entry
stringlengths 6
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stringlengths 5
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| protein_name
stringlengths 3
2.44k
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stringlengths 2
35.2k
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O00626
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CCL22_HUMAN
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C-C motif chemokine 22 (CC chemokine STCP-1) (MDC(1-69)) (Macrophage-derived chemokine) (Small-inducible cytokine A22) (Stimulated T-cell chemotactic protein 1) [Cleaved into: MDC(3-69); MDC(5-69); MDC(7-69)]
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MDRLQTALLVVLVLLAVALQATEAGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ
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May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for chronically activated T-lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active.
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O00628
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PEX7_HUMAN
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Peroxisomal targeting signal 2 receptor (PTS2 receptor) (Peroxin-7)
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MSAVCGGAARMLRTPGRHGYAAEFSPYLPGRLACATAQHYGIAGCGTLLILDPDEAGLRLFRSFDWNDGLFDVTWSENNEHVLITCSGDGSLQLWDTAKAAGPLQVYKEHAQEVYSVDWSQTRGEQLVVSGSWDQTVKLWDPTVGKSLCTFRGHESIIYSTIWSPHIPGCFASASGDQTLRIWDVKAAGVRIVIPAHQAEILSCDWCKYNENLLVTGAVDCSLRGWDLRNVRQPVFELLGHTYAIRRVKFSPFHASVLASCSYDFTVRFWNFSKPDSLLETVEHHTEFTCGLDFSLQSPTQVADCSWDETIKIYDPACLTIPA
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Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal. Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol. Cargo protein-binding triggers interaction with PEX5 and formation of a ternary complex composed of PEX5 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex.
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O00629
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IMA3_HUMAN
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Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4)
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MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTVKDAQVVQVVLDGLSNILKMAEDEAETIGNLIEECGGLEKIEQLQNHENEDIYKLAYEIIDQFFSSDDIDEDPSLVPEAIQGGTFGFNSSANVPTEGFQF
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Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.
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O00631
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SARCO_HUMAN
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Sarcolipin
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MGINTRELFLNFTIVLITVILMWLLVRSYQY
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Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis (By similarity).
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O00635
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TRI38_HUMAN
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E3 ubiquitin-protein ligase TRIM38 (EC 2.3.2.27) (RING finger protein 15) (Tripartite motif-containing protein 38) (Zinc finger protein RoRet)
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MASTTSTKKMMEEATCSICLSLMTNPVSINCGHSYCHLCITDFFKNPSQKQLRQETFCCPQCRAPFHMDSLRPNKQLGSLIEALKETDQEMSCEEHGEQFHLFCEDEGQLICWRCERAPQHKGHTTALVEDVCQGYKEKLQKAVTKLKQLEDRCTEQKLSTAMRITKWKEKVQIQRQKIRSDFKNLQCFLHEEEKSYLWRLEKEEQQTLSRLRDYEAGLGLKSNELKSHILELEEKCQGSAQKLLQNVNDTLSRSWAVKLETSEAVSLELHTMCNVSKLYFDVKKMLRSHQVSVTLDPDTAHHELILSEDRRQVTRGYTQENQDTSSRRFTAFPCVLGCEGFTSGRRYFEVDVGEGTGWDLGVCMENVQRGTGMKQEPQSGFWTLRLCKKKGYVALTSPPTSLHLHEQPLLVGIFLDYEAGVVSFYNGNTGCHIFTFPKASFSDTLRPYFQVYQYSPLFLPPPGD
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E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as a regulator of innate immunity. Acts as a negative regulator of type I interferon IFN-beta production by catalyzing 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation (By similarity). Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling. Acts as positive regulator of the cGAS-STING pathway by acting as a E3 SUMO-protein ligase: mediates sumoylation of CGAS and STING, preventing their degradation and thereby activating the innate immune response to DNA virus (By similarity). Also acts as a negative regulator of NF-kappa-B signaling independently of its E3 protein ligase activity by promoting lysosome-dependent degradation of TAB2 and TAB3 adapters.
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O00712
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NFIB_HUMAN
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Nuclear factor 1 B-type (NF1-B) (Nuclear factor 1/B) (CCAAT-box-binding transcription factor) (CTF) (Nuclear factor I/B) (NF-I/B) (NFI-B) (TGGCA-binding protein)
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MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQSWYLG
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Transcriptional activator of GFAP, essential for proper brain development. Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
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O00716
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E2F3_HUMAN
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Transcription factor E2F3 (E2F-3)
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MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS
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Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity).
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O00743
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PPP6_HUMAN
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Serine/threonine-protein phosphatase 6 catalytic subunit (PP6C) (EC 3.1.3.16) [Cleaved into: Serine/threonine-protein phosphatase 6 catalytic subunit, N-terminally processed]
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MAPLDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQFYDLCELFRTGGQVPDTNYIFMGDFVDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL
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Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. During mitosis, regulates spindle positioning. Down-regulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7. Participates also in the innate immune defense against viruses by desphosphorylating RIGI, an essential step that triggers RIGI-mediated signaling activation. Also regulates innate immunity by acting as a negative regulator of the cGAS-STING pathway: mediates dephosphorylation and inactivation of CGAS and STING1. CGAS dephosphorylation at 'Ser-435' impairs its ability to bind GTP, thereby inactivating it.
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O00744
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WN10B_HUMAN
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Protein Wnt-10b (Protein Wnt-12)
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MLEEPRPRPPPSGLAGLLFLALCSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRNPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKSFPHSLPSPGPGSSPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAVGAALRERLGRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCERDPTMGSPGTRGRACNKTSRLLDGCGSLCCGRGHNVLRQTRVERCHCRFHWCCYVLCDECKVTEWVNVCK
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Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin.
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O00746
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NDKM_HUMAN
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Nucleoside diphosphate kinase, mitochondrial (NDK) (NDP kinase, mitochondrial) (EC 2.7.4.6) (Nucleoside diphosphate kinase D) (NDPKD) (nm23-H4)
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MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA
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Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling.
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O00748
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EST2_HUMAN
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Cocaine esterase (EC 3.1.1.84) (Carboxylesterase 2) (CE-2) (hCE-2) (EC 3.1.1.1) (Methylumbelliferyl-acetate deacetylase 2) (EC 3.1.1.56)
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MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL
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Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine. Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins.
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O00750
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P3C2B_HUMAN
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Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta (PI3K-C2-beta) (PtdIns-3-kinase C2 subunit beta) (EC 2.7.1.137) (EC 2.7.1.154) (C2-PI3K) (Phosphoinositide 3-kinase-C2-beta)
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MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHDKEENRAKQNADPSLISWDEPGVDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSLSPQEGPPNHSTSQGPQPGSDPWPKGSLSGDYLYIFDGSDGGVSSSPGPGDIEGSCKKLSPPPLPPRASIWDTPPLPPRKGSPSSSKISQPSDINTFSLVEQLPGKLLEHRILEEEEVLGGGGQGRLLGSVDYDGINDAITRLNLKSTYDAEMLRDATRGWKEGRGPLDFSKDTSGKPVARSKTMPPQVPPRTYASRYGNRKNATPGKNRRISAAPVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRSGSDIQDYFLTGYVWSAVTPSPEHLGDEVNLKVTVLCDRLQEALTFTCNCSSTVDLLIYQTLCYTHDDLRNVDVGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDIDIRLQLMEQKVVRSDLARTVNDDQSPSTLNYLVHLQERPVKQTISRQALSLLFDTYHNEVDAFLLADGDFPLKADRVVQSVKAICNALAAVETPEITSALNQLPPCPSRMQPKIQKDPSVLAVRENREKVVEALTAAILDLVELYCNTFNADFQTAVPGSRKHDLVQEACHFARSLAFTVYATHRIPIIWATSYEDFYLSCSLSHGGKELCSPLQTRRAHFSKYLFHLIVWDQQICFPVQVNRLPRETLLCATLYALPIPPPGSSSEANKQRRVPEALGWVTTPLFNFRQVLTCGRKLLGLWPATQENPSARWSAPNFHQPDSVILQIDFPTSAFDIKFTSPPGDKFSPRYEFGSLREEDQRKLKDIMQKESLYWLTDADKKRLWEKRYYCHSEVSSLPLVLASAPSWEWACLPDIYVLLKQWTHMNHQDALGLLHATFPDQEVRRMAVQWIGSLSDAELLDYLPQLVQALKYECYLDSPLVRFLLKRAVSDLRVTHYFFWLLKDGLKDSQFSIRYQYLLAALLCCCGKGLREEFNRQCWLVNALAKLAQQVREAAPSARQGILRTGLEEVKQFFALNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKLSFQNVDPLGENIRVIFKCGDDLRQDMLTLQMIRIMSKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHGVTGSFKDRPLADWLQKHNPGEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMFGNIKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLSCGIPELSDLEDLKYVYDALRPQDTEANATTYFTRLIESSLGSVATKLNFFIHNLAQMKFTGSDDRLTLSFASRTHTLKSSGRISDVFLCRHEKIFHPNKGYIYVVKVMRENTHEATYIQRTFEEFQELHNKLRLLFPSSHLPSFPSRFVIGRSRGEAVAERRREELNGYIWHLIHAPPEVAECDLVYTFFHPLPRDEKAMGTSPAPKSSDGTWARPVGKVGGEVKLSISYKNNKLFIMVMHIRGLQLLQDGNDPDPYVKIYLLPDPQKTTKRKTKVARKTCNPTYNEMLVYDGIPKGDLQQRELQLSVLSEQGFWENVLLGEVNIRLRELDLAQEKTGWFALGSRSHGTL
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Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades.
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O00754
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MA2B1_HUMAN
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Lysosomal alpha-mannosidase (Laman) (EC 3.2.1.24) (Lysosomal acid alpha-mannosidase) (Mannosidase alpha class 2B member 1) (Mannosidase alpha-B) [Cleaved into: Lysosomal alpha-mannosidase A peptide; Lysosomal alpha-mannosidase B peptide; Lysosomal alpha-mannosidase C peptide; Lysosomal alpha-mannosidase D peptide; Lysosomal alpha-mannosidase E peptide]
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MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG
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Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.
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O00755
|
WNT7A_HUMAN
|
Protein Wnt-7a
|
MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYARVWQCNCKFHWCCYVKCNTCSERTEMYTCK
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Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes (By similarity). Required for normal neural stem cell proliferation in the hippocampus dentate gyrus (By similarity). Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation (By similarity). Promotes formation of synapses via its interaction with FZD5 (By similarity).
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O00757
|
F16P2_HUMAN
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Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase)
|
MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMVQSSYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQKNQAGS
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Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.
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O00762
|
UBE2C_HUMAN
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Ubiquitin-conjugating enzyme E2 C (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme C) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme C) (UbcH10) (Ubiquitin carrier protein C) (Ubiquitin-protein ligase C)
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MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP
|
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit.
|
O00763
|
ACACB_HUMAN
|
Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta)
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MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGALNVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVARLELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIKLKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRVEHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVPILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPKDILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFKYLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSRAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVKQEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIRENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
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Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism. Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA. Through the production of malonyl-CoA that allosterically inhibits carnitine palmitoyltransferase 1 at the mitochondria, negatively regulates fatty acid oxidation (By similarity). Together with its cytosolic isozyme ACACA, which is involved in de novo fatty acid biosynthesis, promotes lipid storage (By similarity).
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O00764
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PDXK_HUMAN
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Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase)
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MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL
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Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (Probable). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions.
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O00767
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SCD_HUMAN
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Stearoyl-CoA desaturase (hSCD1) (EC 1.14.19.1) (Acyl-CoA desaturase) (Delta(9)-desaturase) (Delta-9 desaturase) (Fatty acid desaturase)
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MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG
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Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).
