWGASLNTSPAPDAGTGYTLDANGKVTALRIVTYLNERDSKGATVEVALPRVDDGTLPPPEFGPELYRLPLPDKILRNHWYKYEVEI
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Tip subunit of the minor fimbriae. These filamentous pili are attached to the cell surface they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are recognized as major virulence factors (Probable).
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B2RID1
|
DPP11_PORG3
|
Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11)
|
MKKRLLLPLFAALCLSQIAHADEGMWLMQQLGRKYAQMKERGLKMKEYDLYNPNGTSLKDAVVLFDGGCTGEVVSDRGLVLTNHHCGYDMIQAHSTLEHNYLENGFWAMREADELPNKDISVVFIDKIEDVTDYVKKELKAIKDPNSMDYLSPKYLQKLADKKAGKNFSAKNPGLSVEIKAFYGGNLYLMFTKKTYTDVRLVGAPPSSIGKFGADTDNWIWPRHTGDFSIFRIYADKNGNPAPYSEDNVPLKPKRFFNISLGGVQENDYAMIMGFPGTTHRYFTASEVDEWKSIDNDIRIRMRDIRQGVMLREMLADPQIKIMYSAKYAASQNAYKRAIGANWAIKTRGLRQNKQAMQDRLIAWGAKQGTPRYEEAVHEIDATVAKRADLRRRYWMIEEGIIRGIEFARSPIPTEDETKALQGNDASARKEAIDKIRTRYSKFANKDYSAEVDKKVAVAMLTEYLKEIPYENLPLHLRLVKDRFAGDVQAYVDDIFARSVFGSEAQFDAFAAVPSVEKLAEDPMVLFASSVFDEYRKLYNELRPYDDPILRAQRTYIAGLLEMDGDQDQFPDANLTLRFTYGQVKGYSPRDNVYYGHQTTLDGVMEKEDPDNWEFVVDPKLKAVYERKDFGRYADRSGRMPVAFCATTHTTGGNSGSPVMNANGELIGLNFDRNWEGVGGDIQYLADYQRSIIVDIRYVLLVIDKVGGCQRLLDEMNIVP
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Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Preferentially cleaves the synthetic substrate Leu-Asp-methylcoumaryl-7-amide (Leu-Asp-MCA) as compared to Leu-Glu-MCA. Is involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
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B2RIT0
|
DPP5_PORG3
|
Dipeptidyl-peptidase 5 (DPP5) (EC 3.4.14.-) (MER034615)
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MNKKIFSMMAASIIGSAAMTPSAGTNTGEHLTPELFMTLSRVSEMALSPDGKTAVYAVSFPDVKTNKATRELFTVNLDGSGRKQITDTESNEYAPAWMADGKRIAFMSNEGGSMQLWVMNADGTERRQLSNIEGGITGFLFSPDEKQVLFTKDIKFGKRTKDIYPDLDKATGRIITDLMYKHWDEWVETIPHPFIANATDGMITTGKDIMEGEPYEAPMKPWSGIEDFSWSPDGQNIAYASRKKTGMAYSLSTNSDIYIYNLTSGRTHNISEGMMGYDTYPKFSPDGKSIAWISMERDGYESDLKRLFVADLATGKRTHVNPTFDYNVDMIQWAPDSKGIYFLACKEAETNLWEITLKTGKIRQITQGQHDYADFSVRNDVMLAKRHSFELPDDLYRVNPKNGAAQAVTAENKAILDRLTPIACEKRWMKTTDGGNMLTWVVLPPDFDKNKKYPAILYCQGGPQNTVSQFWSFRWNLRLMAEQGYIVIAPNRHGVPGFGQKWNEQISGDYGGQNMRDYLTAVDEMKKEPYVDGDRIGAVGASYGGFSVYWLAGHHDKRFAAFIAHAGIFNLEMQYATTEEMWFANWDIGGPFWEKDNVVAQRTYATSPHKYVQNWDTPILMIHGELDFRILASQAMAAFDAAQLRGVPSEMLIYPDENHWVLQPQNALLFHRTFFGWLDRWLKK
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Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Prefers Ala and hydrophobic residues except Pro at the P1 position, and has no preference for P2 residues. Shows high dipeptidyl peptidase activity toward the synthetic substrates Lys-Ala-, Gly-Phe-, Met-Leu-, and Ser-Tyr-methylcoumaryl-7-amide (MCA), and slowly hydrolyzes Val-Tyr-MCA. Is likely involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
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B2RKV3
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DPP7_PORG3
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Dipeptidyl-peptidase 7 (DPP-7) (DPP7) (EC 3.4.14.-)
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MQMKLKSILLGAALLLGASGVAKADKGMWLLNELNQENLDRMRELGFTLPLDSLYSFDKPSIANAVVIFGGGCTGITVSDQGLIFTNHHCGYGAIQSQSTVDHDYLRDGFVSRTMGEELPIPGLSVKYLRKIVKVTDKVEGQLKGITDEMERLRKAQEVCQELAKKENADENQLCIVEPFYSNNEYFLIVYDVFKDVRMVFAPPSSVGKFGGDTDNWMWPRHTGDFSVFRVYAGADNRPAEYSKDNKPYKPVYFAAVSMQGYKADDYAMTIGFPGSTDRYLTSWGVEDRIENENNPRIEVRGIKQGIWKEAMSADQATRIKYASKYAQSANYWKNSIGMNRGLARLDVIGRKRAEERAFADWIRKNGKSAVYGDVLSSLEKAYKEGAKANREMTYLSETLFGGTEVVRFAQFANALATNPDAHAGILKSLDDKYKDYLPSLDRKVLPAMLDIVRRRIPADKLPDIFKNVIDKKFKGDTKKYADFVFDKSVVPYSDKFHAMLKSMDKEKFAKAIEKDPAVELSKSVIAAARAIQADAMANAYAIEKGKRLFFAGLREMYPGRALPSDANFTMRMSYGSIKGYEPQDGAWYNYHTTGKGVLEKQDPKSDEFAVQENILDLFRTKNYGRYAENGQLHIAFLSNNDITGGNSGSPVFDKNGRLIGLAFDGNWEAMSGDIEFEPDLQRTISVDIRYVLFMIDKWGQCPRLIQELKLI
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Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a broad specificity for both aliphatic and aromatic residues in the P1 position, with glycine or proline being not acceptable in this position. Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), Leu-Arg-MCA and Lys-Ala-MCA to a lesser extent. Is likely involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
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B2RLK2
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KGP_PORG3
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Lys-gingipain (EC 3.4.22.47) (Lysine-specific cysteine proteinase Kgp) [Cleaved into: Lys-gingipain catalytic subunit; 39 kDa adhesin; 15 kDa adhesin; 44 kDa adhesin]
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MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKALLIAGADSYWNPKIGQQTIKYAVQYYYNQDHGYTDVYSYPKAPYTGCYSHLNTGVGFANYTAHGSETSWADPSLTATQVKALTNKDKYFLAIGNCCVTAQFDYPQPCFGEVMTRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYVAISKDGVLYGTGVANASGVATVNMTKQITENGNYDVVITRSNYLPVIKQIQAGEPSPYQPVSNLTATTQGQKVTLKWDAPSAKKAEASREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLIPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIQEGLTATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTPNPNPNPNPGTTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPEAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQDWLCLSSGQLDWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKVCVNVTINPTQFNPVKNLKAQPDGGDVVLKWEAPSGKRGELLNEDFEGDAIPTGWTALDADGDGNNWDITLNEFTRGERHVLSPLRASNVAISYSSLLQGQEYLPLTPNNFLITPKVEGAKKITYKVGSPGLPQWSHDHYALCISKSGTAAADFEVIFEETMTYTQGGANLTREKDLPAGTKYVAFRHYNCTDVLGIMIDDVVITGEGEGPSYTYTVYRDGTKIQEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAIK
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Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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B2RPY5
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GP161_MOUSE
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G-protein coupled receptor 161
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MDFVQHALLTASRGALTMSLNSSLSYRKELSNLTATEGGEGGAVSEFIAIIIITVLVCLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGVIAIDRYYAVLYPMVYPMKITGNRAVMALVYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHQEPGYTIFWQIWCALFPFLIMLVCYGFIFRVARVKARKVHCGTVVTVEEDSQRSGRKNSSTSTSSSGSRRNALQGVVYSANQCKALITILVVIGAFMVTWGPYMVVITSEALWGKNCVSPTLETWATWLSFTSAICHPLIYGLWNKTVRKELLGMCFGDRYYRESFVQRQRTSRLFSISNRITDLGLSPHLTALMAGGQSLGHSSSTGDTGFSYSQDSGTDVMLLEDGTSEDNPPQHCTCPPKRRSSVTFEDEVEQIKEAAKNSLLHVKAEVHKSLDSYAASLAKAIEAEAKINLFGEEALPGVLFTARTVPGAGFGGRRGSRTLVNQRLQLQSIKEGNVLAAEQR
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Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown.
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B2RQC2
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UBP42_MOUSE
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Ubiquitin carboxyl-terminal hydrolase 42 (EC 3.4.19.12) (Deubiquitinating enzyme 42) (Ubiquitin thioesterase 42) (Ubiquitin-specific-processing protease 42)
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MTIVDKTEPSDPSTCQNQPGSCEAVSPEDMDTGSASWGAVSSISDVSSHTLPLGPVPGAVVYSNSSVPEKSKPSPPKDQVLGDGIAPPQKVLFPSEKICLKWQQSHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQTHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVTKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTISLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIIYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRAVLNQQAYVLFYIRSHDVKNGGESAHPAHSPGQSSPRPGVSQRVVNNKQVAPGFIGPQLPSHVMKNTPHLNGTTPVKDTPSSSVSSPNGNTSVNRASPATASTSVQNWSVTRPSVIPDHPKKQKITISIHNKLPARQGQAPLNNSLHGPCLEAPSKAAPSSTITNPSAIQSTSNVPTTSTSPSEACPKPMVNGKAKVGASVLVPYGAESSEESDEESKGLAKENGVDMMAGTHSDRPEAAADDGAEASSHELQEPVLLNGANSADSDSQENSLAFDSASCQVQPELHTENLFSKLNGLPGKVTPAPLQSVPEDRILETFKLTNQAKGPAGEESWTTTGGSSPKDPVSQLEPISDEPSPLEIPEAVTNGSTQTPSTTSPLEPTISCTKEDSSVVVSAEPVEGLPSVPALCNSTGTILGDTPVPELCDPGDLTANPSQPTEAVKGDTAEKAQDSAMAEVVERLSPAPSVLTGDGCEQKLLLYLSAEGSEETEDSSRSSAVSADTMPPKPDRTTTSSCEGAAEQAAGDRGDGGHVGPKAQEPSPAKEKMSSLRKVDRGHYRSRRERSSSGEHVRDSRPRPEDHHHKKRHCYSRERPKQDRHPTNSYCNGGQHLGHGDRASPERRSLSRYSHHHSRIRSGLEQDWSRYHHLENEHAWVRERFYQDKLRWDKCRYYHDRYTPLYTARDAREWRPLHGREHDRLVQSGRPYKDSYWGRKGWELQSRGKERPHFNSPREAPSLAVPLERHLQEKAALSVQDSSHSLPERFHEHKSVKSRKRRYETLENNDGRLEKKVHKSLEKDTLEEPRVKKHKKSKKKKKSKDKHRDRESRHQQESDFSGAYSDADLHRHRKKKKKKKRHSRKSEDFIKDVEMRLPKLSSYEAGGHFRRTEGSFLLADGLPVEDSGPFREKTKHLRMESRPDRCRLSEYGQGD
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Deubiquitinating enzyme which may play an important role during spermatogenesis.
