entry
stringlengths 6
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stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
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stringlengths 7
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L0N7N1
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KIF14_MOUSE
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Kinesin-like protein KIF14
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MSVHTSHSRHNIGSLEVSSSQKISASSGLVHSSRLELHLKADMSECENHDPFVNAGSKTIDINSTYVISACKKTRETPVTSDPRRLSLQRRATCGDRESSLLGSELGNRRTADTSLRLQRRHGRADYVGKWETLNPVGGNPGSDSASQASRTEAKGVNNDTRVLSSVVSVKDSNDTGLTRCKDPGPPVGASNEKVTVKDTNSRAPVGSQRQTEAMRSGHLVVQLTESKSDTPVSGGRNSHRGNAGKDTAKQVGTFGSSDTRTPVKCVLEHRWTPRHDPPPPKSPALSTPKNNGKDIPKHGSTFRSASSESRTPVKCVPEHRWTPRHDLPPPKSPALSTLKNRIASPRVKPRPKSSLFANKRESSRESTLPPEENSLVQKTFTEPDSLKVENSQVTVAVRVRPFSKREKTEKASQVVFTNGEEITVEHPDMKQVYSFIYDVSFWSFDECHPGYASQTTVYETLAAPLLDRAFEGYNTCLFAYGQTGSGKSYTMMGLNEEPGIIPRFCEDLFAQIAKKQTSEVSYHLEMSFFEVYNEKIHDLLVCKGENGQRKQPLRAREHPVSGPYVEGLSMNVVSSYSDIQSWLELGNKQRATAATGMNDKSSRSHSVFTLVMTQTKTEVVEGEEHDHRITSRINLVDLAGSERCSTAHSSGQRLKEGVSINKSLLTLGKVISALSEQANGKRVFIPYRESTLTWLLKESLGGNSKTAMIATVSPAASNIEETLSTLRYATQARLIVNIAKVNEDMNAKLIRELKAEIEKLKAAQRSNRNIDPERYRLCRQEITSLRMKLHQQERDMAEIQRVWKEKFEQAEKRKLQETKELQKAGVTFQMDNHLPNLVNLNEDPQLSEMLLYMVKEGVTTVGKHTPSSSHDIQLSGVLIADDHCTIRNFGGTVSIVPAGEAKTYVNGTHISEPTVLHHGDRVVLGGDHYFRFNHPVEVQKGKKLSSRNNLTTSEGPKDFEFAKNELLTAQRSRLEAEIKDAQLKAKEEMMQGIQIAKEMAQQELSSQKAVYERKIQALEAELREESQRKRLEELNNQKASHKIEELERAKQHLEQEVYVNKRRLEMETLATKQALEDHRIRHARILEALEIEKQKIAEEVQMLQENRGNRDKTFTIQPNWNSMKLSTMIQEANAISDKFKKCYIFGRHDASDKGRSDTSVRVRNLQLGISTFWSLEKFESKLAAMKELYESNGGDRDEDVFCDPADEWEPDITSTPVSSLSRRRSRSLMKNRRVSGCLHDIHPIQSMQSSHSSGLMEKPSTIYSNSSESFLPGICKELIGSSIDFLGQSFDEEKTIADSLINNLLRLHNGVIAISKAHEEQDEESQDNLFSDRAAQALTIQVACAFEQLVVLFKHWLGDFLPCTGSARLEDELRQDIKKLGGYLQLFLQGCCSDISSMVKEAQNKVMKIIQQAVQCVGQLAVLKGSKLCVLENSSKVSSTQEFMAALQDGVTSGMKSLLDSGLETAQDLRQDLSRQSAREEVTKQMKASTVEWVGSLENAVAEWRTKSFRTQAQEGSRQQVSKLLSLASEFLKLKSCLQQTVEMIVSALRGCPSDLHCLRSCTETICSLARKLHSDFSAHSASAGSCGNELPRADCEELESLAKSLLLCFECGESPGLSKPWESCSSNSKEEQCKSDRADCGKSGPRRACEPHGDATPAVSSGDCTPNRIQWV
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Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (By similarity). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (By similarity). Regulates cell growth through regulation of cell cycle progression and cytokinesis. During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (By similarity). During late neurogenesis, regulates the cerebellar and cerebral cortex development and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division. Also is required for chromosome congression and alignment during mitotic cell cycle process (By similarity). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (By similarity).
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L0PIN3
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BRKP1_AGADC
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[Thr6]-bradykinyl-Val,Asp (Bradykinin-related peptide RD-11) [Cleaved into: [Thr6]-bradykinin]
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MSFLKKSLFLVLFLGFVSFSICEEEKREDEEEENEREENKESEEKRNQEERPPGFTPFRVD
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[[Thr6]-bradykinin]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=16.8 nM) and contraction of that from ileum (EC(50)=205 nM), urinary bladder (EC(50)=895 nM) and uterus (EC(50)=60.3 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). [Hyp3,Thr6]-bradykinin: Induces relaxation of rat smooth muscle from tail artery (EC(50)=56.7 nM) and contraction of that from ileum (EC(50)=588 nM), urinary bladder (EC(50)=4.6 uM) and uterus (EC(50)=3.9 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). In arterial smooth muscle, the effect via BDKRB1 is stronger, in uterus, ileum and urinary bladder the effect via BDKRB2. [[Thr6]-bradykinyl-Val,Asp]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=10.8 nM) and contraction of that from ileum (EC(50)=645 nM), urinary bladder (EC(50)=1.1 uM) and uterus (EC(50)=1.2 uM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). Apart from uterus smooth muscle, the effect via BDKRB2 is stronger. [Hyp3,Thr6]-bradykinyl-Val,Asp: Induces relaxation of rat smooth muscle from tail artery (EC(50)=3.5 nM) and contraction of that from ileum (EC(50)=223 nM), urinary bladder (EC(50)=1.5 uM) and uterus (EC(50)=356 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2) the effects via BDKRB2 are stronger.
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L0PJV8
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BRKP1_AGACL
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[Thr6]-bradykinyl-Val,Asp (Bradykinin-related peptide RD-11) [Cleaved into: [Thr6]-bradykinin]
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MSFLKKSLFLVLFLGLVSFSICEEEKRETEEEENEDEMDKESEEKRESPERPPGFTPFRVD
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[[Thr6]-bradykinin]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=16.8 nM) and contraction of that from ileum (EC(50)=205 nM), urinary bladder (EC(50)=895 nM) and uterus (EC(50)=60.3 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). [Hyp3,Thr6]-bradykinin: Induces relaxation of rat smooth muscle from tail artery (EC(50)=56.7 nM) and contraction of that from ileum (EC(50)=588 nM), urinary bladder (EC(50)=4.6 uM) and uterus (EC(50)=3.9 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). In arterial smooth muscle, the effect via BDKRB1 is stronger, in uterus, ileum and urinary bladder that via BDKRB2. [[Thr6]-bradykinyl-Val,Asp]: Induces relaxation of rat smooth muscle from tail artery (EC(50)=10.8 nM) and contraction of that from ileum (EC(50)=645 nM), urinary bladder (EC(50)=1.1 uM) and uterus (EC(50)=1.2 uM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2). Apart from uterus smooth muscle, the effect via B2 is stronger. [Hyp3,Thr6]-bradykinyl-Val,Asp: Induces relaxation of rat smooth muscle from tail artery (EC(50)=3.5 nM) and contraction of that from ileum (EC(50)=223 nM), urinary bladder (EC(50)=1.5 uM) and uterus (EC(50)=356 nM). Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2) the effects via B2 a stronger.
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L0R8F8
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MIDUO_HUMAN
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Mitochondrial ribosome and complex I assembly factor AltMIEF1 (Alternative MIEF1 protein) (AltMIEF1) (MIEF1 microprotein) (MIEF1-MP) (alternative transcript upstream of MiD51) (AltMiD51)
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MAPWSREAVLSLYRALLRQGRQLRYTDRDFYFASIRREFRKNQKLEDAEARERQLEKGLVFLNGKLGRII
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Assembly factor involved in the biogenesis of the mitochondrial-specific ribosomes (mitoribosomes). Specifically associates with intermediates of the mitochondrial ribosome large subunit (mt-LSU) and is required for proper ribosome assembly, possibly preventing premature association of the large and small ribosomal subunits. Thereby, indirectly regulates mitochondrial translation. It is also required for complete assembly of the mitochondrial respiratory chain complex I. May also function in DNM1L-mediated mitochondrial fission.
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L0T905
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RSEA_MYCTU
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Anti-sigma-E factor RseA (Regulator of SigE) (Sigma-E anti-sigma factor RseA)
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MADPGSVGHVFRRAFSWLPAQFASQSDAPVGAPRQFRSTEHLSIEAIAAFVDGELRMNAHLRAAHHLSLCAQCAAEVDDQSRARAALRDSHPIRIPSTLLGLLSEIPRCPPEGPSKGSSGGSSQGPPDGAAAGFGDRFADGDGGNRGRQSRVRR
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An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigE. ECF sigma factors are held in an inactive form by an anti-sigma factor.
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L0T911
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PBPB_MYCTU
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Penicillin-binding protein PbpB (Penicillin-binding protein 3) (PBP3)
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MSRAAPRRASQSQSTRPARGLRRPPGAQEVGQRKRPGKTQKARQAQEATKSRPATRSDVAPAGRSTRARRTRQVVDVGTRGASFVFRHRTGNAVILVLMLVAATQLFFLQVSHAAGLRAQAAGQLKVTDVQPAARGSIVDRNNDRLAFTIEARALTFQPKRIRRQLEEARKKTSAAPDPQQRLRDIAQEVAGKLNNKPDAAAVLKKLQSDETFVYLARAVDPAVASAICAKYPEVGAERQDLRQYPGGSLAANVVGGIDWDGHGLLGLEDSLDAVLAGTDGSVTYDRGSDGVVIPGSYRNRHKAVHGSTVVLTLDNDIQFYVQQQVQQAKNLSGAHNVSAVVLDAKTGEVLAMANDNTFDPSQDIGRQGDKQLGNPAVSSPFEPGSVNKIVAASAVIEHGLSSPDEVLQVPGSIQMGGVTVHDAWEHGVMPYTTTGVFGKSSNVGTLMLSQRVGPERYYDMLRKFGLGQRTGVGLPGESAGLVPPIDQWSGSTFANLPIGQGLSMTLLQMTGMYQAIANDGVRVPPRIIKATVAPDGSRTEEPRPDDIRVVSAQTAQTVRQMLRAVVQRDPMGYQQGTGPTAGVPGYQMAGKTGTAQQINPGCGCYFDDVYWITFAGIATADNPRYVIGIMLDNPARNSDGAPGHSAAPLFHNIAGWLMQRENVPLSPDPGPPLVLQAT
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Synthesis of cross-linked peptidoglycan from the lipid intermediates. {ECO:0000250, ECO:0000269|PubMed:19496931}.
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L0TC47
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LIPV_MYCTU
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Lipase LipV (EC 3.1.1.1)
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MIIDLHVQRYGPSGPARVLTIHGVTEHGRIWHRLAHHLPEIPIAAPDLLGHGRSPWAAPWTIDANVSALAALLDNQGDGPVVVVGHSFGGAVAMHLAAARPDQVAALVLLDPAVALDGSRVREVVDAMLASPDYLDPAEARAEKATGAWADVDPPVLDAELDEHLVALPNGRYGWRISLPAMVCYWSELARDIVLPPVGTATTLVRAVRASPAYVSDQLLAALDKRLGADFELLDFDCGHMVPQAKPTEVAAVIRSRLGPR
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Lipase that displays broad substrate specificity and preferentially hydrolyzes p-nitrophenyl myristate in vitro. Also shows significant activity with pNP-butyrate (68%), pNP-octanoate (82%), pNP-decanoate (90%), and pNP-laurate (74%). Is probably involved in lipid catabolism. Is active at low pH, and might play some important role in mycobacterial biology in macrophages where the bacteria encounters acidic stress.
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L5KLU7
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S39A4_PTEAL
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Zinc transporter ZIP4 (Solute carrier family 39 member 4) (Zrt- and Irt-like protein 4) (ZIP-4)
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MAILAWLEPRPLLAVLVLVLTMRMAQPAHLLTLLSSGQGALDRVALGGLLNTLAARVHCTSGPCGKCLSVDDLLALGRPEEPGHLARLSAAAALYLSDPEGTCEDIRAGRWASRADHLLALLEGPKALAPGLSRLLQRIQAQTTGQPSAGEACVDPPQLLREAGVAGAPGSPGPVLATLLEHVGRGSCFHTLPTPQYFVDFVFQQSHGNTPNISVAELAALMQRLGVGGVTETHSDHHHQEKRVNRQGPTPLTAPNSSSDTWDTVCLSARDVMAVYGLSEQTGVTPEAWAQLSPALLQQQLSGACSPQPSHPAQNQLSQAEKYLYGSLATLLICLCSTFGLLLLTCAACSTAAHYVIQTFLGMAVGALTGDALLHLTPKVLGLHQHGGDSEHRADSHGPQTTWRLVVALSGLYVFFLFEKLCDLLLPQDPEDRKGTPRSHSGHSHGMSLQLAPRELRPPKQPHEGSRADLVAEESPELLSPEPRRKSPELRLLPYMITLGDGLHNFADGLAVGAAFASSWKTGLATSLAVFCHEVPHELGDFAALLHAGLPVSRALLLNLASGLTAFAGLYVALALGVGEESESWTLAVAIGLFLYVALCDMLPAMLNVRDPRPWLLFLLHNVGLLGGWAVLLLLSLYEDSIAL
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Selective transporter that mediates the uptake of Zn(2+). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher concentrations (By similarity).
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L7N1X6
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FBW15_MOUSE
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F-box/WD repeat-containing protein 15
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MAIHLPCLPMMKILSYLDAYSLLQAAQVNKDWNELASSDVLWRKLCQKRWLYCDMDTLQLQGKETWKQFFIDRIWQERAKFRAKAKDFTYKEIPLMCGLFGYACYISGCGLTRKGQDKSVVCMVNSKNTISTWDVHKSVITWKSPEQPASIKLLTTLPEMHIAVTVDIQSTIKLWDCHNREALATNNLKSPCKSLKAVFTKDGPIVLIGDTLGNIHIFRIPDLYLISTVNVLPYGFDGIYCSPQKKWVLLSKKHPHILPKVFYMSSFLRTSEFSAPVSTVLKLSLYERVFWTPRREDRITLMSRSGFPQVKMFETYDIKLEEFGNKRIVKGKLIASFELQCHKVNPQRFGVSDKNVIVCSTESSLLLFDINGLRLKTFQYCPEMIVKLSVDPLHVIVICNTGSMDVYAWEERSLLLRKCYRLHIERPLPLYGFIYKAACDDVSIIQLITDELSLSSLTSYALNICS
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Substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes KAT7 ubiquitination and subsequent degradation in collaboration with MAP2K1 kinase, leading to reduced histone H3K14 acetylation and increased cell proliferation.
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L7N6F8
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DEP23_DERPT
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Major mite allergen Der p 23 (Major house dust mite allergen Der p 23) (Major HDM allergen Der p 23) (Peritrophin-like protein Der p 23) (allergen Der p 23)
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MKFNIIIVFISLAILVHSSYAANDNDDDPTTTVHPTTTEQPDDKFECPSRFGYFADPKDPHKFYICSNWEAVHKDCPGNTRWNEDEETCT
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Does not bind chitin in vitro.
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L7NCQ3
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TBSYN_GARMA
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2,4,6-trihydroxybenzophenone synthase (GmBPS) (EC 2.3.1.220)
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MAPAMDSAQNGHQSRGSANVLAIGTANPPNVILQEDYPDFYFKVTNSEHLTDLKEKFKRICVKSKTRKRHFYLTEQILKENPGIATYGAGSLDSRQKILETEIPKLGKEAAMVAIQEWGQPVSKITHVVFATTSGFMMPGADYSITRLLGLNPNVRRVMIYNQGCFAGGTALRVAKDLAENNKGARVLVVCAENTAMTFHGPNENHLDVLVGQAMFSDGAAALIIGANPNLPEERPVYEMVAAHQTIVPESDGAIVAHFYEMGMSYFLKENVIPLFGNNIEACMEAAFKEYGISDWNSLFYSVHPGGRAIVDGIAEKLGLDEENLKATRHVLSEYGNMGSACVIFILDELRKKSKEEKKLTTGDGKEWGCLIGLGPGLTVETVVLRSVPIA
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Type III polyketide synthase involved in the biosynthesis of benzophenones and xanthones. Produces mainly 2,4,6-trihydroxybenzophenone together with minor amounts of tetraketide lactone, triketide lactone and diketide lactone. The preferred substrate is benzoyl-CoA, but can also use acetyl-CoA, phenylacetyl-CoA, hexanoyl-CoA, cinnamoyl-CoA, p-coumaroyl-CoA and salicoyl-CoA.
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L7R9Z0
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EOBI_PETHY
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MYB-like transcription factor EOBI (Protein EMISSION OF BENZENOIDS I) (PhEOBI)
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MDKRTCNSQDVEVRKGPWTMEEDLILINYIANHGEGVWNSLARSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLLIMELHAKWGNRWSKIAKHLPGRTDNEIKNYWRTRIQKHIKQADQNMKKPSKCEQNDQKAISTSQASTGPTDTIDSYSPSSYTENTNNNMENITFQGNFPTETNENIWSMEDLWSLQLLNDATN
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MYB-type transcription factor controlling the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) by regulating the expression of ODO1, a key regulator of the shikimate pathway, and of several biosynthetic floral scent-related genes (e.g. IGS, EGS, BSMT1, BSMT2, PAL1, PAL2, EPSPS, DAHPS, CS, CM1, ADT1 and PPA-AT). Binds to and activates the promoters of at least ODO1, IGS1 and PAL1.
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L7X3S1
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MSH_PAPSO
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Methyltetrahydroprotoberberine 14-monooxygenase (EC 1.14.14.97) ((S)-cis-N-methylstylopine 14-hydroxylase) ((S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase) (Cytochrome P450 82N4) (Methyltetrahydroprotoberberine 14-hydroxylase) (N-methylstylopine hydroxylase) (PsMSH)
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MRTESIKTNRPMDLLLQYLQPISVALVVIALVWNYGRRNPTKKLAPEASGGRPIMGHLHLFNDGELTHRKLGAMADTYGPVFNIRFGSHKTLVVSDWEIVKECFTTNDKLFSNRPGTLGIKLMFYDADSVGYAPYGAYWRDLRKISTLKLLSNHRIDTIKHLRSSEVESCFESLYSQWGNGEKSGEFAPVRMDSWLGDLTFNVVARIVAGKKNFSANGDVGAQRYKAAMDEAMRLMRFFAFSDVIPSLSWLDNLRGLVREMKKCASEIDSIMATWVEEHRVKRNSGGNSQLEHDFIDVCLDIMEHSSLPGDDPDLVVKSTCLDMILGGSDTTTVTLTWAMSLLLNHPQVLQKAKEELETQVGKNRQVDDSDIPNLPFIQAIIKETMRLYPAGPLIERRTMEDCEVAGYQVPAGTRLLVNVWKMQRDGNVYKGDPLEFRPDRFLTSNADVDLKGQHYELIPFGAGRRICPGVSFAVQLMHLVLARLLHEFEITTVEPETKVDMAESGGLLCYKIMPLEVLIKPRLEI
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Involved in the biosynthesis of the isoquinoline alkaloid sanguinarine (PubMed:23313486, Ref.2). Catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively (PubMed:23313486, Ref.2). Can also use (S)-cis-N-methyltetrahydrothalifendine and (S)-cis-N-methyltetrahydropalmatine as substrates (Ref.2).
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L7YAI7
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B4GA1_DANRE
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Beta-1,4-glucuronyltransferase 1 (EC 2.4.1.-) (I-beta-1,3-N-acetylglucosaminyltransferase) (N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase) (Poly-N-acetyllactosamine extension enzyme) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1)
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MHFSKKCSVFKVVLSALLIVALLQLLYLSFLSKLHGKQQRYKYSELFGSKKNANQGEKNPRREHLRYSLSTGGIFDGSGQYRVYKNLIKSDFSTNQKPGADPRSHHLALATHTTINNLHHLESLLERWKNPISVAIFANGEDVKFATAIIYALSLFCPQVQALVDFHLVCHSGEMATFPDQDREHFVGLQEMGCPAVFAKLESHRDKYKNYAIGSNVSYPNNLLRNVARGGTDAAYILVIDIDMIPSANLHHQFVTMLMKREPAADEVLVLPAFEIRHIRKMPASKPELVQLYQVGEVRPFYDELCSRCQAPTNYSLWVNLASKSSGPLEVSYTINWVDPWEPFYIGARSVPLYDESFRQYGFNRISQACELHIAGYRFSVVSNAFLLHKGFKVQGEFHSRKDEENRKNRILFRSFKESLKAKYPTSPRRC
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Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE, during synthesis of phosphorylated O-mannosyl glycan (By similarity). Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). Required for axon guidance via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity).
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L8B068
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MALA_HALJT
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Alpha-amylase MalA (EC 3.2.1.1)
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MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ
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Alpha-amylase that cleaves starch into oligosaccharides, the first step in starch degradation (By similarity). Endo-acting enzyme which prefers a linear polysaccharide to branched polysaccharides hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also transglycosylation activity, but does not act on alpha-1,6 bonds. Higher activities of 100%, 79% and 67.8% against amylose, soluble starch and amylopectin, respectively. Lower activity of 22% against glycogen and faint or no activity against alpha-, beta- and gamma-cyclodextrin.
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L8E946
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UNC42_CAEEL
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Homeobox protein unc-42 (Uncoordinated protein 42)
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MSDNLLNGANGASTVSQFQEKVKDLGVSLHDFTAYYPSSLDTVSASLRPISDPSSDGAFKKIKTEGLGGSVFGSSIAGVTNTPARLCSLERPESERLNSRRRHRTTFTQEQLQELDAAFQKSHYPDIYVREELARITKLNEARIQVWFQNRRAKHRKHEKQLNKAINPPHSFLSNPANTLMRQGMYPAALNRDGFWYQSYQRPMPYPTASPSYSNSFTNPIANFGHSITSFQADDEFYQKSLALRMTTTPSAATAATSLANINYQQTQPSEASTNPPSI
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Probable transcription factor. Required for initial outgrowth and pathfinding of axon growth cones along the ventral nerve cord (VNC). Involved in specifying neuron identity, in concert with nuclear hormone receptor family member fax-1, or with transcription factors unc-3, cfi-1, or hlh-34, perhaps acting via positive feedforward loops. Establishes electrically- and chemically-interconnected neuron circuits, acting by modulating the expression of neurotransmitter pathway genes, neurotransmitter receptors, neuropeptides, and neuropeptide receptors. Required for cholinergic and glutamatergic synaptic communication. Plays a role in locomotion and mechanosensory response, perhaps via regulation of chemosensory receptor expression, and is required for expression of glutamate receptors, including glr-1, glr-4 and glr-5.