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O00835
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ERCC3_DICDI
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General transcription and DNA repair factor IIH helicase subunit XPB (TFIIH subunit XPB) (EC 3.6.4.12) (DNA excision repair cross-complementing protein-3 homolog) (DNA repair helicase repB) (DNA repair protein B)
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MSSGDSNLKRRRGGNTGQSSKSYNTWTDYEEDLEESGEFNQSIKKTTNTSSATLTSSEEKGSLLDYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITVLGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTGFIINKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNSDQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFRNDTVNPNLNIDLKPTTMIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLSGITAACTVKKSILVLCTSAVSVEQWKYQFKLWSNIEERQISKFTSDNKEKISNVAGVTITTYTMVAFGGRRSAESLKIMNEITNREWGLVLLDEVHVVPAAMFRKVLTVTKAHCKLGLTATLLREDEKIQDLNFLIGPKLYEANWLDLQKAGFLANVSCSEVWCPMTAEFYKEYLINDSQGKKKLLYTMNPNKFRACEYLIRFHEQRGDKIIVFSDNVYALQKYAKGLGRYFIYGPTSGHERMSILSKFQHDPTVRTIFISKVGDTSIDIPEATVIIQVSSHYGSRRQEAQRLGRILRPKPKSDGLYNAFFYSLVSKDTQEMYYSTKRQQFLIDQGYSFKVISELPGIDQEVNLKYSSKQDQLDLLAQVLGEGEDSGKNEILEEDFDDITRGAKKSKSSAPTVSRTTGGSTRALSGGNDMNYMEYQAPAIYKSIPTQHALFKQRAKNKQ
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ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/repB, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/repB is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
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O00841
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CUDA_DICDI
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Putative transcriptional regulator cudA
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MNQSQNFHNIDLGHYGAQGSNQSFNNNNNGNNGMMMNQQQMQQHVVPHLHHLQQQQQQPQQQQLRNVPDYSNSPNGTTNGSTMSPNCINTNNNNNNNNNNNNNSNNNNNNNNNASNNLTSNKSSSTNTPQIGQLQASPANLTNSPSAISSPITISNNSSLNSPSTTSSPNLLLNGTSNKRIMISQQTCLVEEKFSKNGVQKNVHVVVKNNPFLLTLSLLDSSLNFHQLTPEVQLVYDSESLKEVDSATVKPLEYKTRANEEGDQLTIELRIKVLSSQLEDMLFRAKVKIVDPRTRKETHGLSVITHPIRVVSKPDQVKKKAKKRKRAPTDSLMDTLNRIEHQQKEQQRLLKKLCYHDKENNIIQLIQQQQQQQQLLNNVTNNINNNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTSTTTTTTTTTSSCNNNNNNNNENNEHIVKIENTECNNNNNNIINNTENDENINKPILNSKDEFQSAFKEFIGAFKQLQCLDPDGADGAFKINTCANDAQTMCEILEMVKVELKKDENFKDKCGGSSGGACGENNPDNPCSCKVCPYKQKVDHINQSYETYFNMFNPSNSNSVVPQQSQQLQQQQIQQQQQSQQQVQQQQQQQMQQQPQQQQQQPQQQQQNQQQGQQPQQQQQQGQLDYTTYIDPQLQMQQQLQMQQAAQQQYMQQTMDQQQQQQYYMQQYHLQQQQQQQQAQRYLMQQQYMQQQAQQQQQQHQQVAIQQQQQQNQQQNQQQNQQQQNQSPQNQQSLDFQNANNFIDFNSGLGFMNFPNINFGDMGFSAV
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Essential for normal culmination. May function as a transcriptional regulator.
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O00899
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GAPA_DICDI
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Ras GTPase-activating-like protein gapA (IQGAP-related protein gapA)
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MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQIIAPILENNVVNAPDLNLELNAVQVYQNMISEQEIQTGAKSTLNRGLAEDQIIQLKEVQSILEPRVEKCIQICERFFTGIIQSLNRLPYGIRWICKQIQSIAQKNFDSKPDEIAKVIGYFVYYRFINLAIVTPDAFEILDKELSITSRKNLVNIAKVLQNLFTLKTFQNQGSERWMQPLNKWILSKTSIVRQYLEDLIQVTDPSEYLRVDKYNELTLKLNPVVVISLGEISQTHRLLIANLAALKMKEKEDPLELILKALPAPLEVVDENDREIQLTLINRFKENIEKEISISASLLAETKELVISVLRSIPIQQKQQQQQHDDEKRDDLISILQNAIKHGKETNNPQLSSNAEKIINNLKKMEAEGSIQSENNQYEGFIKVIALEVINRQEIREQQRKERMRLTIALRDLRKHQSYLNDQIQHYTSYLKDVLLHYGPKDKKKSTKPMKISFKELTKKGVIVESDIPKLSHGSTSFYISSDAPGIFDIEARIGVASVGTLSLSLDDLLDKSSAGIPYLKLENIVLDVNMTLHLLNRHFLKNI
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Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA in the absence of rgaA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of the dividing cell.
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O00909
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ARF1_DICDI
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ADP-ribosylation factor 1 (EC 3.6.5.2)
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MGLAFGKLFSRFFGKKDMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEFKNINFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEACDELTKMLNEDELRDAVLLVFCNKQDLPNAMSVAEVTDKLNLHSLRSRKWYIQSTCATSGDGLYEGLDWLSNTLTSSSK
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GTP-binding protein involved in protein trafficking may modulate vesicle budding and uncoating within the Golgi apparatus.
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O00910
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STATA_DICDI
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Signal transducer and activator of transcription A (Dd-STATa) (STAT5 homolog A)
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MSSAEFSMDDFEDTFDSNATISTKDLFEGSDRLPLNQSINTTIQNLYLPNGGFAIGDQSQQQYYQAMPPLNQSDQFNLGRSNNLTPRTNQLQQLQQQQQQQQQPQQQQQQQTYGTQSPIHMSQTPSSPLSSPLPSPTPFSRQQSYNNNNSNNTSSSQNYNNNNININNNNNNNNTNNNNNNNNGNNSNGNNGNNNNNNNNNNNNNTNNNNNNNQQQQQQQQQQQQQQQQQQQQQQQGNPNLSSPQPILDTIYKLLSEQEQTLVQMIHEQSLLLNRLPPTLDENSLAPLKSLSQKQITLSGQMNTEMSALDATKKGMILEPTDLAKLFALKQDLQIQFKQLSLLHNEIQSILNPQHSAPKPNVALVLKSQPFPVVISKGKQLGENQLVVLVLTGARSNFHINGPVKATMICDSHPTNKNNPTTPLEMDSQPIYPATLTAHFPLKFLAGTRKCSVNLKFGVNIRDLDNVTTTVESDASNPFVVITNECQWEGSAGVLLKKDAFDGQLEITWAQFINTLQRHFLIATKQDPVRPKRPLSSYDLKYIQTHFFGNRSIIHQQDFDKFWVWFGKSMQTLRYQRHISTLWQEGIIYGYMGRQEVNDALQNQDPGTFIIRFSERNPGQFGIAYIGVEMPARIKHYLVQPNDTAAAKKTFPDFLSEHSQFVNLLQWTKDTNGAPRFLKLHKDTALGSFAPKRTAPVPVGGYEPLNS
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Transcription factor that binds to 5'-TTGAATTGA-3' elements in the promoter region of target genes. Functions as repressor of the ecmB gene. Regulates the differentiation of prestalk cells during development.
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O01326
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RNC_CAEEL
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Ribonuclease 3 (EC 3.1.26.3) (Protein drosha) (Ribonuclease III) (RNase III)
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MSDEKISMTLNFPKHKRARRKKYQKEYQERHKEEMMQQLGRRFQNQPSTSSAPPDTVEKIPLPTESTSALPFGDSPRLTEKDYETNYMIDPPVVSTHSAELIKSNRVVIKAEEAEKYMMIKAKSTTSKILQDFQTKILETVKTKRRLQADVPYIIHPCHSMKGRKTPKQKGGDESFTASDVSDDSNDSQDEASTSEPTNRQAPEADKTGEVKDEKQTCNRRNQQRKAKRLRNFEEKERQITLLKKGIDRKKTHPNGIHPDISFNEKGLGNEGPECRCPEPIKTCGLKHGYYAGEDKAIDCKKSNGENLHYYTLRVTPLPSENQLYRTHMAINGEEFEFEGFSLITHAPLPDCMTRAPICKYSMDYEFQLVEEFMPDECFDPEDCDMLFEYIFHEIFEMLDFELRPKHIPSDVESCPMIHIMPRFVQTKDDLVQLWSSKTVLAYFTSKGSSEIMSPEDVNRLCDAQIDQFTRNTSKHKQSIVLNTKFKPSAIRADWFERDEEKKEVYVVHNAIRAQTYTAISLPRIAFLEKTLNKMIQEKQSSGVYNKDFEKTKNELEHLKRENRSARNLKLREPVAGFIETGLKPDVAAHVVMTILACHHIRYNFSLDVFEEVIEYKFNDRRVIELALMHSSFKSHYGTPIDHVKNMITNCGYRRKYGAEDKREKKRVAGIMSLFNIMKGTSGGEPILHNERLEYLGDAVVELIVSHHLYFMLTHHFEGGLATYRTALVQNRNLATLAKNCRIDEMLQYSHGADLINVAEFKHALANAFEAVMAAIYLDGGLAPCDVIFSKAMYGHQPVLKEKWDHINEHELKREDPQGDRDLSFITPTLSTFHALEERLGIQFNNIRLLAKAFTRRNIPNNDLTKGHNQRLEWLGDSVLQLIVSDFLYRRFPYHHEGHMSLLRTSLVSNQTQAVVCDDLGFTEFVIKAPYKTPELKLKDKADLVEAFIGALYVDRGIEHCRAFIRIVFCPRLKHFIESEKWNDAKSHLQQWCLAMRDPSSSEPDMPEYRVLGIEGPTNNRIFKIAVYYKGKRLASAAESNVHKAELRVAELALANLESMSFSKMKAKNNSWFQNMRRRLEQDTSD
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Executes the initial step of microRNA (miRNA) processing in the nucleus, that is the cleavage of pri-miRNA to release pre-miRNA. Involved in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in fertility. Required for the function or synthesis of the let-7 miRNA.
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O01346
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EGH_DROME
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Beta-1,4-mannosyltransferase egh (EC 2.4.1.-) (Protein egghead) (Protein zeste-white 4)
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MNSTTKHLLHCTLLITVIVTFEVFSGGIKIDENSFTLVDPWTEYGQLATVLLYLLRFLTLLTLPQVLFNFCGLVFYNAFPEKVVLKGSPLLAPFICIRVVTRGDFPDLVKTNVLRNMNTCLDTGLENFLIEVVTDKAVNLSQHRRIREIVVPKEYKTRTGALFKSRALQYCLEDNVNVLNDSDWIVHLDEETLLTENSVRGIINFVLDGKHPFGQGLITYANENVVNWLTTLADSFRVSDDMGKLRLQFKLFHKPLFSWKGSYVVTQVSAERSVSFDNGIDGSVAEDCFFAMRAFSQGYTFNFIEGEMYEKSPFTLLDFLQQRKRWLQGILLVVHSKMIPFKHKLLLGISVYSWVTMPLSTSNIIFAALYPIPCPNLVDFVCAFIAAINIYMYVFGVIKSFSLYRFGLFRFLACVLGAVCTIPVNVVIENVAVIWGLVGKKHKFYVVQKDVRVLETV
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Glycosyltransferase with a proposed role in glycosphingolipid biosynthesis. Neurogenic protein implicated in epithelial development. Critical component of a differential oocyte-follicle cell adhesive system.
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O01367
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HOW_DROME
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Protein held out wings (KH domain protein KH93F) (Protein muscle-specific) (Protein struthio) (Protein wings held out) (Putative RNA-binding protein) (Quaking-related 93F)
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MSVCESKAVVQQQLQQHLQQQAAAAVVAVAQQQQAQAQAQAQAQAQQQQQAPQVVVPMTPQHLTPQQQQQSTQSIADYLAQLLKDRKQLAAFPNVFTHVERLLDEEIARVRASLFQINGVKKEPLTLPEPEGSVVTMNEKVYVPVREHPDFNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDANRGKPNWEHLSDDLHVLITVEDTENRATVKLAQAVAEVQKLLVPQAEGEDELKKRQLMELAIINGTYRDTTAKSVAVCDEEWRRLVAASDSRLLTSTGLPGLAAQIRAPAAAPLGAPLILNPRMTVPTTAASILSAQAAPTAAFDQTGHGMIFAPYDYANYAALAGNPLLTEYADHSVGAIKQQRRLATNREHPYQRATVGVPAKPAGFIEIQ
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Required for integrin-mediated cell-adhesion in wing blade. Vital role in steroid regulation of muscle development and to control heart rate. Required during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.
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O01382
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DRICE_DROME
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Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
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MDATNNGESADQVGIRVGNPEQPNDHTDALGSVGSGGAGSSGLVAGSSHPYGSGAIGQLANGYSSPSSSYRKNVAKMVTDRHAAEYNMRHKNRGMALIFNHEHFEVPTLKSRAGTNVDCENLTRVLKQLDFEVTVYKDCRYKDILRTIEYAASQNHSDSDCILVAILSHGEMGYIYAKDTQYKLDNIWSFFTANHCPSLAGKPKLFFIQACQGDRLDGGVTMQRSQTETDGDSSMSYKIPVHADFLIAYSTVPGFYSWRNTTRGSWFMQSLCAELAANGKRLDILTLLTFVCQRVAVDFESCTPDTPEMHQQKQIPCITTMLTRILRFSDKQLAPAGRV
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Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro.
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O01404
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PHM_DROME
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Peptidylglycine alpha-hydroxylating monooxygenase (dPHM) (EC 1.14.17.3)
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MPRISEIAASVGLLLLIGVISVDGLVKEGDYQNSLYQQNLESNSATGATASFPFLMPNVSPQTPDLYLCTPIKVDPTTTYYIVGFNPNATMNTAHHMLLYGCGEPGTSKTTWNCGEMNRASQEESASPCGPHSNSQIVYAWARDAQKLNLPEGVGFKVGKNSPIKYLVLQVHYAHIDKFKDGSTDDSGVFLDYTEEPRKKLAGTLLLGTDGQIPAMKTEHLETACEVNEQKVLHPFAYRVHTHGLGKVVSGYRVRTNSDGEQEWLQLGKRDPLTPQMFYNTSNTDPIIEGDKIAVRCTMQSTRHRTTKIGPTNEDEMCNFYLMYYVDHGETLNMKFCFSQGAPYYFWSNPDSGLHNIPHIEASTL
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Monooxygenase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-hydroxyglycine) intermediate. C-terminal amidation of peptides is required for normal developmental transitions and for biosynthesis of secretory peptides throughout the life.