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B2RQC6
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PYR1_MOUSE
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CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate carbamoyltransferase (EC 2.1.3.2); Dihydroorotase (EC 3.5.2.3)]
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MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSANCTLHEWLQQRGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRICALDCGLKYNQIRCLCQLGAEVTVVPWDHELDSQKYDGLFLSNGPGDPASYPGVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDSLPFFSVQFHPEHRAGPSDMELLFDVFLETVREAAAGNIGGQTVRERLAQRLCPPELPIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITLHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAQLLEQHRGQALPQDLLHQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRAPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCHTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPEKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPAHLPIVAHAERQSVAAVLMVAQLTQRPVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKARWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGVVPQPPPSTPATTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKPPRKVVEPELMGTPDGPCYPAPPVPRQASPQNLGSSGLLHPQMSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVIVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPSVRDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSVQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
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This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).
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B2RQL2
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STOX1_MOUSE
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Storkhead-box protein 1
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MARPVQLAPGSLALVLSPREAGQAAGEPGGRALFRAFRRANARCFWNARLARAASRLAFLGWLRRGVLLVRAPQPCVQVLRDAWRRRALRPPRGFRITAVGDVFPVQMSPIAQCRFVPLAEVLCCAIADMNAAQVMVTQQSLLEHLIKHYPGIAVPSPDILYSTLGALIQERKIYHTGEGYFIVTPSTYFITNTPMQGNKSALLSNEGCSGPTSGTYLVSVDCCAEPTQENEALFSHCPSCQCYPDTSMCDSKDLLTAAEVTRKSQEGLEETTALTENQVVSASEDTHICVNPKPLPYTKDKGKRFGFGFLWRSLSRKEKPKAEYHSFSAQFPPEEWPVRDEDSSTKIPRDVEHALIKRINPVLTVDNLTKHTALMQKYEEQKKYNSQGTSMDILTTRHKDSSKEVIGKRQGQFAKSRRRGSSHKGRHKARSQGSELEPGNPGQEKEKQPKVPAAQPAPRTKSPSEQVHHLQGRNPAVLGSHLIYKKQINNPFQGMHLRKHSVSKGHAVQKTHGLKPTCVGPEEKPFWSAGSSDPSGVFDGEAQPPYPEQCRDKLEAGSTQVAKAPVHPVSDDFRGGPGNYPPRRVLPGPSRCCSFRESMLRPGVYHEENKDLPEVLRKSWSTCDMFLGTKEKKQALPAQRCSLDPDSSSVHAEDKTVDKILHQFQNLGLLDCPAGANRLRTHERQDGNSEELSRKALQIPEAEIVNMENEGLSDSEQDQVALSHSDPGAGDDGGCSSLCLEDDDFSETDDFCPSLPGHTQHSFAGGGTWNHLGTPAMTGKSLTDCNSKAHRLELLAIERNPWYKATGLFSNAGESPNPDLSDNPGQNSRIPWGFNYEGEPTVAHVQTPAAAAGRSLLACSTVRTTSFPVEILQESPGDRGKSPIVWRQSLPSQEMKEHFTDKLQLVKTSHGPVSAQEPQGEHLEGTENYSMTGDSGIDSPRTQSLVSTNSAILDGFKRRQHFLPNREGVQKSQNLASNSLFQLTPAINV
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Involved in regulating the levels of reactive oxidative species and reactive nitrogen species and in mitochondrial homeostasis in the placenta (By similarity). Required for regulation of inner ear epithelial cell proliferation via the AKT signaling pathway. Involved in cell cycle regulation by binding to the CCNB1 promoter, up-regulating its expression and promoting mitotic entry (By similarity). Induces phosphorylation of MAPT/tau (By similarity).
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B2RQR8
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ECE2_MOUSE
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Endothelin-converting enzyme 2 (ECE-2) (EC 3.4.24.71)
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MNVALHELGGGGSMVEYKRAKLRDEESPEITVEGRATRDSLEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW
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Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides (By similarity). May play a role in amyloid-beta processing.
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B2RR83
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YTDC2_MOUSE
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3'-5' RNA helicase YTHDC2 (EC 3.6.4.13) (Keen to exit meiosis leaving testes under-populated protein) (Ketu) (YTH domain-containing protein C2) (mYTHDC2)
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MSRPSSVSPRPPAPSGGGTGGGGGGSGGGGGGGGGGPASCGPGGGGRAKGLKDIRIDEEVKIAVNIALERFRYGDQREMEFPSSLTSTERAFIHRLSQSLGLVSKSKGKGANRYLTVKKKDGSETAHAMMTCNLTHNTKHAVRSLIQRFPVTNKERTELLPKTERGNVFAVEAENREMSKTSGRLNNGIPQVPVKRGESEFDSFRQSLPVFEKQEEIVKIIKENKVVLIVGETGSGKTTQIPQFLLDDCFKNGIPCRIFCTQPRRLAAIAVAERVAAERRERIGQTIGYQIRLESRVSPKTLLTFCTNGVLLRTLMAGDSTLSTVTHVIVDEVHERDRFSDFLLTKLRDLLQKHPTLKLILSSAALDVNLFIRYFGSCPVIYIQGRPFEVKEMFLEDILRTTGYTNKEMLKYKKEKQREEKQQTTLTEWYSAQENTFKPESQRQRAVASVSEEYDLLDDGGDAVFSQLTEKDVNCLEPWLIKEMDACLSDIWLHKDVDAFAQVFHLILTENVSVDYRHSETSATALMVAAGRGFTSQVEQLISMGANVHSKASNGWMALDWAKHFGQTEIVDLLESYSASLEFGNLDESSLVQTNGNDLSAEDRELLKAYHHSFDDEKVDLDLIMHLLYNICHSCDAGAILIFLPGYDEIVGLRDRILFDDKRFADNTHRYQVFMLHSNMQTSDQKKVLKNPPAGVRKIILSTNIAETSITVNDVVFVIDSGKVKEKSFDALNFVTMLKMVWISKASAIQRKGRAGRCRPGICFRLFSRLRFQNMLEFQTPELLRMPLQELCLHTKLLAPVNCTIADFLMKAPEPPPALIVRNAVQMLKTIDAMDAWEDLTELGYHLADLPVEPHLGKMVLCAVVLKCLDPILTIACTLAYRDPFVLPTQASQKRAAMLCRKRFTAGTFSDHMALLRAFQAWQKARSDGWERAFCEKNFLSQATMEIIIGMRTQLLGQLRASGFVRARGGGDIRDVNTNSENWAVVKAALVAGMYPNLVHVDRENVILTGPKEKKVRFHPTSVLSQPQYKKIPPANGQAAAIQALPTDWLIYDEMTRAHRIANIRCCSAVTPVTVLVFCGPARLASNALQEPSSFRADGIPNDSSDSEMEDRTTANLAALKLDEWLNFKLEPEAASLLLQLRQKWHSLFLRRMRAPSKPWSQVDEATIRAIIAVLSTEEQSAGLQQPSGIGQRPRPMSSEELPLASSWRSNNSRKSTADTEFADGSTTGERVLMKSPSPALHPPQKYKDRGILHPKRSTDDRSDQSSVKSTDSSSYPSPCASPSPPSSGKGSKSPSPRPNMPIRYFIMKSSNLRNLEISQQKGIWSTTPSNERKLNRAFWESSMVYLVFSVQGSGHFQGFSRMSSEIGREKSQDWGSAGLGGVFKVEWIRKESLPFQFAHHLLNPWNDNKKVQISRDGQELEPQVGEQLLQLWERLPLGEKTTSD
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3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells. Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability. Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs. Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease. Required for both spermatogenesis and oogenesis.
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B2RRD7
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BRPF1_MOUSE
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Peregrin (Bromodomain and PHD finger-containing protein 1)
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MGVDFDVKTFCHNLRATKPPYECPVETCRKVYKSYSGIEYHLYHYDHDSPPPPQQTPLRKHKKKGRQSRPANKQSPSPSEVSQSPGREVMSYAQAQRMVEVDLHGRVHRISIFDNLDVVSEDEEAPEEAPENGSNKENTETPAATPKSGKHKNKEKRKDSNHHHHSAPASAAPKLPEVVYRELEQDTPDAPPRPTSYYRYIEKSAEELDEEVEYDMDEEDYIWLDIMNERRKTEGVSPIPQEIFEYLMDRLEKESYFESHNKGDPNALVDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSRAVDCALCPNKGGAFKQTDDGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQCHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPPGSARRLPALSHSEGEEEEDEEEDEGKSWSSEKVKKAKAKSRIKMKKARKILAEKRAAAPVVSVPCIPPHRLSKITNRLTIQRKSQFMQRLHSYWTLKRQSRNGVPLLRRLQTHLQSQRNCEQVGRDSDDKNWALKEQLKSWQRLRHDLERARLLVELIRKREKLKRETIKIQQIAMEMQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGIDFETGMHIPHNLAGDEVSHHTEDVEEERLVLLENQKHLPVEEQLKLLLERLDEVNASKQSVGRSRRAKMIKKEMTALRRKLAHQRETGRDGPERHGPSGRGNLTPHPAACDKDGQTDSAAEESSSQETSKGLGPNMSSTPAHEVGRRTSVLFSKKNPKTAGPPKRPGRPPKNRESQMTPSHGGSPVGPPQLPIMGSLRQRKRGRSPRPSSSSDSDSDKSTEDPPMDLPANGFSSGNQPVKKSFLVYRNDCNLPRSSSDSESSSSSSSSAASDRTSTTPSKQGRGKPSFSRGTFPEDSSEDTSGTENEAYSVGTGRGVGHSMVRKSLGRGAGWLSEDEDSPLDALDLVWAKCRGYPSYPALIIDPKMPREGMFHHGVPIPVPPLEVLKLGEQMTQEAREHLYLVLFFDNKRTWQWLPRTKLVPLGVNQDLDKEKMLEGRKSNIRKSVQIAYHRALQHRSKVQGEQSSETSDSD
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Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (By similarity). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac) (By similarity). Some HAT complexes preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation. Positively regulates the transcription of RUNX1 and RUNX2 (By similarity).
|
B2RRE7
|
OTUD4_MOUSE
|
OTU domain-containing protein 4 (EC 3.4.19.12)
|
MEAAVGAPDGVDQGGVGPLEDETPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIRYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFVIYQEPNVSPSHVTENNFPEKVLLCFSNGNHYDIVYPITYKDSSAMCQSLLYELLYEKVFKTDVSKIMMGLEASEVAEESNSEISDSEDDSCKSKSTAATDVNGFKPSGSENPKNNGNSADLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCHQVRLDHNGKLSNADIHGVHSENGLVLSEELGKKHTPKNLKPPPPESWNTVSGKKMKKPNSGQNFHSDTDYRGPKNLNKPIKAPSALPPRLQHPSSGVRQHAFSSHSTGSQSQKSSSEHKNLSRMPSQITRKPDRERAEDFDHVSRESYYFGLSPEERREKQAIEESRLLYEIQNRDEQAFPALSSSSVSQSPSQNSNACVPRKSSHARDRKGSMRRADAEERKDKDSLRGHTHVDKKPEPSTLEISDDKCTRVSSPSKSKKECPSPVEQKPAEHIPLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVPAQIPILSVTQTTGPDAAVSQAHLTPSPVPVSIQAVNQPLMPLPQTMSLYQDPLYPGFPCSEKGDRAIAPPYSLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYMAACRMYPKVPVPVYPQNTWFQEAPPAQSESDCPCTDAHYSLHPEASVNGQMPQAEMGPPAFASPLVIPPSQVSEGHGQLSYQPELESENPGQLLHAEYEESLSGKNMYPQQSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFVENPVMRQNIVLPPDDKGELDLPLENLDLSKECDSVSAVDEFPDARVEGAHSLSAASVSSKHEGRVEQSSQTRKADIDLASGSSAVEGKGHPPTQILNREREPGSAEPEPKRTIQSLKEKPEKVKDPKTAADVVSPGANSVDRLQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGSSGRGGYQHVRGEESWKGQPNRSRDEGYQYHRHVRGRPYRGDRRRSGMGDGHRGQHT
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Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions (By similarity).