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M0QWB7
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ASCL5_MOUSE
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Achaete-scute homolog 5 (Achaete-scute family bHLH transcription factor 5)
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MNSNFCRALVDRGPPGGMQLGVVAPAGQTPLAATEPLSNVPFLLYPGHSEPPYYDAYTGVFPYVPFPGAFGVYDYPFEPAFIQKRNERERQRVKCVNEGYARLRGHLPGALTEKRLSKVETLRAAIRYIKYLQELLSATPDGAPPPATSPPPAHTGHSNVPQPSSLVAESSGSPFSSSPFLESEEPSL
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Transcription factor. Probably binds E-box motifs 5'-CANNTG-3' in complex with transcription factor TCF3/E12. Negatively modulates transcription of target genes such as CDH1/E-cadherin, perhaps by recruiting the PRC2 repressive complex to regulatory elements. Regulates ameloblast development and tooth germ growth, perhaps acting by positively modulating migration of inner enamel epithelium (IEE) cells. Plays a role in enamel formation.
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M0R2J8
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DCDC1_HUMAN
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Doublecortin domain-containing protein 1 (Doublecortin domain-containing 5 protein)
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MAKTGAEDHREALSQSSLSLLTEAMEVLQQSSPEGTLDGNTVNPIYKYILNDLPREFMSSQAKAVIKTTDDYLQSQFGPNRLVHSAAVSEGSGLQDCSTHQTASDHSHDEISDLDSYKSNSKNNSCSISASKRNRPVSAPVGQLRVAEFSSLKFQSARNWQKLSQRHKLQPRVIKVTAYKNGSRTVFARVTVPTITLLLEECTEKLNLNMAARRVFLADGKEALEPEDIPHEADVYVSTGEPFLNPFKKIKDHLLLIKKVTWTMNGLMLPTDIKRRKTKPVLSIRMKKLTERTSVRILFFKNGMGQDGHEITVGKETMKKVLDTCTIRMNLNLPARYFYDLYGRKIEDISKVPLLEKCLQNSITPLRGLLWVSKGEGFSPSGAKMYIQGVLLALYQRLKSAKKYYKQLNLVMNEQKEKITEKVILSMTAKEHHKEQEEVSRLIDELQTAIKSNIGHLCKLGPQLQAEQEQFSSYVYQHIKSLPANTLVPGGLQLKVFENGKNTGEISVGISKKDLGSDSPIQTDHMMERLLLKIHQRLQGSSINPPGLNYSSMRLFDENGQEIKNPLSLKNEQKIWVSYGRAYRSPLNLALGLTFDRVSAFARGDIMVAYKTFLDPNAVLLPGCGNWEVCEGFPINFNCTSQQIPDQFEKVDLENHFLQNKVDPNIVLHASVSIGKWSFSGSEASSRSQIAPSILWPVASVWLITKTGMILSRAITQGCLAIGHPIRVKAAEGTSLEGYKLILQKRHSGDDSQKWVFGTDGCIYSKAYPQFVLTYLEELNAQVDVTQTEYHIHHGAWTTAHQEHGRNLAEEVLQESASNLGLKQLPEPSDTHLMPEGSLEETGELTVALVRKLEEKHPKASAQRWAIKHEGTSKPGQWKHSRVENPLWNKLTYMWPVLPSGQLNEEFDWPIQGLLVPSSPPMKKPICKTTEPYAPVRLRVLQNGEKNKNRSVTILGPDISPGRKTQCTEILNLPSAARRLYNEKGKEIFALKDLQRDELVYVSCGELWINPDLSIAQQKKQIFLRNLESDIAKIQIFCSTHKIEALVLEVQSDIVSGSKLAVHKPVAIFGEEKQVTEPEEKQMQEDPLTTENASSEILDSHVRAHLRMKACHTLPRYAWQETSHDFDEDDSLPKKTEKGLFENVEPQKKHSCSPKHSKLHKHCHQQFEYRDGQIISHAAPQLVLGVQGPNLRSGMEVVLVEKKSDGSHQRWIHQEDSRTFHLVSNPDLVLAVSMTKTRNEVCGYPVIVQKYKPYNNGAANQKWHYMKNIKALVAFHSTALDKEITSANYAGVCTSSVIKEENIDQPGYCYLSPDGKRKTMLCLACGQSMRTEKGLKQLLPGVPFLCISGTKTQKPFLQGPFKVISVAEVDLSCDKAEKTLSYYQARLLSLRMKTCTQAASHSGMAATHQKAVKIIAYKNGDGYRNGKLIVAGTFPMLLTECTEQLGLARAASKVYTKDGTPIFTLRDLVLWALDESFLQRDSEKQKQDAAPVGKEQIIVEKNPRMKVKNRLFAKSVTSDSLDGIDKSLLTLILRNPIAIWVSCGEPFLPPNALQKAEKLEKQNWLKKDRILADLDTMRHKMRQLKGRRVAACQPATMVPTKSPVQPVVVEGGWTEQTQQEIKLMELIRHTEAHLSEIQEMESKINFPIATKRIAVKPSNLYKQPNTKRVWIYLNGGRPEDGTYAWGKTISELLQDCSSRLKMTHPARALYTPSGEPIQSWDDIERDMVICVSMGHGFKTPKELKQLMEIRANYARIRRQQGPQATDIVVSPSTKLLSLAHLHN
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Microtubule-binding protein which plays an important role in mediating dynein-dependent transport of RAB8A-positive vesicles to the midbody during cytokinesis.
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M0R4F8
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DNMBP_RAT
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Dynamin-binding protein (Scaffold protein Tuba)
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MEPGSVVRAIFDFCPSVSEELPLFVGDVIEVLTVVDEFWLLGKKEDVTGQFPSSFVEIVTIPSLKEGERLFVCTCDFISREPNSLSLHRGDLVIIDGTPTAGWLQGRSSLGARGFFPSSCIHELCLSSQSRQWHSQNMLLQVPEYSMGQARALMGLSAQLDEELDFREGDVITIIGVPEPGWFEGELEGRRGIFPEGFVELLGPLRTADESVNAGSGDDSTLNDEVDVSPEEVESEGDEDDQQAGTYGIALYRFQALESNELDFEVGDKIRILGTLEDGWLEGRLKGKTGIFPHRFVKLCPSNRSEETMALPQGDSFPKNSESSAGEMGDSVVEEARQDPQECEEETPDSGLPEQTSEEPLDHVAPECVVDKISGQDEDASGSSPDVDLEGPRAEDPSTPDLSQEVNGISSLPPQVPLQPEEEKSQHYLTAGGSRQCPDTFSKLFPLEAKTRNYSSLPPRRTYTQGWSLQKPAPHLHRASSLTASRVNRPGHFSHTAMASCAQKHQTSAENAASLCCAPERPKRRPGLPDKEPATEITPASQGDNLDLDSKLTQQLIEFEKSLSGPSTEPKKIVRRFSIMDFYSEKDIVRGSSNSLPSRNFPERRKALRPPPPRPHTPTSTSPHLLVDQSPKPGPPLVVRPSRPAPLPPPTQQRLNTASPKPTSCALPGWEAPEKEGSEYTEKSPAQLFPCPSVLARIQDVEHDLDMHTRAQEELNLLLEEKQDESLRAETLETLKSYESTIQSLNLELQQLREMTLLSSQSSSLAAPSGSVSTEKPEQRMLEKRAKVVAELLQTEKDYIRDLEMCVERVMVPLQQAQVPNIDFEGLFGNMQTVIKVSKQLLAALEITDAVGPVFLDHRDELEGTYRLYCQNHDEAISLLDIYEKDERIQKHLQDYLADLKSLYHEWGCTNYINLGSFLIKPVQRIMRYPLLLMELLNSTPESHPDKAPLTSAVLAIKEINANINEYKRRKDLVLKYRKADEDSLMEKISKLNIHSIIKKSSRVSSHLKHLTGFAPQLKDEAFEETEKNFRMQERLIKSFIRDLSLYLQHIRESACVKVVAAMSIWDLCMERGHHDLEQFEKVHRYISDQLFTRFKERTERLVINPLNQLLNMFTGPYKLVQKRFDKLLDFYNCTERAEKLKDKKTLEDLQSARNNYEALNSQLLDELPKFQQYAQSLFTNCIHGYAEAHCDFVQKALEQLQPLLSLLKASDREGNLIAIFHEEHSRVLQQLQVFTFFPEALPAPRKPFERKTTDRQSSRKALLGMPSYMLQSEELRSSLLARYPPEKLFHVQRNFNAAQDLDVSLLEGDLVGVIKKKDPMGSQNRWLVDNGVTKGFVYSSFLKPYNPRCSHSDSSVVSHSSTESEHSGSSPSFHRQNSSSALTFNSNSMTVSFTSGLPQKQPQDTSPLRECVPETLGVSSNTGNPETGPSPCPSDPGFSCQRRPGNPADGTREISQPASTLRGCQRRSLHSEVLGYPVPGRSDQGSDSIKGTSRACQTAGDRDRGLGSSEAEGNQVYFAIYTFKARNPNELTVLANQRLRILEFKDVTGNTEWWLAEVNGKKGYVPSNYIRKTEYT
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Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions in epithelial cells (By similarity). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation (By similarity). Plays a role in ciliogenesis (By similarity). May play a role in membrane trafficking between the cell surface and the Golgi.
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M0R5D6
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RN157_RAT
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E3 ubiquitin ligase Rnf157 (EC 2.3.2.27) (RING finger protein 157) (RING-type E3 ubiquitin transferase Rnf157)
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MGALTSRQHAGVEEVDIPSNSVYRYPPKSGSYFASHFIMGGEKFDCTHPEGYLFGENSDLNFLGNRPVSFPYAAPPPHEPVKTLRSLINIRKDTLRLVKCAEEVKSHGEEAGKAKVHYNVEFTFDTDARVAITIYYQATEEFQNGIASYIPKDNSLQSETVHYKRGVCQQFCLPSHTVDPSEWAEEELGFDLDREVYPLVVHAVVDEGDEYFGHCHVLLGTFEKHSDGTFCVKPLKQKQVWDGVTYLLQEDYGIENKSNTQDFKVAEDDVRDNSAECVVCLSDVRDTLILPCRHCASCNVHCADTLRYQANNCPICRLPFRALLQIRAMRKKLGPLSPSSFNPIISSQTSDSEEHSSSENIPAGYEVVSLLEALNGPLTSSPAVPPLHVLGDGHLSGMLPSYGSDGHLPPVRTLSPLDHLSDCNSQGLKLNKSLSKSISQNSSVLHEEEDERSCSESDTQLSQRLSAQHPEEGPDVTPESENLTLSSSGAVDQSSCTGTPLSSTISSPEDPASSSLAQSVMSMASSQISTDTVSSMSGSYIAPGTEEEGEAPPSPRAASRAPSEEEETPAESPDSNFAGLPAGEQDAEGNDIMEEEDRSPVQEDGQRTCAFLGMECDNNNDFDVASVKALDNKLCSEVCLPGTWQHDAAIINRHNTQRRRLSPSSLEDPEEDRPCVWDPLAV
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E3 ubiquitin ligase that ubiquitinates APBB1 for its degradation by the proteasome and thus prevents apoptosis and promotes survival of neurons (By similarity). Has a dual role in neurons as it is also required for dendrite growth and maintenance for which its ligase activity is not critical (By similarity). May act as a scaffold molecule to regulate this process (By similarity). Acts as a downstream effector of the interconnected PI3K and MAPK signaling pathways and thus participates in the regulation of the cell cycle (By similarity).
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M0R6D8
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MNX1_RAT
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Motor neuron and pancreas homeobox 1 (Homeobox protein HB9)
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MEKSKNFRIDALLAVDPPRAASTQSAPLALVTSLAATPSGPGRGGSGGGGTSSGASRSCSPASSEATAAPGDRLRAESPSPPRLLTAHCALLPKPGFLGAGGGGGAAGGPGTPHHHAHPGAAAAAAAAAAAAAAGGLALGLHPGGAQGGAGLPAQAALYGHPVYSYSAAAAAAALAGQHPALSYSYPQVQGAHPAHPADPIKLGAGTFQLDQWLRASTAGMILPKMPDFSSQAQSNLLGKCRRPRTAFTSQQLLELEHQFKLNKYLSRPKRFEVATSLMLTETQVKIWFQNRRMKWKRSKKAKEQAAQEAEKQKGSGGGAGKGGTEEKTEEELLGPPVSGDKASGRRLRDLRDSDPDEDEDDEEDHFPYSNGVGAHAASSDCSSEDDSPPPRPGGPGHQPLPQ
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Transcription factor. Recognizes and binds to the regulatory elements of target genes, such as visual system homeobox CHX10, negatively modulating transcription (By similarity). Plays a role in establishing motor neuron identity, in concert with LIM domain transcription factor LMO4 (By similarity). Involved in negatively modulating transcription of interneuron genes in motor neurons, acting, at least in part, by blocking regulatory sequence interactions of the ISL1-LHX3 complex (By similarity). Involved in pancreas development and function may play a role in pancreatic cell fate specification (By similarity).
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M0R7T6
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RBM24_RAT
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RNA-binding protein 24 (RNA-binding motif protein 24)
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MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAATGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ
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Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation. Plays a major role in pre-mRNA alternative splicing regulation (By similarity). Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (By similarity). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (By similarity). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes (By similarity). Plays a role in the regulation of mRNA stability (By similarity). Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities (By similarity). Involved in myogenic differentiation by regulating MYOG levels (By similarity). Binds to multiple regions in the mRNA 3'-UTR of TP63 isoform 2, hence inducing its destabilization (By similarity). Promotes also the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence (By similarity). Plays a role in the regulation of mRNA translation (By similarity). Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation (By similarity). Binds to a huge amount of mRNAs (By similarity). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (By similarity). Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes.
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M0R7Z9
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PLIN5_RAT
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Perilipin-5 (Lipid storage droplet protein 5)
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MDQRGKDTTLALHSRMSGDQTAQDPGSSLGELDQHNVVKRVVALPLVRATCTAVSGAYNSAKDRHPLLGSACRFAEHCVCSVATCALDHAQPLLEHLQPKLATVNDLACRGLDKLEEKLPFLQQPSDTVVTSAKDAVAKSVTGVVDLAQRGRRWSGELRRSVSQAMDTVLRRSVSQAMDTVLGKSEELVDHFLPMTEAELVALATESQGPEVGSVEEQRQKQGYFVRLGSLSARLRHLAYQHSLGKLRESKHRTQEMLAQLQKTLELIQHMQSRASPTPTFHHPKVQELCGDWSPCLENGYRHSQVELETLALSRSLTLELQSAVDALAGCVRGLPPSAQAKVAEVQRSVDALQATFADAHCLGDVAPTALAEGQDSVAQAHACVDEFLDLVLRAMPLAWLVGPFAPILVERSEPLINLATCVDEVVGDPDPRWAHMDWPAQQRAWEAEPADPGGQEAEPPLGQVKHTMMPELDF
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Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE.
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M0R8L2
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SPXN_RAT
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Spexin (Liver regeneration-related protein LRRGT00060) (NPQ) (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1; Spexin-2 (NPQ 53-70)]
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MKGPSILAVAALALLLVLSVLENSSGAPQRLSEKRNWTPQAMLYLKGAQGHRFISDQSRRKELADRPPPERRNPNLQLLTLPEAAALFLASLEKPQKDEGGDFDKSKLLEDRRFYW
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Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release. [Spexin-1]: Acts as a ligand for galanin receptors GALR2 and GALR3 (By similarity). Intracerebroventricular administration of the peptide induces an increase in arterial blood pressure, a decrease in both heart rate and renal excretion and delayed natriuresis. Intraventricular administration of the peptide induces antinociceptive activity. Intraperitoneal administration of the peptide induces a reduction in food consumption and body weight. Inhibits long chain fatty acid uptake into adipocytes. Also induces contraction of muscarinic-like stomach smooth muscles. {ECO:0000250, ECO:0000269|PubMed:24550067}. [Spexin-2]: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity.
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M0R8U1
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DYH5_RAT
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Dynein axonemal heavy chain 5 (Axonemal beta dynein heavy chain 5) (Ciliary dynein heavy chain 5)
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MFRIGRRQLWKQSVTRVLTQRLKEEKEAKRARLDGRHDYLFAIVASCLDLNKPEVEDALLEGNQIERIDQLFAVGGLRHLMFYYQDVEGAEAGQFGSSGGVNPASGKMKKPKVFVTEGKDVALMGACVFFTRADPSKAITAENIHREVSFNTLDTADGGLLNSVRRLLSDIFIPALRASSHGWGELEGLQDASSIQQEFLSSLEGFVGILSGAQNSLKEKVNLQKCDIVELKSLKEPMDYLALASNPETVEKVECCMRVWIKQMEQILAENNQLRKEADDVGPRAELEHWKKRLSKFNYLLDQLKSPDVKAVLAMLAAAKSKLLKVWRDADIRVTDAANEAKDNVKYLYTLEKCCDPLYSSDPVTMVDAIPTLINAIKMIYSISHYYNTSERITSLFVKVTNQMISACKAHITNNGTATIWSQPQDIVMQKIAAAIKLKQGYQCCFQETKQKLKQNPSEKQFDFSEMYIFGKFETFHQRLAKIMDIFTTFKTYSVLQDSKIEGLEDMVTKYQDVVAGIKKKEYNFLDQRKMDFDQDYDEFCKQTNELHSELQRFMDTTFEKIQSTRQALSTLKKFERLNIPNLGIEAKYQIVFQNFGTDIDMISKLYTKQKYDPPLARDQPPIAGKILWARQLFHRLEQPMQLFQQHPFVLRTVEAKPVIRSYNRIAKVLLEFEVLYHRAWLQQIEEIHVGLEASLLVKAPGTGQLFVNFDPQILILFRETQCMSQMGLPVSPFAAALFEKRDMYKKNFSDMKMMLSEYQRVKLKMPPAIEQLMLPHLARVDEALQPGLAVLTWTSLNIGTYLENAFEKIKDLELLLDRINDLIEFRIHAILEEMSSVALCQLPQDDPLTCEEFLQMTKDLCVNGAQKLHFKSSLVEEAVNELINMLLDVDVLPEEASEKVRHENASPNGDTSGGGEGCAEALASSFNAGTSSLPLTTIARKKKEMEVLEEARELLSYFNHQNTDALLKVTRNTLEAIRRRIHFSHMINFRDSKGASKVKQNHLPIFRASVTLAIPNISMTPALEDIQQTLNKAVECIISVPKGVRQWSSELLSKRKMRERKMAAVQSNEDSDSDTEVEESELQETLELASVNLPIPVQTQNYYKNISDNKEIVKLVSVLSTVISSTKKEVITSMDRFKCYNHIWQKEKEDTIMTFIAQNPLLSEFESRILYFQSLEQEINAEPEYICVGSIALYTADLKFSLTAETKAWMMVLGRHCNRKYRSEMENIFTVVEEFQKKLNRPIKDLDDIRIAMAALKEIREQQISTDFQVGPIEESYALLNKYGLLVAKEEMDKVDTLRYAWEKLLARASDVQNELGALQPSFRKELISTVEVFLQDCQQFYLDYDLNGPMVSGLKPQEASDRLIIFQNQFDNIYRKYITYTGGEELFGLPVTQYPQLLEIKKQLNLLQKIYSLYNNVIETVNSYQDTLWSEVNIEKINSELLEFQNRCRKLPRALKDWQAFLDMKKTIDDFSECCPLLEYMASNAMVERHWQRITTLTGHSLDVGNETFKLRNIMEVPLLKYKEEIEDICISAVKERDIEQKLKQVINEWDNKTLTFSSFKTRGELLLRGDSTSEVIASMEDSLMLLGSLLSNRYNMPFKAQIQNWVQCLSNSTDIIENWMTVQNLWIYLEAVFVGGDIAKQLPKEAKRFSNIDKSWVKIMTRAHEIPNVVQCCVGDETMGQLLPHLLDQLEICQKSLTGYLEKKRLCFPRFFFVSDPALLEILGQASDSHTIQAHLLNVFDNIKTVKFHDKIYDRILSISSREGETIELDKPVMAEGNVEVWLNSLLEESQSSLHLVIRQAAANIQESGFQLIEFLSSFPAQVGLLGIQMLWTRDSEEALQNAKFDKKIMQKTNQSFLELLNMLIEMTTKDLSSMERVKYETLITIHVHQRDIFDDLCHMHVKSPTDFEWLKQCRFYFKEDSDKTMIHITDVAFTYQNEFLGCTDRLVITPLTDRCYITLAQALGMSMGGAPAGPAGTGKTETTKDMGRCLGKYVVVFNCSDQMDFRGLGRIFKGLAQSGSWGCFDEFNRIDLPVLSVAAQQISIILTCKKEHKKSFIFTDGDNVTMNPEFGLFLTMNPGYAGRQELPENLKINFRSVAMMVPDRQIIIRVKLASCGFIDNVVLARKFFTLYQLCEEQLSKQVHYDFGLRNILSVLRTLGAAKRASHTDTESTIVMRVLRDMNLSKLIDEDEPLFLSLIEDLFPNILLDKAGYPELETAISKQVEEAGLINHPPWKLKVIQLFETQRVRHGMMTLGPSGSGKTSCIHTLMKAMTDCGKPHREMRMNPKAITAPQMFGRLDVATNDWTDGIFSTLWRKTLKAKKGEHIWIVLDGPVDAIWIENLNSVLDDNKTLTLANGDRIPMAPNCKIVFEPHNIDNASPATVSRNGMVFMSSSVLDWSPILEGFLKRRSPQEAEILRQLYAETFPDLYRFSIQNLEFKMEILEAFVITQSTHMLQGLIPTKEQAGDVDPEHLGRLFVFAMMWSVGAVLELEGRRRMELWLRSREGPTLHLPQLTDPGDTMFDYYVAPDGTWRHWSMCIPEYVYPPDTTPEYGSILVPNVDNVRTDFLIKTIAKQGKAVLLIGEQGTAKTVIIKGFMSKFDPESHTVKNLNFSSATTPLMFQRTIESYVDKRMGTTYGPPAGKKMAVFIDDLNMPVINEWGDQVTNEIVRQLMEQNGFYNLEKPGEFTSIVDIQFLAAMIHPGGGRNDIPQRLKRQFSIFNCTLPSDASMDKIFGVIGEGYYCAQRGFSKEVQDAVIKLVPLTRRLWQMTKLKMLPTPAKFHYVFNLRDLSRIWQGMLNITSEVIKDTDELLRLWKHECKRVIADRFSMSSDVTWFDKAVVSLVEEEFGEEKTPVVDCGVDAYFVDFLRDAPEATGETPEETDAEMPKLYEPIASLNHLQERLSVFLQLYNESIRGTGMDMVFFRDAMVHLVKISRVIRTPRGNALLVGVGGSGKQSLTRLASFIAGYTSFQITLTRSYNTSNLMEDLKVLYRTAGQQGKGITFIFTDNEIKEESFLEYMNNVLSSGEVSNLFARDEIDEINSDLTSIMKKEHPKRPPTNDNLYEYFMSRVRGNLHIVLCFSPVGEKFRNRALKFPALISGCTIDWFSRWPKDALVAVSEHFLSSYNIDCTAEIKKELVQCMGSFQDGVAEKCADYFQRFRRSTHVTPKSYLSFIQGYKFIYEEKHVEVQSLANRMNTGLEKLKEASESVAALSQELAVKEKELQVANEKADMVLKEVTMKAQAAEKVKAEVQKVKDKAQAIVDSISKDKAIAEEKLEAAKPALEEAEAALQTIKPSDIATVRTLGRPPHLIMRIMDCVLLLFHRRVNAVKIDLDKSCTVPSWQESLKLMTAGNFLQNLQQFPKDTINEEVIEFLSPYFEMSDYNIETAKRVCGNVAGLCSWTKAMASFFSINKEVLPLKANLIVQENRHALAMQDLQKAQAELDDKQAELDVVQAEYEQAMTEKQ
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Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles.