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O01422
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CSN2_CAEEL
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COP9 signalosome complex subunit 2 (Signalosome subunit 2)
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MGDEYMDDDEDYGFEYEDDSGSEPDVDMENQYYTAKGLRSDGKLDEAIKSFEKVLELEGEKGEWGFKALKQMIKITFGQNRLEKMLEYYRQLLTYIKSAVTKNYSEKSINAILDYISTSRQMDLLQHFYETTLDALKDAKNERLWFKTNTKLGKLFFDLHEFTKLEKIVKQLKVSCKNEQGEEDQRKGTQLLEIYALEIQMYTEQKNNKALKWVYELATQAIHTKSAIPHPLILGTIRECGGKMHLRDGRFLDAHTDFFEAFKNYDESGSPRRTTCLKYLVLANMLIKSDINPFDSQEAKPFKNEPEIVAMTQMVQAYQDNDIQAFEQIMAAHQDSIMADPFIREHTEELMNNIRTQVLLRLIRPYTNVRISYLSQKLKVSQKEVIHLLVDAILDDGLEAKINEESGMIEMPKNKKKMMVTSLVVPNAGDQGTTKSDSKPGTSSEPSTTTSVTSSILQGPPATSSCHQELSMDGLRVWAERIDSIQSNIGTRIKF
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Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-3/katanin targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3.
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O01427
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AIR2_CAEEL
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Aurora/IPL1-related protein kinase 2 (EC 2.7.11.1) (Serine/threonine-protein kinase aurora-B)
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MENKPPVINLPEKETVNTPQKGGKFTINDFEIGRPLGKGKFGSVYLARTKTGHFHVAIKVLFKSQLISGGVEHQLEREIEIQSHLNHPNIIKLYTYFWDAKKIYLVLEYAPGGEMYKQLTVSKRFSEPTAAKYMYEIADALSYCHRKNVIHRDIKPENLLIGSQGELKIGDFGWSVHAPSNKRQTMCGTMDYLPPEMVNGADHSDAVDLWAIGVLCYEFLVGKPPFEHEDQSKTYAAIKAARFTYPDSVKKGARDLIGRLLVVDPKARCTLEQVKEHYWIQGMMEAKIRAEKQQKIEKEASLRNH
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Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation. Required for histone H3 phosphorylation during segregation of homologous chromosomes in meiosis and mitosis. Required for histone H3 'Ser-10' phosphorylation. Phosphorylates tlk-1 at 'Ser-634', which enhances its activity. Phosphorylates zen-4 at 'Ser-680'(PubMed:15854913). Required for the recruitment of bub-1 to the ring-shaped domain between chromosomes during meiotic anaphase I. Also required for the localization of the condensin I complex subunit smc-4 to mitotic chromosomes. Acts at the spindle midzone and the midbody to prevent cleavage furrow regression upon chromatin obstructions during cytokinesis.
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O01479
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TMOD_CAEEL
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Tropomodulin (Tmod-like protein) (cTmd1) (Uncoordinated protein 94)
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MSQAKTDYYSEEKTFSAPSANSQQGTQLPSKVYNKGLKDLEDNDIEGLLSSLSIDELEDLNNDFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWEDVCPYTPGQKRGKVYDSDSGRNSEEPENGKMEMPIEIDLDDDEEELECALVTAPEKDLVDLAGILGMHNVLNQPQYYNALKGKTQDESTGTTFNGIMQSYVPRIVPDEPDNDTDVESCINRLREDDTDLKEVNINNMKRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLLRSTLVTQSIVEFKADNQRQSVLGNQVEMDMMMAIEENESLLRVGISFASMEARHRVSEALERNYERVRLRRLGKDPNV
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Acts as the pointed end capping protein which maintains the length and dynamics of the actin filament. Blocks the elongation and depolymerization of the actin filaments at the pointed end (By similarity).
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O01498
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STAM1_CAEEL
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Signal transducing adapter molecule 1 (STAM-1) (Prion-like-(Q/N-rich) domain-bearing protein 19)
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MKKQKSFPMSAYEDLLGKITAPTITVENWEGILAFCDMINNDFEGSKTGIKSLRKRLNNRDPHVVLLAISVLDSCWANCEERFRKEVSSAQFINELKALCTSSQRQVAEKMRLTVQKWVDTECKTEQSLSLIVTLHKNLVADGYSFVVDDPKSKTKAIDAKFANDPNYVGSAQEEEAIAKAIAASLADAEKQEKAKKSTSTMYPSAKASSPAVQTNSNIPEKNVRALYDFEAAESNELSFVAGDIITITDESNPHWWTGRIGTQQGLFPSSFVTNQLDDLKSKETDSSQKAPEVVASINEAILVRCLQVLHECDPTGERQDPEDLAQLEAASYAQGNLIDAHLASIDRQSNSLAQIDVAIRDVLALYDDAIQKGGFQHQSQGMYQQPMQQYNYQQPPNRAYYPPTGPVQQQQPQQYPPQHYPAPGAQPQYACPPNSVPQPQQQQQQWPAPSSQPQQY
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Binds, sorts and targets the polycystin complex (lov-1 and pkd-2) for lysosomal degradation, acting on early endosomes located at the ciliary base. Functions in the germline together with the ephrin receptor (vab-1) signaling pathway to negatively regulate MAPK activation. May have a role as a positive regulator of meiotic maturation in oocytes, acting independently of vab-1.
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O01501
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CCNE_CAEEL
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G1/S-specific cyclin-E
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MAGRKSSRTAERVPTTQKPERKSAILSPHDELRERLLETAIDMKENIPQRNTRNSSVGSQKSDCSETRKRRSTKEGPAAKRHSGEKHRNGSREDSLEYISEYSDDREVGSSSSQSSRTRGQPLPAMPEEEEVFDKSSSSDNLAESEESHEMVRLEERQDIEEEIEDDFDDEEEDVVNDKEEYEEIESEDEDDYPVQNEGFAVTKRLMNDEHMVTAPTFLSTAKCDGIGSPTKVWSLMVKRDEIPRATRFLLGNHPDMDDEKRRILIDWMMEVCESEKLHRETFHLAVDYVDRYLESSNVECSTDNFQLVGTAALFIAAKYEEIYPPKCIDFAHLTDSAFTCDNIRTMEVLIVKYIGWSLGPITSIQWLSTYLQLLGTGKKNKSDHYEEQNMYVPELLRSEYLEMCKILDFLLFEIDSFTFSYRTIAAAVLFVNYEPTCAVEKATGFMQAQLEKVIEYVEPVCRAFAKQRQLLDDVIPKHESIKSDDSHNIQVYVKRSSMEPIVKSERERIQHLKARRLHPQRLF
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Essential for the control of the cell cycle at the G1/S (start) transition. In association with cdk-2, regulates proliferation, quiescent state and cell fate during the development of several cell lineages. In the embryo, initiates the establishment of cell polarity through the recruitment of the centrosomal proteins spd-2 and spd-5 during prophase. During the development of the vulva, controls the onset of vulval cell terminal differentiation by controlling the duration of G1 phase. During hypoderm development at early larval stages, controls syncytial fate of seam cell daughter cells. Involved in the progression of cell division in the intestinal lineage in larvae, and in particular in endoreplication, a specific growth pathway in the intestinal epithelium, required for feeding and gut development in growing larvae. By controlling the activity of translational repressor gld-1, regulates the pool of germline stem cells and the size of the mitotic zone by preventing entry into meiosis. In addition, repression of expression by gld-1 prevents mitosis re-entry in meiotic germline cells.
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O01510
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SMG1_CAEEL
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Serine/threonine-protein kinase smg-1 (EC 2.7.11.1) (Suppressor with morphogenetic effect on genitalia protein 1)
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MITSRNNDIGNLIEQFRQRDTPQKERKAILARIEEILQTTKNVESLCVKWTYLLDNLCWPSLTKHDRNDMKTLAGKVIRLVGVLLFDTESYPEFLIYLGTLYQSVTKKSEETRADIVFSVYFIVGVISQKTENRLIATDTENVEKSLDWIIKVLPNSSISVYNHCLKGFVLVANTFPNVYAAMFESTLRAILTNLPDFNSHEKNFELLIDTVMRFSDQLNEKPHLAEEMVRIIRPDIKKNGLGNMRELKKRMKLTMALVKMAKSQKMLEETNQMISEMSIELEENGGKWSSASLITIVCDVFNELLILGKDDVKLQKGVEESLCNVLKDLNLSNQSTMEKQAFFNSLAKIVKQLPAESQVKTRVHQIVFNTETGLFTPKNRDNRMFGHNMIYKDLINLVSVLLTPTSLNHLQATYTDLRKIMIDSMSRLKQSEDTPYSDNIRWNESILLLFFSSLQSISCAKSSLIVMMGIRPSIFEFFSSELPLTEYWLASNHPEVYHLFITIFVGHLKAHDFYIVQSDYIVRGDSIGQSIGQTKRDYARKQVVALQKIINNFGDKLWKKTRLMISSWLHSLIATACEHQIGSDSFSQREWVRLRNTVIHQSVLTWNNECVNQALTILSTATKWSELTSDIHRDIADKTKKAKWKEATTIWESGDCNTYIRQSMSTVYQMSQERQQKTITSTSFGAEEFIIITNFLLKQATPTTFKKGQNSWMDEVLETFTQGCRTLEKPDSYVPETFIEKWDWIINQTANFCIVNKMKTPLGKPMQTFAAFENEIKRLAKEVIVRKNSDKKLNKSSTEDPNQSPPLKYSVQWLRVHLLLKLIVVLEKLMNSAIHGGSSVFNLTEIPVSSRQFFTVNAASCEVWLNRVYYPALLVAYFNGYYGLVIRFGSNALSHFARQKDGDNDKKIVNGVCTASLMSLSMAVLGEPMEIVGLRRKVREEFGTDMGQSLMEALGEMANARYETALVALEAVLVTDAATNETLKMIIQLAMVDILNRIRLPQATDYYKVVLFGEESNDSTITEDFRSVELLTKFEKLNNTVNEKRQVVDWSARERFQFVESAFSQTMRRTELLDIQKDFSAMGALALSADSSCKLYSDISSTSLIIANLVNKMTGVSQWKNKLTDTEIFDRNEEGNDGDKLAICRKLMHWGRHTKSNRGQSCAAHSEIIRLSRKTSNCELAFFHINSAIRGEKLAAWQRLEVERQRLKLVKTQNLDVRIREMNEVFGSLAEVFTTSCQLKSDFQMVDGMIKEKMISEGYNEDIAKREEHMSRASIQLADFFQSLPELENVLAPNLFPTIIWSELQRRSDSLSAGYHGIVGSLFHLASEMCPSLAKAHLKMARWAYEIAKIKNFPAENLSFYKFGKDETENEELLKSLEATSLVNLEKLVRAAISDDLRANNILAPNSHFMHIWKMVRDHRTKFLSIAVTSYFQFIQNMSGDCDNLPYSKKEETTLATLRILELLVKHGDVLIDVINDGLNKTNVHIWKEILPQLFARLSHPSEHIRKTLVDLISKICTAAPHAVVFQVVSGAASSSTDGEELEEQQNDDRNRVRACCEKLETNMSQSYPNLVKDVRQFVAELERINLLNEEKWSVVMGTMEHEMEKRLSLIRTENAKTESALHLTASVKNDIIVKRTQLLTRQIFDVLDELYQQTVIEPPKSKNEEEFVTAFAEVLTNAFQESRISRTTSPEKSWIPFKNLIANFVHRNSKKGMQTFETEDISPYLASLSNSCVPMPGQESVEFDRVVSISRVARQVTILPTKTRPKKLGFVGSDGKQVAFLFKGREDLHLDERVMQFLRLCNVMLQPGKGKHRQSVAAYQAHHYAVIPLGPRSGLIKWVEGATPMFHIYRKWQMKEKALKQATKKNGETVPEIERPSNMYHNMIRLAFADHKIDSSITSDRSKWPAEILEEVFESLTAKTPTDLISRELWMRANDATTWWSVTKRYSRSLAVMSMVGSVLGLGDRHLDNLLVDLKWGHVVHIDYNICFDKGKNLRIPETVPFRLTRNMRHALGPSEMYGTFRESCVHVLSTLRSGHQVLTMLLDAFVFDPLVDWTSHEHTATSGVSLALQLAVYGSNWKTKAKERLTDAMELLNLRMSEVQTLWLANRDDLLHWMKQVTECLLIENSMLGANAIYAQQRVKAGTELREAVTRHHALAKELRPLIRVIGKEREEFADYLKFYKQALFDPLLKGHSALRNELDIDTCVYNFNIVMQNIDNVFGALVNLSFTPIETITSRTSQQEFKPPPGLENVWVVKQDQQENSQAREVVRRVERRLNGWLDGSAGPDRKLSPREEADILIAEATSTPNLSQMYEGWTAWV
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Serine/threonine protein kinase involved in mRNA surveillance. Recognizes the substrate consensus sequence [ST]-Q. Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating smg-2.