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B2RS91
|
RRN3_MOUSE
|
RNA polymerase I-specific transcription initiation factor RRN3
|
MAAPLLHTRLSGDVTAAASATLSASRTGLSDMLALESDFFNSPPKKTVRFGGTVTEVLLKYKKGETNDLELLKNQLSDPDIKDDQIINWLLEFRSSVMYLTKDFEQLINIILRLPWLNRSQRVVEEYLAFLGNLVSAQTVFLRPCLSMIASHFVPPRVIVKEGGIDVSDSDDEDDNLPAIFDTCHRALQIITRYVPSTPWFLMPILVEKFPFVRKSERTLECYVHNLLRISLYFPTLRREILELVIEKLLKLDVSVSRQDIEDAEEKAAQTCGGTDTTEGLFNMDEDEDTDPEKKADQEQPNQMAHPTAERLDVLLCLLLSYIEDVCRVHGKIDNNKTKDLYRDLISIFDKLLLPTHASCHVQFFMFFLCSFKLGFAEAFLEHLWKKLQDPNNPAIIRQAAANYIGSFLARAKFIPLITVKTCLDLLVNWLHMYLTNQDSGTKAFCDVALHGPFYSACQAVFYTVVFRHKQLLSGNLKQGLQYLQSLNFERIVLSQLNPLKICLPQVVNFFAAITNKYQLVFCYTIMERNSRQMLPVIRSTAGGDSVQTCTNPLDTFFPFDPCVLKRSKKFIDPIYQIWEDGSAEELQEFKKSTKKEVVEDEDDDFLKGEVPQSDTVTGLTPSSFDTHFQSPSSSVGSPPVLYIPGQSPLLTRIYD
|
Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction.
|
B2RSH2
|
GNAI1_MOUSE
|
Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
|
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
|
Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis. Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity).
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B2RTY4
|
MYO9A_HUMAN
|
Unconventional myosin-IXa (Unconventional myosin-9a)
|
MNINDGGRRRFEDNEHTLRIYPGAISEGTIYCPIPARKNSTAAEVIESLINKLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMALENRLSGEDYRFLLREKNLDGSIHYGSLQSWLRVTEERRRMMERGFLPQPQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIVINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEDERSAFHLKQPEEYHYLNQITKKPLRQSWDDYCYDSEPDCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNICYKKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEHNTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEDNSYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSKNAFISGMIGIDPVAVFRWAILRAFFRAMVAFREAGKRNIHRKTGHDDTAPCAILKSMDSFSFLQHPVHQRSLEILQRCKEEKYSITRKNPRTPLSDLQGMNALNEKNQHDTFDIAWNGRTGIRQSRLSSGTSLLDKDGIFANSTSSKLLERAHGILTRNKNFKSKPALPKHLLEVNSLKHLTRLTLQDRITKSLLHLHKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDVLVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPRNIIPSKFNIQDFFRKINLNPDNYQVGKTMVFLKEQERQHLQDLLHQEVLRRIILLQRWFRVLLCRQHFLHLRQASVIIQRFWRNYLNQKQVRDAAVQKDAFVMASAAALLQASWRAHLERQRYLELRAAAIVIQQKWRDYYRRRHMAAICIQARWKAYRESKRYQEQRKKIILLQSTCRGFRARQRFKALKEQRLRETKPEVGLVNIKGYGSLEIQGSDPSGWEDCSFDNRIKAIEECKSVIESNRISRESSVDCLKESPNKQQERAQSQSGVDLQEDVLVRERPRSLEDLHQKKVGRAKRESRRMRELEQAIFSLELLKVRSLGGISPSEDRRWSTELVPEGLQSPRGTPDSESSQGSLELLSYEESQKSKLESVISDEGDLQFPSPKISSSPKFDSRDNALSASNETSSAEHLKDGTMKEMVVCSSESITCKPQLKDSFISNSLPTFFYIPQQDPLKTNSQLDTSIQRNKLLENEDTAGEALTLDINRETRRYHCSGKDQIVPSLNTESSNPVLKKLEKLNTEKEERQKQLQQQNEKEMMEQIRQQTDILEKERKAFKTIEKPRIGECLVAPSSYQSKQRVERPSSLLSLNTSNKGELNVLGSLSLKDAALAQKDSSSAHLPPKDRPVTVFFERKGSPCQSSTVKELSKTDRMGTQLNVACKLSNNRISKREHFRPTQSYSHNSDDLSREGNARPIFFTPKDNMSIPLVSKEALNSKNPQLHKEDEPAWKPVKLAGPGQRETSQRFSSVDEQAKLHKTMSQGEITKLAVRQKASDSDIRPQRAKMRFWAKGKQGEKKTTRVKPTTQSEVSPLFAGTDVIPAHQFPDELAAYHPTPPLSPELPGSCRKEFKENKEPSPKAKRKRSVKISNVALDSMHWQNDSVQIIASVSDLKSMDEFLLKKVNDLDNEDSKKDTLVDVVFKKALKEFRQNIFSFYSSALAMDDGKSIRYKDLYALFEQILEKTMRLEQRDSLGESPVRVWVNTFKVFLDEYMNEFKTSDCTATKVPKTERKKRRKKETDLVEEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKYDPELSSRQFGVELSRLTSEDRTVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPDTTDPLQSVQDISKTTTCVELIVVEQMNKYKARLKDISSLEFAENKAKTRLSLIRRSMGKGRIRRGNYPGPSSPVVVRLPSVSDVSEETLTSEAAMETDITEQQQAAMQQEERVLTEQIENLQKEKEELTFEMLVLEPRASDDETLESEASIGTADSSENLNMESEYAISEKSERSLALSSLKTAGKSEPSSKLRKQLKKQQDSLDVVDSSVSSLCLSNTASSHGTRKLFQIYSKSPFYRAASGNEALGMEGPLGQTKFLEDKPQFISRGTFNPEKGKQKLKNVKNSPQKTKETPEGTVMSGRRKTVDPDCTSNQQLALFGNNEFMV
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Regulates Rho by stimulating it's GTPase activity in neurons. Required for the regulation of neurite branching and motor neuron axon guidance (By similarity).
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B2RU80
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PTPRB_MOUSE
|
Receptor-type tyrosine-protein phosphatase beta (Protein-tyrosine phosphatase beta) (R-PTP-beta) (EC 3.1.3.48) (Vascular endothelial protein tyrosine phosphatase) (VE-PTP)
|
MLRHGALTALWITLSVVQTGVAEQVKCNFTLLESRVSSLSASIQWRTFASPCNFSLIYSSDTSGPMWCHPIRIDNFTYGCNPKDLQAGTVYNFRIVSLDGEESTLVLQTDPLPPARFEVNREKTASTTLQVRWTPSSGKVSWYEVQLFDHNNQKIQEVQVQESTTWSQYTFLNLTEGNSYKVAITAVSGEKRSFPVYINGSTVPSPVKDLGISPNPNSLLISWSRGSGNVEQYRLVLMDKGAIVQDTNVDRRDTSYAFHELTPGHLYNLTIVTMASGLQNSRWKLVRTAPMEVSNLKVTNDGRLTSLNVKWQKPPGDVDSYSITLSHQGTIKESKTLAPPVTETQFKDLVPGRLYQVTISCISGELSAEKSAAGRTVPEKVRNLVSYNEIWMKSFTVNWTPPAGDWEHYRIVLFNESLVLLNTTVGKEETHYALDGLELIPGRQYEIEVIVESGNLRNSERCQGRTVPLAVLQLRVKHANETSLGITWRAPLGEWEKYIISLMDRELLVIHKSLSKDAKEFTFTDLMPGRNYKATVTSMSGDLKQSSSIKGRTVPAQVTDLHVNNQGMTSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDTSRYSFRALKPGSLYSVVVTTVSGGISSRQVVAEGRTVPSSVSGVTVNNSGRNDYLSVSWLPAPGEVDHYVVSLSHEGKVDQFLIIAKSVSECSFSSLTPGRLYNVTVTTKSGNYASHSFTEERTVPDKVQGISVSNSARSDYLKVSWVHATGDFDHYEVTIKNRESFIQTKTIPKSENECEFIELVPGRLYSVTVSTKSGQYEASEQGTGRTIPEPVKDLTLLNRSTEDLHVTWSRANGDVDQYEVQLLFNDMKVFPHIHLVNTATEYKFTALTPGRHYKILVLTISGDVQQSAFIEGLTVPSTVKNIHISANGATDRLMVTWSPGGGDVDSYVVSAFRQDEKVDSQTIPKHASEHTFHRLEAGAKYRIAIVSVSGSLRNQIDALGQTVPASVQGVVAANAYSSNSLTVSWQKALGVAERYDILLLNENGLLLSNVSEPATARQHKFEDLTPGKKYKMQILTVSGGLFSKESQAEGRTVPAAVTNLRITENSSRYLSFGWTASEGELSWYNIFLYNPDRTLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPAAVNHLKGSHRNTTDSLWFSWSPASGDFDFYELILYNPNGTKKENWKEKDVTEWRFQGLVPGRKYTLYVVTHSGDLSNKVTGEGRTAPSPPSLLSFADVANTSLAITWKGPPDWTDYNDFELQWFPGDALTIFNPYSSRKSEGRIVYGLHPGRSYQFSVKTVSGDSWKTYSKPISGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDSTITMIDRPPQPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFAVVVREADSMDELKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAESPDSSSKSFNIKLGAEMDSLGGKCDPSQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSMPITTESEPLFGVIEGVSAGLFLIGMLVALVAFFICRQKASHSRERPSARLSIRRDRPLSVHLNLGQKGNRKTSCPIKINQFEGHFMKLQADSNYLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRAKKLRNEQENPLFPIYENVNPEYHRDAIYSRH
|
Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin.
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B2RUJ5
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APBA1_MOUSE
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Amyloid-beta A4 precursor protein-binding family A member 1 (Adapter protein X11alpha) (Neuron-specific X11 protein) (Neuronal Munc18-1-interacting protein 1) (Mint-1)
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MNHLEGSAEVEVADEAPGGEVNESVEADLEHPEVVEGQQPSPSPPPPAGHEPEDHRGHPAPPPPPPPQEEEEEERGECLARSASTESGFHNHTDTAEGDVLAAARDGYEAERAQDADDESAYAVQYRPEAEEYTEQAEAEHVEAAQRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRAEDEPYAEPYADYGGLQEHVYEEIGDAPELEARDGLRLYERERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERAPTPGGGHPDSPGLPAPAGQQQRVVGTPGGSEVGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPVDGDSPSPGSSSPLGAESSSIPLHPGDPTEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKTAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQEPMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
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Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of AAP-beta (By similarity). Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules. {ECO:0000250, ECO:0000269|PubMed:10846156}.