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M0RC99
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RAB5A_RAT
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Ras-related protein Rab-5A (EC 3.6.5.2) (Small GTP-binding protein rab5)
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MANRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFSRAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTPMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPAQPARSQCCSN
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Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Active GTP-bound form is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan. Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3.
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M1C146
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ATG8C_SOLTU
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Autophagy-related protein 8C-like (Autophagy-related ubiquitin-like modifier ATG8CL)
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MAKSSFKLEHPLERRQAEAARIREKYPDRIPVIVEKAERSDIPDIDKKKYLVPADLTVGQFVYVVRKRIKLSAEKAIFIFVKNILPPTAAMMSAIYEEHKDEDGFLYMTYSGENTFGSF
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Ubiquitin-like modifier involved in autophagosomes formation (Probable). May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton (Probable). ATG8CL-mediated selective autophagy contributes to defense against the fungal pathogen Phytophtora infestans.
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M1J8U6
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IFI4E_PRUDO
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Eukaryotic translation initiation factor isoform 4E (eIF(iso)-4E) (eIF(iso)4E) (eIF-(iso)4F 25 kDa subunit) (eIF-(iso)4F p28 subunit) (mRNA cap-binding protein)
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MATEVAAAVPPPQLDAEENSGLEAAAAEAKIQPSSGPHKLERKWTFWFDNQSKPKQGAAWGSSLRKAYTFETVQEFWCLYDQVFKPSKFPPNADFHLFRAGVEPKWEDPECANGGKWTVTSRSKASLDTMWLETLMALIGEQFDEADEICGVVASVRQRQDKLALWTRNAANEAAQMGIGRKWKEIIDVTDKITYSFHDDSKRERSAKPRYNV
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Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses such as the plum pox virus (PPV) strain D.
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M1MR49
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JAP_RHIAP
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Japanin (18 kDa immune-modulatory lipocalin) (Cholesterol binding protein)
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MKVLRCLVCSFYIIVSLITTMTIGTPSMPAINTQTLYLAGHSSKLFERNVGCVKTRYLNQTGDWVTRSLIYVFTFDTEPWVTQAGAFQVKWEPYSPLLRVKASDYVRDNLGAKPDYFIRTYDNDFLLLSDLKEVRSTCSLWVTLKYVDRIPETINRTFYTICPDPVPVPFDERCYP
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Salivary tick protein that modulates host immune response. This protein blocks dendritic cell (DC) differentiation from monocytes. In addition, it inhibits up-regulation of costimulatory molecules and pro-inflammatory cytokines in response to stimuli and promotes up-regulation of co-inhibitory molecules and the anti-inflammatory cytokine interleukin-10. It has a pocket to accomodate cholesterol, which may have immune-modulatory roles, either directly or through interactions with the host gut microbiota (Probable).
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M1RNJ8
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ATH1_CANGB
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Periplasmic/secreted acid trehalase ATH1 (cgATH1) (EC 3.2.1.28)
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MGFKDKILFWKDEVQYRTLAVADQVANRFLHSFENVYQGDESVEDADSRPVGLTNETLSHSSDFFVLPEERISTRVKIRRQNILNTTLILGMLIALVIWTAILSTNSYFSSSLASASPLFNKEGRVVRPMRESNLGLHADPQTRKSSKTLYDLLSDFDNAFYDDENMILGSLAFGENTYSRQPYVANGYIGSRIPNIGFGYALDTLNLYADAPGALNNGWPLRNRRFAGSFVSDFYSLQAKLNSTNFPELDEKGYTTVISSIPEWTDLQFTVDLNGTKWFNPQSVLIDDVINYNQNLSMKDGIVSTNMDWLNGMINIKSEVWAHRKIHSLGITRLEISLNLDALPDEFTELPVTVYDIIDLNTSHRTTLYEKGQDEDNKAIYMIVNPDNVPYSNAVVYSTCTIKGTENNFSPYNFTSDDRIARNYMTNLTEENPKVVIYKYTSVVSSEYNNDEPNPNVNLKFASNIANTAKGNYKSLLSNHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRQYNVSTTRGLPVGVGGLSSDSYGGMVFWDADVWMAPALLPFFPNIAMNMNNYRNATHQQAIENAKQYNYPGAVYPWTSGRYANCTSTGPCIDYEYHINVDIALASFSIYMNGAEGADEDYLRFTTWPMVKDAAVFFKAYVKYNETLGEYETYNLTDPDEFANHVNNGAFTNAGIKTLLKWATDIGTHLGEEVDPKWMEIADNIHIPRSDSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAASLLNHGSSSQSYLYKSVLPYLRSPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGLRYSYEVTPRTKKISRLLKFDPVKLPLLPGGIAIRNFKYMGQVLDIIIDDNNGTIAHKGGDKPIRIKVPNRDILHDRNITSALYSKRDDDLSATDDYYGTYFTLYPNEELVIPLYDTKLNIDGNIAESKQITNLTAGVPGDVGFSALDGNNYTHWQPFDKSDNAKLLIDLGFNSTHVIKKGIILWGQRPAKNISLSVLPHSERIEQLFANITDLLETSSITKGGLPLNQMLGQTQSNVTAEIDDDILALLNWKGDDLDQLIPYLPDMHLLQEKFIPILKDYPIKPNQRYYEEIIDDDIIKLLPSNTTEFTIDYNSIPGGEKRARYVVLTVHGTYDDDDDLKGATIREIVLQE
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Periplasmic/secreted acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source. Growth on trehalose is not restricted to respiration.
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M1V4Y8
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CFA73_CHLRE
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Cilia- and flagella-associated protein 73 (Flagella-associated protein 73) (Modifier of inner arms 2 protein) (Mia2p)
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MDEEGSATARAKMMPQTLVLDHVSPATRLLEKRRQMFEVQEALEAQKQDFNRKEEVFKRREEALKLKDLELQESLIRFSKFLQENDSKRARAEKKANDEIKARIQKEKEIEQLTEVLEELKSEKERILEVLEKNMRYQHYLESVLEVADEYQEVADLLLRHATLSATNADLKDHQRKCSELAEKVRTELQIYVKQKTDEILNLNNQVAKLKTELEGYEAEAMVQEAKKDSSLQIASQRTLEYGQVVLSADNIFNRCRSKSSIGHPAESNPLHQLDVIGNFVSDLGSIIKQFKQEQAKRASLASRAEIE
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As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of inner dynein arm.
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M1VMF7
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FDHL_GLUJA
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Fructose dehydrogenase large subunit (EC 1.1.5.14) (Fructose dehydrogenase subunit I)
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MSNETLSADVVIIGAGICGSLLAHKLVRNGLSVLLLDAGPRRDRSQIVENWRNMPPDNKSQYDYATPYPSVPWAPHTNYFPDNNYLIVKGPDRTAYKQGIIKGVGGTTWHWAASSWRYLPNDFKLHSTYGVGRDYAMSYDELEPYYYEAECEMGVMGPNGEEITPSAPRQNPWPMTSMPYGYGDRTFTEIVSKLGFSNTPVPQARNSRPYDGRPQCCGNNNCMPICPIGAMYNGVYAAIKAEKLGAKIIPNAVVYAMETDAKNRITAISFYDPDKQSHRVVAKTFVIAANGIETPKLLLLAANDRNPHGIANSSDLVGRNMMDHPGIGMSFQSAEPIWAGGGSVQMSSITNFRDGDFRSEYAATQIGYNNTAQNSRAGMKALSMGLVGKKLDEEIRRRTAHGVDIYANHEVLPDPNNRLVLSKDYKDALGIPHPEVTYDVGEYVRKSAAISRQRLMDIAKAMGGTEIEMTPYFTPNNHITGGTIMGHDPRDSVVDKWLRTHDHSNLFLATGATMAASGTVNSTLTMAALSLRAADAILNDLKQG
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Catalytic subunit of fructose dehydrogenase, an enzyme that catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose.
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M2XHU6
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HEXB_DOTSN
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Fatty acid synthase beta subunit hexB (EC 2.3.1.86) (S-acyl fatty acid synthase thioesterase) (EC 3.1.2.14) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39) (Dothistromin biosynthesis protein hexB)]
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MGSQHQSQHNSALIQAARDGEATLSVAFGGQGPSNLNCFNDLLELNKTYGSTLRPLIHTADATLSELASLPHRSGFHEDEGFETLDWLQDPKQAPSREYLALSPMSFPINTLLSLCNYCVTLRALRLDPGQFRSSLHNVVGHSQGIFAAAAIAKADSWESFLEAAEIALKISFWVGLESHTAAPPSHISAAAVQDCVEHGEGQPSSMLGITGLNRAQVEMLVERVNKSLSDDDRHVCLALANSRDKYTIAGPPHSLRAVCVQIREIRAADGVDQSRILFNKRKQEVDALFLPISAPYHSQYLKQVSNNVLDALDVDLVGSELGIPLLHTQSGQNLQDWKSKSIIKAIVCAVTTDMVEWPDVCQRLGSSYILGFGPGNIGNLIHESTEGTGVRVIQMNDRSPGSRGIGARAELFSEEMPPQALDWKQTFGPRLVLDHRGDVQIQTRMTQLLNAPPVMVAGMTPTTVTWDFVSCVMQAGYHVELAGGGYSSEARFEEALRRLAASIPIYRGITCNLLYANPQTIAWQVAVLRRLIKEGISIEGVTIGAGVPSPDVIKEYIAIGLKHISFKPGSIAAIDEVIEIAQAHPQFPIGLQWTGGRAGGHHSHEDLHLPILKTYARIRRCSNIVLIAGSGFGGGSDTYPYISGDWSKSLSYPPMPFDGILLGSRVMVAKEAHTSPQAKQLIVQTEGVGDNDWHTSFETPTGGVITITSEHGQPIHMLATRGVMLWKEFDKRIFSIKDAAKRLSYIRAHREEIITRLNKDYQKPWFGVNGDGQNVDLDRMTYREVLGRMCQLMSRGDNGWTDPSWLAMVKDFVEIAGERFGCQVDAHATKAPEVRTAFEATLGGSVDETLYPEDVALVLELLRRRGRKPPPFVPALDENFETWCKKDSLWQSEDVDSLVGKDVQRACIIQGPVAVRHSTIHDEPVQDILDNICNFHIESLLQSGETPGVARKQDLGRPNSIKKSVPGVQITTEKTTIRYQVHKTDKLPPEMDTLIEHIVGPAADCWTHHCLKDEWVFRDQARLRNPIRAAFLRQIQPGEVIEVRLSRDGNTQAIALKTALFGKSSLQTVLRIASTDGKSIKVALTPPSFLSDKPLGLQFAYQLSRKSRGSKLVEVTPNRLDAIKGFYAQLWVDSNQDVKEAGLNSEFWGEPTTLLAQDVQNYTAVVSRSTSPQLQAWNPTGSVPVDYCIVLAWTALTKPLTIPALQCDLLNLLHRSVNFKYAANARPLRLGDVTQTVSRITSLTIQPTGKLVEVSAELRRNDETVVTITTEFFIVGQFEDYETQFKSFEEPLFEVRVHSVTRQALLQSRKWLVLDDPSMDLAGLTLAFKLNTHTTFDHEGKVGALQVTGSVSRVESTGFDTRIGKVYFKKDSCNGNPVVDFLNRHGYPRVTRQPLENPGWNEGSTVLMKAPAKSNQYAMASKDTNPLHVCGVFARYAGLPDTVVHGMHTSAIVRRAVEWAVGDSDRSRFKKWQVSFEGMVRPNDRLKIQLQHTAMEHGRMIMKVQAFNDETGDKVIEAEAEVEQPRTGYVFCGQGSQEKGMGMSLYNARPEAKALWDRGDQFLREQYGFSLLSLVRENPTTLTINFGGRRGKRIRDNYLAMTKKTSLKADAKDVCIVQGLTPTSTSHTFSETKGLLFSTQFSQPAIALMEMVEHEHLFAKGVVQPSALFAGHSLGEYAALGACTTFMPFESLLTLIFYRGLKMQNALERDANGRTDYSMMAADPSRVGKAGFDERAFQCLVELVNEETGLLMEIVNHNVRSQQYVCAGHFRALWILGKVCDDLAKHPKIHLLSMQDLKDMVTTHVPAAGKLTNDIVLTRGKATIPLNGIDIPFHSTMLRGEIEHFRRYLLTKVNVPDIKPNELVGKWIPNVVGRPFSLDRSYIEHVQSVTGSEPLQKMLKAMA
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Fatty acid synthase beta subunit part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B. The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA. PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by adhA that transforms HAVN to averufin (AVF). Averufin might then be converted to hydroxyversicolorone by cypX and avfA. Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY. VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring. Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA. Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step. It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step. Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA. However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis. Alternatively, opening of the epoxide ring could be achieved non-enzymatically. The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1. The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran. OrdB and norB might have oxidative roles here. An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps.
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M2YJJ3
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HEXA_DOTSN
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Fatty acid synthase alpha subunit hexA (EC 2.3.1.86) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Dothistromin biosynthesis protein hexA)]
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MGQKTIKRKIQSAERPAEADVAFLASTQHSKDLCYEYDAPEEVAVEEPVDETPAPETAPERPPLSRAKTAAVKPQETAAPTTATIADVPLSAEEIVRALVARKLKKPILSIPTSKSVKELCNGKSTLQNEIVGDFHSEFTNLPDRPEDIPLKELVPASQSLMLGRVSSALLSKLVSSKMPARFNADAIGKYLASKWGLGPLRSVAVMLFAIAAEPEARLGSVAAAEKYLDDTAAKYAEWAGITLQERSTQSSAGGGGSSGTVDPTVLAELTKTNTRLAKRQFQALAEYLQVDLMKPSSEQESEALAVELQQKLDAWTAEFSEEFLAGVAPTFSEKKSRRYNAWWNAARQDVLALFSGNLQEDLSRDAAALEAFLDRLSNRAGESLLAMTRSLSRRNQANAIPGLTDIARRAEKAISSCIDRPATAKVHLPATRPRTTVSDEGDIKFNEVPRPDVSGHAAYADVLQAKDLNGHPAAARFVSLKSAHSHTDLTNGMLDRIRTALDSGMSFAGKNILITGAGQGSIGAEVVRILLTGGARVIVTTSREPSSTAKYFQQMYEESGAKGSELILTRFNQASAKDCENLVDHIYDSSGLDRDLDAVLPFAAAPEGGTEIQDVGAKNELVHRLMLASVFRMLGRVIKNKRDRSIDCHPTQVLLPLSPNHGTFGGDGMYAESKLGLESLVNRVQSESWSDELAICGVKIGWTRGTGLMNANDIVAEAIEDHGVLTFSVQEMAFNIAMLMTPELVDLCENAPLMADFGGGLSALEDCAKILSAARTEINTAADVARAVKAEDDLERAASRTLPAPSSTSPVAKKSMLRIGFPRLPDFELELSPLEHLRDIKDPSETVVVVGFSELGPWGSARLRWEIESKGDFSQVGYMEMAWMMDLIKHVDGPTKNGYYVGWVDSKTGESVHDAEIEARYGEVIRKHSGIRFVDPEGSAGYDPSKKEYLHEVAVEEDLPEFEASSATAEAFRLRHGTNVSISPIEGTENCRVQVKRGASIKIPKSVPFTWGSVAGQLPKGWSPKKYGIPEDLIPQLDPVSLYTICCVAEAFYSAGITDPLEIFKYIHLSEIGNFLGSSMGGALKTRQMYRDIYLDKDIQSDVLQETYLNTTGAWVNMLLLGSTGPIKTPMGACATGVESIDSAFESIMSDKTRMCIVGGFDDFHEDESYGFSTMKATVNVEEELAKGRLPSEMSRPTAESRSGFVEAHGCGVQILCRGDVALEMGLPVYGIIAGSTMAADKVGRSVPAPGQGILTFARETGQAQLDKSSPSTNTTSRTSSVSLARRGATVSPLRASLDAWGLTIDDLDVASLHGTSTKANDLNEPEVICKQMDHLGRTPGRPLWAICQKSVTGHPKAPAAAWMLNGCLQVMDSRTIPANRNADNVDPALQTATHLCFPTRPVRVQDVRAFILTSFGFGQKGGQVVGVAPKYFFATLDEEVYKDYSVRVTKRSKTADRAYAKALMSNAIVKVQDHSPYEQEDQSRIFMDPLSRITEDAETGSYHFDTKDIRNVADVKARLTRLVRGERLNARPDAASGLAQAARSAQAWIEKQTGGRSSVDTSTVGIDLVDLSAFSAHENETFIERNFTEQEKAFAKQSLDQKMAFASRWAAKEAVFKCLHTQTKGAGAAMKDIEIVKSDNAPKVKLHNDCIKAGRKAGLEDIQLSISHGEDCLIAVAIGIAGNGPAKYTL
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Fatty acid synthase alpha subunit part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B. The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA. PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by adhA that transforms HAVN to averufin (AVF). Averufin might then be converted to hydroxyversicolorone by cypX and avfA. Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY. VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring. Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA. Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step. It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step. Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA. However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis. Alternatively, opening of the epoxide ring could be achieved non-enzymatically. The next step is the deoxygenation of ring A to yield the 5,8-dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1. The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran. OrdB and norB might have oxidative roles here. An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps.
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M3TYT0
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ROCK2_PIG
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Rho-associated protein kinase 2 (EC 2.7.11.1) (Rho kinase 2) (Rho-associated, coiled-coil-containing protein kinase 2) (Rho-associated, coiled-coil-containing protein kinase II) (ROCK-II) (p164 ROCK-2)
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MSRPPPTGKMPGAPEAVSGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCKENDSIQIRKNEESQEIQKKLYTLEEHLSTEIQAKEELEQKCKSVNTRLEKVAKELEEEIALRKNVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKDFINLQSVLESERRDRTHGSEIINDLQGRISGLEEDLKNGKILLTKVEMEKRQLQERFTDLEKEKNNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSILDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMSLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLCKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDTTIASLEETNRTLTSDVANLANEKEELNNKLKDAQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDMRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNCICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAANKPS
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Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation.
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M3X9S6
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FGF5_FELCA
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Fibroblast growth factor 5 (FGF-5)
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MSLSFLLLLFLSHLILSAWAHGEKHLAPKGQPGPAATGRNPAGASSSRSSRGTTSSSSSSVSSSHSASLGNQGSGLEQSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLSILEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASAIHRTEPAGREWYVALNKRGKAKRGCSPRVKPQHISTHFLPRFKQLEQPELSFTVTVPEKKKPPSPVKPKVPLSAPRKSPNTVKYRLKFRFG
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Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase (By similarity).
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M3XFH7
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AMPQ_FELCA
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Aminopeptidase Q (EC 3.4.11.-) (Laeverin) (Tabulin) (Transmembrane Aminopeptidase Q)
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MGPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHSGVPDAASSPRGTQEEPLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCAAATARLLLHSLFLDCESAEVRGPLSSGPRDGALGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTVTTFSTTPHMPTYLVALAICDYDHVSRTERGQEIRIWARKDAIANGNAAFALNITGPIFSFLEDLFNISYPLPKTDIIALPTFDNSAMENWGLLIFDESLLLMQPNDQVTDKKAVISFILSHEIGHQWFGNLVTMNWWNDIWLKEGFASYFEFGVINYFNPKFRRNEVFFSNILHHVLSEDHALVSRAVSLKVENFTETSEINELFDLFTYNKGASLARMLSSFLNENVFISALKSYLKTFSYSNAEQDDLWRHFQMVVDNQSKILLPAPVKSIMDRWTHQSGFPVITLNVSTGAMKQEPFYLGKVQNQTLLTHNDTWIVPILWIKNGITQSLVWLDKSSEIFPEMQVSDSDHDWVILNLNMTGYYRVNYDKVGWKKLKQQLEKDPKAIPVIHRLQMIDDAFSLSKNNYVEIETALDLTKYLAEEDEIIVWYAVLVNLVTKDLVFDVNNYDMYPLLKKYLLKRLISIWNMYSTVIRENVAALQDDYLALVALEKLFETACWLGLEDCLQLSRELFKNWTNHPENEIPYPIKSVVLCYGVAFGSDEEWDFLLNMYSNKTKEEERIQLTYAMSCSKDPWILHRYLEYAVTAAPFTFNETNIMEVVAESEVGRYIVKDFLINNWQAVSERYGTQSLVNLMYIIGRTISTDLQITELQQFFGNMLEEHQKLTVRAKLQTIKNKNLENKKRNARMTAWLRKNT
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Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface (By similarity). Involved in coat pigmentation patterns. During skin development, may be required to establish the periodicity of tabby markings, initiating a pre-pattern at or before hair follicle development.