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O01583
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MRCK_CAEEL
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Serine/threonine-protein kinase mrck-1 (EC 2.7.11.1) (Myotonic dystrophy kinase-related CDC42-binding kinase homolog)
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MAEPPPDDSAPVRLKTLENIYMDGPSKKPEALSFETLIDSLICLYDECCNSTLRKEKCIAEFVESVKTVISKAKKLRLSRDDFEVLKVIGKGAFGEVAVVRMRGVGEIYAMKILNKWEMVKRAETACFREERDVLVYGDRRWITNLHYAFQDEKNLYFVMDYYIGGDMLTLLSKFVDHIPESMAKFYIAEMVLAIDSLHRLGYVHRDVKPDNVLLDMQGHIRLADFGSCLRILADGSVASNVAVGTPDYISPEILRAMEDGRGRYGKECDWWSLGICMYEMLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDWVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIRDSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCLQETQPPRVLAAFTGNHLPFVGFSYTHGSLLSDARSLTDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSSDSAFSSTMGRGDLMISMNNDYEMSNSSLMRQEMISRQSTPSYENAILLHDHQVPKRVDDLRYKQKPMKTASGIFSPVSISAMERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEERRPLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDRQNKMQDVKNEIRLVLDMRDPDFTVCGVSEADVIHAQKGDIPKIFRVTTTQILNSSSEYSSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRSKLADRKAFLVKEVFDVTTLPSIRVAQCCAIIDRSKIVIGFSDHGLYCIEISRQLLIPVGGEKENKQRCVETVEYDEAEQLLMMIVGPAKDRHVRIVPSAALDGRDLKWIKVNDTKGCHLLAVGTNNPGGRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLAMPGTPQSIAIFNGRLYVGFSHSFRSWSLVGVDSSPVGSGDASGAVLQHISLVNMEDTSLQFLNQQTSYEAKLIVNVPGSPDEYLLVFNMIGLYVNEMGRRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRSAKPLSGDGILSTCLCNDSPIFVLLQNVLQDQDSIEVPVNLASGSTDGRKVTRRKFTFRTIGKDDRSASERRSHIQISTPSDFMHIVHMGPAPVMELQQNFIDLQSNHSHTSSDKDSLNRSVNND
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Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation. Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation.
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O01658
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NO66_CAEEL
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Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66) (Jumanjic domain protein 1)
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MGKKKNSNKSAAAAPAVKHNDRWSSIELGEAKSAAVSHYKEPSKEPKFVHPAKLEKVKRIHDGLNIDRVLSHGPVPKQNGGTKRKHVEVTTQKLENKKPKVEVKKEDEKSKNKKMKNQNKHTALVQNETSTRSTYFVEEPDNENKVTLISNGREIAFKKTEVVESDDEQMIGLDSDEELEDEDETDIDEDEMMIDPKDIERYINFESVEDEEDMEDEEIEDEEFEDEEFEDEEEEADEQEEEEEDVSDEESVVSEMDADSDDEGFIAGKDREAHVISKDKFTRNAPAVDFDKFPFTDEDSVVTSSRAFGFMISPCDVQTFFDKFYQSNVLVVRRKQPTYFGNLFSTARLGELLEKNHLEYGRNINIAQYKNGVRTTLNGQGRAYPQIVKQHLHNMCSVQLVNPQTYDDRIWYLCEVIQEQFGCFVGANTYLTPAGSSGFAPHWDEIDAFLLQVEGRKYWRVWAPESAEEELPLESSDNFTEDDMKGREPVFEGWIEKGDMIYIPRGYIHQARTDSKVHSLHVTVSTGRQWSFANLMEKVVPEAIGVLTDTRHKLRRGLPTGLFDMGGVIDLDYSQEDHFVEKFKMVVDRHMSMLRNLVADQLLESSVDSLAKEFMKQALPPRLTEQEKKLSVLGSSTNLLGDDLVDFTARTKVRLIRRHTQRLLMESEDACFISHRINNSRLFEGRPEQIVEYPISGIDAYRVLSNSYPEWRTLYEIFSLRETKTKSRKENLAAIQLLFQIGVLLVKN
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Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Mediates response to multiple stress stimuli, including heat shock and osmotic, oxidative, and ethanol stress. {ECO:0000250, ECO:0000269|PubMed:20057358}.
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O01668
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OPS6_DROME
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Opsin Rh6 (Rhodopsin Rh6, long-wavelength)
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MASLHPPSFAYMRDGRNLSLAESVPAEIMHMVDPYWYQWPPLEPMWFGIIGFVIAILGTMSLAGNFIVMYIFTSSKGLRTPSNMFVVNLAFSDFMMMFTMFPPVVLNGFYGTWIMGPFLCELYGMFGSLFGCVSIWSMTLIAYDRYCVIVKGMARKPLTATAAVLRLMVVWTICGAWALMPLFGWNRYVPEGNMTACGTDYFAKDWWNRSYIIVYSLWVYLTPLLTIIFSYWHIMKAVAAHEKAMREQAKKMNVASLRNSEADKSKAIEIKLAKVALTTISLWFFAWTPYTIINYAGIFESMHLSPLSTICGSVFAKANAVCNPIVYGLSHPKYKQVLREKMPCLACGKDDLTSDSRTQATAEISESQA
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Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
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O01683
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SSP1B_CAEEL
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FACT complex subunit ssrp1-B (Facilitates chromatin transcription complex subunit ssrp1-B) (HMG box-containing protein 3) (Structure-specific recognition protein 1-B)
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MTELKFKGVYVEDIGHLTCGTLTLTENSINFIGDKGGKSVYITGTDVDKLKWQKLGNKPGLRVGLSDGGAHRFGGFLDDDLQKIQSFTSSNWSKSINQSNLFINGWNYGQADVKGKNIEFSWENEPIFEIPCTNVSNVIANKNEAILEFHQNEQSKVQLMEMRFHMPVDLENEEDTDKVEEFKKAVLAYAGLEAETEQPICLLTDILCTTPRGRYDIKVYPTSIALHGKTYDYKIPVKTINRLFLVPHKDGRQVYFVLSLNPPIRQGQTHYSYLIFEFGKDEEEDLELSLTDEQLDYFNGNLQREMTGPIYETISILFKSICNLKVTVPGRFLGSSGTPAIQCTHRQNLGLLYPMEKGFLFIQKPVMYIRFEEISSCHFARSDSGTVTRTFDFEIDLKTGSSLTFSAMDKEENNKLFDYLNKKEIKIRNSHRIDNKSAGYGSSDEDDIDPYKSTVKAEGREQDDDSDDESTDEDYDLDKDMKKQKNDKDSSEGSGSEPDDEYDSGSEKDASGTGESDPDEENIEPKKKESKEKKNKREKKEKPVKEKAVKKGKKTKDPNEPKRATTAYIIWFNANRNSMKEDGDTLGDVAKKAGAKWKSMSADDKKEWNDKAAQDKARYEAEMKEYKKNGGGVEKASGPSTKKSSDQSPGKQFKSKEHISDTDDSDDDEPLKAKKDESDAASESSGESD
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Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity). In embryos, may function redundantly with hmg-4 to promote cell cycle progression and development of the anterior pharynx. In the germline, acts non-redundantly with hmg-4 to play a role in oocyte development.
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O01700
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DLK1_CAEEL
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Mitogen-activated protein kinase kinase kinase dlk-1 (EC 2.7.11.25) (DAP kinase-like kinase) (Death-associated protein kinase-like kinase)
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MTSTTMVTTLDLVTPTSEEQPGPAPESSDFSTVVLSPDGSELVTQSAPNTPIQHREQANAEFGQKEGSPDPKNMVAATGNASKPSLNSFYADGLGQLRNGLFSCFQPVFGYFGTKTTVEIEKSEDELWEIPFDAISELEWLGSGSQGAVFRGQLENRTVAVKKVNQLKETEIKHLRHLRHQNIIEFLGVCSKSPCYCIVMEYCSKGQLCTVLKSRNTITRELFAQWVKEIADGMHYLHQNKVIHRDLKSPNILISAEDSIKICDFGTSHMQKKMDSTMMSFCGTVSWMAPEMIKKQPCNEKVDVYSFGVVLWEMLTRETPYANIAQMAIIFGVGTNILSLPMPEEAPKGLVLLIKQCLSQKGRNRPSFSHIRQHWEIFKPELFEMTEEEWQLAWDSYREFAKCIQYPSTVTRDHGGPKSAFAMEEEIQRKRHEQLNHIKDIRNMYEMKLKRTNKMYDKLQGCFTELKLKESELAEWEKDLTEREQWHNQNSPKAVAAPRAQLRGYPNEGYDDMSSDEDVQPCRGSPYRCSNTSSSSGVQSSPFSRQSSSRSSAGQQTRRSEGANPPKILRNDAIRHSGSYWETLGGARGSPARDSGFSQDSGMWSAGAGSCTAINGGGQQVCYSQTLYRNGDGRWSDGRIASRRRVSTSVNKSTAVPGQPVFFTRDSPSRVPHGVISCSSPRSSSKLNRSSYPSRNAPHQLEDGCCCAHARAPRAKSIAVPMTSSSRARSPTPYDNDFENAESFVDPESPKNLKNLEKIVNLPESTSYDEALCNSDVTMNPIYTSPITTYSNPCHVELVDEENANDVDLTSSMDSRRSRSDDADVESSEEDEGNGNNILNTSMESEDLRYRIDTSQSTMMSSLERSLEIGATRSDGLSDNEMRVQAVKMSIKTHRRTGSNPQALIHQCIDEYTTSATDDSDDAGAVRI
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Component of a MAP kinase pathway that functions presynaptically to regulate synaptic architecture and presynaptic differentiation. Phosphorylates and activates mkk-4. Has a role in axonal regrowth following injury and synaptogenesis. Plays a role in modulating polymerization of neuronal microtubules. Also promotes tubulin post-translational modifications that protect microtubules. Plays a role in cilium length regulation, possibly by reducing rab-5 mediated endocytosis, and may also have a role in intraflagellar transport in cilia. Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord. [Isoform a]: Has a role in synapse and axon development, and in axonal regrowth following injury. [Isoform c]: By forming heterooligomers with isoform a, acts as an inhibitor of isoform a activation. Its inhibitory function is independent of its catalytic activity.
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O01704
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EXT1_CAEEL
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Exostosin-1 homolog (Multiple exostoses homolog 1) (Related to mammalian RIB protein 1)
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MQNVMKFHLVIFMLFGSVRLQNPTIERKQCTMSNCFDFSKCSTSKKVYIHPMEKRFEESPQSVIYSKILKHFLESNHYTNDPNEACIFLLGIDTTDRDVRSQNYVKNVNDYIESLDPSVWNNGRNHLIFNFYHGTFPDYDDHNLNFDTGEAMIARASSSENNFIKVFDVSLPLFHENHPYEIKESKSERNDDRIENQRKYLVSFKGKRYVYGIGSGTRNLVHHLHNGDDIVMVTTCKHNNDWQVYQDDRCQRDNDEYDRWEYDELLANSTFCLVPRGRRLGSFRFLETLRSGCVPVVISDSWILPFSETIDWNSAAIVVAERDALSIPELLMSTSRRRVKELRESARNVYDAYLRSIQVISDHVLRIIFKRIDNKIELEDHQ
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Required for the biosynthesis of heparan sulfate by positively regulating N-acetylglucosamine transferase II (GlcNAcT-II) and glucuronyl transferase II (GlcAT-II) activities of glycosyltransferase rib-2. Probably not directly involved in chondroitin sulfate biosynthesis but negatively regulates chondroitin sulfate levels. Maternally required for normal ventral epidermal enclosure and for embryo elongation during the early stages of embryonic development. In addition, involved in the elongation of the pharyngeal isthmus and in the organization of the actin cytoskeleton in the pharyngeal muscles during the later stages embryonic development. In adults, regulates egg-laying and the normal morphogenesis of the vulva. Also involved in the directed migration of hermaphrodite-specific neurons.
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O01705
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EXT2_CAEEL
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Exostosin-2 homolog (EC 2.4.1.223) (EC 2.4.1.224) (EC 2.4.1.225) (Glucuronyl-galactosyl-proteoglycan 4-alpha-N- acetylglucosaminyltransferase) (GlcNAc transferase I) (GlcNAcT-I) (Glucuronyl-galactosyl-proteoglycan/Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (GlcAT-II) (GlcNAc transferase II) (GlcNAcT-II) (Glucuronyl transferase II) (Multiple exostoses homolog 2)
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MAIKLNGSSRSFVPSLRVSAFLIFIFFVITYIIIYNVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQENCSLERRRQLIGSSTFCFLLPSEMFFQDFLSSLQLGCIPIILSNSQLLPFQDLIDWRRATYRLPLARLPEAHFIVQSFEISDIIEMRRVGRLFYETYLADRHLLARSLLAALRYKLQIPTREVRRNQAIPLFNSSFTAPKGSVVNVQANFDDEYLLGPLESRVESTSYAYNFTEFQLYSYDFWNIIMSPHYTKEFLVNAAELPTEAEFFEDTKIGFRPIEPGSGAEFSKALGGNRQREQFTVVLLTYERDAVLTGALERLHQLPYLNKIIVVWNNVNRDPPDTWPSLHIPVEFIRVAENNLNNRFVPWDRIETEAVLSLDDDIDLMQQEIILAFRVWRENRDRIVGFPARHHARYGDSMFYNSNHTCQMSMILTGAAFIHKNYLTAYTYEMPAEIREHVNSIKNCEDIAMNYLVSHLTRKPPIKTTSRWTLKCPTCTESLYKEGTHFEKRHECMRLFTKIYGYNPLKFSQFRADSILFKTRLPQNHQKCFKYV
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Glycosyltransferase required for the biosynthesis of heparan sulfate. Initiates heparan sulfate synthesis by transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core linker (GlcNAcT-I activity). In association with rib-1, is also responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains (GlcNAcT-II and GlcAT-II activities). Required for normal ventral epidermal enclosure during the early stages of embryonic development. In addition, involved in the elongation of the pharyngeal isthmus during the later stages of embryonic development. Involved in the directed migration of hermaphrodite-specific neurons.