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B2RUP2
|
UN13D_MOUSE
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Protein unc-13 homolog D (Munc13-4)
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MATHLSHPQRRPLLRQAIKIRRRRVRDLQDPPPQATQEVQVQSHHFSPEERDLLYEEALYTVLHRLGQPEPNHVKEASELLSYLQEAFQVQPEEHQQMLRRVRELEKPVFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQKVGVAEGSPVSRRRQKAVVKHTIPEEETHRTQVKSQTLNPVWDETFILEFEDIANASFHLDMWDLDTVESVRQKLGELTDLHGLRRIFKEARKDKGQDDFLGNVVLRLQDLRCREDQWFPLEPCTETYPDRGQCHLQFQFIHKRRATAASRSQPSYTVHFHLLQQLVSHEVTQHQAGSTSWDASLSPQAVTILFLHATQKDLSDFHQSMAQWLAYSRLYQSLEFPSSCLLHPITSIEYQWIQGRLKAEQREELATSFTSLLAYGLSLIRKFRSVFPLSVSDSPSRLQSLLRVLVQMCKMKAFGELCPDSAPLSQLVSEALRMGTVEWFHLMQQHHQPMVQGILEAGKALLNLVQDVMGDLYQCRRTWNKIFHNVLKIDLFSMAFLELQWLVAKRVQDHTVAAGNLVSPDIGESLFQLYVSLKELCQLGPVPSDSREVLALDGFHRWFQPAIPSWLQKTYSVALERVQRAVQMDTLVPLGELTKHSTSAVDLSTCFAQISHTARQLDWPDPEEAFMITVKFVEDTCRLALVYCSLIKARARELSAVQKDQSQAADMLCVVVNNMEQLRLIIDKLPTQLAWEALEQRVGAVLEEGQLQNTLHAQLQGALAGLGHEIRTGVRTLAEQLEVGIATHIQKLIGVKESVLPEDAILPLMKFLEVKLCYMNTNLVQENFSSLLTLLWTHTLTVLVEVASSQRSSSLASGRLKVALQNLEVCFHAEGCGLPPEALHTDTFQALQNDLELQAASSRELIQKYFCSRIQQQAETTSERLGAVTVKVSYRASEQRLRVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPEVAPRETQKHKKELHPLFDETFEFLVPAEPCQKAWACLLLTVLDHDRLGADDLEGEAFLPLCRVPGLTDCAEPGEAPQMRLPLTYPAPNGDPILRLLESRKGDREAQAFVKLRRQRAKQASQHAP
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Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis (By similarity). Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. {ECO:0000250, ECO:0000269|PubMed:18354201}.
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B2RUR8
|
OTU7B_MOUSE
|
OTU domain-containing protein 7B (EC 3.4.19.12) (Cellular zinc finger anti-NF-kappa-B protein) (Zinc finger A20 domain-containing protein 1) (Zinc finger protein Cezanne)
|
MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVSAALSDFEQLRQVHAGNLSPPFSGGSTCPKTPEKGGSDREPTRPSRPILQRQDDVIQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSSEHPLEMPICAFQLPDLTVYKEDFRSFIERDLIEQSMLVALEQAGRLNWWVSMDSTCQRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYALMEKGVEKEALRRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGSNGASGGGVESSEEPVYESLEEFHVFVLAHVLKRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKESAKEQAVIPLTDSEHKLLPLHFAVDPGKGWEWGKDDNDNVRLASIILSLEVKLHLLHSYMNVKWIPLSSDSQAPLAQPESPTASAGDEPRSTPESGESDKESVGSSSLGNEGSRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGPKPGGLGSGSGISSGTETLEKKKKNNTLKSWKGGKEEAAGDGPVSEKPPSESVGNGGSKYSQEVMQSLSTMRIAMQGEGKYIFVGTLKMGHRHQYQEEMIQRYLADAEERFLAEQKQKEVERKIMNGGLVSGPPPAKKPEPDGGEDQPSDSPAEPKAMAFSTAYPGGFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPSYATFPRQYPGRPYPHQDNIPALEPGKDGVHRGALLPPQFRVADSYSNGYREPPEPDGWAGAPRGLPPTQTKCKQPNCSFYGHPETNNLCSCCYREELRRREREPGGELLAHRF
|
Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B. Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2. Mediates deubiquitination of EGFR (By similarity). Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains. Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro) however the physiological significance of these data are unsure. Hydrolyzes both linear and branched forms of polyubiquitin (By similarity).
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B2RUY7
|
VWC2L_HUMAN
|
von Willebrand factor C domain-containing protein 2-like (VWC2-like protein) (Brorin-like)
|
MALHIHEACILLLVIPGLVTSAAISHEDYPADEGDQISSNDNLIFDDYRGKGCVDDSGFVYKLGERFFPGHSNCPCVCALDGPVCDQPECPKIHPKCTKVEHNGCCPECKEVKNFCEYHGKNYKILEEFKPSPCEWCRCEPSNEVHCVVADCAVPECVNPVYEPEQCCPVCKNGPNCFAGTTIIPAGIEVKVDECNICHCHNGDWWKPAQCSKRECQGKQTV
|
May play a role in neurogenesis. May play a role in bone differentiation and matrix mineralization.
|
B2RUZ4
|
SMIM1_HUMAN
|
Small integral membrane protein 1 (Vel blood group antigen)
|
MQPQESHVHYSRWEDGSRDGVSLGAVSSTEEASRCRRISQRLCTGKLGIAMKVLGGVALFWIIFILGYLTGYYVHKCK
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Regulator of red blood cell formation.
|
B2RVY9
|
TM182_MOUSE
|
Transmembrane protein 182
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MRLNVAVFFGALFGALGVLLFLVAFGSDYWLLATEVGRCSGEQNIENITFHHEGFFWRCWFSGVVEENNSNIWKFWYTNQPPSKNCTHAYLSPYPFMRGEHNSTSYDSAIIYRGFWAVLLLLGVVAALTASFLIICAAPFSSHFLYKAGGGSYIASGVLFSLVVILYVIWVQAVADMESYRALRMRDCWEFTPSILYGWSFFLAPAGVFFSLLAGLLFLVVGRHIQIHH
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Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1. Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis.
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B2RW38
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CFA58_MOUSE
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Cilia- and flagella-associated protein 58
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MTEDKAEKVMPEETAFEEIEKDFQEVLSELSGDKSLEKFRTEYEKLHSIMKKSYENEKRLMAKCRELNAEIVVNSAKVATALKLSQDDQTTIASLKKEIEKAWKMVDSAYDKEQKAKETILALKEEIVNLTKLVEQGSGLSMDQDSNIRDLLKFKEEVTKERDQLLSEVVKLRENLAQTIEKQQAAEHAKEEAEMAISQFQQEIQHRQNEASRESRKKEKLEKELRQIQTDMDGRQAEIKAMQQYMHKSKEELQRLEQQLKEQKILNERAAKEVEQFQMRNAKLQQENDQHTLTCEQLSQENQQKALELKAKEDEIHQMRLDLGKLNKIREQIHKKLHQLDDQKAEVEQQKDTLKNQILGLEREVESSKKQAELDKKAMEELLRERDILNKNMLKAVSATQKQVDLVKLHEQAKKNLEEEIQNYKDEAQKQRKIIFQLEKERDRYINEASDLTQRVLANMEDIKVREIQIFDYRKKIAESETKLKQQQNLYEAVRSDRNLYSKNLVEAQDEITEMKRKLKIMTHQVDQLKEEISAKEAALVKLHLEQQRIEKEKETLKAELQKLRQQALETKHFIEKQEVEERKLLRIIAEADGERVRQKKELDQVISERDILGSQLVRRNDELALLYEKIKIQQSVLNKGETQYNQRVEDMRILKLEIKKLRREKGILARSVANVEELRQELYHMQREFLKERTRCRALEEELENPMNVHRWRKLEASDPSTFELIQKIHTLQKRLISKTEEVVEKELLLQEKEKLYVELKHILARQPGPEAAEQLQIYRHTLREKTKQLKVLSSELNMYESQSQEYKYEIERLGNELMSLKKKYLAQKRKELVLKNKDRMSMNNIFSETKKSVPRFTGGGFPLHQATKVKF
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Has an essential role in the assembly and organization of the sperm flagellar axoneme. Required for the elongation of the primary cilium and sperm flagellar midpiece via modulation of the Notch signaling pathway.
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B2RWS6
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EP300_MOUSE
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Histone acetyltransferase p300 (p300 HAT) (EC 2.3.1.48) (E1A-associated protein p300) (Histone butyryltransferase p300) (EC 2.3.1.-) (Histone crotonyltransferase p300) (EC 2.3.1.-) (Protein 2-hydroxyisobutyryltransferase p300) (EC 2.3.1.-) (Protein lactyltransferas p300) (EC 2.3.1.-) (Protein propionyltransferase p300) (EC 2.3.1.-)
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MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQAMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGIGSSGPNQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQPLKMGMMNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVPGGGMPSMGQQPTPSVQQPGLVTPVAAGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQSILTGAPVGLGNPSSLGVGQQSTPSLSTVSQIDPSSIERAYAALGLPYQVNQIPPQPQVQAKNQQSQPSGQSPQGMRSVNNMSASPMGVNGGVGVQTPNLLSDSMLHSTINSQNPMMSENAGVASLGPLPTAAQPSSTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAPGMGPVPMNTGSNMGQQPTGMTTNGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQNQFLSQTQFTSQGMNVTNMPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPTLPQQAHQNSPSPVPSRTPTPHHTPPSIGNQPPPATAIPTPVPTPPAIPPGPQPPSLHPSSRQTPTPPTHLPPQVQPSLPAAPSADQSQQQPRSQQSTAVSVPTPTAPLLPPQPSTPLSQPAVSIEGQVSNPPSTSSTEVNSQTIPEKQPSQEVKMESKMEVDKPEPADAQPEDTKEAKGEDVKVEPTEMEERGPELKTDGKEEEEQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLKKTARTRKENKLSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDILKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIACPAPNSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQQPATPQTPQPQPTSQPQPTPPNNMTPYLPRTQTTGPVSQGKAPGQVTPPTPPQTAQAPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGVSPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANPNPQPLPGQPGMTQGQPGLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQQLQPPMGAMSPQAQQMNMNHNTMPSQFRDILRRQMMQQQGAGPGIGPGMANQFQQPQGIGYPPQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQAANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSSDNADLNSNLSQSTLDIH
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Functions as histone acetyltransferase and regulates transcription via chromatin remodeling (By similarity). Acetylates all four core histones in nucleosomes (By similarity). Histone acetylation gives an epigenetic tag for transcriptional activation (By similarity). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity). Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac) (By similarity). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2. Acetylates 'Lys-131' of ALX1 and acts as its coactivator (By similarity). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (By similarity). Following DNA damage, forms a stress-responsive p53/TP53 coactivator complex with JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent transcription and apoptosis (By similarity). Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (By similarity). Acetylates HDAC1 leading to its inactivation and modulation of transcription (By similarity). Acetylates 'Lys-247' of EGR2. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (By similarity). Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium (By similarity). Promotes cardiac myocyte enlargement (By similarity). Can also mediate transcriptional repression (By similarity). Acetylates FOXO1 and enhances its transcriptional activity (By similarity). Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (By similarity). Participates in CLOCK or NPAS2-regulated rhythmic gene transcription exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter (By similarity). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity. Acetylates XBP1 isoform 2 acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity. Acetylates PCNA acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (By similarity). Acetylates MEF2D (By similarity). Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation. Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity. Acetylates PCK1 and promotes PCK1 anaplerotic activity (By similarity). Acetylates RXRA and RXRG (By similarity). Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (By similarity). Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or propionylation, respectively. Acts as a histone crotonyltransferase crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (By similarity). Also acts as a histone butyryltransferase butyrylation marks active promoters. Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (By similarity). Acts as a protein-lysine 2-hydroxyisobutyryltransferase regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (By similarity).