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M4DUF2
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ASO_BRARP
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L-ascorbate oxidase (AAO) (AO) (ASO) (Ascorbase) (EC 1.10.3.3)
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MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGCGLTKQFLMNRNNP
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Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA). The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (By similarity). Negative regulator of defense responses toward incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA).
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M4GGR9
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LYR_PROMI
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Lysine racemase (EC 5.1.1.5)
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MSLGIRYLALLPLFVITACQQPVNYNPPATQVAQVQPAIVNNSWIEISRSALDFNVKKVQSLLGKQSSLCAVLKGDAYGHDLSLVAPIMIENNVKCIGVTNNQELKEVRDLGFKGRLMRVRNATEQEMAQATNYNVEELIGDLDMAKRLDAIAKQQNKVIPIHLALNSGGMSRNGLEVDNKSGLEKAKQISQLANLKVVGIMSHYPEEDANKVREDLARFKQQSQQVLEVMGLERNNVTLHMANTFATITVPESWLDMVRVGGIFYGDTIASTDYKRVMTFKSNIASINYYPKGNTVGYDRTYTLKRDSVLANIPVGYADGYRRVFSNAGHALIAGQRVPVLGKTSMNTVIVDITSLNNIKPGDEVVFFGKQGNSEITAEEIEDISGALFTEMSILWGATNQRVLVD
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Amino-acid racemase that catalyzes the interconversion of L-lysine and D-lysine. To a lesser extent, is also able to interconvert arginine enantiomers (Ref.1, PubMed:23118975). Cannot use methionine, asparagine, alanine, leucine, glutamine, phenylalanine and histidine as substrates (Ref.1).
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M4IQQ5
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CCL4_HUMLU
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2-methylpropanoate--CoA ligase CCL4 (HlCCL4) (EC 6.2.1.-) (2-methylbutanoate--CoA ligase CCL4) (EC 6.2.1.-) (Butanoate--CoA ligase CCL3) (EC 6.2.1.-) (Propionate--CoA ligase CCL3) (EC 6.2.1.17)
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MEDLKPRPASSSPLTPLGFLERAATVYGDCTSVVYDAVSYTWSQTHRRCLCLASSIASLGIENGHVVSVLAPNVPQMYELHFAVPMAGAILNAVNLRLDARTISILLHHSESKLIFVDHLSRDLILEAIALFPKQAPVPRLVFMADESESGNSSELGKEFFCSYKDLIDRGDPDFKWVMPKSEWDPMILNYTSGTTSSPKGVVHCHRGIFIMTVDSLIDWGVPKQPVYLWTLPMFHANGWSYPWGMAAVGGTNICLRKFDSEIIYDMIKRHGVTHMCGAPVVLNMLSNAPGSEPLKTTVQIMTAGAPPPSAVLFRTESLGFAVSHGYGLTETAGLVVSCAWKKEWNHLPATERARLKSRQGVGTVMQTKIDVVDPVTGAAVKRDGSTLGEVVLRGGSVMLGYLKDPEGTAKSMTADGWFYTGDVGVMHPDGYLEIKDRSKDVIISGGENLSSVEVESILYSHPDILEAAVVARPDEFWGETPCAFVSLKKGLTKKPTEKEIVEYCRSKLPRYMVPKTVVFKEELPKTSTGKVQKFILRDMARGMGSATAGASRSRM
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Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on 2-methylpropanoate (isobutyric acid) and 2-methylbutanoate to produce 2-methylpropanoyl-CoA and 2-methylbutanoyl-CoA, respectively. Can also use propanoate and butanoate as substrates with a lower efficiency.
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M4IRL4
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CCL2_HUMLU
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Isovalerate--CoA ligase CCL2 (HlCCL2) (EC 6.2.1.-) (3-methylpentanoate--CoA ligase AAE2) (EC 6.2.1.-) (4-methylpentanoate--CoA ligase AAE2) (EC 6.2.1.-) (Butanoate--CoA ligase CCL3) (EC 6.2.1.-) (Hexanoate--CoA ligase CCL3) (EC 6.2.1.-) (Pentanoate--CoA ligase CCL3) (EC 6.2.1.-)
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MDNYRRLHTPVALCVASPPAPPTTSWKSMEGLVQCSANHVPLSPITFLERSSKAYRDNTSLVYGSVRYTWAQTHHRCLKLASALTTHLGISPGDVVATFSYNLPEIYELHFAVPMAGGILCTLNARNDSAMVSTLLAHSEAKLIFVEPQLLETARAALDLLAQKDIKPPTLVLLTDSESFTSSSYDHYNHLLANGSDDFEIRRPKNEWDPISINYTSGTTARPKAVVYSHRGAYLNSIATVLLHGMGTTSVYLWSVPMFHCNGWCFPWGAAAQGATNICIRKVSPKAIFDNIHLHKVTHFGAAPTVLNMIVNSPEGNLHTPLPHKVEVMTGGSPPPPKVIARMEEMGFQVNHIYGLTETCGPAANCVCKPEWDALQPEERYALKARQGLNHLAMEEMDVRDPVTMESVRADGATIGEVMFRGNTVMSGYFKDLKATEEAFEGGWFRSGDLGVKHEDGYIQLKDRKKDVVISGGENISTVEVETVLYSHEAVLEAAVVARPDKLWGETPCAFVTLKEGFDNDVSADQIIKFCRDRLPHYMAPKTVVFEELPKTSTGKIQKYILKEKAMAMGSLS
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Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on isovalerate to produce 3-methylbutanoyl-CoA. Can also use butanoate, hexanoate, pentanoate, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency.
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M4IS88
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CCL3_HUMLU
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Acetate--CoA ligase CCL3 (HlCCL3) (EC 6.2.1.1) (2-methylbutanoate--CoA ligase CCL4) (EC 6.2.1.-) (2-methylpropanoate--CoA ligase CCL4) (EC 6.2.1.-) (Butanoate--CoA ligase CCL3) (EC 6.2.1.-) (Hexanoate--CoA ligase CCL3) (EC 6.2.1.-) (Isovalerate--CoA ligase CCL3) (EC 6.2.1.-) (Pentanoate--CoA ligase CCL3) (EC 6.2.1.-) (Propionate--CoA ligase CCL3) (EC 6.2.1.17)
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MGMVGRDIDDLPKNAANYTALTPLWFLERAATVHPTRTSVIHGSRHYTWLQTYHRCRQFASALNNHSIGLGSTVAVIAPNVPALYEAHFAVPMAGAVVNCVNIRLNASTIAFLLGHSSAAAVMVDQEFFSLAEEALKILAQESKSHYKPPLLVVIGDESCDPKTLEYALKTGAIEYEKFLEGGDPEFDWKPPEDEWQSISLGYTSGTTASPKGVVLSHRGAYLMSLSASVVWGINEGAIYLWTLPMFHCNGWCYTWGMAAFCGTNICLRQVTAKGVYSAIAKYGVTHFCAAPVVLNTIVNAPPEEAIIPLPHLVHVMTAGAAPPPSVLFAMSEKGFKVAHTYGLSETYGPSTICAWKPEWDSLPPIKQARLNARQGVRYIALEGLDVVDTKTMKPVPADGTTMGEIVMRGNAVMKGYLKNPKANEESFADGWFHSGDLAVKHPDGYIEIKDRSKDIIISGGENISSLEVENTLYLHPAVLEVSVVARPDERWGESPCAFVTLKPNIDKSNEQVLAEDIIKFCKSKMPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMGALKKSNL
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Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on propanoate to produce propanoyl-CoA. Can also use 2-methylpropanoate (isobutyric acid), acetate, butanoate, isovalerate, pentanoate, hexanoate, 2-methylbutanoate, 2-methylpentanoate, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency. Triggers the formation of very short chain acyl-CoAs from the corresponding fatty acids, including acetic acid, propanoic acid, butyric acid and its isomer.
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M5A7P9
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SL9A3_TRISC
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Sodium/hydrogen exchanger 3 (Na(+)/H(+) exchanger 3) (NHE-3) (Solute carrier family 9 member 3)
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MGRNRSGCVARCVSLTALVLLLCCPVVRSSEAETDPDSHTEHGDSHGGSREGNDTGFQIVTFRWEHVQTPYVIALWILVASLGKIVFHLSEKVTSVVPESALLIVLGLILGGIVWAADHSASFTLTPTVFFFYLLPPIVLDAGYFMPNRHFFGNLGTILTYAVIGTVWNAATTGLSLYGVFLLGLMGDLKAGLLEFLLFGSLIAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFNSFVEVGAGNVQGLDYFKGIVSFFVVSLGGTAVGIIFAFILSLVTRFTKHVRVIEPGFVFVISYLSYLTADMLSLSAILAITFCGICCQKYVKANLCEQSITTVRYAMKMLASGAETIIFMFLGISAVNPTIWTWNTAFILLTLVFISVYRVIGVVIQTWILNHYRVVQLEIIDQVVMSYGGLRGAVAFALVVLLDSNYVGERRLFVSTTIIVVYFTVIFQGLTIKPLVKWLKVKRSQHKEPLLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWTNFDRKYLSKIMMRKSAQISRDKILSVFRELNLKDAISYVSEGERKGSLAFIRSSSDVNVDFTGPRHSVVDSSVSAVLRESTSEVCLDMHAVENRAKSPKDREEIVTHHMLQQHLYKPRKRYRLNYSRHKLARSEGEKQDKEIFQRTMKKRLENFKPTKLGTNYTTKFRNMKKERAAKKKHSDAVPNGRLATHSVSFHVNKDSEVEDPADGGISFLITPASNDADETGTGIDNPSFSNEEDQSIYQMIPPWISNEETVIPSQRARLQIPRSPTNFRRLTPLQLSNRSIDAFLLADISDEHPLSFLPESSM
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Plasma membrane Na(+)/H(+) antiporter. Exchanges intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry, playing a key role in salt and fluid absorption and pH homeostasis. Major apical Na(+)/H(+) exchanger in kidney and intestine playing an important role in renal and intestine Na(+) absorption and blood pressure regulation.
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M9MRD1
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MS300_DROME
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Muscle-specific protein 300 kDa (Nesprin-like protein Msp300)
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MADSGGPGSKHMDPTTIDAGGGGAGAAGGDDVPPVPAVRRRRAHEQKSSREQVLEEEKSQQLETSTVTRTYMKTITTSLTTSSSSNVEEFILGEHAAGAAAAPSPNQQRLRQKVAQYEKVWSDGSSPVKRPAEQSSDELRLTDDQDEYDAENPFEIDVHEIERRLRQERQRGLAEAEAAKLAFQQVQLRHTTPPRRVEVTSDQVASPFNVTLRTTSRMSPGAEHGNVEEHLAPFNVTLRTTRRTKKKEFKELENFLEGERTVREVPSADGVRTIITSSMTSDGGYAEEKIYRHGEGYVSPRDSPSWSRSSYSSERSSVTPPRSVDLTAGGRRILIKLEQESELTEENQTRDETDLSFGRQEVAMATGNIDITVGGSNPRRRLYQQTTVQVGGGNRTSPQDSTPQRPRDLDLAGTTKTMLTSTPIGTKEQPQTGPKTLVSPAATCQLRGSSTEEPRKIVSHKTITSTTTKSTSSSTSATSSSSTSRKLIETSPVVVGKIAQIRTGKSNASDNDIDIDNDSDTEGRPASSIVIVSTPTRPTTPATASVSASAVTPSASISATAAHALSGIGTFSKSLRQDYQTLATQSGRSNESPSDQEYQEFQSTMASINYARSNSQYDSHIKEKREEQERVQKKTFTNWINSYLLKRVPPLRIDDLINDLRDGTKLIALLEVLSGERLPVEKGRVLRRPHFLSNANTALQFLASKRIKLVNINPADLVDGRPPVVLGLIWTIILYFQIEENSRNLEYLGHGIGGSVSSLDSVGNQKHGDLKAEKWKQGARKTLLNWVTNALPKDSGVEVKDFGASWRDGVAFLALIDAIKANLVNLAELKKTSNRQRLETAFDVAESKLGIAKLLDAEDVDVPKPDEKSIMTYVAQFLHKYPEPKGASRDQSHVQQEADELRRFLVEKTTEYEPMVMMSSFPRDFGEYLLARSEVDAHLAAYNRLKQLIESQSGFLQVSRQSWEEINELWQRLQYQMMYWLWLLDSELPGDFGTVGKWLAEAEKLLMDNDIPNAMNEETAAVISRKLEEHKLFFADLPRILAMFDNAKRSPVAQQIPLEQLRNMERRLQEVGPKAAERRIRLKFLEHKCCLIAFLNLVENKMRGWTGKYGHEEKVAQQLEQYKNFVSRNKIFQEFQKAFVDMQQVVEEYKRDGNVPRKEINDIDRFMYETEERWKRVSMELKCCQNSLEEVVNCWRSWNQLAPTCEEWLQLAEQKVNQSEDERLDFFQDIPVWKDKFDALASSANYLIASCEEPIAQQLRQRHGALSERFERLFANTKQYMHAGDIIRSRQEYKSGIEQLSRWLRGAESVLDQRQVLGNSEQVKEYGQQLQQLASEIDDNEELFKTISRNFQSLIQDLSRDEVDKMMKLLKQEKESLVRIRAQLPAKLHLFHQLQIQQESLEAGQKEIHQWLSEAEQLLGTHNLSGGRDAINEQLHKHKTYFSRTVYYRSMLESKNKVFQNLLKAVSSDDKIDTAPASQQMQQLNERFNYVIQNAQQWEQRLDSAAGGWSNFKDNERVVSEWLTQAESMLVEKHIESKTTIETQKYFFEQVNDRWMNDLVQSAQQLLTTLPAQEQPAVVHSVEQLQSRWKNVLSQAPLHLLKLEFRLDENAFYQSLKDVEKELQLEQQALNRNEDVDSILQRNQQFLLQQDVVPRLERCLQNMQRLAQAHRQQQPGDISLDQAYDNAKSQWQLLSNKLGDMRQTLQQIPAQWQGYHLKFNDMVDWMNGVDQSLKNIVNEVNTMEEFEKEKVVFQKICQDADNKREDMKWLVKTLDSLLSYATEDEANLEQKKLEDLIARYKNLIPTIEITMVKTEVFSKCYTYRREVHEVVCLLSKVKDQTANIPAPDSLDRVNRLIEEQQYAINQLDHQRPHIMSMLQRGRDLIKDVHAPAFVNAEVKNLETGWNQAYTETSDKLQALKGTQAVWSEFVDQKNDIFSMLQTAETELRSLTPLQTDPKNVSQDLKSKRDLNVQLQQASHQLLPKLHALKSELAPLAAPDKRPILEKEVTEVEKMFFNTMEHVKDRVGYLEDYSAKWNNYKTRLAELQEWANKVAPKNIEALQSEDLTPEERVVKVQAFKRILGDRMKQLDLLAADASELAPKEGNIAEAKRLKGEITKLQEVLSAINRNVDHQAQAVQEDLVNWQQFQAGLQQIKPAVEQSEVKVNNVVSKPISLEEAVAMQQNAQQFETQCQEQLDKLHGISNISHKMLCKTNAPDELDAMHSRWTAVHENAKQASAKLEKLVANWKSFDADAAKLEDWVGQGEQQMSRRPAVLNTPHIDKLEKELVKLKSFNNEISQQQAKLVTLGQNADQISLHLAPEGAAALKDRVNQMKGKLQKLSEATRGHINEVSDAIISRQDFNAKLVNFSNWMEQLRNQVTQVEEINPERVETSLHVIHALLQEHADKKPSFNAIYDEVKQLALGATPEESNALNDAYTALVVNYQNLETNMLQKKAALEKWTELLGWKNDTESHLNYLKHQLDKPEGPAAEELSKVIDEIDNLGQGIGYWKGQAKEIDENPAIQLRDALSRRPLIATQIVNDVENKLENLKLRSQSQQQQIQQMTVRKDKFHALEHNFGQALQENRAKLDEILRQHPTLNNIDQIIADLVALNDALKYQADLKNRIHDEGSLLMREDIASMPAIQESLLIMDKNYDSLQNEIADRIQKYNLISQALREYADSKDKFSKELKKAEDLYNAIPQQPRDETELHQASEKTRKTMEQLRKSKLSLDELERRGNNVGKLFSAIGEPIPQEVPQEVTAAKQHWQDLHDKTAKNAHVYETEAVIWSQIEDAKKDLLPWLSETNQGLCDAADNSIEIEFGPMRLSKYRTELPSYQALKDSIVEKTNDLVKINKGAEIPALSALNKLLSEQFAEVNNNADRLSAITTSFNDQEQELRRRSKEAGERVSKLREQLIKCDDMSGDNNKIMERLQQCRALRGELDNSGNEIDNIKQKVDELRNLYPTFSESIIPKELNNVQKRYENVDLYAKKIESSLLQFLKKFHADKVGMLKRIIATQREKVAWCQPESSSDKYNLDVKKSSLQEVSKSIDDCKARHAETLKSLEMLKAVESPQNLAELTSDAELLRKDMQALQDSFDQIKGILDENVDLWSQYEQSNEQISNWLRDVEGRVKAETSSQVNLSEVPQKLQELSILQQDVLAHEPIINNLEQTSQQLIEKNPEARIGQFVTHLVQRYQAVSKALTSYIDKIRGAQLSNANFAKAAKDFNEWFGDAKIEFQELARMGSPGSSSATAQQLQTVKNYIKTFDNGQILLNNAVDIGEALYPVVSPDNRERIRADLRQMREKFDYLRDEANAFMQQVEGVLIQKTSIEESYTQVSHYLNESKAKVPTTDELYPTLATKKAALQNYKTQLQEITLHKNALKQLHDKAVTLCDDESERKTDESIQEYNTLSKKISDRITTVGNHVVKHEAYDQVLEKAQDWLNTIKSEAIDILNETTFEKEGAEEKLLVVENLLQHKPEGDSIFDTCHKLLETVLTQTHPSGHPALLKGFEEPKQSWEDFMTLCQDSLVKLKQLCSKWDEFDTIIEELDNWMKNVEAVVKNQNLKSTAEAKNAHLKQLQDISKDIERRGAAINELMDQGREIEGETDLNLKLSRLNTRYQTLKNLCKESIAKYVNYVKDHESFDKDFDSFKQNLQSSVDELAKTNEIVGDQSVLQDQQNKLREMSDKRILDSTLFEGLIDRGEKLYGHTSPEGREIIRQQLRALRTLWDNYTDDLNSATQKIDQCLLQFNEFSIAQDQLTKWLKDVDKAMQSHTEPKTTLQEKRAQLQNHKLLHQEITTHNVLVDNVCDKAQILVDQIKDNSLNVYLTSIKQLFQSIVQKSDEILHNLDDCVQKHNELNNALSSAKTWISNEKAKLLECDDAYGEKADIKRKIETLGQLAQNKPQAMKIISDIRDLFEKVKATTSEKGNEVLDKEIEELETTMKSHFDDIEGIEGKQKDVLAQWDKFEKALEELTKWCRSAEAVFREQQLQSTLHEKVEQLEKYKIQRELILQKEKEIDAFGDAAHALLNNCGADRLKTLTTQITNRYQLLQVLSKEVVNRWSNLVDDHQFYQDKYNEVDLWLQPIESQMAKVLLDEPTQSSNILQVLLSEKEQAESLFAALNAAGEKALPETSTQGREKIRKDLRDIRDRWDKLDEGIRNLEKRQEAQGVQLSSYQDILNQTVNWLDQVEKLIHNENPASWTSAQEIRSKLYKYKATNQDINSHKRIVEAVNEKAAALLGSAAPANADEISKAVAEVNKRYDQVGQDCAKLVADLDGAFDVYQQFSELQKAQQDYQKNLWDRLTGYSDYSGNKAALQARLQKINEIQDALPEGVAKLKSLEDHIEQQASNIPARSKEVMARDLANLHADFEKFGASLSDVKSGLENRLQQWNDYEINLDRLITWLGEAENSLKNYNLKSSFEEKEEQLNGFQSLAQNLRQNEADFDKVKDDTSELVQSSGETRIAVNVQQVSSRFQSIQATAKEILKKCEQAVQDHGHFNDKYKQCADWLANAQARYDDCCDLSTVASRDDLLKKQVVIQELLAQQPTATQLLNSTVELGEKCYGSTATEGREAIRSQLDDLTFDQLFDNIAITARKIQDKIAKWSGFDEIADSLKSWLDETENALPADIELKTTLDEKRNKLQTYRDILNDINNHQVELGNLQEIAANLPEKTELVDQIIKDISDRFGKLQKRAQNYVERYEGIVSAHQQYSKAVMDAQEFIDATLNTVHYWGDLDLEQISLHTNLDRLKNLKASLADEFPRVDQVRALGEKVIPGTVDVGQVNIKSQIDTTQQEWESLLTTISSTIEAIEARLQHWSEYEQLRDQCLAWIRDTDNNLHAIDLKEDLPKKRAQLDALKALQGDVRAKELEVDNVTEKAQTLLKGPSSNRASGPELVTKYQQIFHKVKELNNRWQQYVTSHEDFDNAISDCSSWINEIKEKLDYCSDMSSMSPKELDKKLATIQDVILLKDEGSARVLKILEQAQHVLANTAPGGHEAINKELTDLQDLWSGIALRIMDVKSNLDDSITQWSGFLDQVQNVRKFNEWLDGQVKELSEHQTTMTEKRAQLDRVKSTEEKVRVEKIDVDALKIQAKEMIASGQQSQAAFQAQKVLDTFDELFAKTQKLLSHRQDQYRDHRLFKEAYDDLVSWIGRAREKFPSLKQSSLSDKLAIENAVQATEALLNKQAQGELLVEHLVHTGEVVLASTSAQGQEIIRNDIRALRDSFEGLFREINQQKENLEVTMVQWRAYKEEYERLMEWLQQIDILVKNHKLNLCPNLPEKEKQVADMKEVMSRLEKGKDDIDKFNASAASLLKSHLDTYVNNQLRHLSSVYQVQVNLAKDVLKKVETNRDQHREYDANMKSAKDWIANAKATIQSAGEGAGSKEALQRRLEQIQDLIRNRELGQNLVHTAINNGEKIIRNTRSDGRDAINTEMKELQTEWDRLVKKMSTAKVQLETNLLQWADYSSSYSQLQQWITDREAKLQQACEQKIVKSKRGQPGLSSGLSERKANLRQTNNIVQDIVSFEPMIQSVTSKASVLQQGAPGTEISDKYENLTKQAKDLYEKQKNTIESYQSLIDAGNEFATWLRNAKERLSKCSEPTGDKQALAEKTHQLKILQGELPEGAQKLKNALEQGEIACRSAEPEDCEIIEQEVALLQEEFDAYREALNKAKDYLEVGIVKWSDYQDQYTEALEWLSKTEALVQSYNKLQDSLIQKKVVLEQFQGHLQTLFDWQKTLDDLNMKAQVLLETCSDTRISNAIMQLTTKYNALLTLAKEVMRRLEMHYQEHQQHHSLYEECQSWIEKTREKLSECEQIPGTLNEVQIKLNTVKNLRQGFETGQNKLRYLLELKEKVIMNTEQNGAAKIQEDTEALKQDFDKLLVDLNDVRQKLANRLAQLEEIFKLYKILIEWLEDVEPSVKTSDEFLNDLSEKRAALEKFRVIQRDINGHNDIVEKINQRLKEDNSLDLKDFQPGLTKFDDLQTQVNKIIESLENQVNSHEKYKQAYNELQDWLRRTRIEVEQCADCHGEKDQVESRLNRLGDIQSSSLEGKALLEACEELSQAVIATSGSEGQDNVAQEIKHLTSEWETLQTISRDARSSLESCLAAWQTFLQKFNKINLWIETMNKRVTKSQEGENKTPEDLVNAKKLLEEVLAEKDNVEDLNDNCELLMEQSACTRIRDQTIETQANYTKLLTSAQGLVAKIEKNLSDHTEFLNYKKEMDAWIEKAQQVLDDCSTDGDAAIIAQKLDTVNSLASRLPEGQHLLALVQDAYSKASNITPEDKQEKLRELMTKVREDWDALGLAVKQKLSDLKQAQNRWNDFAANKDKLEKWLNETETTLKVAPETKGELSEMKTLLERYKTLSNELKLKGNELEQLQSEARDLGTEVDAVNRLQSRCDKLKNDCSAHITALEQEMFDYNAYHQSLQDVEKWLLQISFQLMAHNSLFISNREQTQEQIKQHEALLVEIQKYQTNLDDLNAKGQAQIKRYESSTPAIRPTVESQLKNIQDSYNSLLQTSVQIKNRLLESLAKFQEYEDTLDSIMRNLETYEPIIQTELDAPATSLELAQNQLRCAQEMQNKLNNEKSRLAAAVQACEAATASISRPSSPLETAMQAIPERELIVRAKLEDLLDQKPPPKTRSSTGGVSTDDDKDEADVEIQVELSDVNEALLDPIAHERVKNYRRIVRLNSAHVGKLNELVAKVQSHLGGLTASVSELEQQQKQRAELQDWVKKQQSSVSDWMMRPCKLRPEAAQQELVSMNDLLNSIGDKRSQLMLEMTGSLGDEDTDLDDNIDKLESELMDAIAKKQAGQNVIDGYRQGMADVQNWFDTLIKRMDVLDRGSGLNCAQKMAAINEIKNEYELQGHPKIQELKGKAAQVAEVISNLDGQQVEEQMKSLDRRFADLGKRIDRKSQLLDVTNKGVEGAKGEIDQLQNWVKQQIEELQAPKPLGYTPKDAEARQQKIKSLMKDAEAKQSLADVLEKRVANMQQELEPVEYSQLESALRNLNTENRNLSGVLKAELDRALEASKARKSLENDLDKARQWLKTKISEVRKLPVYHPLTSAEIEKKIQENRKYDDDAKQFNDSVLTDVQRQAANIMKDCDDADKAALQQILDEIAADYQTLKDESSKRGKSLDDLLQGRKAFEDSMKNMGDWLNEMETATEGELRTTSLPVLEEQLAHYKKLLSDAENKGGLINDVSEQGKSILPTLSNADKLKLNDDIKNMKDRYGRIKNTIDDRVNALGDHIKKYKDAKSRLAECSQFLGNIQQKLRELNRPIGSRIEDVQDLLGAYEGILKELKDSKSKMGDMQMDDLPELQSILAQQDDMIKLIEDQLAHLRQLLLLREQFIALINEIIAFIMKYTDVIIDIENSPDSLEDKINKYDDVIVKIQECEGVLASANDKGQKIASEGNAADKNSITEQLQSLKNQLQNLRKAVESQRQKHQLQLESHKKMAAELSEILDWLHSHEGAAKSRPLLDRDPESVERELQKHQSLSQDIESYLNKFNKINDGVKTEIGMPSSLLEMLSEGRSLVASLPHELEEREKYLKNNRDSRLEYMQLVAKFNDWVHEAELRLQNSQHGIDYEHLVQDLDEHKIFFGNEAPIRNLVHKQIQEAADKIWSSLNNYEQSELSAELAQFQTKLTNTLANAKTQQSELEKEAERWREYQQSIDRVKATIERTKFVDEPVQNLAGLHFNIQKLSHAIGNVQSQNSDLTLVNQQAQSLIRQADARNRQLIEQDNAGLNRSWQDLVRSLEQRRDNLQQLAEHWDGFENSLHAWEKALGRLEDKFRNVDPTVRSRRHLEDTKNAIQELREESNQLKSSHKEIEALSKSILTFLGEVHKPSAEAIQAKVDKLVEQQAKLNDTLRDKEQQVSKDLEEIEQVFRRISQLQDKLNALHEQLQSVHVYDEHIAQTEQLLITLNSQVQQAAEESKLLVAQTTAHYQAKQNQLPSDIAQEFTALELLAERVQVTMETKEKDFKRAKTVRTEYVDGVDEVQRWLLQAEVQVQERSLTPTQMKELLQRINHEITAIYERFTLVKTNGQLIIENCRNSEEKTLVQTTIDQLAASLAQVRGWLDEKKQAVGDSLDAWTRFMNLYQIVMSWASEKRNFIDQTIELRTLPEARNKLNDYVTSVKSIKPIVKHLSEMDKELEHIGQVTTVGDLKDKLQEAEDAKISVEAVLLERNSLLQEACEEWDQCERKIKDIRSWHEKTKQGLDSSQQQKKPLRDQLGFCEKTLADINVQKTKLRLSIEKLEVHFRNGMGGDPRLSENVDDLVRVLDGLGELVKAKSQSLEQTLAQIDVYQQQMQSLRQRIIQEEQQLRLVMAPTYLPHDRERALAEQQDLITQELDELLQSLSSVEDGIANMNQSSLDGMLHGLKLIQSNLEVHERDAIELKNQAKKLPTDPATERLLNDTVDRIDLLLRRTQQGITMIANAMHGQKKRQQEIDEYQQHLLELEQWIIEVSAELASFEPTSDSSTDEQVLKSQVERSQQLLRTLKDRQQSMEDLVEQTRQLQSHPDVSPLADTLMEQLQSIITILREQVTVATKRIFTIEKRIVDLRKAKSEEAQRQRVLADSLIKPPTEAPASPEAHESIESNENTIDSSSMPEEEIKPTGVYVETQTSLSLQQPPVQVVTTTTVEAQTSFKEPAVETAEVALQTQKERSPTENIMVTQTVHHGQETIQIDTTRNKDVPDEPEDVQIEARYHQRPKGDVDRATELILKNVPQAFETTFVEPDETTTEVIVGPDGTKHIVLKKVTRTRQQVVQQQQISSIETISDSDGNIEVHSTGQINLENVHTTDTKADPEEGSVHTVITQQTRGAVVDSTQPEGVILQEFETEPTIETYEEVIAPGSQAQLIPMQPGDVQTQGTIRAVVQQVTRKVIRKTRKIIKRVVIIDGKEHITEEVVEEPEEVEITEEETAPHINVNIVRTVDGKVVSEEEFQRMMQEPGVLIEEVATDLQKPTAEPQQEVFDIESTQVTTTTRTTTATTQEQEQPEQQTQPTTTETTKEAPVELPAPQVDVEQPVVVATTSPVHVPTADVVEPKDSSPTSTTAAVVDVEAVVEDINEIWPLEHHLKPTNIDFSQHVEELAAPAAVTAETEASMPVEEIWPTSPETGNSLTLEQYEFEPQSPHEESTKSDLVKPQETEPQVVAETKPEGITTGSITITKTTTTITSSTEVPEETLVQNVPADEQQPPANKIKTDIQSFLEAEQTLAAALKEQSSTPTGASVAEDVQTQPEEIVLEERTVEISTIKTEENQQEPVIVEEVKSLPVEPEPVEPELEEVAIAIVEQTEEKPEEPVIEKQPASGPIDLRAATQLFISGEAAASTAPQKTFQISAPSLEDNGAGVLKVVLGKESTNEEDTAAPTTGKVSMTIIETAAAPAADAKRRRKKKKRRDTKHEEELEQEQETEPEPVAAVKEPEVSSDVPVSPEDSPRDTVRHESIVEISPDSDLSSIEIDTKVKIVEDAVVSSPSESPRTPMVELVIPTEVVELALVEDEEQQTTPRIPSPTEKSEVEQDIKSVQTSPQHQPKLDETAVQTSLEVQPDNQENESQTLIVEITETEAQTTPRSEEQSVAVEISTTEIQTDVSGQPAETVEISSQTTVTTTIEKELQTTPKDSPRAPEAGSSDVVESLVQDLVKDMTTDLPVRTSEQSTVTETTTTTETHVQTTTPEPREQTEVIKPETAHEETSTVELVQFADGEMQTTPPGDQQPASLDDSSLTATSISVSEPYELEVKTTVAIPADSDTSVAEPTVYEYTQTMQLPKQEKKSKKDKKKKQKNVPEVEQQLPEDQQISVTVEIAPELLSESGIVVSTNQQIEDVPHVTPVVDTPIESEEVETPKAQRVQLQITKTTVYDEYPDLPVHITEQNKVLIASQQSKRSGAGPTSSAVTIEEVGSPTEELVVPITPGPDNLSGEPHNIWFSATTSVDKTPIELSQALIMSESLQHYPGQQKLTQEPILISTKEAIGDRIKQLKQASPQQATPLSNVLHLATLSEQIKELPTEQRILEVNEGLKDLDVAIKNGDKTVIQTTVITVIEKVSTWLETIEYRVYLIRQNSNEGPSEEKLDNYNQLNDELSTIKQNVVQLERQLSKAEPEPQLLQCVDSLKEHVDAVEQVTQQNQVQDSNDLDKWHNFEVLLYNVSSVLADLQQSYDLLINQEYPLSAKLAQLDELEQQHEAAQQQLAHLCQNARAFQRDFPGKKMPQDVHNAFETSKNIANNIQAERERVLQLQSLAEEYEQTLKEFTKITVLADKLVESPIVSSSLEQLNNEVQKQRKFFVNLSHCRAMLESLEENIDSETREKHSELHKELYNRATSLLDKASERSSKLVQAASRWTVLEKGMRDELQWLQVAQQRVPDLSAVTSADYDQYTTLYQSLSNDISHHYVKMTQLSGIANKLQLLVQAPNLVEETNEALIVLLKLREEVALYLHRLLVFKEIWVQYEQQTDKLEAFVREAEQELRNIQIPSQPTHQPIEHMRQFWEIKARFELHNNVRTDTGLSFEKSLQVIPLADEMLQRQFHAQLEDRWQAVAQAIELIQHNIVECLSSEDVPADEKLKMVERELQEIYLTMTSMKGVIKNEEELCLYIERVQVLRTRVGFIGNELGRIGLQEPAIEPEKVGELFSLSHKISTQIAEELEGASVLRDQLQAIQEGISNQRKHQAKISVILDECEAAERQGADVLEKAVADCQAAGEELVISWQEIMRIRQMLHTLPMRLKMSVSPVKLERDISQLQDDHAFLESKCTNIMAILRSRLAVWLRYERQLELVHGSVQETDFMMELIRVHGQVDYERLRKATERLEGLAGDLHNREQLIDELKGAAKPLIESCDVQIVEQIESAVQEAVVAWNDTSENLQQLRTRYQRAVELWDKYRNASAAVKNSIDQQMDAVKSLEQPLDALQHAKVCQDNLTTQNDRILELRDIVAKIAADVGLDASALMQGELDALGQRLAECKDAITTLANVAETQDKERKELDKEVTLAKAYFNNVQQDISREAPQNPKESEEQLAALRAHLQTLARTEEQLRQLKERHQNSEVAPSVASSDDDGILEVLALWQKIFQDTFQEYHRLSTRLARSQNSSEALRLWRQYLQHVQSFLSCAIPEDYSSLREQQQLCAIHQNLLISQQSVLSETPLESELSEQYKALTNLHNETLSRIMQRNGELERRVSGWNAYRQQLAALLDWLRQREAERNALQLRYIHLKRVPHLKHRLDAMIQQLDQGEQQSKALQEQQQELARHCDDALATAMRMEQASIGQRISNLRAALKTWQGFLQRVTQLSESYEQRVNQLQQEFGAAQKLLDANSESLPTQPAAIEQLLGSLRAQRVQLGAQVSALESLTVTQEELKECISPHDMKTIRQRNWLLWQQHADLDYQLANLINSIEERLSLLSNYQIRYDRISQWLQRLEQRVEKDADVTAMTNPEQAAKQLEQQVNSELQLRDKEREWLLSTSRELLTLYSEPEVRSQVQQQSDSLIDRWQRLKYLAKQKATKIGELKMTLLRLEERIALIRAWLFEVESQLDKPLNFESYTPNVIEAKLKEHEQIQRSIEHHSSNVGEVLNLVEMLLNDADSWRTQVNTSGLAASAQNLEQRWKNVCSQSAERKARILTIWNLLQQLIKLTAEHKNWLGKQESQIAGFERDQKSHSKHKLEERQMELRAKLEELESQSVNLRQLEQIYAKLAMSAGVEPENIQKLTLPTKVMVSMWRQLTPRCHALLDAIDKDAKLMREFNNAQLEATNSLNAIQKALEQLPSAENQQTSKAEPKAVLQRLESLEKKLQDAQQHVQQADNLAQEAKTRTKQQPQLKQLLELVSAYTTLWQTVQTRIVTLKTTWLTRAAQAAASLPVSEAANAAVQVNTLSQRKLRQAQQMQRETSITAKDAYIMELQTAITECQNNLDELQRTVVDKTRKPGPQKIAKLLGNAQSSTELVKHLSHLLLTECKADDQAAEVDTVAELTLRFDTLQSQWKARQQHDQNASEVGRLTCPLCTQRNWQQIDNDLWRLEQWLQFAESTQKAQSAPPSNIELLEDVTQDHREFLLDLESHKSIISSLNVVGDHLATHTLDTEKARQLRSRLEADNERWNNVCINATKWQGLLQTALMGNSEFHQTIGELVEWLQRTEQNIKASEPVDLTEERSVLETKFKKFKDLRAELERCEPRVVSLQDAADQLLRSVEGSEQQSQHTYERTLSRLTDLRLRLQSLRRLSGIYIVKLGAVLGYEGDNLGVPLHMLSSELLDNTTLSTSSMQAAAPNTENANNTDGGDAVDGDVINTTVLARGARFLGRVARASLPIQALMLLLLGVATLVPHGEDYTCMFSNTFARSLEPMLSYPHGPPPT
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Component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (By similarity). Collaborates with Klar to promote even spacing of the myonuclei at the periphery of striated muscle fibers by mediating a tight association between a nuclear ring structure of Msp300 and the plus ends of a unique astral MT network. In addition, is essential for anchoring nuclei, mitochondria and endoplasmic reticulum (ER) structures to the Z-disks.
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M9MRI4
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TRIM9_DROME
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E3 ubiquitin-protein ligase TRIM9 (EC 2.3.2.27) (Anomalies in sensory axon patterning protein) (asap) (RING-type E3 ubiquitin transferase TRIM9) (Tripartite motif containing protein 9)
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MEDELRCPTCKQLYANPVLLPCFHALCLGCALDIQTPYSPGSALPGAVNGAGAASAAGHNGLHGNGGGAGGGAAAPVTNPNGPGTRHSSHSSAASTASSNTGSESVTSDQDQSDKVSIFSEADSGVVCCSNTSRPVSYAGTGLLPGVGNVVAPPGAAYCLTCPLCRKLVFFDDGGVRNLPTYRAMEAIVDRFCAREALRCQMCETDPKVASLICEQCEIRYCDACRELTHPARGPLAKHTLVKPRGAAQQRESVCGEHEETLSQYCLSCKAPACGLCIGELRHQAHDVQSINVTCKAQKTELSHNLQQLSEKARSTTEFIQRLKGMSDKVTESCMEFERLVHAQCEALIQAIHDRREYLLEAIRMDKDTKIRILKDQQSNCTGKLQQTTGLIQFCIEALKETDSAAFLQVGSMLINRVTNTDMTWHQEVTNAAPRVSPIVDLTLDDAALARAIDNLNFIQMRAVKDGDERCPAAPMTPTILPSDCSAENNSVTVAWQPPNHSFVEGYVLELDDGSGGEFREVYCGKETICTVDGLHFNSMYNARVKAFNSAGEGEYSELIGLQTAEVAWFTFDPVLSGGAGSGLIFSKNNATVSVEGWEHRVALGSVGFSRGVHYWEFTIDNYTADTDPAFGVARIDVARNKMLGKDEKSFAMYIDRQRSWFQHNSIHERRVEGGITTGSTIGVLLDLERHTLSFLVNEMPQGSVAFRDLYGVFYPAVSINRGVTLTMHTAMDAPKMDYF
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E3 ubiquitin-protein ligase activity (By similarity). During embryonic and larval development, regulates the pattern of axonal projections of class IV nociceptive sensory neurons (C4da) downstream of netrin receptor fra. Regulates fine-scale topography of C4da axon terminals upon neuronal activity. During eye development, consolidates the attachment of R8 photoreceptor growth cones to the target medulla layer, probably downstream of fra.
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M9NDE3
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BARK_DROME
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Protein bark beetle (Protein anakonda)
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MKLQHHKTNRQRISKPHRDPKWASICLWLLVTLAFSTHLARSQESRQTEDSKEVELLQDNDIEFASLDGASQLLPATRHSGADVTVAPQGSTPSMTSSSSYTELQGGEILSDRILRRSESPYLARDDIEVLRGARLTIEPGVTIEFAPTKGLKINGVLQAVGTPTSRIVLKSQSNTANYKLELPDDQEKGIRLVDGPTPVEGRLQLFHKGAWRSVCSNSRNWTLADYGVACKQLGYRGGRFWNWVERTPGYYPRLLYEQPKCKGGEGSLQDCAWTSRQMGAGACDYHNDLGIQCLPVHSETLGHWRGIYFDNAPSTKALGRDNIVYAAQSESRLKYVDIIRAGSGAGFNAKSAVEVQGLPPQMEHVVISHSAYTGFNSTRPWAGFQLQNVTVRKCNGIGVFVNSSQGAVQLDGCSIVDNAGDGIKYVGHDLRGTERKDRASIYDFCTLPTTSGQTYPISLSFTQKYYAGSGKECGKYFFTRPGYLLTLHFENFVLMQNETATVEIYDGASTNDRLLFEWKARNFTRPQSVTSTREKMFVRIRADARQELNGFFRMTSGDSVAYDLKVSQSTVEDNGGRGVAIDNIRSKLHVHSSSVSGNGHVAGVHVTSGAGDVNITSSNISFNNGAGVNITYYGGNRNISRSALTANKGYGVATWLNQTSDVNRMEYIPFNQTSVVEYSQIGGNLETGVFHGNFCRPIWVNITGNSFNGSQQNDIFIESCYQATANGRPNMQLQLGHNQFKYSQANSIYLSPALNLQGRIEYNMFRFGSYGCLFINNDYIYPEFNYFPVKLIIQSNYFMRNSGVHVVSLGLSPYSRAEVQYILFTRNFVRGNNITEAFGPLIAGSEGSDGAGRLNPRSRVAAPVVVGSSNVDIFRNILHNLDSMYEIGSQLTDQSKIINATCNWLGHTDENKIYARLFHRNDRYNLAKINYLPYLLHSSNPGSTAMITVSTVVPRFFHEGSDVIGGEVDGQDMVPAGTYTVTKDINIRPGGKLILQPGTTLKFEPSVGMMVAGKLEARGRRPDDILFTLKRETIMGESNDTETIDLDSETEAIDMETEVIPADGVPRVPVRLVGGAGANEGRLQVYLKGRWGTVCDYGWNVLNAALVCHQLGYSLNPQDWRLLRSQLPNAGTSEDILMANVRCTLQDRDVTKCRAEYEFENTCSHENDVGLRCYEGAWAGVRFSMLAERADLQYVTVEKAGLFDYTTNAFKPAVQMDHARHNLENVRIVNNLQDGLGIIYADIYAGKSVNNIKNSEFSGNKGSGISLKQLDFRVSGSIIKDNKGSGVSHDAVISALDQKEIGGWFNMATDFNSFDTDYDPYLLPREISNIDLGTFEHKYIRTEELLGQNINRKIVVQCPAGYVIGIQLLNPIHNLSTESINILNARTENIRSDLWQVKRDLNVFPVTSSSYGIIIYYESGLQALGGAVLMLSTVTAPVQNIRNRIVSGAVPTLTIRSTKIQKNLRGITGIYYNRYIGDNGEYYLRKANESIKLINSELSYNEREAILIRSPFWDVISSNLSEVTLHVNGSLITQNGLGIRQMSKDLRSSNNLFHYVIQDTTFEQNTHGGFQVSLPYVWQYNENFTHSIYFGNSTWQRNRDFRISVSGHYTVFNITSNVFRENNCPGALISLDGMEKRLRFDNNRFESNNAKFVLLFKADSLSEIIGQVPASIEFNSFKGNNIVTMTANYRNHYMKVARRIRKQHKIPTAVIRLDGVQNVRLYRNLIAENEMDYNLVAGVRSARLNNYFEARENWWGTKDTAFIEAKIFDFDNWNDHADVIYQPFLIEDSYDASVSVVVPFNQDQEIDLTNYKGGRVYKDLLLTKQSTPYYISSDITVMPGKTLTINHGVTMEFEPNVGILVLGTLVAIGYRESPIVMRPFRNATRESLIDVQPKKRALEDMSAPLTEFDSIRLCTSANNCTGDADGLFGLNEGFLEYFNHTTLQWVPICDSRFTERNAQVVCRELGYDPLNVYYGHDRRIEFHTNSLTRIWSWVQPLECRGDEERMEDCAERLNGQLYGHRHECRWDDVFVFVSCNGIADDEVYWGGIRFANSKFEEIQYEHRLHNTRSHARLPLRESQLEFVRIEQAGILHNHKAAAIQAIHKNPSITSVSIENSANHGINMIAPSGKLNLNHLNINNTLGTGISIVSLSGEGRDSDESSFTPLKKLDLPYKLFSLVDICDPQKVLTIEERMLIYYKYDNNPVNCVKIFTSAFRAKPIGFRLLQSNLFNHSKLYGRTDFIKLYDGDIYNVTATYLGKIESDTDNQRSFFKTKGPTMSLQLVASGAPETHGFIAEVVTVPISTLGQYRDALHNITDTHISGAIKGAVTYSSAGEVTPTLTLIGNRIEKNCRQLYGNFSTCTSALNLDVQNMNSLYFMNNLITENQGGLRIRADSRGSATSLRGFVHHNLFMRNRNRPALYVEGRQSSPYQEVELYRNYFAQNMAGYEDVIRLCQVVSNFSYNYVHSNVGGRIMEVSGFEKVRLQIYQTTAHNGFYRNFATNWMTRATIVAGTAGQQYVDNIFENHENDYELLTVNNSILSFDYENRTFETWSSKIDARHNYWSYNNTISVQSRIRDKSDDPMLLEVLAVPFQMNNETILDGKCPPGWALVHDTCFIYVGAPMTFHEARDFCRSENSTMPFIRTDKTTLWKYLQSQMRHLKYPDKVWIQDYNHIDRCTSFVFGEIEIEDCNKERGFICESDPRVIIDPLSWRADIFAISIISAFVLAIILLILVAFCWFAKSKHRHTQRLQRRNSIRQSLRSLNSIDPQGSLRRRPNYNMSSNGTLSKGQDYKQMVANGSIDSMDKSVLSSEAGSFEGYEQKPHYNEYVNQNALRPAHPAQDHQSHKVATISKASGHRARAAAAAAAALEPDAFELSYRNEGFRDNSTYGDNTRANSISTSVAEDTPIIHHTDQEIDEGGSDYYGNASTLPLRTEGGTPAGRRGQPGLAFLSELKQNLPEYQRSSHSSFMPHRSSGDSLPFDQKLDQFNYSTESSLYRPAPAVPSSQQATPADMRRPDSYYTAVRSSKAPVSHYRTPRPLAQPPAAPNVAPAGGPAQRRPKTVYQTASEESSPTTPSPLTNQYHRSKSEALLETDFDGDGGSVGLQPLQTNGRSHSQPLETAM
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Required for the maturation but not the establishment of septate junctions in developing epithelial cells and is involved in epithelial cell adhesion during septate junction maturation. Plays a role in the proper localization of the septate junction core components pck/mega, kune, Nrx-IV and Nrg during late embryogenesis. Involved in the formation of tricellular junctions which mediate cell contact where three epithelial cells meet but not of bicellular junctions. Required for the accumulation of Gli at tricellular junctions.