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O01737
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SBNO_CAEEL
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Protein strawberry notch homolog (Lethal protein 765) (Notch signaling pathway homolog 1)
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MDDILSAALAESGLDFLCQQSSPTPSTSGSIHDDAGQSFSNNTHTPSVSQFFDETSNDSHSSSAYYTPMATPFVSTEDGGVPTSFFGMDEEDGGCTIMTTAGTSGSNNIDGIEDAGGGMYYPHVKVIPRKHTAPTVNQSEPSTPTVTIVPKKEDPLFETNTADSPTPSGDTSTTASYEGNDGLEDQETTSDRQNPMFVQTARSTDGRLDTPSTSATVSPHITSSLTQRSHTSSPASSASEGTVVPPRKKGLPITTGSIVKRTVQTKDGLQTQYLKAFVNENGEKIYKLLSPVAASAVARGTLPPGMGRGGSTIGRGGTMVNKNGERLMVVKNHVGPNGQMLVKRMVSPAGTRIVANGGQGRGQPIYRAVDGSNGPTHLLRRTTTTGQPTRGAPVGMAARHAVRGGTVYGGGNGYRVNLVGRGTGGSTMVHHQPLNRISSQRSVAPVGRVLNRGALRNGAQQPLHVSTSSPAFHYMEEQPSPTTNGMVIQAKTPGAGVIQARHMQSQQSFPSGGPARVLMNRSSTNAGLSRMVGGGYDQQLPTAPNGRLMIPSTAVRVPGSGMASPRLQTTPQPLTKSQKAKDEMKMAYQVGREEALQQRRNDLEDDEENLGYAETYSEYTPAKLRSGMAHPDSVVESASLSSVSPPDVKYQISIPEYLIDMGHISALQLEAVIYACQMHERRMPSGERYGYLIGDGAGVGKGRTVACIIFENYLQGRKRAIWLSVSSDLKFDAERDLRDCGAPNIPVYALNKMKYAKISGKENGSIKKGVMFATYTSLIGECRGAKSRKYRSRISQLIQWFGQDYDGVIILDECHRAKNLVPTAGAKPTKTGRMVLELQKALPNARVVYASATGATEPRNMAYMTRLGLWGERQAFPEFHDFISAVERRGVGAMEIVAMDMKQRGLYLARQLSFRGVSFAVQEVQLSSEFVKMYDAAVKLWMEARRQFQTVIETMDEEERSTCKTVWGQFWACHQRFFKYLCIAAKVDTCVQLSREAIKAKKCVVIGLQSTGESATLETLEEMGGELNEFVSTAKTVLYGLIDKHFPTDASFSMGDRDIFKDFDDFERPAKRRKTRETLSFLGDVGFDTWTGVTTGMGGRVGDGVTKNITRGLSGIGRSSMSSSTGNTNNEDANSTTSESSDGSDDEVENDMISENGGESGDLESAREEAEGARTLEDGEQDEWVKALLAEAESSSDDSDEEVVKDEDEDEEAESKSGETHEQEEEFNPFMCDFTNDDPWAHNQQIVEDTPQKDRKAKKRKRDEEEAERLREKVRKREERREKKRRRAIRRAEREKQRRNEELQARGSATDFITSSRICGNGSGEQDDINPMLIKTELLAAVERLAPSLPANTLDQLIDEMGGPEYVAEMTGRRGHMVTSETGDVMYQRRNANAEVSLELINMEEKEKFMRGEKLIAIISEAASSGISLQSDRRAINKRRRVHITLELPWSADKAIQQFGRTHRSNQVSGPEYVFLISELAGEKRFASIVAKRLESLGALTHGDRRATETRDLSQFNMDNKYGRVALDTLLKTVIGQAGTPLIDPPKDYKAGEFFEDMRLYMEGVGLLAKNKTGQYTIEKEAATIPKFLNRILGLPVHAQNSLFHYFSEIVAELIAQSKHDGTYDTGIMDLGTGDDQVRKLETRVFTGRVDNGSFRVEIHKIGVERGVSWEEAMELHKEHSNDDDGFYICHPGGANTANTKKVAALVYGIGKIRMDNGARLYAITRPSTGRSPKLMTMADLSKRFHKVSIDEAKEVWKQQYDSAANMCQHNYVYGKCRTESNGTYCEVGRRTRTYFVLSGSVLSVWPIVEEVLAGSDRKSSRMQVIRVRTEQDQKIVGLLVLPTHVRHLVQQLETHCGRSYVKTEP
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Transcriptional activator that functions upstream of the let-60/Ras and let-23/EGFR signaling pathways to positively regulate lin-3 expression and thereby promote vulval induction. Plays a role in excretory duct development. Plays a role in male tail development.
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O01739
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OXDD3_CAEEL
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D-aspartate oxidase 3 (DASOX 3) (DDO-3) (EC 1.4.3.1)
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MLYALLLLFGGVSTVSSLRVAVVGEGVIGLSTATAILDLAEKRNIPAPEIHIFHHKPFEKILSRHIAGLFRIDSGSEIDRKYGYDTFEKLATLWREYGGLSGVQLVSGHILSDSKTKLDSQRESYGSLVYNYRDLAEPELFGPTSLFDLPRNTTTRGIHYTAYTSEGLRFCPFLKKELMTKGVRFTQRRIGNLEELGAEFDVVVNSAGLLGGVLAGDDAGNMKPIRGVLIRVDAPWQKHFLYRDFSTITIPVIDHVYMGTVKQEGAFGPNNVTSADIQDITSRYVALQPSFKRVHMLSSFVGYRPGRKQVRVEKQIRETNGSKKFTVVHNYGHSGNGFTLGYGSAVHAAHIVLDLPLDAYHGLVPEPLPINATISEWVKYLDD
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Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Has no activity towards L-amino acids or N-methyl-L-aspartic acid. May play a role in the egg-laying events and maturation processes of the reproductive organs.
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O01761
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UNC89_CAEEL
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Muscle M-line assembly protein unc-89 (Inactive serine/threonine-protein kinase unc-89) (Obscurin) (Uncoordinated protein 89)
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MASRRQKQFDRKYSSYRKFTATEDVNYSTHSSRSSYRSESLTSRTDGRGRSTSSEIIAGSESRSYPVYIAIQDYTPDKEDVEAIPLEQGQIVEVLDKKNSVRWLVRTKARPPRSGWVPGSYFETPTEFYKQRRRTREIENVSLSDEQAALVKRDQVYHELLRSEEEFVSSLRTCVDDYIKVLDDPEVPEAVKKNREELTLNIPELYNFHANVMLKGLNYYSDDPGKVGQTFVRLEKDFESHVEFYKQYADTLKLLEEPEIKRFFEGLSAKNDAGASSFVDHVKEIADRMVQYQNYFKEFVKYSARAHGSSKSIQKALELVTTIPQRVHDLEFTNNLKQHPGDTGKLGRIIRHDAFQVWEGDEPPKLRYVFLFRNKIMFTEQDASTSPPSYTHYSSIRLDKYNIRQHTTDEDTIVLQPQEPGLPSFRIKPKDFETSEYVRKAWLRDIAEEQEKYAAERDAISMTATSEMTASSVDFDMNASDQQSEFSEWSGSRKSSLFPGPEEGGPPRKKVKSPPVISPTGSSTSIYSGGSSSIDWTTTGTTLEMQGTRVTRTQYGFRTLQESSAKMCLKVTGYPLPDITWYKDDVQLHEDERHTFYSDEDGFFAMTIDPVQVTDTGRYTCMATNEYGQASTSAFFRVLKVEKEAAPPAFVTKLRDKECKEGDVIDFECEVEGWPEPELVWLVDDQPLRPSHDFRLQYDGQTAKLEIRDAQPDDTGVYTVKIQNEFGSIESKAELFVQADPDKNHVAPEFQATIEYVECDEGEEVRFKSVITGDPNPEIIWFINGKPLSESEKVKFISEDGICILTIKDVTRHFDGMVTCQGSNRLGSASCDGRLKVRVPPAPPTFNKPLEDKTVQEKSTVVFEVDVSGWPEPTLTFTLCGKELKNGEEGVEIVGHDGFYRISIPNTSMDKHDGEIVAKAQNEHGTAESRARLTVEQEEEESRSAPTFLKDIEDQTVKTGEFAVFETTVRGNPNPEVTWFINGHKMDQGSPGVKIEAHNHDHKLTIDSAQYAGTVLCRAENAVGRFETKARLVVLAPEKQKKPPKFVEILVDKTETVDNTVVFEVRVEGEPKPTVTWYLKGEELKQSDRVEIREFDGSIKISIKNIKIEDAGEIRAVATNSEGSDETKAKLTVQKKPFAPEFDLRPVSLTVEKGSEAVFSAHAFGIPLPTYEWSVNGRKVRDGQEGARVTRDESTVDGASILTIDTATYYSEVNHLTISVVAENTLGAEETGAQLTIEPKKESVVVEKQDLSSSEVQKEIAQQVKEASPEATTTITMETSLTSTKTTTMSTTEVTSTVGGVTVETKESESESATTVIGGGSGGVTEGSISVSKIEVVSKTDSQTDVREGTPKRRVSFAEEELPKEVIDSDRKKKKSPSPDKKEKSPEKTEEKPASPTKKTGEEVKSPKEKSPASPTKKEKSPAAEEVKSPTKKEKSPSSPTKKEKSPSSPTKKTGDEVKEKSPPKSPTKKEKSPEKPEDVKSPVKKEKSPDATNIVEVSSETTIEKTETTMTTEMTHESEESRTSVKKEKTPEKVDEKPKSPTKKDKSPEKSITEEIKSPVKKEKSPEKVEEKPASPTKKEKSPEKPASPTKKSENEVKSPTKKEKSPEKSVVEELKSPKEKSPEKADDKPKSPTKKEKSPEKSATEDVKSPTKKEKSPEKVEEKPTSPTKKESSPTKKTDDEVKSPTKKEKSPQTVEEKPASPTKKEKSPEKSVVEEVKSPKEKSPEKAEEKPKSPTKKEKSPEKSAAEEVKSPTKKEKSPEKSAEEKPKSPTKKESSPVKMADDEVKSPTKKEKSPEKVEEKPASPTKKEKTPEKSAAEELKSPTKKEKSPSSPTKKTGDESKEKSPEKPEEKPKSPTPKKSPPGSPKKKKSKSPEAEKPPAPKLTRDLKLQTVNKTDLAHFEVVVEHATECKWFLDGKEITTAQGVTVSKDDQFEFRCSIDTTMFGSGTVSVVASNAAGSVETKTELKVLETPKETKKPEFTDKLRDMEVTKGDTVQMDVIALHSPLYKWYQNGNLLEDGKNGVTIKNEENKSSLIIPNAQDSGKITVEASNEVGSSESSAQLTVNPPSTTPIVVDGPKSVTIKETETAEFKATISGFPAPTVKWTINEKIVEESRTITTIKTEDVYTLKISNAKIEQTGTVKVTAQNSAGQDSKQADLKVEPNVKAPKFKSQLTDKVADEGEPLRWNLELDGPSPGTEVSWLLNGQPLTKSDTVQVVDHGDGTYHVTIAEAKPEMSGTLTAKAKNAAGECETSAKVTVNGGNKKPEFVQAPQNHETTLEESVKFSAIVTGKPMPNVTWYLNNKKLIQSEEVKVKYVHETGKTSIRIQKPLMEHNGTIRVEAENVSGKVQATAQLKVDKKTEVPKFTTNMDDRQVKEGEDVKFTANVEGYPEPSVAWTLNGEPVSKHPNITVTDKDGEHTIEISAVTPEQAGELSCEATNPVGSKKRDVQLAVKKVGDAPTFAKNLEDRLITEGELTLMDAKLNIVKPKPKITWLKDGVEITSDGHYKIVEEEDGSLKLSILQTKLEDKGRITIKAESEFGVAECSASLGVVKGRPMAKPAFQSDIAPINLTEGDTLECKLLITGDPTPFVKWYIGTQLVCATEDTEISNANGVYTMKIHGVTADMTGKIKCVAYNKAGEVSTEGPLKVVAPIPVEFETSLCDATCREGDTLKLRAVLLGEPEPVVSWYVNGKKLEESQNIKIHSEKGTYTVTIKDITCDYSGQVVCEAINEYGKATSEATLLVLPRGEPPDFLEWLSNVRARTGTKVVHKVVFTGDPKPSLTWYINNKEILNSDLYTIVTDDKTSTLTINSFNPDVHVGEIICKAENDAGEVSCTANMITYTSDMFSESESEAQAEEFVGDDLTEDESLREEMHRTPTPVMAPKFITKIKDTKAKKGHSAVFECVVPDTKGVCCKWLKDGKEIELIARIRVQTRTGPEGHITQELVLDNVTPEDAGKYTCIVENTAGKDTCEATLTVIESLEKKSEKKAPEFIVALQDKTTKTSEKVVLECKVIGEPKPKVSWLHDNKTITQESITVESVEGVERVTITSSELSHQGKYTCIAENTEGTSKTEAFLTVQGEAPVFTKELQNKELSIGEKLVLSCSVKGSPQPHVDFYSFSETTKVETKITSSSRIAIEHDQTNTHWRMVISQITKEDIVSYKAIATNSIGTATSTSKITTKVEAPVFEQGLKKTSVKEKEEIKMEVKVGGSAPDVEWFKDDKPVSEDGNHEMKKNPETGVFTLVVKQAATTDAGKYTAKASNPAGTAESSAEAEVTQSLEKPTFVRELVTTEVKINETATLSVTVKGVPDPSVEWLKDGQPVQTDSSHVIAKVEGSGSYSITIKDARLEDSGKYACRATNPAGEAKTEANFAVVKNLVPPEFVEKLSPLEVKEKESTTLSVKVVGTPEPSVEWFKDDTPISIDNVHVIQKQTAVGSFSLTINDARQGDVGIYSCRARNEAGEALTTANFGIIRDSIPPEFTQKLRPLEVREQETLDLKVTVIGTPVPNVEWFKDDKPINIDNSHIFAKDEGSGHHTLTIKQARGEDVGVYTCKATNEAGEAKTTANMAVQEEIEAPLFVQGLKPYEVEQGKPAELVVRVEGKPEPEVKWFKDGVPIAIDNQHVIEKKGENGSHTLVIKDTNNADFGKYTCQATNKAGKDETVGELKIPKYSFEKQTAEEVKPLFIEPLKETFAVEGDTVVLECKVNKESHPQIKFFKNDQPVEIGQHMQLEVLEDGNIKLTIQNAKKEDVGAYRCEAVNVAGKANTNADLKIQFAAKVEEHVTDESGQLEEIGQFETVGDTASSKTDTGRGAPEFVELLRSCTVTEKQQAILKCKVKGEPRPKIKWTKEGKEVEMSARVRAEHKDDGTLTLTFDNVTQADAGEYRCEAENEYGSAWTEGPIIVTLEGAPKIDGEAPDFLQPVKPAVVTVGETAVLEGKISGKPKPSVKWYKNGEELKPSDRVKIENLDDGTQRLTVTNAKLDDMDEYRCEASNEFGDVWSDVTLTVKEPAQVAPGFFKELSAIQVKETETAKFECKVSGTKPDVKWFKDGTPLKEDKRVHFESTDDGTQRLVIEDSKTDDQGNYRIEVSNDAGVANSKVPLTVVPSETLKIKKGLTDVNVTQGTKILLSVEVEGKPKTVKWYKGTETVTSSQTTKIVQVTESEYKLEIESAEMSDTGAYRVVLSTDSFSVESSATVTVTKAAEKISLPSFKKGLADQSVPKGTPLVLEVEIEGKPKDVKWYKNGDEIKDGKVEDLGNGKYRLTIPDFQEKDVGEYSVTAANEAGEIESKAKVNVSAKPEIVSGLVPTTVKQGETATFNVKVKGPVKGVKWYKNGKEIPDAKTKDNGDGSYSLEIPNAQVEDAADYKVVVSNDAGDADSSAALTVKLADDGKDKVKPEIVSGLIPTTVKQGETATFNVKVKGPVKQVKWYKNGKEIPNAKAKDNGDGSYSLEIPNAQLDDTADYKVVVSNDAGDADSSAALTVKLPGIAIVKGLEDAEVPKGKKAVLQVETNKKPKEIKWYKNGKEITPSDKAQPGSDGDNKPQLVIPDAGDDDAAEYKVVLTDEDGNTADSSCALTVKLPAKEPKIIKGLEDQVVSIGSPIKLEIETSGSPKTVKWYKNGKELPGAAAKTIKIQKIDDNKYVLEIPSSVVEDTGDYKVEVANEAGSANSSGKITVEPKITFLKPLKDQSITEGENAEFSVETNTKPRIVKWYKNGQEIKPNSRFIIEQKTDTKYQLVIKNAVRDDADTYKIVLENTAGEAESSAQLTVKKAKAGLCKIVKGLEDQVVAKGAKMVFEVKIQGEPEDVRWLRDANVISAGANAIIEKIDDTTYRLIIPSADLKDAGEYTVEVINESGKAKSDAKGEVDEKPEIVRGLENIEIPEGDDDVFKVEVSAPVRQVKWYKNDQEIKPNSHLEAKKIGPKKYELAINRAQLDDGADYKVVLSNAAGDCDSSAALTVVKPNVLKIVDGLKDVDVEEPQPVELKVKVEGIPKVIKWYKNGQELKPDADGFKFEEKPESGEFSLTIPSSKKSDGGAYRVVLGNDKGEVYSGSVVHVKSAKSSEPTSGANFLSPLKDTEVEEGDMLTLQCTIAGEPFPEVIWEKDGVVLQKDDRITMRVALDGTATLRIRSAKKSDIGQYRVTAKNEAGSATSDCKVTVTEQGEQPSKPKFVIPLKTGAALPGDKKEFNVKVRGLPKPTLQWFLNGIPIKFDDRITLDDMADGNYCLTIRDVREEDFGTLKCIAKNENGTDETVCEFQQGAGHDDGSRDDLRYPPRFNVPLWDRRIPVGDPMFIECHVDANPTAEVEWFKDGKKIEHTAHTEIRNTVDGACRIKIIPFEESDIGVYMCVAVNELGQAETQATYQVEILEHVEEEKRREYAPKINPPLEDKTVNGGQPIRLSCKVDAIPRASVVWYKDGLPLRADSRTSIQYEEDGTATLAINDSTEEDIGAYRCVATNAHGTINTSCSVNVKVPKQEVKKEGEEPFFTKGLVDLWADRGDSFTLKCAVTGDPFPEIKWYRNGQLLRNGPRTVIETSPDGSCSLTVNESTMSDEGIYRCEAENAHGKAKTQATAHVQMALGKTEKPKMDEGKPPKFILELSDMSVSLGNVIDLECKVTGLPNPSVKWSKDGGPLIEDSRFEWSNEASKGVYQLRIKNATVHDEGTYRCVATNENGSATTKSFVRMDDGLGSGVVTASQPPRFTLKMGDVRTTEGQPLKLECKVDASPLPEMVWYKDGAIVTPSDRIQISLSPDGVATLLIPSCVYDDDGIYRVIATNPSGTAQDKGTATVKKLPRDSGARRSADRDVFDANKAPKLMEPLENIRIPEKQSFRLRCKFSGDPKPTIKWFKDGERVFPYGRLQLIESPDGVCELVVDSATRQDAGGYRCVAENTYGSARTSCDVNVIRGDRKPRDIDSSIREGKAPGFTTPLTIRRAKPGDSVTFECLPFGNPFPSIKWLKDGLELFSDEKIKMEAAADGTQRLILSDVTFLSEGYFRCVATNEHGTASTKAELVIEGDRTIGSRPLPEVNGEPEECKPRIRRGLYNMSIHEGNVVEMIVCATGIPTPTVKWYKDGQEIVGDGPDGKRVIFTDERGIHHLVIVNASPDDEGEYSLEATNKLGSAKTEGSLNIIRPRHIADADERGGMPFPPGFVRQLKNKHVFNHMPTIFDCLVVGHPAPEVEWFHNGKKIVPGGRIKIQSCGGGSHALIILDTTLEDAGEYVATAKNSHGSASSSAVLDVTVPFLDSIKFNGEIDVTPYLTEEYGFKKLNTASLPTPPDRGPFIKEVTGHYLTLSWIPTKRAPPRYPQVTYVIEIRELPEKQWSLLEYNIPEPVCKVRNLELGKSYQFRVRAENIYGISDPSPASPPSRLMAPPQPVFDRRTNKVIPLLDPYAEKALDMRYSEQYACAPWFSPGVVEKRYCAENDTLTIVLNVSGFPDPDIKWKFRGWDIDTSSPTSKCKVYTYGGSETTLAITGFSKENVGQYQCFAKNDYGDAQQNIMVDLATRPNFIQPLVNKTFSSAQPMRMDVRVDGEPFPELKWMKEWRPIVESSRIKFVQDGPYLCSLIINDPMWRDSGIYSCVAVNDAGQATTSCTVTVEAEGDYNDVELPRRRVTIESRRVRELYEISEKDEKLAAEGAPFRVKEKATGREFLAQLRPIDDALMRHVDIHNSLDHPGIVQMHRVLRDEKLALVVFDNANSTIDGLSSLAHPGVEIAEPKGVNRETCVRVFVRQLLLALKHMHDLRIAHLDLRPETILLQDDKLKLADFGQARRLLRGLITGEIKGSPEFVSPEIVRSYPLTLATDMWSTGVLTYVLLTGLSPFHGDNDNETLANVDSCQFDSSPLGNFSYDAGDFVKKLLTEIPVSRLTVDEALDHPWINDEKLKTEPLSADTLREFKYQHKWLERRVFVQQTPSEQILEAILGPATAQAQQNAPVAPEGRRPAEIYDYLRIQPKKPPPTVEYVPQPRKEHPPFIDEFGQLIDGDAFDRPEGTGFEGPHRQPPQIPPQPQRPNQAAHDSRRHEQQPQHQGQPQRIPVDQYGRPLVDPRYLNDPSHRPSSLDDAPFYVDKYGNPVHFDKYGRPMAPQNLEKRKLIPQDKGETPSHSKKEKTQHPVATPILASPGGDQQQQKIPMRMIRGERREIEEEIANRILSDISEEGSIAGSLASLEDFEIPKDFQVEASEPSTPTLTPEVTIRETIPKPTPSPTSPQKSPVPQPQGLLIPAKVTYSDSILAGLPAADKKVLEDAENDPSIPVGAPLFLEGLHGSDLTIDTTSASGLIKVTSPAINLSPNPKSPRRSTPGTKSPVVLSPRQEHSMEVLIATKRGKPGFLPPGELAEDIDDEDAFMDDRKKQVKPKDHDGENDFKDEKERLEKDKNRRTVNLDDLDKYRPSAFYKDDSDFGHPGYDIDATPWDSHYQIGPDTYLMAARGAAFNSRVRNYREELFGMGAPTVKQGFLGVRNRDITVRERRRYTDILRETTQGLEPKSHEQSTALLQKAPSATAIERIKADIEKVTPCATKKNDDGTFAPIFTARLRDVYLRKNQPAIFECAVSASPAPKVTWDFQGKILESNDRVTIEQDNNVARLILNHAAPYDLGEYVCTAINEYGTDKSSCRLISGETPSRPGRPEAELSSDTEIFIQWEAPEGPTYLEGITYRLEYRVAGPNDHGDPWITVSEKIDDESVIVKHLSPLGIYQFRVTAQNGFGLGLPSLSSRIVQTHGKGAPKLQIDVLKSEIRLNVVSMPQKSTNQLGGISEESEEDSEARTANEDMKSNLQLQTDDPTGRFQIGGLKFKGRFSVIRDAVDSTTEGHAHCAVKIRHPSSEAISEYESLRDGQHENVQRLIAAFNNSNFLYLLSERLYEDVFSRFVFNDYYTEEQVALTMRQVTSALHFLHFKGIAHLDVNPHNIMFQSKRSWVVKLVDFGRAQKVSGAVKPVDFDTKWASPEFHIPETPVTVQSDMWGMGVVTFCLLAGFHPFTSEYDREEEIKENVINVKCDPNLIPVNASQECLSFATWALKKSPVRRMRTDEALSHKFLSSDPSMVRRRESIKYSASRLRKLAAMIRQPTFSQPISEELESKYGK
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Structural component of the muscle M line which is involved in assembly and organization of sarcomere myofilaments. The large isoform a, isoform b, isoform d and isoform f play an essential role in maintaining the organization of sarcomeres but not myofilament alignment during body wall muscle development whereas the small isoform c and isoform d appear to have a minor role. Isoform b and isoform f are required for the organization of unc-15/paramyosin into sarcomere thick filaments in body wall muscles. By binding mel-26, a substrate adapter of the cul-3 E3 ubiquitin-protein ligase complex, regulates the organization of myosin thick filaments, likely by preventing the degradation of microtubule severing protein mei-1. Acts as guanine nucleotide exchange factor (GEF) for Rho GTPase rho-1 but not ced-10, mig-2 and cdc-42. The large isoforms regulate Ca(2+) signaling during muscle contraction by ensuring the correct localization of sarco-endoplamic reticulum Ca(2+) ATPase sca-1 and ryanodine receptor unc-68. By controlling the contraction and/or organization of pharyngeal muscles, plays a role in the formation of pharyngeal gland cell extension.
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O01767
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EGG4_CAEEL
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Inactive protein-tyrosine phosphatase egg-4 (Egg sterile protein 4) (Protein-tyrosine phosphatase-like protein egg-4)
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MALNSEVMFREQINAMRSQAGRKRATSLQSFCSGNTDDSSADSTDNMDMMVDYPQQKGVSCMRARFNSESTLSKSFRKKVKKLAQKDRRSKERLNGNSEEDAIEVPRGAPSTYAAPSKLRKSKALDCLVSEKPKDEGRREDSGHGADIEMAKGHFNNVRMKVFAARTAMQVEPALVMKTRKALEMKNAVLENHQSPGAFSLHAAYKIAASAESRVGSITPCNKKVTKEAMANLIRSSYDDTEITQELLFSSKFDTKWKGRYTDIYMRRDENGKKPKRPVNGQGWVMPLKSICEKFGINSTFFTNHRIDLKSARDQVLLMRLLSHDQTSTWISDIHPEAVKNETMAEYLLRELDASTMQKRVQAFKANVLADRDRVRVAGQFYNNIRIGKRMFGAARKAKYLSTIIGGMERRFEILENSVNHIPFTHSASDNNQEKCRNPRVHCKDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFFRDVIGSAKELDVDYERWLQERSERMFLDDLAAPIPGYRLLSPRADPDIVRMVGRPERPNYRREAPDCVGEMPNKVATVDGILSPAKSVFEF
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Inactive phosphatase which acts redundantly with egg-5 in the oocyte-to-zygote transition. Required for the polarization of cortical actin cytoskeleton rearrangement in the oocyte before and after fertilization. Together with egg-5, required for the cortical localization of kinase mbk-2 and for the inhibition of mbk-2 kinase activity in maturing oocyte until the end of meiosis I. Also required for kinase mbk-2, pseudophosphatase egg-3 and chitin synthase chs-1 localization to cytoplasmic foci after fertilization.