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B2RX12
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MRP3_MOUSE
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ATP-binding cassette sub-family C member 3 (EC 7.6.2.-) (EC 7.6.2.2) (EC 7.6.2.3) (Canalicular multispecific organic anion transporter 2) (Multidrug resistance-associated protein 3)
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MDRLCGSGELGSKFWDSNLSIYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHQLGYIVLSWLSRLKTALGVLLWCVSWVDLFYSFHGLIHGSSPAPVFFVTPLVVGITMLLATLLIQYERLRGVQSSGVLIIFWLLCVICAIIPFRSKILSALAEGKILDPFRFTTFYIYFALVFCALILSCFKEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTRLAILGYRRPLEDRDLWSLSEEDCSHKVVQRLLEAWQKQQNQASRSQTATAEPKIPGEDAVLLKPRPKSKQPSFLRALVRTFTSSLLMSACFNLIQNLLGFVNPQLLSILIRFISDPTAPTWWGFLLAGLMFLSSTMQTLILHQYYHCIFVMALRLRTAIIGVIYRKALVITNSVKRESTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVKQMKFKDSRIKLMSEILNGIKVLKLYAWEPSFLEQVKGIRQSELQLLRKGAYLQAISTFIWICTPFLVTLITLGVYVYVDESNVLDAEKAFVSLSLFNILKIPLNMLPQLISGLTQASVSLKRIQDFLNQNELDPQCVERKTISPGYAITIHNGTFTWAQDLPPTLHSLNIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGVVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLAGGQVSEMGHYSALLQHDGSFANFLRNYAPDEDQEDHEAALQNANEEVLLLEDTLSTHTDLTDNEPAIYEVRKQFMREMSSLSSEGEVQNRTMPKKHTNSLEKEALVTKTKETGALIKEEIAETGNVKLSVYWDYAKSMGLCTTLSICLLYGGQSAAAIGANVWLSAWSNDAEEHGQQNKTSVRLGVYAALGILQGLLVMLSAFTMVVGAIQAARLLHEALLHNKIRSPQSFFDTTPSGRILNRFSKDIYVIDEVLAPTILMLLNSFFTSISTIMVIVASTPLFMVVVLPLAVLYGFVQRFYVATSRQLKRLESISRSPIFSHFSETVTGTSVIRAYGRIQDFKVLSDTKVDNNQKSSYPYIASNRWLGVHVEFVGNCVVLFAALFAVIGRNSLNPGLVGLSVSYALQVTMALNWMIRMISDLESNIIAVERVKEYSKTKTEAPWVVESNRAPEGWPTRGMVEFRNYSVRYRPGLELVLKNVTVHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIVIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSEEDIWRALELSHLNTFVSSQPAGLDFQCAEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA
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ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (By similarity). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By similarity). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes. May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
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B2RX14
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TUT4_MOUSE
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Terminal uridylyltransferase 4 (TUTase 4) (EC 2.7.7.52) (Zinc finger CCHC domain-containing protein 11)
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MEEPKTSKNENHEPKKNIICEESKAVKIISNQTLKPRNDKSEIGTSSLNRNSSKKTKQNDICIEKTEAKSCKVNAASVPGPKDLGLVHRDQSHCKMKKLPNSPMKAQKGSSQTKLEKTPSLQTKAEKVPKSPNLPVKAEKAPCTTAEATTEKALNSQRKEENTPTSQMKLQKTPRSPLEPENVPSLLLKENVKQTESQQTGKKLTSSFVSMDKRKSEALQGEKSALENSSLSQKQQTQTDNIADSDDSASGIEDTADDLSKMKSEESNKENSSEMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNILEKQEESELRSLPSPSSAHLAALSVAVVELAKEQGITDDDLRIRQDIVEEMSKVIMTFLPECSLRLYGSSLTKFALKSSDVNIDIKFPPKMNHPDLLIQVLGILKKSALYIDVESDFHAKVPVVVCKDRKSALLCRVSAGNDMACLTTDLLAALGKVEPVFTPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLLPCLLGSWIEGFDPKRMDDFQLKGIVEEKFVKWEYNSSSATEKNLIADENKAKADEPKDDTKKTETDNQSNAAKAKHGKSPLTLEAPNQVPLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKRRIAIEDPFSVKRNVARSLNSQLVYEYVVERFRAAYRYFACPQKKGGNKSTMDPKKKEKGKLSSKKPVKSDCSATNCCILGESAEKIHMERGQPAKHDETEFTSQRCIVDNDSLLVNELGLANHGQDSSSLSTASGGSDLKQKSAEKQGDLTPSETSLKKELSQCICIGTPDGAESAGTDCRSNLEMDSSHQIVCNNVSATSCNCKATEVTSDLVDEDNLPSQELYYVFDKFILTSGKPPTIVCSICKKDGHSKNDCPEDFRKIDLKPLPPMTNRFREILDLVCKRCFDELSPPCSEQHNREQILIGLEKFIQKEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEIIENLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPVIPVLQEIFDGKQIPQRMVDGWNAFFFDKTEELKKRLPSLGKNTESLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWTSKCIAIEDPFDLNHNLGAGVSRKMTNFIMKAFINGRKLFGTPFYPLIGREAEYFFDSRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKRLKKKDSEEEKEGNEEEKDSRDLLDSRDLRCFICGDAGHVRRECPEVKMARQRNSSVAAAQLVRNLVNAQQVAGSAQQQSDQSIRTRQSSECSDSPSYSPQPQPFPQNSPQPSALPPPPSQPGSQPKLGPPQQGGQPPHQVQMPLYNFPQSPPAHYSPMHSMGLLPMHPLQIPAPSWPIHGPMLHSAPGSTPSNIGLNDPSIIFAQPAARPMAIPSPSHDGHWPRTVAPNSLVNNGAVGNSEPRFRGLNPPIPWEHAPRHFPLVPASWPYGLHQNFMHQGNPRFQPKPFYAQADRCATRRCRERCPHPPRGNVSE
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Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay. Essential for both oocyte maturation and fertility. Through 3' terminal uridylation of mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating transcripts during oocyte growth. Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also functions as an integral regulator of microRNA biogenesiS using 3 different uridylation mechanisms (By similarity). Acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression. In the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs, which includes most of pre-let7 members, that shapes an optimal 3' end overhang for efficient processing. Add oligo-U tails to truncated pre-miRNAS with a 5' overhang which may promote rapid degradation of non-functional pre-miRNA species (By similarity). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP (By similarity). Does not play a role in replication-dependent histone mRNA degradation (By similarity). Due to functional redundancy between TUT4 and TUT7, the identification of the specific role of each of these proteins is difficult. TUT4 and TUT7 restrict retrotransposition of long interspersed element-1 (LINE-1) in cooperation with MOV10 counteracting the RNA chaperonne activity of L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits initiation of reverse transcription once in the nucleus, whereas uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein granules (By similarity).
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B2RX88
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CSPP1_MOUSE
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Centrosome and spindle pole associated protein 1
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MADSLDEFIEEQKAKLAKDKAELESDPPYMEMKGKASEKLSENSKILISMAKENIPPSSQQQPKGPLGIEYGLSLPLGEDYEQKKHKLKEELRQDYRRYLTQGITQAKRKKNFLSTGETDPSTLGVSLPIDERLSAKERLKLERNREYNQFLRGKAESTEKVRQVEKNIEPKSQRNKNPISQGKSDLPLQIQTAYTHSEGPWLSRQEEGLYRQLDGEIELRSRRPLKQTKEEVGISGAEHPSLSGSAGVPERRARRANGERVLDRQHCRADRDPGVSEDMDERFRFESDFDRRLLRVYTNGRPHGSRRGYVDGDDVPEEPNTQISAAENKSVHCNGPPRSADLDITSPFAGMLFGGEDRELTKRRKEKYRQELLEQIAEQQKKKRREKDLAFGITTSGVQDPEKSPDRLKQFSLTPRHFEEMPPERPRVAFQTPPPPFSAPSSPSVPPVHSAPSHNEDLHSGLGSTLGELAHPRVLPVPLNPPPPPLLAPPASNYRTPYDDAYYFYGARNTLDPNIVYYGSGMIGGQPAPHVSAPVTHQVAPPAVNTVGQNEQKVLSDGLRNSGLVFEDKPKPSTQSLQSYQEALQEQIREREARRKKERLEKEEYEAKLEAEMRIYNPWGKGGGGAPLRDAKGNLITDLNRMHRQNIDAYHNPDARTYEDKRAVVSIDQNLATSNAENLEDSANKNSGPLQTQSSPFARGNTFGEPLSELQIKQQELYKNFLRFQIEEKRQREEAEREKLRVAEEKEEKRLAEQRARIQQEYEEEQERRREKEEEQRLKNEELIRLAEERRKEAERKKKEEEEKHNLQLQHYYERENIIGDETKHLRQPSPVVPALQNKIASKLQRPPSVDTIISSFIHESSMSRAQSPPVPARKNQLRAEEEKKNVIMELSEMRKQLRSEERRLQGRLLHLDSDDEIPMRKRERNPMDIFDMARHRVQAPVRRPSPKGLDATTFQNIHDFNELRERDSDTRVDLRLMYPDPPRDHHTLEIQQQALLREQQKRLNRIKMRRDAGADLDTICTDNAQGRRMPRDDTNDFLKNSLLESDSAFIGAYGETYPVIEDNAFPPPSQLPSARERRRNKLKGLDFDSSRLHTPQDGLSLKSISSVNVDQVRMRNEDRMRRLTEQQKKPTNTDDEGSLVDPDDIMRHLSDDGRNSAATEPWLRPGTSESLKRFMAEHLNEEQHKGPGKPGTFTWQGLSAAHA
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May play a role in cell-cycle-dependent microtubule organization.