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M9NEY8
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TET_DROME
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Methylcytosine dioxygenase TET (EC 1.14.11.80) (DNA 6mA demethylase) (DNA N6-methyl adenine demethylase) (EC 1.14.11.51)
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MASSILAQSSTGATVDSSNLGATAAAATSVEATVSSLHNTHLNQLSSLSQHYTTPYHHPHSHSHPHHHYQQHYPQQQHLQQQQQQQHHAQQQHQQQQQQQQQQQQQHWDYYARQQQQHQQQQQQQQQPAAATGNTNGNSSNNGNNGNNGNNSNPDGSNTTVPAPLGSSNNSSSNHANAASGGNSGQRHGDANANAISAASAAVGNPGNQQPNNSAGNANSNSNSNSNSNGSYTRPWEMESKDNGPQPPQTQPHLQLKSGFEPFSKLPSFQSQFHGFNEQLLPDGTPMPVPIGAGVPPGSAAAVAAATGSIPPGSVGPNSVAGPVGPTAMSSLQTVAMSPASISVSSPGMMSVGSPLTQLSSLQTSITPPSAGSFPAPPPPNAFAHHHALNPHHHHRGASGYPTPYAELPLYPGFTPLSVKKEPISGGSDFEMLLKKEDFDLSNSGGAGLIHHPLQHGQPHPIPMGMHTPTSYDGNNSNNSYPQAAGGGSGSHTPHTTTTQPTPTTTTPVKVEKLLQSPIARLEARKKERRKQRPNSLESSAESEASGMDVDPSNPGQVDAVSSTANFKSPLSALGMGDSNDANASGCDKQSKKKRKRCGECVGCQRKDNCGECAPCRNDKSHQICKQRRCEKLTEKKIVFGADGQPVRPDSKRGRGKGKSSGSGNGTVNATGIAAGNGTPTTGQSRARKNSTKANKLNAAAASATSPRLSPVPAATLLPQQSPNTTSATGNLQQQQQQQQQQYQQHQQLLSQQQLLSQQQQQYQQPQQQQQHFQQQQQQHLQQQHAQQQHLPQQQHQITAQIQTMKDQPQQPMAPMAFYPTWQADPSQGWQNQFIQQIPQNTPAITSLNSLDFQTQSYAYPSNGYVQSGLGFDPNYGRSPYAAPVQRYDFQSQQLSTAPSAINQVGLQSVAGFAPSYAGQVSAAPVPPSQQQQQQQQQQQQQHLGADLNKTMSGNDTPGYPRVSSVPPRSLNCNGYSGDYSGSPATNSNSNNNSSSNTSNTNNSNASNNNATTVVSGGTTTPAPPPTVVAQPASSPMQPPNQAVPQSPTRSNMLQQQQQQHQSPTGNGLQPYVAPQQQQQQQQQQHLSSPPMQDWNWQQQQQQQQSLGGEGYAQGERLHLNTRIKSMIMRKSDPKDPPPDLQQQPQQVQQQQQTGHFLSYSHHLRPEAALSANGPSSATPTHPLPNLQQQQQQVQQVQQVQQQQQQQQAVGGQVAAEPIGGGGDHIWKPHHANSFKKPSVVSGYPASQDAQLQLQLQQHQPGQHTTINHSVDPPVVPPQQHPPVAAAQPKKSRSRSKASRAAAAAAAAAEAAAEIDRDRNSTDPGGGGLKPLSAHYPPHPHAAGGPPPGQDYHSQYIKTEPGLLGPPQPNKMEGYERNYQNFIQYADFCQNDGQGQPVQQHHGHGQQDYAGYHHNSAYYGAGASSFQQNFQQNFVPGYQHSTYGARGKPPANQPHQIHGHGQSLMELDRKPDTNSIIPLPTNYEKDIPAYPIPPHRYALGHGAPPHLSHHGMLEPKIEDMGMLGHGGGYAYLGSEGKPLNNGFSCCRQGGTRPPTAEHLKDGTCLGLGIQPKEELIDEDELIDTHGNGLKPIGGVGKAKGKQKPDEIPEIVVKHEKINPMFDTTDRLEKGNKTEIPECECFQSDKNPPEPGTYYTHLGTASSLMDLRREFEERCNLTGRQLRIEKIVYTGKEGKTSQGCPVAKWVIRRADLEEKILVVVKKRPGHRCIAAYIVVCMVAWDGMPRLEADNAYKNLIPKLNKYGLPTTRRCATNENRTCACQGLDPESSGASYSFGCSWSMYYNGCKYARSKTVRKFRLSVKSEEAAIEDHMNLIATLLAPVFKQVCPRSYDNQTKYEHEASDCRLGLEPGKPFSGVTACLDFCAHSHRDLHNMQDGCTVHVALLKPGNRDTRLPDDEQFHVLPLYTMDGTDEFESVEGQRDKHRTGAVQMLDKFPCEVRVRSTPLIPCRRHGKKRKDGDEAAPPDGDQDAVGDANSQSSSSNGAQSQTQANNQQSSPPALGTAHIKKENGNGVNANGASSKSKGKGKSNQSNNSSASTPGSAPPSTPSPRCQTPVTNNPSPAGSAFSTPPVHGSNANPQSNGGQGTGNQPGQLMSSNSSLMNMATMIDTFTDAQLQSNQISSTVLDSPYSYDYQTASYIDSRNYYGQWPTPHAPMGMQAQVGGLGGGGPGGTVAGVPPLTPSTPTAQPQLGVPPATSIAGGTTTGAPTGALPATAPPTATPTQLETSNGYGPGNYQTLVSNPASNLTNPGGVTTEVQQQHQQAQQQSALTGGVGPGGLPVVGGAPGDLKGRLVSEENPDSTTLVNHHHHHHNLTESKLTALTAMQPMTNLAPLTTSHHPQEGFVKPKPPPSDYTAQYTAQYPNNYQMYPPPPPPPHSAYSAYDAYQNMNYNYGYHQAYSPYGMYPQQTPPPTPPPPSPNWNMYGHHQTGSVNSGYGSANPAAGAGSLISSHGSVASAGVGLQKAMVPVPGPLHHQQQQVLQQQQQQQQQQQQQQQQQQQQQQQQVQQLQQEAPQTILPDLSNGQTNSDTVATPTPTGDSSSNDAGPGNPGAGNQAPASGAGAATTAPPIASPGSTNSTKIEPIGEVAEINENIEAFQDPQMGGVAIALNHGSVLIECAKHEMHATTAVRRPDRHHPTRMTLIFYQHRNLNRCRHGIDEWEEKMRVKKINTDLDNKAKEERERLIKKAAGEDMDELDEDALMQDEPVPIKKESSANGQQLKNGASGSKKKKSSDSKKSQANEQSKNEKVALHAPTLTTTSWTTLFPTHPCVVSGKYPEGNSSPTSSTNNAPNGGGCPAQQQQHLPPPPGSGLIHPPPGTPTGTAAPPPLPTPHQQLPQQQQT
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Dioxygenase that specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA. N(6)-methyladenosine (m6A) DNA is present at a relatively high level at the very earliest embryonic stages but at low levels at the late embryonic stages and may act as a regulator of gene expression. Promotes differentiation of early germ cells in ovary. Contributes to neuronal morphology, development, and function in the brain. By interacting with histone modifier wds, binds to a specific set of genes, modulates intragenic (N(6)-methyladenosine) DNA levels and thereby maintains transcriptional activation. Also able to catalyze the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC).
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M9PBE2
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HAKAI_DROME
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E3 ubiquitin-protein ligase Hakai (EC 2.3.2.27)
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MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIASRPVLSRLPLTGGVGNIGSIGSIPPPGSAAAAQNAIHGGHSTLTLANLTRINNANAQECHQGKASLHHTLKKGTPHQSESVADASYYSSVLASFGSAAGNPGSGPPGGGATAAAQPANPSGSHSAVGPGALIGGSTDAPTGGSSGNWQQSQYYR
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E3 ubiquitin-protein ligase required during early development. E3 ubiquitin-protein ligases mediate ubiquitination of target proteins. Required for epithelial integrity and midgut morphogenesis. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Its function in the WMM complex is unknown.
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M9PE65
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AXO_DROME
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Axotactin
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MAFPYIWALLPLICSASGLSLPNMTSTDAVVAGGGILPILVAGNPGNLGSSNMSLSGGGGLAGSSTGGQSLPDTGGGNSAGGSPAGGSSGTGGGGSNSGISGNNSAMIQGQKSNQYEKCAGPGDPGPCKQYIYKWRYEPTTNECTNFIWGGCEGNPQNRFGTEAECLFHCIGGPHTLPPFLQSTTREPSTTESSMLLGLPYTQSPAQSPDGMGGAEGGDGTTPVPIEQRGPELTFAETGQGKTFIFAKNNTFIQMDGDIIQTFQLRLCREISFQFRTRLPHGLLVYHNVKNPDRINLDPYALYVIVEKGQLKVVHVFGKHSTSVTVGESLNRDEWHSVMVRIDVHGARLIARVDNSQEEVYLKGLNHEYNYGVSTNLPSVVLVGGLSSEEKLHGVKYITESFVGCIRNVVLSSGKAASDLLPIAPLVATKHENVNEGCSDMCESRHNLCFVGSRCINHYGGISCDCFGTHYEGEHCDIYTATIITLRGASYVSYRIYDWKDRVHSSTRRISLMFRTNFDDSALFYASGESLKHQYIAASIKNQSVHVEMDFGDNVMSTVLTDDLTRGYWHNLTILHEQRTVSIILDQQQKVLELPATASGNMLFDPEIYFGGGPELHKKKGLASHNNFVGSLKYVYYNDISILYELQRGNPKVHYHGVLEAEFVENEVNVIPITYPFATSHIWWPINHAEEFNIKFDFRSSRPGAVLAYSDVTTSAGNGFWEIRLTSDKLSFDLVPDVNNNVTHSTTIKINRATSWHSVELDYKLGEIRFTVDYRHTLSQMYGLTFNIGDKLIIGSSLKSAAMGLVGCIRDIEINGHLIEPRHVVKTERVVGEVALDNCNYIDPCKRPNTCEHGGKCFVKDDRVTCDCKHTGYIGKNCHFTKYRKTCEELALLGFTKSDVYLIDIDGNGVFPPAHVKCDFQSLENATKTIVEHNLPSQVDVRSARESDFSFNIRYREFSPHMLQELISHSLYCTQYIKYDCYRAQLELHSATWFTSSAKNLTVDFLGNVKRGACPCSVNKTCVDPNQSCNCDVKENKWNSDEGYYQDPQSLGITNMYFLQQKDMDDEAQGRITLGPLECVETNTQKYVVTFTTSQSYIEVPGWRKGDIAFSFRTTGEKAILLFQPPIRPHYPSFMVALTGDDQLTFTFTLSTGTTRELVINSHRRLNGGEWHKIWIDYNQYHVRFMINTDYQMLDLLPEEEFGPFEGSMYIGGATFDLLKKLSVKAGLIGCFRGLVVNGEILDIYSYMSVHLSEIIKDCKPSCVPSPCRNGAQCKELWSSFKCVCNNPWAHIGEFCETNINEKALTFINRESFLMRNYLSVGATPVILMHGINGERDVLKGILNQDLLINLRTYDTNALVLYANDHYNNFVHLYISLNREIVFLYNYGDEIVNLTLLDDTLMASLKSIQVAIVRGEQETRMHVNEHSVSIDRGTLLLDEYANKPWSNPEKEVLSPHRPPAPPTEYFQFHVGGYDPANLLRPNVDAPALEGYIGCVRGLKIGAQLIDLADINERNIAPTQEGVLPNCQIKCDAEPCKNGGTCQEHFAEQLSTCDCEHTSFLGEFCSEEKGADFSGESTLQRKFELPGTGRVDYVRLQLAFSSFDLRRANRIMLLMQTEAERSYYLLLAITSDGYLQLEEDRDNGQTVGARIDRNFLNSARHSVYYVRNGTQSQLFIDREQVPLSEFAARVLTTGGDAGSNRVQIGGINSTDSRFAVFKSYSGCLSNIYIQVNGHVMKPLEEYMLFTKSGADNITVINPQGVRSAQCNAKFDVSEQPTQEPMVNVSMIPEPWVEEPPARVPYIPRFVYDENKQEDSTQVVFLTLTSVFVIIVICCLLEVYRSHLAYKKRIERETDEDIIWSKEQATKMHESPGVKAGLLGGVTAGSGNGLPPYTYKALPQEDKKPGNGAPLVGILKNGSATPSQPGTPTALSKNGDIASRIEEEEEEEDEAPAQKAAEKSGENEEPPAKDTTASEIKESQAQPPEQLAKDTTDASAAPKASKETEAQAEPSEPSSQLNSAQNGQLAQMEQAARGDEVQVPSLPHPIQPPDAIFMPNLPQKAQQRQPQEHKSRHKATDDTEAPKQQQQQQQQQQSFDVATNANGSSLPASRVKNPEEPGGKSPLVPMRQHHSKVTRPPPPPTLFLENSLLQRQFANPISYLGGPRLQPRSNRTSIDSILSLD
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May have serine protease inhibitor activity (Probable). Might play a role in the glial-neuronal signaling pathway that is important in establishing the electrical properties of axonal membranes.
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M9PFN0
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HZG_DROME
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Phosphatase Herzog (EC 3.1.3.16)
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MDATSIITQVSRDDEQLNVYPSYPNDKDAWLGFSGSVWLPDCPADHAQLTHDVDRLKPQKRGLFHSLLCCWRRNRTKTNQNGTQIDGSTTPPPLPDQQRYLLPQVRLTDMHRKCMVIDLDETLVHSSFKPIPNADFIVPVEIDGTVHQVYVLKRPHVDEFLQKMGELYECVLFTASLAKYADPVADLLDKWNVFRARLFRESCVYYRGNYIKDLNRLGRDLQKIVIVDNSPASYIFHPDNAVPVKSWFDDVTDCELRELIPLFEKLSKVDSVYSVLCNSNQPLNNQTNQQQHPQELQQAPNQLHQQLQQQQQQQTISATTVITQATTLSAPTMLNQQQTSPPSPQSELLQKT
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Prion-like membrane-associated phosphatase. Phosphatase activity depends on amyloid-like assembly at the membrane. Might have a role in establishment of segment polarity in embryos.
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M9PGC5
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WNK_DROME
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Serine/threonine-protein kinase Wnk (EC 2.7.11.1) (Protein kinase with no lysine)
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MGQTLCDFVRQQEVVPANRARKGSAISEDGTTSCTTQPQRNTSISSEEQTVQGANIQKSGHRSFNRSASSRQKPNPTSKLKDTLNRKPTCKQGTLSAHTSTSSTTSIQSSPIEPASSLPTLNTTPTPPAASKSNLFVRVLRRFSNNTLPGKTASSPKNVDDVPKVNDNNNGDLGKQQSTDVEVLCSQDNQSREQNEDEMDSKIEPADAISNQKAGLTSGKPKKDKSVKGTSQAVVSDTKKMEARKSSSDTVIEPLIKQQAPLHSSKTTPTTLTANFVQNIRFVRKNVEQSGRNTNPLQFVELETEFPRDYDDNIEMLSREAEHLEEQFRTPTRSNATDATSHHVAGIIDNIITEASRSLTIEKTEDDVPLKSSTKHSSGVKRVGFQVEDKDDTEVQSEKQAKSFDDITKKAESSEASAEEAAVTGSSTDASASPLPSTSLVSTTSSATSITKSKSDEDDDPVAMSPCGRFFKYDKEVGRGSFKTVYRGLDTLTGVPVAWCELLDKQVKKSERTRFREEADMLKKLQHPNIVRFYTYWEFPIGRKKNIVLVTELMLSGTLKSYLKRFKKIHPKVLKSWCRQILKGLNFLHTRQFPIIHRDLKCDNIFITGTTGSVKIGDLGLATLKNRSHAKSVIGTPEFMAPEMYEEHYDESVDVYAFGMCMLEMAISEYPYSECKGPAQIYKKVISGIKPAALAKVEDPNVRDIIERCIELKKEDRPSCNELLESEFFDEDIGIRVEPTASEQFLSDPSISIIEFRLRFMDPKKRSSRHKENEAIQFEYNIRHDEYEQIAQEMMKENIISEDDSRAVARLLKVQVVSLLKERAQRQTQIKLQNEKSRLEKLALQKQRESLPTNVDEDEEEEEESEDEEDGVKWNQRLQLRYDLLNTDSETSLALSTNSVEPQQLSTRSNTSIPNSGIQQPVQVPGQVPVSQLISVQPQAIPSPAIPMQQKPTVHYIQPPQLASYQNSNASMQEMTNNQVISPTGSQQMQQQQPVVAPTVNHQVMPQQQVNQQQQQPQMMQQIPQQVQVQQPQTVLPPQPHEQQPQQQQQPLQQQLQQLMHTNVQAPDLTQQQQMAQQQAQQYFQQQQQQPQQAVNMQQAYAMQQAGQQQQLSQPLQIQQQILQQQQVAVSHQQQIMQQQLAQHQLQQLQQQQLQQQQLQQQQQIQQQQLQQQQLQQQQFVQQYAQAMPQQQHQQLVTGSQVMAPHQHQQPIQIPVQMQVPPTSVAPPIQHTYNQQGGQVTLSDAQQQQHPGFSAVPQQAAPFIQQPTQQPIQLSMPLEQQLQQLLHSQPAQQQQAMSQQQQQPLVQQQQLPLVQQQPPLVQQQQPLVQHQQPSVQHQQPLVQQPQQQQPQPQNQQPQPQTQQTHVVQQQPPQQQPAVEQISQISSQVPVQQENLQPIQVNKDANVATDAMSLNSAHGALEPAPKTEPQNSADAEKQQKQTGTGTRSQKPRRSNRSGNERIPKLSVTSVDEGSVINCHMENKLKTITFKFDIGDVNPVEIANKLIAQDLLSNCQSTVFVEMINEIVDQVKQNPNQIPIPTNYRRNIEKVRHASLTRQRSTFRSHQRHRSRDETASDITKMFEPTIHGVETLPSGGGGAEQSNCNLTLEARSHLSNIPNAKEPQLNVSTPPTTTSTMSSSSTASRDAPNSSNDVTIGSGSVSRKTSTASEYTSLSIDYMPDSNITPTGPEPPLDDGKDKKPCSLAIARMQKLLESAGNGAPRSLNLPLNRHLKIQEDLKHTRSLDDLTAVKITFDMPNKAALDTSENAQQATEAEAEKPKDKSGQAVGNQGTGAANTLEQLKIELENITHAHAFASAVVASINNRAPHQASPAMSSLKATSGQPQTQEITKPNNGAGPSVPSVGQNTPTAALTSARGSGSSVYNSRRTSIDNSVGSDMHLHTATNLEGTVSNPDPIPTEASVGITIATGHEKQLSKQPSLEKPSATSILTNNSDPPQRNPSNGSINQNSIADLEKKLAALRNTENTEESATATLSVVPKQVEEVVNPSARKISRFSVSRVQEQKTSTGVEEPAQGQLKIDLQVAGPGGQVQTNNSVQNGSVVNTPTEVISSPIQNVPLAINGIQLMYQQPQQIHQLPGGTSTTTSGAGTQCIVVPQVVNQNGTHVQQPSNLQPQQQSVHPNMTQQPQQTPLNGHPSMVNTLQQQPPQQSLPMQTIQSQQQQHNQMPIISQQQQQQILMQQQQQQGSQQGSQQFNLPGTQQTHPQHQFIQSQPNQLHSLPPQVVSMAQGNLPHQLPPMQTMGAQQQMISQQQHQLQMQSHMHQQNVPGMYNQQTGARVAAPQNFAGAVPNHLLQQSPLMASQQPAQPMQHVMQPIFNATSGEVTEEPVSLAATHPHLLPSDIQSDIKHNLDSLVNQLCNTRLGTNQHQRLLLLRQRQLIEEDELRLKHYVEYEKFQKALRQSISTNVPANAAYYSAAAAQLPTNLAAPAAPSSSNPTSTSSANT
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Serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as positive regulator of the canonical Wnt signaling pathway during wing disk development.