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O01775
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NEKL2_CAEEL
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Serine/threonine-protein kinase nekl-2 (EC 2.7.11.1) (Never in mitosis A kinase-like 2) (NimA-kinase-like 2)
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MDNYEKVRVVGRGAFGVCWLCRGKNDASHQKVIIKLINTHGMTEKEENSIQSEVNLLKKVQHPLIIGYIDSFIMDNQLGIVMQYAEGGTLERLINDQRAIKDSNMREYFPEKTVLDYFTQILIALNHMHQKNIVHRDLKPQNILMNRRKTVLKLSDFGISKELGTKSAASTVIGTPNYLSPEICESRPYNQKSDMWSLGCVLYELLQLERAFDGENLPAIVMKITRSKQNPLGDHVSNDVKMLVENLLKTHTDKRPDVSQLLSDPLVLPYLISIHCDLGRIEPPPTDKRKPSASLSSRLRTYPTQSTLRPYSLSSNAPTTHLTQLTPMPSHIDSGFFSSGRTSNQRTQSRSQVHSKY
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Probable serine/threonine-protein kinase required for the completion of molting. May play a role in endocytosis in the hypodermis syncytium.
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O01789
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SMC1_CAEEL
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Structural maintenance of chromosomes protein 1 (High incidence of males protein 1)
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MRGGSSLDSFPGKGTLHTLEIENFKSYKGKHTIGPFTRFTAIIGPNGSGKSNLMDAISFVLGEKPSSLRVRKYADLIHGAPINKPVAKKCRVTMNYKYSDGKVKAFTRGVNNGTSEHLLDGQTVTSAAYSQEMESINIFIKARNFLVYQGAIENIAMKTPKERTQLFEELSRSHEFQAEYERLKVEMTKAEDDTQHNMNKRRGIAQEKREAKMEKDEAEKYQTMKNELAAKSTMLFLHQLFHCERTIDESKEEINAQKKTIASLEATRSKEEAKIAAVHQEHRKALREVQKMTRKLDQKETDLAEKQQNMLTLKVSVAHEHKKLEIAKKMLAAAESKAENNSTQLADLKKSKKELEKKKAAYEAEIQDMMQRGELNLSDEQVREYGQLKDQAQRESAMVQRELLMAEQVFEGDKSSLNHELRRQKEHQERVKAKEGDVRRIETQIATLAQRIKETEEETKILKADLKKIENDVVIDKSAAAEYNKELVAVVRQLSEASGDSAEGERNQRRTEALEGLKKNFPESVYGRLVDLCQPSHKRFNIATTKILQKHMNSIVCDTEETAAKAIVYLKDHRYPPETFLPNDALVVNPLNEKLREIKKPAGVKLVFDVINPQHQAARKALQFVCGNALVCESQEDAKQLAYGGGELKDRFKAVSMDGTLFQQSGVMSGGSADLRQKSKKWDEKVVKQLREKRNQLNEKIADLQKHRRRELEVESVRSKINGNEQRLAMMKRDLKNMREMQLERLQNELEGMTAEMNMLPPRISNCQEKLERSESTLKSLQTKSNEVADRIFADFCTRVGIASIRDYENREMRIKQEMEDKLRSFDDDIQKLAYEIDFVTEQDGNRKVEVEKEKVSQIDRQYKDMKKKEKTAAAALKEHTESMEQDKEVLEEKKALSHKLETEWNEVKKIAQVAMKDFTKAEKELLRLESLLTKKQYERHSLLHSVKLGQIALPLKSGSMADVEYEEDDGDDTASQSSQSATDGPSVSEEQIQREQHIKINYDSLPREYKDVDDDDGVRQMSNRLNVEIDELQKNVSKMNAPNLKANQRMAEVKEREAESTEELENARKKAKRIRQQFEKVKTDRYRRFQDFFDPVANTIDDIYKQLSRNTSAQAFLGADNMEEPYLDGIQYNCVAPGKRFRPMDNLSGGEKTIAALALLFAVHGRNPAPFFVLDEIDAALDNTNIGKVASYICESAREHMQIIVISLKEEFYNKADSLIGIFPYPAACTTSGVLTFDLTRFKQIGLNEMTENPPTPSIAT
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Involved in chromosome cohesion during cell cycle and in DNA repair (By similarity). Required for chromosome segregation during mitosis. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped (By similarity). At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate (By similarity).
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O01798
|
SPE8_CAEEL
|
Spermatocyte protein spe-8 (EC 2.7.10.2) (Defective spermatogenesis protein spe-8)
|
MRSKSSEGDLQPEDTQSREDKETTATYSEDTKPETQKERNAALDNLAKTPIQLVVQPTPLTPAITPCEAPPPPPPPKPSSDNNNSKRLKVKDQLIEVPSDEVGRVENNIDNFPFYHGFMGRNECEAMLSNHGDFLIRMTEIGKRVAYVISIKWKYQNIHVLVKRTKTKKLYWTKKYAFKSICELIAYHKRNHKPIYEGMTLICGLARHGWQLNNEQVTLNKKLGEGQFGEVHKGSLKTSVFAAPVTVAVKTLHQNHLSANEKILFLREANVMLTLSHPNVIKFYGVCTMKEPIMIVMEFCDGKSLEDALLSKEEKVSAEDKILYLFHAACGIDYLHGKQVIHRDIAARNCLLNSKKILKISDFGLSVKGVAIKERKGGCLPVKYMAPETLKKGLYSTASDIYSYGALMYEVYTDGKTPFETCGLRGNELRKAIIGKRISLAVEVELPVFIANIFEQSRQYETEDRISSKQIIQIFKEEVGFHEIETSGILHKLVNSLPRIHNKERKPAAVAV
|
Probable non-receptor tyrosine-protein kinase which plays a role in spermatid activation (spermiogenesis) in hermaphrodites.
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O01803
|
RB11A_CAEEL
|
Ras-related protein rab-11.1 (Rab GTPase rab-11.1)
|
MGSRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSISVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHVTYENVERWLKELRDHADQNIVIMLVGNKSDLRHLRAVPTDEAKIYAERNQLSFIETSALDSTNVEAAFTNILTEIYKSVSNKHVGTDRQGYGGGSGTIIPSPASDPPKKQCCIP
|
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Involved in regulating the meiotic maturation of oocytes. Plays a role in egg shell formation, regulating exocytosis of chondroitin proteoglycans following fertilization. Controls cortical granule localization and targets them to the plasma membrane for exocytosis. Acts as a major regulator of membrane delivery during cytokinesis. Regulates the cytoskeleton by facilitating astral microtubule elongation and organization during metaphase to ensure proper spindle alignment and polarity in the first embryonic cell division. Maintains normal endoplasmic reticulum morphology during metaphase. Involved in vesicle formation and plasma membrane repair following exposure to pore forming toxins. Regulates endocytic recycling. May play a role in yolk receptor endocytosis in growing oocytes. Plays a role in the shedding of pathogen spores from intestinal cells via its involvement in spore fusion and endocytic trafficking.
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O01811
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MEC6_CAEEL
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Mechanosensory abnormality protein 6
|
MGLQSAAAHFINRFIIWITIFMVACFLLRLLVVLDLNKRVYNHTPGPCRVLTDNYKGTAGMTYVESQKRVYITLGYGRAHDLKTKTGIAFYKTNRTDGRSQQEMYDLIEMTINWNGYEYKKEFIPTGIDSYSSSNGRVLLYVINAHPNHQCIHFFQIVESSKLNHRKAICDPSFSSLQDIAVVGPDRLFVTNMAAFGRGWAQILEFSLQTGQGAVYYYDGSKLSTAASSLIAPTGIGYDAKRRILYVGSMIRESIFAYKVAKDTTLELLYEMMLLTSPIGVFVESKTGDIWIAAHPVIHESAWHYTHPENQNIHSPSQILRIRIQEEGNSWVTTEPYANDGATISASSSVVFTDEQMLIGSSFGRLLHCDLTHSYIT
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Subunit of an amiloride-sensitive cation channel (degenerin channel complex) permeable for sodium, potassium, lithium and N-methylglucamine, and required for mechanosensory transduction (touch sensitivity). Interacts with degenerin channel proteins and stabilizes the channel. Plays a role in mechanosensory transduction (touch sensitivity).
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O01822
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BL1S6_CAEEL
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Biogenesis of lysosome-related organelles complex 1 subunit 6 (BLOC-1 subunit 6) (Pallid protein homolog)
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MSNTEHNVESKNVTDTLDEILRLQEDIQARIGSSNHNLETNFESIKDFVSRAHAYIPILNQISKDMIEICERTQALKKKTSQLELSDTNIEDGSTTSTPTTTNKSQ
|
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis.
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O01836
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GLH3_CAEEL
|
ATP-dependent RNA helicase glh-3 (EC 3.6.4.13) (Germline helicase 3)
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MDKSPTKTSIRTKFARHQPISDVDTTEQSSSCIKKDDRGLSSFGVQSSVFSRRSCRMSELEAKPTIISEDQRIAVRSEIGGSFSGFDDKVDNVFHSNNNLHGSPSTTELECPGIMNPRFLVGRSLNSRSRAVTRGSKRTSNVKENEGSIHRSDDQVSTENCSAKDEERDRDSGGVSSYGNKRSDEFCGTSPILEAKGFGISNTCFNCKKYGHRATECSAPQRECANCGDPNHRANECASWSKNGVQEPTKVTYVPVVDKMEEVFSMLKINAGDFFDKFFDASVQLVSRGQPVTIQPCKSFSDSDIPQSMRRNVERAGYTRTTPIQQYTLPLVADGKDILACAQTGSGKTAAFLLPIMSRLILEKDLNYGAEGGCYPRCIILTPTRELADQIYNEGRKFSYQSVMEIKPVYGGINVGYNKSQIMKGCTIIVGTIGRVKHFCEDGAIKLDKCRYLVLDEADRMIDSMGFGPEIEQIINYKNMPKNDKRQTMMFSATFPSSVQEAARKLLREDYTMITIDKIGAANKCVIQEFELCDRTSKVDKLLKLLGIDIDTYTTEKNSDVFVKKTIVFVAQQKMADTLASIMSAAQVPAITIHGAREQKERSAALKLFRSGAKPVLIATAVVERGLDIKGVDHVINYDMPNNIDDYIHRIGRTGRVGNSGRATSFISLADDVQILPQLVRTLADAEQVVPSWMKEAAGGTSNPNKFEKSIDTEEPEEAW
|
Probable ATP-binding RNA helicase.
|
O01839
|
VPS51_CAEEL
|
Vacuolar protein sorting-associated protein 51 homolog (Protein fat-free homolog)
|
MSSVLDVTKPDFDVEAFVVKLLREKSLDGLVKEEEEMVSAVRRLDSDVHQIVYENYNKFLTATNTVRKIQDEFTQLDSEMKSLSRSMSTISTLIGNLDGVLGEKRDDILQLGSSYKVVNSLKHIFDLPHVLRSEFDERNYGEVLRMFKLAEESLSQYKDVPTVQLVLQKSKKIYDMTENQLMDQLRNPASGAELVSEAVDLLLTIGRDEDEVQKVLLTCSEQSLRVDLKELSANHSDVLDLVDKASESFIPNLTLIATTHDRLFEDKREDLITVLKTEMNSLHALVSKVFLSSSDAKDCSIVVRALDRYFRKISTCRYVIPGLDFLPLTIELINAVSKHEIDLSLTRIKEELKNGLNEVRKALINEEKDLSALASKIEQVFVHQVKTALANLLLFTASDVTFANLPPDEFRQSFSFNAHERLLVQAFHRFSELADEYESGAGEIRFVDPRVHLVFAVALQHLSNKSAVYLLNLCREQFSLSPDDGLTDITVVMSEVKTRAQKLVRCYAEKTGLSMGETLIKGCAMLVQPAATPSAVRASVRRLVEEMNTCDSELTLLLGGDSKPKDSRVSRRPITTALDAARDSLWCERIDFHLQIHFNRASIITVIVKVVLKIFIESIRLQTYSKFGVEQVQVDCYYLQRCLAALVSDEVVVNSMVDQALSSALKRCQDPVLVHPSRLAQLCEQPPANRPSSQASSLGY
|
Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi. Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1. Important for neuronal function.