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B2RXA7
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CP26C_MOUSE
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Cytochrome P450 26C1 (Cyp26c1) (EC 1.14.14.1) (Cytochrome P450, family 26, subfamily c, polypeptide 1)
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MISWGLSCLSVLGAAGTTLLCAGLLLGLAQQLWTLRWTLSRDWASTLPLPKGSMGWPFFGETLHWLVQGSRFHSSRRERYGTVFKTHLLGRPVIRVSGAENVRTILLGEHRLVRSQWPQSAHILLGSHTLLGAVGEPHRQRRKVLARVFSRSSLEQFVPRLQGALRREVRSWCAAQRPVAVYQAAKALTFRMAARILLGLQLDEARCTELAHTFEQLVENLFSLPLDVPFSGLRKGIRARDQLYEHLDEAVAEKLQEKQTAEPGDALLLIINSARELGHEPSVQELKELAVELLFAAFFTTASASTSLILLLLQHPAAITKIQQELSAQGLGRACTCTPRASGSPPDCGCEPDLSLAMLGRLRYVDCVVKEVLRLLPPVSGGYRTALRTFELDGYQIPKGWSVMYSIRDTHETAAVYRSPPEGFDPERFGVESGDARGSGGRFHYIPFGGGARSCLGQELAQAVLQLLAVELVRTARWELATPAFPVMQTVPIVHPVDGLLLFFHPLPTSGAGDGLPF
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A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (Probable). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (Probable). Catalyzes the oxidation of atRA primarily at C-4 (Probable). Oxidation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination, thereby contributes to the regulation of atRA homeostasis and signaling. Able to metabolize other RAs such as 9-cis with high efficiency (By similarity). Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (Probable). Shares sequence similarity with other CYP26 family members, but has higher affinity to 9-cis-RA and is much less sensitive to the inhibitory effects of ketoconazole (By similarity). In cooperation with Cyp26a1, contributes to the CNS patterning and the development of regions of higher visual acuity.
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B2RXE2
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SL9A5_MOUSE
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Sodium/hydrogen exchanger 5 (Na(+)/H(+) exchanger 5) (NHE-5) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 5)
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MLSAALLLLPGLPLAGAGATEEPTQESGPLGEPPPGLALFRWQWHEVEAPYLVALWILVASLAKIVFHLSRKVTSLVPESCLLILLGLVLGGIVLAVAKKAEYQLEPGTFFLFLLPPIVLDSGYFMPSRLFFDNLGAILTYAVVGTLWNAFTTGVALWGLQQAGLVAPRVQAGLLDFLLFGSLISAVDPVAVLAVFEEVHVNQTLFIIIFGESLLNDAVTVVLYKVCNSFVEMGSANVQATDYLKGVASLFVVSLGGAAVGLVFAFLLALTTRFTKRVRIIEPLLVFLLAYAAYLTAEMASLSAILAVTMCGLGCKKYVEANISHKSRTAVKYTMKTLASCAETVIFMLLGISAVDSSKWAWDSGLVLGTLFFILFFRALGVVLQTWALNQFRLVPLDKIDQVVMSYGGLRGAVAFALVILLDRTKVPAKDYFVATTIVVVFFTVIVQGLTIKPLVKWLRVKRSDYHKPTLNQELHEHTFDHILAAVEDVVGHHGYHYWRDRWEQFDKKYLSQLLMRRSAYRIRDQIWDVYYRLNIRDAISFVDQGGHVLSSTGLTLPSMPSRNSVAETSVTNLLRESGSGACLDLQVIDTVRSGRDREDAVMHHLLCGGLYKPRRRYKASCGRHFISEDAQERQDKEIFQQNMKRRLESFKSTKHNICFTKSKPRPRKTSHKKKDGVANPEATNGKPPRDLGFQDTAAVILTVESEEEEESDSSETEKEDDEGIIFVARATSEVLQEGKVSGSLEVCPSPRIIPPSPTCAEKELPWKSGQGDLAVYVSSETTKIVPVDMQTGWNQSISSLESLASPPCTQPPTLTRLPPHPLVTEEPQVPIDLSSDPRSSFAFPPSLAKAGRSRSESSADIPQQELQPLMGHKDHTHLSPGTANSHWCIQFNRGGRL
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Plasma membrane Na(+)/H(+) antiporter. Mediates the electroneutral exchange of intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry. Responsible for regulating intracellular pH homeostasis, in particular in neural tissues. Acts as a negative regulator of dendritic spine growth. Plays a role in postsynaptic remodeling and signaling. Can also contribute to organellar pH regulation, with consequences for receptor tyrosine kinase trafficking.
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B2RXF5
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ZBT42_HUMAN
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Zinc finger and BTB domain-containing protein 42
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MEFPEHGGRLLGRLRQQRELGFLCDCTVLVGDARFPAHRAVLAACSVYFHLFYRDRPAGSRDTVRLNGDIVTAPAFGRLLDFMYEGRLDLRSLPVEDVLAAASYLHMYDIVKVCKGRLQEKDRSLDPGNPAPGAEPAQPPCPWPVWTADLCPAARKAKLPPFGVKAALPPRASGPPPCQVPEESDQALDLSLKSGPRQERVHPPCVLQTPLCSQRQPGAQPLVKDERDSLSEQEESSSSRSPHSPPKPPPVPAAKGLVVGLQPLPLSGEGSRELELGAGRLASEDELGPGGPLCICPLCSKLFPSSHVLQLHLSAHFRERDSTRARLSPDGVAPTCPLCGKTFSCTYTLKRHERTHSGEKPYTCVQCGKSFQYSHNLSRHTVVHTREKPHACRWCERRFTQSGDLYRHVRKFHCGLVKSLLV
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Transcriptional repressor. Specifically binds DNA and probably acts by recruiting chromatin remodeling multiprotein complexes.
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B2RXH2
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KDM4E_HUMAN
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Lysine-specific demethylase 4E (EC 1.14.11.66) (KDM4D-like protein) (Lysine-specific demethylase 4D-like) ([histone H3]-trimethyl-L-lysine(9) demethylase 4E)
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MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL
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Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code.
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B2RXS4
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PLXB2_MOUSE
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Plexin-B2
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MALPLWALTFLGLTGLGLSLRSRKPESFRSETELNHLAVDEVTGVVYVGAVNALYQLSADLHVQQHVVTGPFMDNKKCTPPIEASQCHEAVLTDNFNQLLLLDPPGKRLVECGSLFKGICALRAMSNISVRLFYEDGSGEKSFVASNDERVATVGLVTSTRPDGERVLFVGKGNGPHDNGIIVSTRLLDRAEGREAFEAYSDHTTFKAGYLSTNTQQFVAAFEDDFYVFFVFNHQDKHPAKNRTLLARMCKDDPSYYSYVEMDLQCQDPSDPQDSAFGTCLAASVATSGAGRALYAVFSRDGRSTGGPGAGLCVFPLDKVREKIEANRNACYTGAREAGRTIFYKPFHGEIQCGGHLIGASESFPCGSEHLPYPLGSRDGLVATAVLHRGGLNLTAVTVTAENDHTVAFLGTSDGRILKVYLAPDGTSAEYGSIPVDINKKIKQDLALSGNLSSLYAMTQDKVFRLPVQECLSYVTCAQCRDSQDPYCGWCVIEGRCTRKSECSRAEETGHWLWSREKSCVAITDAFPQNMSRRAQGEVRLSVSPLPTLTEDDELLCLFGDSPPHPARVEDDTVICNSPSSIPSTPPGQDHVDVSIQLLLKSGSVFLTSHQYPFYDCREAMSLVENLPCISCASNRWTCQWDLQYYECREASPNPEEGIIRAHMEDNCPQFLAPDPLVIPMNHETEVTFQGKNLETVKVSSLYVGSELLNFEETVTMHESDTFSFRTPKLSHDGNETLPLHLYVKSFGKNIDSKLQVTLYNCSFGRSDCSLCLAADPAYRCVWCRGQNRCVYEALCSNVTSECPPPVITRIQPETGPLGGGILVTIHGSNLGVKADDVKKITVAGQNCAFEPRGYSVSTRIVCAIEASEMPFTGGIEVDVNGKLGHSPPHVQFTYQQPQPLSVEPRQGPQAGGTTLTINGTHLDTGSKEDVRVTLNDVPCEVTKFGAQLQCVTGQQLAPGQVTLEIYYGGSRVPSPGISFTYCENPMIRAFEPLRSFVSGGRSINVTGQGFSLIQKFAMVVIAEPLRSWRRRRREAGALERVTVEGMEYVFYNDTKVVFLSPAVPEEPEAYNLTVLIRMDGHCAPLRTEAGVFEYVADPTFENFTGGVKKQVNKLIHARGTNLNKAMTLEEAEAFVGAERCIMKTLTETDLYCEPPEVQPPPKRRQKRDTAHNLPEFIVKFGSREWVLGRVEYDTRASDVPLSLILPLVMVPMVFIIVVSIYCYWRKSQQAEREYEKIKSQLEGLEESVRDRCKKEFTDLMIEMEDQTNDVHEAGIPTLDYKTYTDRVFFLPSKDGDKDVMITGKLDIPESRRPIVEQALYQFSNLLNSKSFLINFIHTLENQREFSARAKVYFASLLTVALHGKLEYYTDIMRTLFLELMEQYVVAKNPKLMLRRSETVVERMLSNWMSICLYQYLKDSAGEPLYKLFKAIKHQVEKGPVDAVQKKAKYTLNDTGLLGDDVEYAPLTVSVIVQDEGIDAIPVKVLNCDTISQVKEKIIDQVYRTQPCSCWPKPDSVVLEWRPGSTAQILSDLDLTSQREGRWKRINTLMHYNVRDGATLILSKVGVSQQPEDSQQDLPGERHALLEEENRVWHLVRPTDEVDEGKSKRGSMKEKERTKAITEIYLTRLLSVKGTLQQFVDNFFQSVLAPGHAVPPAVKYFFDFLDEQAEKHDIRDEDTIHIWKTNSLPLRFWVNILKNPHFIFDVHVHEVVDASLSVIAQTFMDACTRTEHKLSRDSPSNKLLYAKEISTYKKMVEDYYKGIRQMVQVSDQDMNTHLAEISRAHTDSLNTLVALHQLYQYTQKYYDEIINALEEDPAAQKMQLAFRLQQIAAALENKVTDL
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Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling. Plays a role in glutamatergic synapse development and is required for SEMA4A-mediated excitatory synapse development. Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development. Regulates the migration of cerebellar granule cells in the developing brain. Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton (By similarity). Plays a role in axon guidance, invasive growth and cell migration (By similarity). May modulate the activity of RAC1 and CDC42. Down-regulates macrophage migration in wound-healing assays (in vitro).
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B2RXV4
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FLVC1_MOUSE
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Heme transporter FLVCR1 (Feline leukemia virus subgroup C receptor-related protein 1) (Feline leukemia virus subgroup C receptor) (Major facilitator superfamily domain containing 7B) (Mfsd7b)
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MARPDDEVGPAVAPGHPLGKGYLPVPKGAPDGEARLVPQNGPEALNGGPGLGPLIAGAQGGPQALIAAEEETQARLLPAGDGEDVPCPACPPRTALSPRRFVVLLIFSLYSLVNAFQWIQYSSISNVFEDFYEVSPLHINWLSMVYMVAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWVKCGSVQRHLFWVTMLGQILCSVAQVFILGLPSPVASVWFGPKEVSTACATAVLGNQLGTAVGFLLPPVLVPALGTQNSTGLLAHTQNNTDLLAHNINTMFYGTAFISTFLFFLTIIAFKEKPPLPPSQAQAVLRDSPPEEYSYKSSIWNLCRNIPFVLLLVSYGIMTGAFYSISTLLNQIILTYYVGEEVNAGRIGLTLVVAGMVGSILCGLWLDYTKTYKQTTLIVYVLSFIGMLIFTFTLNLGYIIVVFFTGGILGFFMTGYLPLGFEFAVEITYPESEGMSSGLLNTAAQILGIFFTLAQGKITTDYNSPEAGNIFLCAWMFVGIILTALIKSDLRRHNINTGLTNIDVKAVPVDSRVDPKPKVMVSIQSESSL
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[Isoform 1]: Heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythropoiesis, a process in which heme synthesis intensifies. Possibly export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. The molecular mechanism of heme transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated.