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M9Z1G5
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MOMT3_SOLHA
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Myricetin 3-O-methyltransferase 3 (ShMOMT3) (EC 2.1.1.-) (3',5'-dimethyl myricetin 3-O-methyltransferase) (Syringetin 3-O-methyltransferase) (EC 2.1.1.-) (3'-methyl myricetin 3-O-methyltransferase) (Laricitrin 3-O-methyltransferase) (EC 2.1.1.-) (3'-methyl quercetin 3-O-methyltransferase) (Isorhamnetin 3-O-methyltransferase) (EC 2.1.1.-) (4'-methyl kaempferol 3-O-methyltransferase) (Kaempferide 3-O-methyltransferase) (EC 2.1.1.-) (7-methyl quercetin 3-O-methyltransferase) (Rhamnetin 3-O-methyltransferase) (EC 2.1.1.-) (Kaempferol 3-O-methyltransferase) (EC 2.1.1.-) (Quercetin 3-O-methyltransferase) (EC 2.1.1.76)
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MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLKAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGIVHTSYNLTPLSQSLISDKDGSSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRMNGLFNRAMQNVTCTEMKRIVECYNGFQGVKEIIDVGGGLGISLATIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDEYCVKILKNCWRALPKDGKVVVIEQMQPEYPETNLISKNSSSVDMLMMTMLDGGKERTKQQFEDLAKQAGFTVFKIVARAYYCWVIELYK
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Flavonoid 3-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as myricetin derivatives, aroma compounds possessing antioxidant properties and exhibiting pharmacological activities such as anti-carcinogen, anti-viral, anti-thrombotic, anti-diabetic, anti-atherosclerotic, and anti-inflammatory effects. Catalyzes S-adenosylmethionine-dependent regioselective 3-O-methylation of flavonoids active on various hydroxylated flavonoid substrates. Active with myricetin, quercetin, kaempferol, 4'-methyl kaempferol (kaempferide), 3'-methyl quercetin (isorhamnetin), 7-methyl quercetin (rhamnetin), 3'-methyl myricetin (laricitrin) and 3',5'-dimethyl myricetin (syringetin), thus producing 3-methyl myricetin, 3-methyl quercetin, 3-methyl kaempferol, 4',3-methyl kaempferol, 3',3-methyl quercetin, 7,3-dimethyl quercetin, 3',3-dimethyl myricetin and 3',5',3-dimethyl myricetin, respectively. Inactive with flavonol substrates methylated at the 3-hydroxyl position such as 3-O-methyl quercetin.
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N0A5N4
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VAE2_GLOHA
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Thrombin-like enzyme agkihpin-2 (TLE agkihpin-2) (EC 3.4.21.-) (Agkihpin) (Snake venom arginine esterase) (SVAE) (Snake venom thrombin-like enzyme) (SVTLE)
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MILGDDECNINEHRFLVALYTSRTLFCGGTLINQEWVLTAAHCNMEDIQIKLGMHSKKVPNEDEQKRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSAHIAPLSLPSSPPSVGSVCRTMGWGRISSTKETYPDVPHCVNINLLEYEMCRAPYPEFELPATSRTLCAGILEGGKDTCVGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIENIIAGNTDASCPP
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Thrombin-like enzyme that shows fibrinogenolytic activity against bovine fibrinogen alpha and beta chains, but not gamma chain. Hydrolyzes fibrin. Enhances ADP-induced human platelet aggregation. Has arginine esterase activity for TAMe (tosyl-arginine methyl ester) substrate. Reduces thrombin-induced thrombosis. Does not have hemorrhagic activity. Reduces the motility of human liver cancer HepG2 cells in a wound-healing assay.
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N1NVB7
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GCY6_CAEEL
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Receptor-type guanylate cyclase gcy-6 (EC 4.6.1.2)
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MIGVYLRSVIFPLLFVIQTICQPPGNVFHLGFLHCDVLENNVEGSTTYINYRTSASAASIAIDKIKREGLLLGYDFKFTILYDQCDENIAAGNAIKLFAEHNVDVLFGPTTNNAAMPVFILATYYNIPLITWGITSSATLDDESRFPTAGMLSIGSRSLAVTFREVMKEYGWDQFVFAYSLEMNDEKCETLRDDFQNMVAYYGDIVLSYAVQIMDHSEEGLLAILKDVSTRGRIIVPCFHEGNSRGLHRRWMLVAARNGFVNDEYVYIFPSLRSRGYAVPQADGTFRYPWTEATGPQPGDQEALLGFQKSIFIVDMQGQGNVGSNYTQFEHEIIQRMKEPPYNCTDACASPEYQTAATYAGQLHDSVYIYGVVMDQIMKTVPNQYKNGTAFPRKMAGVFNGVGGTVAIDEGGGLQPTLFVLTLDSNNNSSLIMTVDVDQQEAVVTKHYTNEATALWSHRKGIRPPDQPICGYTGSLCPANVFFQYIGWFIAAIIIIFFTIMGAILAFIYLCHAKQQEVERQNALWQIPFKSMMTVTKKGKGEHSMRSISSVPSTISSTRSSTLSEVGETRNYLFFQIQNDVEMERVAAKKHSIRMVFDNKTCATMRQMRLIDHANLNKFIGMSLDAPQLYSVWRFCSRGSLADVIRKASMQMDGFFIYSLMKDIINGLTWIHESSHEFHGMLTSKNCLLNDRWQLKITDFGLRIFRTHDQYNKSDRLWTSPELLRTDDILGSREGDIYSFGIISAELITRSSVFDLENRKEDAEEIIYMLKKGGLQSPRPSLEHDESIEINPALLHLVRDCWTERPSERPDIKQVASQLRSMNTNRNDNLMDHVFNVLESYASTLEDEVAERMKELVEEKKKSDVLLYRMLPRQVADKLKLGQTVEPETFDIVTLFFSDVVSFTTLAGKCTPLQVVNLLNGLYTIFDGIIEQHDVYKVETIGDGYFVASGVPRRNGNEHTRNIASMSINFVKSLADFSIPHLPGEKIKIRVGFHCGSVVAGVVGLTMPRYCLFGDAVNTASRMESNSKPGQIHLSEEANQMLMRLGGFTTEPRGEVIIKGKGVMATYWLLKMDESAAPKILKKKQD
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Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Regulates chemotaxis responses toward the salt ion Mg(2+) and to a lesser extent toward Cl(1-) in ASE left (ASEL) sensory neuron.
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N1P212
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ATH1_YEASC
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Periplasmic acid trehalase ATC1 (EC 3.2.1.28)
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MKRIRSLWFNAEASYSNLNNSPSLRNKNSTGNNSRSKNYRSFSRFDLINSILLLMMLFLLAIFVTALYLTKSSRLTYSHASRAALFNPLGVISPSLGNHTLNYDPEARESSKKLYELLSDFNTAYYDDENMILGSNLFSKNTYSRQPYVANGYIGSRIPNIGFGYALDTLNFYTDAPGALNNGWPLRNHRFAGAFVSDFYCLQPKLNSTNFPELDDVGYSTVISSIPQWTNLQFSLVNDSKWFNPQNVTLDDVTNYSQNLSMKDGIVTTELDWLNSQIHVKSEIWAHRHIHPLGVVSLEISLNTDHLPSDFDSLDVNIWDILDFNTSHRTVLHSTGTDEKNNAVFMIVQPDNVPSSNCAIYSTCTVKYENSTNPINSSESFEEKDVSSNIYNVILTEDQPKIIVHKYVGIMSTEFNKNKEQQDNTNIGLAKMIALNSKGNYEKLLSSHKRAWYDLYNDAFIEIPSDSLLEMTARSSLFHLLANTRDYNVSSDRGLPVGVSGLSSDSYGGMVFWDADIWMEPALLPFFPNVAQNMNNYRNATHSQAKLNAEKYGYPGAIYPWTSGKYANCTSTGPCVDYEYHINVDVAMASFSIYLNGHEGIDDEYLRYTTWPIIKNAAQFFTAYVKYNSSLGLYETYNLTDPDEFANHINNGAFTNAGIKTLLKWATDIGNHLGEVVDPKWSEISKDIYIPRSSSNITLEYSGMNSSVEIKQADVTLMVYPLGYINDESILNNAIKDLYYYSERQSASGPAMTYPVFVAAAAGLLNHGSSSQSYLYKSVLPYLRAPFAQFSEQSDDNFLTNGLTQPAFPFLTANGGFLQSILFGLTGIRYSYEVDPDTKKINRLLRFNPIELPLLPGGIAIRNFKYMNQVLDIIIDDHNGTIVHKSGDVPIHIKIPNRSLIHDQDINFYNGSENERKPNLERRDVDRVGDPMRMDRYGTYYLLKPKQELTVQLFKPGLNARNNIAENKQITNLTAGVPGDVAFSALDGNNYTHWQPLDKIHRAKLLIDLGEYNEKEITKGMILWGQRPAKNISISILPHSEKVENLFANVTEIMQNSGNDQLLNETIGQLLDNAGIPVENVIDFDGIEQEDDESLDDVQALLHWKKEDLAKLIEQIPRLNFLKRKFVKILDNVPVSPSEPYYEASRNQSLIEILPSNRTTFTIDYDKLQVGDKGNTDWRKTRYIVVAVQGVYDDYDDDNKGATIKEIVLND
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Periplasmic acid trehalase that catalyzes hydrolysis of the disaccharide trehalose and required for growth on trehalose as carbon source. Growth on trehalose is strictly respiratory.
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O00092
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PHYA_ASPFU
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3-phytase A (EC 3.1.3.8) (3 phytase A) (Myo-inositol hexakisphosphate phosphohydrolase A) (Myo-inositol-hexaphosphate 3-phosphohydrolase A)
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MVTLTFLLSAAYLLSGRVSAAPSSAGSKSCDTVDLGYQCSPATSHLWGQYSPFFSLEDELSVSSKLPKDCRITLVQVLSRHGARYPTSSKSKKYKKLVTAIQANATDFKGKFAFLKTYNYTLGADDLTPFGEQQLVNSGIKFYQRYKALARSVVPFIRASGSDRVIASGEKFIEGFQQAKLADPGATNRAAPAISVIIPESETFNNTLDHGVCTKFEASQLGDEVAANFTALFAPDIRARAEKHLPGVTLTDEDVVSLMDMCSFDTVARTSDASQLSPFCQLFTHNEWKKYNYLQSLGKYYGYGAGNPLGPAQGIGFTNELIARLTRSPVQDHTSTNSTLVSNPATFPLNATMYVDFSHDNSMVSIFFALGLYNGTEPLSRTSVESAKELDGYSASWVVPFGARAYFETMQCKSEKEPLVRALINDRVVPLHGCDVDKLGRCKLNDFVKGLSWARSGGNWGECFS
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Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
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O00102
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UBC7_SCHPO
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Ubiquitin-conjugating enzyme E2-18 kDa (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 7) (Ubiquitin carrier protein) (Ubiquitin-protein ligase)
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MSKAMALRRLMKEYKELTENGPDGITAGPSNEDDFFTWDCLIQGPDGTPFEGGLYPATLKFPSDYPLGPPTLKFECEFFHPNVYKDGTVCISILHAPGDDPNMYESSSERWSPVQSVEKILLSVMSMLAEPNDESGANIDACKMWREDREEYCRVVRRLARKTLGL
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Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the doa10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the hrd1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) (By similarity). Together with hrd1, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1. Has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12456009, ECO:0000269|PubMed:19520858}.
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O00103
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UBC11_SCHPO
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Ubiquitin-conjugating enzyme E2-20 kDa (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 11) (Ubiquitin carrier protein) (Ubiquitin-protein ligase)
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MDSDMQNQNPHTNSKNSSSAGMAVDGHSVTKRLRSELMSLMMSNTPGISAFPDSDSNLLHWAGTITGPSDTYYEGLKFKISMSFPANYPYSPPTIIFTSPMWHPNVDMSGNICLDILKDKWSAVYNVQTILLSLQSLLGEPNNASPLNAQAAELWSKDPIEYKRLLMQRYKEIDEI
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Catalyzes the covalent attachment of ubiquitin to other proteins.
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O00115
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DNS2A_HUMAN
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Deoxyribonuclease-2-alpha (EC 3.1.22.1) (Acid DNase) (Deoxyribonuclease II alpha) (DNase II alpha) (Lysosomal DNase II) (R31240_2)
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MIPLLLAALLCVPAGALTCYGDSGQPVDWFVVYKLPALRGSGEAAQRGLQYKYLDESSGGWRDGRALINSPEGAVGRSLQPLYRSNTSQLAFLLYNDQPPQPSKAQDSSMRGHTKGVLLLDHDGGFWLVHSVPNFPPPASSAAYSWPHSACTYGQTLLCVSFPFAQFSKMGKQLTYTYPWVYNYQLEGIFAQEFPDLENVVKGHHVSQEPWNSSITLTSQAGAVFQSFAKFSKFGDDLYSGWLAAALGTNLQVQFWHKTVGILPSNCSDIWQVLNVNQIAFPGPAGPSFNSTEDHSKWCVSPKGPWTCVGDMNRNQGEEQRGGGTLCAQLPALWKAFQPLVKNYQPCNGMARKPSRAYKI
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Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells.
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O00116
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ADAS_HUMAN
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Alkyldihydroxyacetonephosphate synthase, peroxisomal (Alkyl-DHAP synthase) (EC 2.5.1.26) (Aging-associated gene 5 protein) (Alkylglycerone-phosphate synthase)
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MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDLCRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNLL
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Catalyzes the exchange of the acyl chain in acyl-dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol, yielding the first ether linked intermediate, i.e. alkyl-dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid biosynthesis.
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O00124
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UBXN8_HUMAN
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UBX domain-containing protein 8 (Reproduction 8 protein) (Rep-8 protein) (UBX domain-containing protein 6)
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MASRGVVGIFFLSAVPLVCLELRRGIPDIGIKDFLLLCGRILLLLALLTLIISVTTSWLNSFKSPQVYLKEEEEKNEKRQKLVRKKQQEAQGEKASRYIENVLKPHQEMKLRKLEERFYQMTGEAWKLSSGHKLGGDEGTSQTSFETSNREAAKSQNLPKPLTEFPSPAEQPTCKEIPDLPEEPSQTAEEVVTVALRCPSGNVLRRRFLKSYSSQVLFDWMTRIGYHISLYSLSTSFPRRPLAVEGGQSLEDIGITVDTVLILEEKEQTN
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Involved in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the endoplasmic reticulum membrane. May play a role in reproduction.
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O00139
|
KIF2A_HUMAN
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Kinesin-like protein KIF2A (Kinesin-2) (hK2)
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MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPSRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPNQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL
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Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity.
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O00141
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SGK1_HUMAN
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Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)
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MTVKTEAAKGTLTYSRMRGMVAILIAFMKQRRMGLNDFIQKIANNSYACKHPEVQSILKISQPQEPELMNANPSPPPSPSQQINLGPSSNPHAKPSDFHFLKVIGKGSFGKVLLARHKAEEVFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTADKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEHNSTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFMEIKSHVFFSLINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTEEPVPNSIGKSPDSVLVTASVKEAAEAFLGFSYAPPTDSFL
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Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na(+) transport than isoform 1.
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O00142
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KITM_HUMAN
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Thymidine kinase 2, mitochondrial (EC 2.7.1.21) (2'-deoxyuridine kinase TK2) (EC 2.7.1.74) (Deoxycytidine kinase TK2) (EC 2.7.1.-) (Mt-TK)
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MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLELFEQNRDRILTPENRKHCP
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Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK. Widely used as target of antiviral and chemotherapeutic agents.
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O00144
|
FZD9_HUMAN
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Frizzled-9 (Fz-9) (hFz9) (FzE6) (CD antigen CD349)
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MAVAPLRGALLLWQLLAAGGAALEIGRFDPERGRGAAPCQAVEIPMCRGIGYNLTRMPNLLGHTSQGEAAAELAEFAPLVQYGCHSHLRFFLCSLYAPMCTDQVSTPIPACRPMCEQARLRCAPIMEQFNFGWPDSLDCARLPTRNDPHALCMEAPENATAGPAEPHKGLGMLPVAPRPARPPGDLGPGAGGSGTCENPEKFQYVEKSRSCAPRCGPGVEVFWSRRDKDFALVWMAVWSALCFFSTAFTVLTFLLEPHRFQYPERPIIFLSMCYNVYSLAFLIRAVAGAQSVACDQEAGALYVIQEGLENTGCTLVFLLLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEAHGSYFHMAAWGLPALKTIVILTLRKVAGDELTGLCYVASTDAAALTGFVLVPLSGYLVLGSSFLLTGFVALFHIRKIMKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYVYERLNMDFWRLRATEQPCAAAAGPGGRRDCSLPGGSVPTVAVFMLKIFMSLVVGITSGVWVWSSKTFQTWQSLCYRKIAAGRARAKACRAPGSYGRGTHCHYKAPTVVLHMTKTDPSLENPTHL
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Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by negatively regulating the clustering of acetylcholine receptors (AChR) through the beta-catenin canonical signaling pathway (By similarity). May play a role in neural progenitor cells (NPCs) viability through the beta-catenin canonical signaling pathway by negatively regulating cell cycle arrest leading to inhibition of neuron apoptotic process. During hippocampal development, regulates neuroblast proliferation and apoptotic cell death. Controls bone formation through non canonical Wnt signaling mediated via ISG15. Positively regulates bone regeneration through non canonical Wnt signaling (By similarity).
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O00148
|
DX39A_HUMAN
|
ATP-dependent RNA helicase DDX39A (EC 3.6.4.13) (DEAD box protein 39) (Nuclear RNA helicase URH49)
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MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGMAQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNVAELPEEIDISTYIEQSR
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[Isoform 1]: Involved in pre-mRNA splicing. Required for the export of mRNA out of the nucleus.
|
O00151
|
PDLI1_HUMAN
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PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1) (Elfin) (LIM domain protein CLP-36)
|
MTTQQIDLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAALANLCIGDVITAIDGENTSNMTHLEAQNRIKGCTDNLTLTVARSEHKVWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPASSTTARVITNQYNNPAGLYSSENISNFNNALESKTAASGVEANSRPLDHAQPPSSLVIDKESEVYKMLQEKQELNEPPKQSTSFLVLQEILESEEKGDPNKPSGFRSVKAPVTKVAASIGNAQKLPMCDKCGTGIVGVFVKLRDRHRHPECYVCTDCGTNLKQKGHFFVEDQIYCEKHARERVTPPEGYEVVTVFPK
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Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton. Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity).
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O00154
|
BACH_HUMAN
|
Cytosolic acyl coenzyme A thioester hydrolase (EC 3.1.2.2) (Acyl-CoA thioesterase 7) (Brain acyl-CoA hydrolase) (BACH) (hBACH) (CTE-IIa) (CTE-II) (Long chain acyl-CoA thioester hydrolase)
|
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVVYSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHAEPQP
|
Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18. May play an important physiological function in brain.
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O00155
|
GPR25_HUMAN
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Probable G-protein coupled receptor 25
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MAPTEPWSPSPGSAPWDYSGLDGLEELELCPAGDLPYGYVYIPALYLAAFAVGLLGNAFVVWLLAGRRGPRRLVDTFVLHLAAADLGFVLTLPLWAAAAALGGRWPFGDGLCKLSSFALAGTRCAGALLLAGMSVDRYLAVVKLLEARPLRTPRCALASCCGVWAVALLAGLPSLVYRGLQPLPGGQDSQCGEEPSHAFQGLSLLLLLLTFVLPLVVTLFCYCRISRRLRRPPHVGRARRNSLRIIFAIESTFVGSWLPFSALRAVFHLARLGALPLPCPLLLALRWGLTIATCLAFVNSCANPLIYLLLDRSFRARALDGACGRTGRLARRISSASSLSRDDSSVFRCRAQAANTASASW
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Orphan receptor.
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O00159
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MYO1C_HUMAN
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Unconventional myosin-Ic (Myosin I beta) (MMI-beta) (MMIb)
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MALQVELVPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANEESNAQVTTENQLKYLTRLLSVEGSTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADQRTRKSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETMCSSKNPIMSQCFDRSELSDKKRPETVATQFKMSLLQLVEILQSKEPAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFPKTLFATEDALEVRRQSLATKIQAAWRGFHWRQKFLRVKRSAICIQSWWRGTLGRRKAAKRKWAAQTIRRLIRGFVLRHAPRCPENAFFLDHVRTSFLLNLRRQLPQNVLDTSWPTPPPALREASELLRELCIKNMVWKYCRSISPEWKQQLQQKAVASEIFKGKKDNYPQSVPRLFISTRLGTDEISPRVLQALGSEPIQYAVPVVKYDRKGYKPRSRQLLLTPNAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQRADNKQKGDVVLQSDHVIETLTKTALSANRVNSININQGSITFAGGPGRDGTIDFTPGSELLITKAKNGHLAVVAPRLNSR
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.
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O00160
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MYO1F_HUMAN
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Unconventional myosin-If (Myosin-Ie)
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MGSKERFHWQSHNVKQSGVDDMVLLPQITEDAIAANLRKRFMDDYIFTYIGSVLISVNPFKQMPYFTDREIDLYQGAAQYENPPHIYALTDNMYRNMLIDCENQCVIISGESGAGKTVAAKYIMGYISKVSGGGEKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSRGGEPDGGKISNFLLEKSRVVMQNENERNFHIYYQLLEGASQEQRQNLGLMTPDYYYYLNQSDTYQVDGTDDRSDFGETLSAMQVIGIPPSIQQLVLQLVAGILHLGNISFCEDGNYARVESVDLLAFPAYLLGIDSGRLQEKLTSRKMDSRWGGRSESINVTLNVEQAAYTRDALAKGLYARLFDFLVEAINRAMQKPQEEYSIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIQYFNNKVVCDLIENKLSPPGIMSVLDDVCATMHATGGGADQTLLQKLQAAVGTHEHFNSWSAGFVIHHYAGKVSYDVSGFCERNRDVLFSDLIELMQTSEQAFLRMLFPEKLDGDKKGRPSTAGSKIKKQANDLVATLMRCTPHYIRCIKPNETKRPRDWEENRVKHQVEYLGLKENIRVRRAGFAYRRQFAKFLQRYAILTPETWPRWRGDERQGVQHLLRAVNMEPDQYQMGSTKVFVKNPESLFLLEEVRERKFDGFARTIQKAWRRHVAVRKYEEMREEASNILLNKKERRRNSINRNFVGDYLGLEERPELRQFLGKRERVDFADSVTKYDRRFKPIKRDLILTPKCVYVIGREKVKKGPEKGQVCEVLKKKVDIQALRGVSLSTRQDDFFILQEDAADSFLESVFKTEFVSLLCKRFEEATRRPLPLTFSDTLQFRVKKEGWGGGGTRSVTFSRGFGDLAVLKVGGRTLTVSVGDGLPKSSKPTRKGMAKGKPRRSSQAPTRAAPAPPRGMDRNGVPPSARGGPLPLEIMSGGGTHRPPRGPPSTSLGASRRPRARPPSEHNTEFLNVPDQGMAGMQRKRSVGQRPVPGVGRPKPQPRTHGPRCRALYQYVGQDVDELSFNVNEVIEILMEDPSGWWKGRLHGQEGLFPGNYVEKI
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Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity).
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O00161
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SNP23_HUMAN
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Synaptosomal-associated protein 23 (SNAP-23) (Vesicle-membrane fusion protein SNAP-23)
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MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKLIDS
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Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
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O00165
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HAX1_HUMAN
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HCLS1-associated protein X-1 (HS1-associating protein X-1) (HAX-1) (HS1-binding protein 1) (HSP1BP-1)
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MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR
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Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools.
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O00167
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EYA2_HUMAN
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Eyes absent homolog 2 (EC 3.1.3.48)
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MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSADGFHSSAPGANLCLGSGVHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL
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Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2 in this it is functionally redundant with EYA1.
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O00168
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PLM_HUMAN
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Phospholemman (FXYD domain-containing ion transport regulator 1) (Sodium/potassium-transporting ATPase subunit FXYD1)
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MASLGHILVFCVGLLTMAKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEEEGTFRSSIRRLSTRRR
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Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone.
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O00170
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AIP_HUMAN
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AH receptor-interacting protein (AIP) (Aryl-hydrocarbon receptor-interacting protein) (HBV X-associated protein 2) (XAP-2) (Immunophilin homolog ARA9)
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MADIIARLREDGIQKRVIQEGRGELPDFQDGTKATFHYRTLHSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAVGKDPLEGQRHCCGVAQMREHSSLGHADLDALQQNPQPLIFHMEMLKVESPGTYQQDPWAMTDEEKAKAVPLIHQEGNRLYREGHVKEAAAKYYDAIACLKNLQMKEQPGSPEWIQLDQQITPLLLNYCQCKLVVEEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALEARIRQKDEEDKARFRGIFSH
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May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting. Cellular negative regulator of the hepatitis B virus (HBV) X protein.
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O00175
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CCL24_HUMAN
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C-C motif chemokine 24 (CK-beta-6) (Eosinophil chemotactic protein 2) (Eotaxin-2) (Myeloid progenitor inhibitory factor 2) (MPIF-2) (Small-inducible cytokine A24)
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MAGLMTIVTSLLFLGVCAHHIIPTGSVVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKAGVIFTTKKGQQFCGDPKQEWVQRYMKNLDAKQKKASPRARAVAVKGPVQRYPGNQTTC
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Chemotactic for resting T-lymphocytes, and eosinophils. Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line. Binds to CCR3.
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O00180
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KCNK1_HUMAN
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Potassium channel subfamily K member 1 (Inward rectifying potassium channel protein TWIK-1) (Potassium channel K2P1) (Potassium channel KCNO1)
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MLQSLAGSSCVRLVERHRSAWCFGFLVLGYLLYLVFGAVVFSSVELPYEDLLRQELRKLKRRFLEEHECLSEQQLEQFLGRVLEASNYGVSVLSNASGNWNWDFTSALFFASTVLSTTGYGHTVPLSDGGKAFCIIYSVIGIPFTLLFLTAVVQRITVHVTRRPVLYFHIRWGFSKQVVAIVHAVLLGFVTVSCFFFIPAAVFSVLEDDWNFLESFYFCFISLSTIGLGDYVPGEGYNQKFRELYKIGITCYLLLGLIAMLVVLETFCELHELKKFRKMFYVKKDKDEDQVHIIEHDQLSFSSITDQAAGMKEDQKQNEPFVATQSSACVDGPANH
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Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues. Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K(+) ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na(+) at subphysiological K(+) levels and upon acidification of the extracellular medium. The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel. Channel activity is modulated by activation of serotonin receptors (By similarity). Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes (By similarity). Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity. Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane-sensitive currents. Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential (By similarity). Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability (By similarity). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity). Required for normal ion and water transport in the kidney (By similarity). Contributes to the regulation of the resting membrane potential of pancreatic beta cells (By similarity). The low channel activity of homodimeric KCNK1 may be due to sumoylation. The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes.
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O00182
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LEG9_HUMAN
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Galectin-9 (Gal-9) (Ecalectin) (Tumor antigen HOM-HD-21)
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MAFSGSQAPYLSPAVPFSGTIQGGLQDGLQITVNGTVLSSSGTRFAVNFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYISFQNPRTVPVQPAFSTVPFSQPVCFPPRPRGRRQKPPGVWPANPAPITQTVIHTVQSAPGQMFSTPAIPPMMYPHPAYPMPFITTILGGLYPSKSILLSGTVLPSAQRFHINLCSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVAVDGQHLFEYYHRLRNLPTINRLEVGGDIQLTHVQT
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Binds galactosides. Has high affinity for the Forssman pentasaccharide. Ligand for HAVCR2/TIM3. Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death. Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (By similarity). Ligand for P4HB the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. Ligand for CD44 the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation. Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection. Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells. Inhibits degranulation and induces apoptosis of mast cells. Induces maturation and migration of dendritic cells. Inhibits natural killer (NK) cell function. Can transform NK cell phenotype from peripheral to decidual during pregnancy. Astrocyte derived galectin-9 enhances microglial TNF production (By similarity). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity).
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O00186
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STXB3_HUMAN
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Syntaxin-binding protein 3 (Platelet Sec1 protein) (PSP) (Protein unc-18 homolog 3) (Unc18-3) (Protein unc-18 homolog C) (Unc-18C)
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MAPPVAERGLKSVVWQKIKATVFDDCKKEGEWKIMLLDEFTTKLLASCCKMTDLLEEGITVVENIYKNREPVRQMKALYFITPTSKSVDCFLHDFASKSENKYKAAYIYFTDFCPDNLFNKIKASCSKSIRRCKEINISFIPHESQVYTLDVPDAFYYCYSPDPGNAKGKDAIMETMADQIVTVCATLDENPGVRYKSKPLDNASKLAQLVEKKLEDYYKIDEKSLIKGKTHSQLLIIDRGFDPVSTVLHELTFQAMAYDLLPIENDTYKYKTDGKEKEAILEEEDDLWVRIRHRHIAVVLEEIPKLMKEISSTKKATEGKTSLSALTQLMKKMPHFRKQITKQVVHLNLAEDCMNKFKLNIEKLCKTEQDLALGTDAEGQKVKDSMRVLLPVLLNKNHDNCDKIRAILLYIFSINGTTEENLDRLIQNVKIENESDMIRNWSYLGVPIVPQSQQGKPLRKDRSAEETFQLSRWTPFIKDIMEDAIDNRLDSKEWPYCSQCPAVWNGSGAVSARQKPRANYLEDRKNGSKLIVFVIGGITYSEVRCAYEVSQAHKSCEVIIGSTHVLTPKKLLDDIKMLNKPKDKVSLIKDE
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Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes.
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O00187
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MASP2_HUMAN
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Mannan-binding lectin serine protease 2 (EC 3.4.21.104) (MBL-associated serine protease 2) (Mannose-binding protein-associated serine protease 2) (MASP-2) [Cleaved into: Mannan-binding lectin serine protease 2 A chain; Mannan-binding lectin serine protease 2 B chain]
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MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF
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Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
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O00189
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AP4M1_HUMAN
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AP-4 complex subunit mu-1 (AP-4 adaptor complex mu subunit) (Adaptor-related protein complex 4 subunit mu-1) (Mu subunit of AP-4) (Mu-adaptin-related protein 2) (mu-ARP2) (Mu4-adaptin) (mu4)
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MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGDESPVVMHHHGRHFIHIRHSGLYLVVTTSENVSPFSLLELLSRLATLLGDYCGSLGEGTISRNVALVYELLDEVLDYGYVQTTSTEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQSKVAPSSAASRPVLSSRSDQSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEMRIGLTEEFCVGKSELRGYGPGIRVDEVSFHSSVNLDEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFPSVQWDRGSGRLQVYLKLRCDLLSKSQALNVRLHLPLPRGVVSLSQELSSPEQKAELAEGALRWDLPRVQGGSQLSGLFQMDVPGPPGPPSHGLSTSASPLGLGPASLSFELPRHTCSGLQVRFLRLAFRPCGNANPHKWVRHLSHSDAYVIRI
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Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons (By similarity). Within AP-4, the mu-type subunit AP4M1 is directly involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos. The adaptor protein complex 4 (AP-4) may also recognize other types of sorting signal (By similarity).
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O00192
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ARVC_HUMAN
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Splicing regulator ARVCF (Armadillo repeat protein deleted in velo-cardio-facial syndrome)
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MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMVSGGMGSGQPLPMAWQQLVLQEQSPGSQASLATMPEAPDVLEETVTVEEDPGTPTSHVSIVTSEDGTTRRTETKVTKTVKTVTTRTVRQVPVGPDGLPLLDGGPPLGPFADGALDRHFLLRGGGPVATLSRAYLSSGGGFPEGPEPRDSPSYGSLSRGLGMRPPRAGPLGPGPGDGCFTLPGHREAFPVGPEPGPPGGRSLPERFQAEPYGLEDDTRSLAADDEGGPELEPDYGTATRRRPECGRGLHTRAYEDTADDGGELADERPAFPMVTAPLAQPERGSMGSLDRLVRRSPSVDSARKEPRWRDPELPEVLAMLRHPVDPVKANAAAYLQHLCFENEGVKRRVRQLRGLPLLVALLDHPRAEVRRRACGALRNLSYGRDTDNKAAIRDCGGVPALVRLLRAARDNEVRELVTGTLWNLSSYEPLKMVIIDHGLQTLTHEVIVPHSGWEREPNEDSKPRDAEWTTVFKNTSGCLRNVSSDGAEARRRLRECEGLVDALLHALQSAVGRKDTDNKSVENCVCIMRNLSYHVHKEVPGADRYQEAEPGPLGSAVGSQRRRRDDASCFGGKKAKEEWFHQGKKDGEMDRNFDTLDLPKRTEAAKGFELLYQPEVVRLYLSLLTESRNFNTLEAAAGALQNLSAGNWMWATYIRATVRKERGLPVLVELLQSETDKVVRAVAIALRNLSLDRRNKDLIGSYAMAELVRNVRNAQAPPRPGACLEEDTVVAVLNTIHEIVSDSLDNARSLLQARGVPALVALVASSQSVREAKAASHVLQTVWSYKELRGTLQKDGWTKARFQSAAATAKGPKGALSPGGFDDSTLPLVDKSLEGEKTGSRDVIPMDALGPDGYSTVDRRERRPRGASSAGEASEKEPLKLDPSRKAPPPGPSRPAVRLVDAVGDAKPQPVDSWV
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Contributes to the regulation of alternative splicing of pre-mRNAs.
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O00194
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RB27B_HUMAN
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Ras-related protein Rab-27B (EC 3.6.5.2) (C25KG)
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MTDGDYDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVVYNAQGPNGSSGKAFKVHLQLWDTAGQERFRSLTTAFFRDAMGFLLMFDLTSQQSFLNVRNWMSQLQANAYCENPDIVLIGNKADLPDQREVNERQARELADKYGIPYFETSAATGQNVEKAVETLLDLIMKRMEQCVEKTQIPDTVNGGNSGNLDGEKPPEKKCIC
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Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion. Plays a role in NTRK2/TRKB axonal anterograde transport by facilitating the association of NTRK2/TRKB with KLC1. May be involved in targeting uroplakins to urothelial apical membranes (By similarity).
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O00198
|
HRK_HUMAN
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Activator of apoptosis harakiri (BH3-interacting domain-containing protein 3) (Neuronal death protein DP5)
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MCPCPLHRGRGPPAVCACSAGRLGLRSSAAQLTAARLKALGDELHQRTMWRRRARSRRAPAPGALPTYWPWLCAAAQVAALAAWLLGRRNL
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Promotes apoptosis.
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O00203
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AP3B1_HUMAN
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AP-3 complex subunit beta-1 (Adaptor protein complex AP-3 subunit beta-1) (Adaptor-related protein complex 3 subunit beta-1) (Beta-3A-adaptin) (Clathrin assembly protein complex 3 beta-1 large chain)
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MSSNSFPYNEQSGGGEATELGQEATSTISPSGAFGLFSSDLKKNEDLKQMLESNKDSAKLDAMKRIVGMIAKGKNASELFPAVVKNVASKNIEIKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEASADLSPYVRKNAAHAIQKLYSLDPEQKEMLIEVIEKLLKDKSTLVAGSVVMAFEEVCPDRIDLIHKNYRKLCNLLVDVEEWGQVVIIHMLTRYARTQFVSPWKEGDELEDNGKNFYESDDDQKEKTDKKKKPYTMDPDHRLLIRNTKPLLQSRNAAVVMAVAQLYWHISPKSEAGIISKSLVRLLRSNREVQYIVLQNIATMSIQRKGMFEPYLKSFYVRSTDPTMIKTLKLEILTNLANEANISTLLREFQTYVKSQDKQFAAATIQTIGRCATNILEVTDTCLNGLVCLLSNRDEIVVAESVVVIKKLLQMQPAQHGEIIKHMAKLLDSITVPVARASILWLIGENCERVPKIAPDVLRKMAKSFTSEDDLVKLQILNLGAKLYLTNSKQTKLLTQYILNLGKYDQNYDIRDRTRFIRQLIVPNVKSGALSKYAKKIFLAQKPAPLLESPFKDRDHFQLGTLSHTLNIKATGYLELSNWPEVAPDPSVRNVEVIELAKEWTPAGKAKQENSAKKFYSESEEEEDSSDSSSDSESESGSESGEQGESGEEGDSNEDSSEDSSSEQDSESGRESGLENKRTAKRNSKAKGKSDSEDGEKENEKSKTSDSSNDESSSIEDSSSDSESESEPESESESRRVTKEKEKKTKQDRTPLTKDVSLLDLDDFNPVSTPVALPTPALSPSLMADLEGLHLSTSSSVISVSTPAFVPTKTHVLLHRMSGKGLAAHYFFPRQPCIFGDKMVSIQITLNNTTDRKIENIHIGEKKLPIGMKMHVFNPIDSLEPEGSITVSMGIDFCDSTQTASFQLCTKDDCFNVNIQPPVGELLLPVAMSEKDFKKEQGVLTGMNETSAVIIAAPQNFTPSVIFQKVVNVANVGAVPSGQDNIHRFAAKTVHSGSLMLVTVELKEGSTAQLIINTEKTVIGSVLLRELKPVLSQG
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Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
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O00204
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ST2B1_HUMAN
|
Sulfotransferase 2B1 (EC 2.8.2.2) (Alcohol sulfotransferase) (Hydroxysteroid sulfotransferase 2) (Sulfotransferase family 2B member 1) (Sulfotransferase family cytosolic 2B member 1) (ST2B1)
|
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS
|
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol. Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). Preferentially sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA. Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation.
|
O00206
|
TLR4_HUMAN
|
Toll-like receptor 4 (hToll) (CD antigen CD284)
|
MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI
|
Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways. At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+). Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production. In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade. In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86. Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway. In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner.
|
O00212
|
RHOD_HUMAN
|
Rho-related GTP-binding protein RhoD (Rho-related protein HP1) (RhoHP1)
|
MTAAQAAGEEAPPGVRSVKVVLVGDGGCGKTSLLMVFADGAFPESYTPTVFERYMVNLQVKGKPVHLHIWDTAGQDDYDRLRPLFYPDASVLLLCFDVTSPNSFDNIFNRWYPEVNHFCKKVPIIVVGCKTDLRKDKSLVNKLRRNGLEPVTYHRGQEMARSVGAVAYLECSARLHDNVHAVFQEAAEVALSSRGRNFWRRITQGFCVVT
|
Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton the function seems to involve WHAMM and includes regulation of filopodia formation and actin filament bundling. Can modulate the effect of DAPK3 in reorganization of actin cytoskeleton and focal adhesion dissolution.
|
O00213
|
APBB1_HUMAN
|
Amyloid beta precursor protein binding family B member 1 (Amyloid-beta A4 precursor protein-binding family B member 1) (Protein Fe65)
|
MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP
|
Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its transcription activation activity. Functions in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning (By similarity). Plays a role in the maintenance of lens transparency (By similarity). May play a role in muscle cell strength (By similarity).
|
O00214
|
LEG8_HUMAN
|
Galectin-8 (Gal-8) (Po66 carbohydrate-binding protein) (Po66-CBP) (Prostate carcinoma tumor antigen 1) (PCTA-1)
|
MMLSLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGTPQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKVAVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW
|
Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy. Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane these ligands becoming exposed to the cytoplasm following rupture. Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52. Required to restrict infection of bacterial invasion such as S.typhimurium. Also required to restrict infection of Picornaviridae viruses. Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.
|
O00217
|
NDUS8_HUMAN
|
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (EC 7.1.1.2) (Complex I-23kD) (CI-23kD) (NADH-ubiquinone oxidoreductase 23 kDa subunit) (TYKY subunit)
|
MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
|
O00219
|
HYAS3_HUMAN
|
Hyaluronan synthase 3 (EC 2.4.1.212) (Hyaluronate synthase 3) (Hyaluronic acid synthase 3) (HA synthase 3)
|
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVMVVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRASTFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV
|
Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis.
|
O00220
|
TR10A_HUMAN
|
Tumor necrosis factor receptor superfamily member 10A (Death receptor 4) (TNF-related apoptosis-inducing ligand receptor 1) (TRAIL receptor 1) (TRAIL-R1) (CD antigen CD261)
|
MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE
|
Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.
|
O00221
|
IKBE_HUMAN
|
NF-kappa-B inhibitor epsilon (NF-kappa-BIE) (I-kappa-B-epsilon) (IkB-E) (IkB-epsilon) (IkappaBepsilon)
|
MNQRRSESRPGNHRLQAYAEPGKGDSGGAGPLSGSARRGRGGGGAIRVRRPCWSGGAGRGGGPAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARRSLEPDPAQTGPRPARAAGMSEARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEAEDPAPRLPLPHVGALSPQQLEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPEPGRGTSHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDDLKISGKLLLCTD
|
Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes.
|
O00222
|
GRM8_HUMAN
|
Metabotropic glutamate receptor 8 (mGluR8)
|
MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFAEFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMHKDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCERCEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPHIIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTYISYSNHSI
|
G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity.
|
O00231
|
PSD11_HUMAN
|
26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)
|
MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTHLAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVERKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALETIQNMSKVVDSLYNKAKKLT
|
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity.
|
O00232
|
PSD12_HUMAN
|
26S proteasome non-ATPase regulatory subunit 12 (26S proteasome regulatory subunit RPN5) (26S proteasome regulatory subunit p55)
|
MADGGSERADGRIVKMEVDYSATVDQRLPECAKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAVVKMCYEAKEWDLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPIKLRLIDTLRMVTEGKIYVEIERARLTKTLATIKEQNGDVKEAASILQELQVETYGSMEKKERVEFILEQMRLCLAVKDYIRTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSYLSICKHYRAIYDTPCIQAESEKWQQALKSVVLYVILAPFDNEQSDLVHRISGDKKLEEIPKYKDLLKLFTTMELMRWSTLVEDYGMELRKGSLESPATDVFGSTEEGEKRWKDLKNRVVEHNIRIMAKYYTRITMKRMAQLLDLSVDESEAFLSNLVVNKTIFAKVDRLAGIINFQRPKDPNNLLNDWSQKLNSLMSLVNKTTHLIAKEEMIHNLQ
|
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
|
O00233
|
PSMD9_HUMAN
|
26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27)
|
MSDEEARQSGGSSQAGVVTVSDVQELMRRKEEIEAQIKANYDVLESQKGIGMNEPLVDCEGYPRSDVDLYQVRTARHNIICLQNDHKAVMKQVEEALHQLHARDKEKQARDMAEAHKEAMSRKLGQSESQGPPRAFAKVNSISPGSPASIAGLQVDDEIVEFGSVNTQNFQSLHNIGSVVQHSEGKPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR
|
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex PSMD9 is released during the further base assembly process.
|
O00237
|
RN103_HUMAN
|
E3 ubiquitin-protein ligase RNF103 (EC 2.3.2.27) (KF-1) (hKF-1) (RING finger protein 103) (RING-type E3 ubiquitin transferase RNF103) (Zinc finger protein 103 homolog) (Zfp-103)
|
MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQPEVNDLFVLSLVLVNLMAWMDLFITQGATIKRFVVLISTLGTYNSLLIISWLPVLGFLQLPYLDSFYEYSLKLLRYSNTTTLASWVRADWMFYSSHPALFLSTYLGHGLLIDYFEKKRRRNNNNDEVNANNLEWLSSLWDWYTSYLFHPIASFQNFPVESDWDEDPDLFLERLAFPDLWLHPLIPTDYIKNLPMWRFKCLGVQSEEEMSEGSQDTENDSESENTDTLSSEKEVFEDKQSVLHNSPGTASHCDAEACSCANKYCQTSPCERKGRSYGSYNTNEDMEPDWLTWPADMLHCTECVVCLENFENGCLLMGLPCGHVFHQNCIVMWLAGGRHCCPVCRWPSYKKKQPYAQHQPLSNDVPS
|
Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway.
|
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