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B2RXZ1
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PNDC1_MOUSE
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Poly(A)-specific ribonuclease PNLDC1 (EC 3.1.13.4) (PARN-like domain-containing protein 1) (Poly(A)-specific ribonuclease domain-containing protein 1)
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MDVGADEFEQSLPLLQELVAGADFVGLDIEFTGLRSNLSRPQQISLFDLPSEWYLKTRQSVQQFTICQIGLSMFSSIEGESNKYVAHSCNFFLFPTTFGILDSEFSFQASSVQFLNQYGFDYNKFLKNGIPYMNEEQEKKIKHSILRGNWRVRSSLDKDQIKVVIDKVTQWLDLAEEGDQMTLPGIAGFQAFEVQLVLRQALPNIWTVLKEEWVIVKKVSQPQRWYLEHASCDQVSCWKEQILLSARGFSVFFQMLVKAQKPLVGHNMMMDLLHLHEKFFRPLPESYDQFKQNIHSLFPVLIDTKNVTKDIWKELRFPRVSNLLEVYEVLSSNLNPTKDSGPVIIHARQCKKYAETKCPHEAAYDAFLCGSVLLKVAHLLLQRVHGNGAVHEPAFPQYLDVLAPYVNQVNLIRAGVPKINFSGPDYPSIRPPVLILTVKRWPGVSEQQVYREFQNLCKFDVRRFTRSQFLLLTNKFKDARSVLKEYRNHPTLQVSLYRSWRHSPNITCLLQVCSIVTTWAMIAFLLGRPMP
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3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. May act as a regulator of multipotency in embryonic stem cells. Is a critical factor for proper spermatogenesis, involved in pre-piRNAs processing to generate mature piRNAs (By similarity).
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B2RY04
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DOCK5_MOUSE
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Dedicator of cytokinesis protein 5 (Lens rupture protein 2) (Rupture of lens cataract protein)
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MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYALQNRSKKGIFPETYIHLKEATVEDGGQHETVIPGELPLVQELTNTLREWAVIWRKLYVNNKVTLFRQLQQMTYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETSTVALFRAHEVASKRIEEKIQEEKSILQNLDLRGQAIFSTVHTYGLYVNFKNFVCNIGEDAELFIALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSTDLIRPRISLVCQIVRVGRMELKEGKKHTCGLRRPFGVAVMDISDIVHGKVDDEEKQHFIPFQQIAMETYIRQRQLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHLVDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVFDEEGNLLEKAIHPGAGYEGVSEYKSVVYYQVKQPCWYETVKVFIAIEEVTRCHIRFTFRHRSSQESRDKSERAFGVAFVKLMNADGTTLQDGRHDLVVYKGDNKKMEDAKYYLTLPGTKAELEEKELQASKNPSVFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEVDGGEIVKFLQDTLDALFNIMMEMSDNETYDFLVFDALVFIISLIGDIKFQHFNPVLETYIYKHFSATLAHVKLSKVLNFYVANAEDPSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQSEDGDEFNDSIRQLFLAFNTLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPMELSVLFCKFIQSIPDNQLVRQKLNCMTKIVESSLFQQAECREVLLPLLTDQLSGQLDDHSTKPDHEASSQLLSNILEVLDRTDVGPTSAHVQLIMERLLRRINRTVIGMSRQSPHIGSFVACMIAVLRQMEDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRAINQFAEVLTKSFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSEAKRNKIVKKYGDMRKEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNLSGNGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLANSGEAFAFLVSSLLENLLDYRTIIIHDESKENRMSCTVNVLNFYKDKKREDIYIRYLYKLRDLHRDCENYTEAAYTLLLHAELLQWSDKPCVPHLLQRDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKLSKELAETYESKVFDYEGLGSLLKKRALFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKIFIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYLQCFTVKPVMSLPPSYKDKPVPEQILNYYRANEVQQFSYSRPFRKGEKDPENEFATMWIERTTYRTAYTFPGILKWFEAKEISVEEISPLENAIETMELTNERVSNCVQQHAWDHSLSVHPLSMLLSGIVDPAVMGGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQIPLLTEGIRIHGEKLTEQLKPLHARLSSCFRELKEKVEKLYGVITLPPSMTERKPSRAGSMVLPYILSSTLRRLSVTSVASSVISTSSNSSDNASSRPGSDGSILEPLFERRASSGARVEDLPPKEDSENRISKFKRKDWNLSKSQVIAEKAPEPDVMSPGKKTQRPKSLQLVDSRLTPFHSPSPLQSTALSPPPLTPKATRTLSSPSLQTDGLTASVPPPPPPKSKPYESSQRNSAEIAPPLPVRRDSKAPPPPPPKARKSGILSSEPGSQ
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Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP. Along with DOCK1, mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on type IV collagen (By similarity).
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B2RY50
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ODAD2_MOUSE
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Outer dynein arm-docking complex subunit 2 (Armadillo repeat-containing protein 4)
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MGVALTRLAQWTAAGYETGTLEITPLNESILNEITKFVESFSYKYPQEAKFVFVEPLEWKTYLEPSAFELGYVVSATTAESEETGKDGQPLLFLSVPYIKVRSFGQLSQLLSIATDSKLQEAQACIEANRDPVVKILGPDYNEMKEDPTRLTLLDTIIKDKETYMKRKVAILLKQLDLHLLNHSLKYISLEISLNPGTFKKDIELLKRFSGKGEQTVLESIEYTSDYEFSNGCRAPPWRQIQGEICYVLVKPHDMETLCLTCSTEGVFLNGGKTEEEGEINYERKGEIYKDLVTCLKDKSPVFSENMSKHEIRFTEEQQKDNQIFEKPKTEDGHSSVAGSEKSKIEKISFGKSPMTKRLEPSLNWRVTVDYKDHKSSIKDSQEEKQGKLEKSSSVSVAPSRAQSHRKGGEKVEETVSESSSESEEDEEPPDHRQEANADLPSEYWQIQKLVKYLKGGNQTATVIALCSMRDFNLAQETCQLAIRDVGGLEVLINLLDTDEVKCKIGSLKILKEISHNPQIRRNIVDLGGLPIMVNILDSPHKSLKCLSAETIANVAKFKRARRAVRQHGGITKLVALLDCGQNSTEPTQPSLYETRDVEVARCGALALWSCSKSHSNKEAIRKAGGIPLLARLLKTSHENMLIPVVGTLQECASEENYRAAIKAERIIENLVKNLNSENEQLQEHCAMAIYQCAEDEETRDLVRLHGGLKPLASLLNNTDNKERLAAVTGAIWKCSISKENVIKFREYKAIETLVGLLTDQPEEVLVNVVGALGECCQEYENRVLVRKCGGIQPLVNLLVGINQALLVNVTKAVGACAVEPESMAIIDRLDGVRLLWSLLKNPHPDVKASAAWALCPCIENAKDAGEMVRSFVGGLELVVNLLKSDNKEVLASVCAAITNIAKDQENLAVITDHGVVPLLSKLANTNNDKLRRHLAEAISRCCMWGRNRVAFGEHKAVAPLVRYLKSNDTNVHRATAQALYQLSEDADNCITMHENGAVKLLLDMVGSPDQDLQEAAAGCISNIRRLALATEKARYN
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Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule (By similarity). Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules.
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B2RY71
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DNAI3_MOUSE
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Dynein axonemal intermediate chain 3 (WD repeat-containing protein 63)
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MAPKPPKSPKGQKKGKKNMKQQLLVPEEEEPMNMESMGHPEIYPLVLTTKTQEIFNCRVDEDMTDEQTYKLIKKEDILADLQNRAAVSDFHPVKKIVREYPGEELLLVYDKDFKYGLNFYLIGTEDGKENFLKPPEVPEEQEEPKEHVQEDVYVYNPPVSKPWVSLGSEKEIEEESVQESGKRVTYMISRKRSEFGAPVTFSDQNASSVKDAYIECTSYPEKNYTLSQVEKDVGLQVIAEVKDTSTQTKWAFPKNATTQYYPREFSEEEKSLIGKSKSLVDFFNNVSTSVEVALQQNEIMNTFIDDWKNLAEEESTFGDKTDTHLKEYQSFTDLHNTMEKMITCVSWHPTIFGLIVVSVAVRLSYEERVQNSGRLLLQPSLLLFWSFSDPIHPQLMLESPDDIFCFEFCPSDPNIIAGGCINGQIVLWDITAHADRIENIKTGGHRSKKTSLKPMFLLEPDSNKESMYIRHCAVSSIENGHRKVITDIHWLPDSFEINRMGSVFENRSGINCQLVTCSADCTICFWDIRPQKPAVTAAAAASAATTATNNANSQQSPVEKKKEENIDIPFDVPSTFLHLDLSWKPLSRLKLSKGDTSLDHCPTKLSLGEDPFLCKIQGTSSIHIILRDKMLSQIKMVKTSEINPYQNLEAGIANILKPIEDFCTKFFVGTEEGEVIYTDWKMERDSDTGRLMAKKPVSLYTVHDGAVHTIQRSPFFNDIVLTVGGWNVAIWKEEVMTGPLLQTCCGPKRYTAGHWSLTRPGVFYIGREDGNVDIWDLLEKTHEPAQSQNICITMITYIKPWTFSSKQQFIAVADYYGTLHILEIPWTLSHPSLNEVSSVNYYFEREVRHLEYVQQRKEIREQEKIDMALELVKKKAKIYQKTKEQMEAELKLEYESYLDLEKSVLFALGLSKVSEKKSYLDSH
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Acts as a negative regulator of cell migration, invasion, and metastasis downstream of p53/TP53, through inhibition of Arp2/3 complex-mediated actin polymerization (By similarity). Via its association with the multisubunit axonemal dynein complex, is potentially involved in the regulation of cilia function. May play a role in osteogenesis of dental tissue-derived mesenchymal stem cells.
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B2RYF7
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WASH1_RAT
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WASH complex subunit 1 (WAS protein family homolog 1)
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MTAVKTQHSLAGQVYAVPLIQPDLRREEAIQQVADALQYLQNISGDIFSRISQRVELSRRQLQAIGERVSLAQAKIEKIKGSKKAIKVFSSAKYPAPEHLQEYNSVFTGALDPGLQRRPRYRIQSKHRPLDERALQEKLKYFPVCVSTKSEPEDEAEEGLGGLPSNISSISSLLLFNTTENLYKKYVFLDPLAGAVTKTHTMLGTEEEKLFDAPLSISKREQLEQPAPENYFYVPGLGQVPEIDVPSYLPDLPGVADDLMYSADLGPGIAPSAPGAIPELPAFHTEVAEPFQPEREDGALLAPPPPPPPPPPPPPPAPTAVVSAPQPPMSPDVVTVTGKVAREEDSGSGEAHSASVQGAPKEVVDPSSGRATLLESIRQAGGIGKAKLRSVKERKLEKKKQKEQEQVRATSQGGDLMSDLFNKLVMRRKGISGKGPGTGTSEGPGGAFSRMSDSIPPLPPPQQPAGDEDEDDWES
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Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting. Regulates the trafficking of endosomal alpha5beta1 integrin to the plasma membrane and involved in invasive cell migration. In T-cells involved in endosome-to-membrane recycling of receptors including T-cell receptor (TCR), CD28 and ITGAL proposed to be implicated in T-cell proliferation and effector function. In dendritic cells involved in endosome-to-membrane recycling of major histocompatibility complex (MHC) class II probably involving retromer and subsequently allowing antigen sampling, loading and presentation during T-cell activation. Involved in cytokinesis and following polar body extrusion during oocyte meiotic maturation. Involved in Arp2/3 complex-dependent actin assembly driving Salmonella typhimurium invasion independent of ruffling. Involved in the exocytosis of MMP14 leading to matrix remodeling during invasive migration and implicating late endosome-to-plasma membrane tubular connections and cooperation with the exocyst complex. Involved in negative regulation of autophagy independently from its role in endosomal sorting by inhibiting BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity.
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B2RYG6
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OTUB1_RAT
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Ubiquitin thioesterase OTUB1 (EC 3.4.19.12) (Deubiquitinating enzyme OTUB1) (OTU domain-containing ubiquitin aldehyde-binding protein 1) (Otubain-1) (Ubiquitin-specific-processing protease OTUB1)
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MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHVFPEGSEPKVYLLYRPGHYDILYK
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Hydrolase that can specifically remove compared to 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation (By similarity). Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen (By similarity). Acts via its interaction with RNF128/GRAIL (By similarity). Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 (By similarity). Deubiquitinates estrogen receptor alpha (ESR1) (By similarity). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (By similarity). Not able to cleave di-ubiquitin (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (By similarity). Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain. When phosphorylated at Tyr-26, acts as an activator of the mTORC1 complex by mediating deubiquitination of RPTOR via a non-catalytic process: acts by binding and inhibiting the activity of the ubiquitin-conjugating enzyme E2 (UBE2D1/UBCH5A, UBE2W/UBC16 and UBE2N/UBC13), thereby preventing ubiquitination of RPTOR.
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B2RYM5
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BRCC3_RAT
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Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-) (BRCA1-A complex subunit BRCC36) (BRCA1/BRCA2-containing complex subunit 3) (BRCA1/BRCA2-containing complex subunit 36) (BRISC complex subunit BRCC36)
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MAVPVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDVRSESKFAHAGSDVCTVPEKVDSIRVVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSVQAQKSSDYERIEIPVHVVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLRELQREKEELMAELRSLE
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Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1 deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly (By similarity). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity).
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B2RYN7
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SPAST_RAT
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Spastin (EC 5.6.1.1)
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MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRFSRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMVSGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
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ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021, ECO:0000269|PubMed:18234839}.
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B2RYR0
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RN168_RAT
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E3 ubiquitin-protein ligase RNF168 (EC 2.3.2.27) (RING finger protein 168) (RING-type E3 ubiquitin transferase RNF168)
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MAAPKNSIPSLAECQCGICMEILVEPVTLPCNHTLCNPCFQSTVEKANLCCPFCRRRVSSWTRYHTRRNSLVNTDLWEIIQKHYAKECKLRISGQESKEIVDEYQPVRLLSKPGELRREYEEEISKVEAERQASKEEENKASEEYIQRLLAEEEEEEKRRTERRRSEMEEQLRGDEELARRLSTSINSNYERNILASPLSSRKSDPVTNKSQKKNTNKQKNFGDIQRYLSPKSKPGTAWACKTEHGEDMCKSKETDSSDTKSPVLQDTDVEESMPTHSPQTCPETQGQGPEPLTEMPVPWLCARNAEQCLEGKAEAVSTNPDDSCIVNDGGPRAIVSNSKEAAVKPPTKIENEEYSVSGVTQLTGGNGVPTESRVYDLLVGKEISERENQESVFEEVMDPCFSAKRRKIFITSSLDQEETEVNFTQKLIDLEHMLFERHKQEEQDRLLALQLQKEADKEKMVPNRQKGSPDQYQLRTSSPPDGLLNGQRKNVKDRNSPKQTADRSKSQRSRKGEYWETFESTWKGSVNGTKMPTPRKDSCNVSKRACPLQHRSAQKSILQMFQR
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E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively). {ECO:0000255|HAMAP-Rule:MF_03066}.
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B2RZ55
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SIR7_RAT
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NAD-dependent protein deacetylase sirtuin-7 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-7) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 7) (SIR2-like protein 7)
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MAAGGGLSRSERKAAERVRRLREEQQRERLRQVSRILRKAAAERSAEEGRLLAESEDLVTELQGRSRRREGLKRRQEEVCDDPEELRRKVRELAGAVRSARHLVVYTGAGISTAASIPDYRGPNGVWTLLQKGRPVSAADLSEAEPTLTHMSITQLHKHKLVQHVVSQNCDGLHLRSGLPRTAISELHGNMYIEVCTSCIPNREYVRVFDVTERTALHRHLTGRTCHKCGTQLRDTIVHFGERGTLGQPLNWEAATEAASKADTILCLGSSLKVLKKYPRLWCMTKPPSRRPKLYIVNLQWTPKDDWAALKLHGKCDDVMRLLMDELGLEIPVYNRWQDPIFSLATPLRAGEEGSHSRKSLCRSREEPPPGDQSAPLASATPILGGWFGRGCAKRAKRKKAA
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NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase, deglutarylase and dedecanoylase), depending on the context. Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes. Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53. Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex. Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region. In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription. Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis. Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex. Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65. Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation. Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II. Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL (By similarity). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51. Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases. In addition to protein deacetylase activity, also acts as protein-lysine deacylase (By similarity). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu) a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (By similarity). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina. Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (By similarity). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity).
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B2TVJ5
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FADB_SHIB3
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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B2TWL8
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HCHA_SHIB3
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQTSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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B2UP57
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H2018_AKKM8
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Beta-hexosaminidase Amuc_2018 (EC 3.2.1.52) (Beta-N-acetylhexosaminidase Am2301)
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MARPLPILGGILLSFSPPAEATAQYSIIPEPSRTELRQETAKTLQLLSDQEVPTLETDAYRLTVTPQGAHLASGGREGRIYGLATLRQLRDQLAGQPEGIPCGVITDKPRYPWRGLMVDPARHFIPAADLKKFVDMMAYYKFNRLHLHLTDNQGWRLPVPGYPKLKSVASRREESFGDGIPHEGMYTKQELKELVAYCAARGIDVIPEIDMPGHNQALHAAYPEFFCFPKPDMNVRTTAGNSKELVCPQKPEVWKFYASVFNELKDIFPSGIVHLGGDEAPTELWEKCPLCREARTRAAMKDEQEQMKAFFAKTAALLAKNGQTPQFWYEGNAGIYHPGETVYAWRQGQALQSIEKTKKAGLNLIMASSEYCYLDFPQIQGQRNWGWMKTTTLQKCYDLDPAFGKPEKEAGHIRGVHAPVWAERLPDLNHLLYRAYPRACAIAEAGWSPMGVRSWENFRRKLADHRQFILKRFNYDMERTQGNEPAFRWENNK
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Hydrolyzes terminal GlcNAc residues from terminally unbranched N-glycans and from chitobiose. Hydrolyzes beta-1,6-linked N-acetylglucosamine and beta-1,4-linked N-acetylgalactosamine from pNP-alpha-GalNAc[beta1,3Gal]beta1,6GlcNAc and pNP-beta-GlcNAc-beta1,4-GalNAc substrates, respectively, as well as beta-1,2-linked N-acetylglucosamine units from the non-reducing end of N-glycans. Hydrolyzes GlcNAc residues linked to alpha1,3- or alpha1,6-mannose branch, but has low activity on substrates with more than one GlcNAc residue on one of the mannose branches. Releases terminal GlcNAc moieties from the N-glycopeptide Gly-Glu-Asn-(GlcNAc2Man3GlcNAc2)-Arg with high efficiency. Has moderate hydrolytic activity on the chitobiose moiety of N-glycopeptide substrate Gly-Glu-Asn-(GlcNAc2)-Arg. Does not hydrolyze GlcNAc residues from N-glycan structures bearing a bisecting GlcNAc moiety (beta1,4-linked GlcNAc to the beta1,4-linked core mannose). Potentially capable of cleaving the specific glycoside linkages in the process of mucin degradation in human intestinal tract (Probable). Hydrolyzes synthetic substrate pNP-beta-GlcNAc with high activity and pNP-beta-GalNAc to a lesser extent. Does not hydrolyze pNP-beta-glucose, pNP-beta-galactose, pNP-alpha-glucose, pNP-alpha-galactose, pNP-alpha-GlcNAc or pNP-alpha-fucose.
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B2ZFP3
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SMAL1_DANRE
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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (EC 3.6.4.-) (HepA-related protein) (Sucrose nonfermenting protein 2-like 1)
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MSVSLTPEQQRRIEENRKKALARRAERQAQIADPGPAQNKHTQSGTTGGPAKNNQHFASDRGQSGAPTRQTQLIDINAACTKTAPPTSITAASTASSFYGQAGKPSTGEKRPPKPPEPAANIPAKKPAVYLRGRCVSHSENRFRVEVGYHADLILVFKSIPSKNYDPATKMWNFSLEDYQMLMEQVAHLPSISLKPLEGMEGLNISASTCRPKDAAAMAALMRLCQGWQKPGATIKGKCVLVSRSRLEVDIGYQADVIGIFKQMPSKSYDMKTRKWTFLLEDYGKLMADLNELPTVETEPLPHAVLQSFSSQFEKTQSQAPVPPEADLSHIDPQLTRSLMPFQRDGVNFAVSREGRLLLADDMGLGKTVQAICIAAYYRSEWPLLVVAPSSVRFTWAEAFRRWLPSVKPDSINVVVKGKDSLRSGLINIISYDLLNKMDKQPPSSPFNVIIMDESHFLKNMKTARCRAALPLLKTAKRVILLSGTPAMSRPAELYTQIQAVRPALFPRFHDFGTRYCDAKQLPWGWDYSSSSNLTELKLLLEESLMLRRLKSEVLSQLPAKQRKVVTVTTDGINSRTKAALNAAARELAKGYHNKSQEKEALLVFFNHTAEAKIRAIMEYISDMLECGREKFLVFAHHKLVLDSITKELGEKSISFIRIDGSTPSAERQLLCERFQASQQSCVAVLSITAANMGLTLHSAALVVFAELFWNPGVLIQAEDRVHRIGQTSNVDIHYLVAKGTADDYLWPMIQAKMNVLEQVGLSESNISENAESASFHSRDRQQLTITEMFQRSFDEDEMLALMDQDP
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ATP-dependent annealing helicase that catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA (By similarity).
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B2ZRS9
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CNL_CLINE
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Ricin B-like lectin (Clitocybe nebularis lectin) (CNL)
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MSITPGTYNITNVAYTNRLIDLTGSNPAENTLIIGHHLNKTPSGYGNQQWTLVQLPHTTIYTMQAVNPQSYVRVRDDNLVDGAALVGSQQPTPVSIESAGNSGQFRIKIPNLGLALTLPSDANSTPIVLGEVDETSTNQLWAFESVSAV
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Lectin specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). Specific also for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Agglutinates human blood group A, AB, B and O erythrocytes with a strong preference for group A. Agglutinates bovine erythrocytes with a very low specificity. Binds carbohydrates bivalently, which is required for its biological activity. Exhibits insecticidal activity against the fruit fly D.melanogaster, mosquito A.aegypti, and amoebozoa A.castellanii. Has anti-nutritional activity against Colorado potato beetle L.decemlineata, and against worm C.elegans. Has antiproliferative activity against human leukemic T-cells. Has an immunostimulatory effect on human antigen-presenting dendritic cells, which are subsequently able to induce efficient T-cell immune responses.
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