|
O01887
|
TRYL5_CAEEL
|
Trypsin-like protease try-5 (EC 3.4.21.-) (Trypsin-like serine protease try-5)
|
MRPRIIVFLFQVLVVIKGTKLKYYNDELCGRQSTYTSFMLTDAAGNTGNPTHLAPWAVQIRVKARKGDFEVICGGTLITLKHVLTAAHCFQKHFGAKKEGGEENSMSGRYCESNQRFTDSEILTRTVVTVGAMCTRLEQKYGCVNEKQNGKTLKISRFAIGDFYKTHCEQGNDIVILELESTIDDVEGANYACLPFLPEVNIQSGANVTSFGWGSDPGKGFDNAAFPMIQVLTLATETLATCEENWGTSIPFDSFCTAEEEDKNVCSGDSGGGLTFHQSDSAREFIIAIVSYGSDCVQLIGGSEPRSQINTDVRKHQKFIVNFINQA
|
Serine protease which, in males, acts as a promoting signal during mating to activate sperm.
|
O01901
|
WASC3_CAEEL
|
WASH complex subunit homolog 3 (Daf-16-dependent longevity protein 1)
|
MNASSRTKPAIDLNKVPPIDHHRTAVTFNCLIMKMTEMLNNFGNKMEDILEKAEQSLDTADRKLRLMESKLAGMSLEDKSTTATPSSAPEIDEIHESNPSSSQIVEETVEEKPEEHTTTVLIKDDPAYSKYFKMLKLGVLEAGVIQKMKSEGVDPSILKRGDEPSRPQAQTSRNYESSGESTASFSDSD
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Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat-shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity.
|
O01925
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MBOA5_CAEEL
|
Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (Probable 1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (Probable 1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Probable 1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Probable lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Probable lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Probable lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase)
|
MGVVGALSEVTSASEDALRLLISVLAGYPLAVVHRTFFYNKPAQHQHLFFVIVGLSLWMFNCGSSVIHPILSIFGAFFITNFMAGTDASIYAAHIVFLGHLLIGYWFHETDTYDITWTTPFCIMTLRFIGLVMDVYDGAQKPEHLKPDQKLTAISDKPGLLEIAAFGLFFQGTLVGPQFTLSKFRSFVNGDWLDSDGQPPKSAFLPSIGRFLAGCTYMVLHQWGQFWIPDQYFNSDAYNNLSFFWRWSWVTLWFRLTMYKYCAMWLITEGASILSGLGHNGKDAEGNDRWDGVRDLHIIKWETGHDYNSVVESFNCGTNTFAKNHIHRRLRWVNNKLASHVITLSYLAIWHGYHLGYFLLFGVELGCVQAQNQLYALIKRTPGWSEAISKPISRPFIWIFGKLTISYSMGFAFLMFGLIKTKYWIGPVKSLYFIGFIIYFIVWPILHMVLLRVLPRHPKKAAAEKPEEVKKEL
|
Probable acyltransferase which may mediate the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). May also catalyze the conversion of lysophosphatidylethanolamine (1-acyl-2-hydroxy-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), as well as the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Required for incorporation of arachidonic acid into PC, PE, and PS.
|
O01965
|
ARI11_CAEEL
|
E3 ubiquitin-protein ligase ari-1.1 (EC 2.3.2.31)
|
MSSDDEINMDDSDSSQGEIDDGCMSDDDGIVLESREQNSSDYKDNGEPDNEVLNHDSLEAEMKKTITDVQAVLQVKTGVCRILLHKYKWNKESLLERFYEHPDTTTFLIDAHVIPRRQERLPAGDAECDICCSLGELSGLSCNHRACTQCWKAYLTNKIANNAQSEIECMAPNCKLLIEDEKVMFYITDPTVIATYRKLIVASYVETNRLLKWCPGIDCGKAVRVSHWEPRLVVCSCGSRFCFSCGHDWHEPVNCRLLKLWLKKCNDDSETSNWINANTKECPKCMITIEKDGGCNHMTCKNTACRFEFCWMCLGPWEPHGSSWYSCNRFDDSAAKNARDAQEVSRANLQRYLFYYNRYMGHQQSLRLEGKLYATVKSKMEQMQTLSMSWIEVQFLRKAVDVLSECRRTLMFTYAFAFYLKRDNNAIIFESNQKDLEMETEQLSGFLERDLDNENLVTLKQKVQDKYRYVEHRRKVLLDHCSEGADQELWVFNE
|
E3 ubiquitin-protein transferase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 ubc-18 (By similarity). Acts with ubc-18 to regulate pharyngeal development.
|
O01971
|
EMR1_CAEEL
|
Emerin homolog 1 (Ce-emerin)
|
MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVSAATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAETNPEDTI
|
Nuclear lamina-associated inner nuclear membrane protein that is involved in cell division, nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis. Involved in chromosome segregation and cell division, probably via its interaction with the nuclear intermediate filament protein lmn-1, the main component of nuclear lamina. Required to organize the distribution of lmn-1, nuclear pore complexes (NPCs) and chromatin in mitotically active cells. Together with lem-2, plays a role in baf-1 enrichment at the nuclear envelope in anaphase. Together with lem-2, involved in muscle cell attachment to hypodermal cells, as well as muscle cell location and sarcomere organization. May play a role in radiation-induced DNA damage repair response. May repress binding of transcription factor pha-4 with target sequences in pharyngeal cells.
|
O01991
|
EF2K_CAEEL
|
Eukaryotic elongation factor 2 kinase (eEF-2 kinase) (eEF-2K) (EC 2.7.11.20) (Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase)
|
MTIDTTNESDNSPTNSPGLEASARTFSLNASKMVRITDDYADEVFIEQNDVVIEKPRMDPLHVRKLMETWRKAARRARTNYIDPWDEFNIHEYPVQRAKRYRYSAIRKQWTEDIVDVRLHPDSFARGAMRECYRLKKCSKHGTSQDWSSNYVAKRYICQVDRRVLFDDVRLQMDAKLWAEEYNRYNPPKKIDIVQMCVIEMIDVKGSPLYHLEHFIEGKYIKYNSNSGFVSNAARLTPQAFSHFTFERSGHQMMVVDIQGVGDLYTDPQIHTVVGTDYGDGNLGTRGMALFFHSHRCNDICETMDLSNFELSPPEIEATEVAMEVAAKQKKSCIVPPTVFEARRNRISSECVHVEHGISMDQLRKRKTLNQSSTDLSAKSHNEDCVCPECIPVVEQLCEPCSEDEEDEEEDYPRSEKSGNSQKSRRSRMSISTRSSGDESASRPRKCGFVDLNSLRQRHDSFRSSVGTYSMNSSRQTRDTEKDEFWKVLRKQSVPANILSLQLQQMAANLENDEDVPQVTGHQFSVLGQIHIDLSRYHELGRFVEVDSEHKEMLEGSENDARVPIKYDKQSAIFHLDIARKCGILEAVLTSAHIVLGLPHELLKEVTVDDLFPNGFGEQENGIRADKGQKPCDLEEFGSDLMEIAAEMGDKGAMLYMAHAYETGQHLGPNRRTDYKKSIDWYQRVVGFQEEEELDSDCGKTTFSSFAPLTRHEILAKMAEMYKEGGYGLNQDFERAYGLFNEAAEAAMEAMNGKLANKYYEKAEMCGE
|
Phosphorylates elongation factor-2 (eEF-2) at two threonine residues that are conserved in all eukaryotes and are located within a GTP-binding domain. Calcium(2+)/calmodulin dependent activity. Inactivates eEF-2 by catalyzing its phosphorylation. eEF-2 catalyzes the movement of the ribosome along mRNA during translation in eukaryotic cells.
|
O02002
|
CASP1_DROME
|
Caspase-1 (EC 3.4.22.-) [Cleaved into: Caspase-1 subunit p22; Caspase-1 subunit p13]
|
MTDECVTRNYGVGIRSPNGSENRGSFIMADNTDAKGCTPESLVVGGATAASPLPANKFVARMPVERYASEYNMSHKHRGVALIFNHEFFDIPSLKSRTGTNVDAQELKKAFENLGFAVSVHKDCKLRDILKHVGKAAELDHTDNDCLAVAILSHGEHGYLYAKDTQYKLDNIWHYFTATFCPSLAGKPKLFFIQACQGDRLDGGITLEKGVTETDGESSTSYKIPIHADFLFSYSTIPGYFSWRNINNGSWYMQSLIRELNANGKKYDLLTLLTFVNQRVALDFESNVPATPMMDRQKQIPCLTSMLTRILRFGDKPNGNKAG
|
Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Loss of zygotic DCP-1 function causes larval lethality and melanotic tumors.
|
O02100
|
HOP1_CAEEL
|
Presenilin hop-1
|
MPRTKRVYSGKTITGVLYPVAICMLFVAINVKLSQPEQQEQSKVVYGLFHSYDTADSGTITLYLIGFLILTTSLGVFCYQMKFYKAIKVYVLANSIGILLVYSVFHFQRIAEAQSIPVSVPTFFFLILQFGGLGITCLHWKSHRRLHQFYLIMLAGLTAIFILNILPDWTVWMALTAISFWDIVAVLTPCGPLKMLVETANRRGDDKFPAILYNSSSYVNEVDSPDTTRSNSTPLTEFNNSSSSRLLESDSLLRPPVIPRQIREVREVEGTIRLGMGDFVFYSLMLGNTVQTCPLPTVVACFVSNLVGLTITLPIVTLSQTALPALPFPLAIAAIFYFSSHIALTPFTDLCTSQLILI
|
Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Probably works redundantly of lin-12, which provides more presenilin function.
|
O02101
|
SWIC2_CAEEL
|
SWI/SNF chromatin-remodeling accessory subunit 2
|
MHSQQRPNPQMNRHPYGTPGSAPQMRRPGGFAGQPPQMHGPRMVAPPAAPLPKKKKYADKCIHPKIRELEPDAENYMALLASEQKLDSTLSRKKLDIQEALKRPSKVKKRLRIYISHTFIEEKQPEKDTDEASLPMWELRVEGRLLDEQPPAPAIPGQRPVPKRKFSSFFKSLVIELDKEMYGPDQHLVEWHRTPQTNETDGFQVKRAGDRPVKCRILLLLDNHPAKFKLHPRLAKVLGIATETRPKIIEALWQYIKTHGLQDPQERDIINCDTFLSQCFGVNRMRFMEVPNKLHQLLQQTDPLEFNHIIQRPKEGQEQVSTCYDIDVEMEDPVKQFMHTFVHSPGLANDIQTLDQKCYDIIEQINELKTRRDFYARFYTEPAEFIKSWVMSQNSDLKTMNELSGDLEAERFAESYVRPETEEGVQRYMFQKVNQKRHELEQSLGVRSN
|
Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Probably regulates vulva development through the let-60/Ras pathway. Involved in nuclear reassembly after mitosis and recruitment of nuclear envelope protein, mel-28, to the nuclear periphery in the early embryo and in the adult germline. Involved in gonadogenesis.
|
O02108
|
CDC37_CAEEL
|
Probable Hsp90 co-chaperone cdc37 (Cell division cycle-related protein 37) (Hsp90 chaperone protein kinase-targeting subunit)
|
MPIDYSKWKDIEVSDDEDDTHPNIDTPSLFRWRHQARLERMAEKKMEQEKIDKEKGTTSKKMEELEKKLAAADVTDKSDIQKQIDEVKAQEEAWRKKEAELEEKERLEPWNVDTIGHEAFSTSRINKITEKKPQAPKTDEEDTHAMSTFFETHESLLEKMAVLKNGAKSTELFLAEHPHMASEYTANWLTIEALNAAIDFNEEKMKTMAEQCIIIQYLLELSKSLNAVATNTTVQKQFFKKFEAAEPVYMKHYQDEVKAFEDRLRTRAQTKRDAAMEEAEAEEKAERMKSAPGGIDPQEVFEQLPEEMRKCFEAHDIEALKGVAQKMDEEVFKYHFDRCIASGLWVPGKADDDDDDEEAAPAEEEPTTSS
|
Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (By similarity). Inhibits daf-21/Hsp90 ATPase activity.
|
O02151
|
NHR14_CAEEL
|
Nuclear hormone receptor family member nhr-14
|
MDFLISTSLSESTSTSADFCVVCGDKAIGKHYGAVACNGCKGFFRRSVWQNLQYTCRFNKQCNIDKDHRNACRYCRFQKCLADGMKPEAIQNERDRIGSTKRRKRSGANSENNSDSEGTPSPKIEVMGNSVSRKLIEMLLDIEHRLASNQSMNALLRDESEMKNSRQRAVNYLIGWTNMLHPLPEVPLADKVLLLKKFSSAFTLLGTLQRSMALPHFVLPNDQVLSISASHPPELFEALTRIIDELLTPLRRLRTDHAEFSCLKALLLLNPDVVGISNNTRERIREARDALLKTLFAYMSNTQNSIDASLRVSSLLMIIPSLISVSSSIMEFPALSDLFGLGDVIKRDTISPKIETPPLEMKPMMPKIAQPPVTSAPTVPTNIMMNKDLISQIMNNPQLFPLLPMPQTASPPMSFMGQSEFGCHLQSMPVKVILS
|
Orphan nuclear receptor. Transcriptional repressor of intestinal metal transporter smf-3 and genes of the innate immune response. Inhibits nuclear localization of transcription factor pqm-1 in response to pathogen stress, may facilitate translocation of pqm-1, leading to transcriptional activation of genes involved in innate immunity and iron uptake.
|
O02193
|
MOF_DROME
|
Males-absent on the first protein (EC 2.3.1.48) (Histone acetyltransferase MOF)
|
MSEAELEQTPSAGHVQEQPIEEEHEPEQEPTDAYTIGGPPRTPVEDAAAELSASLDVSGSDQSAEQSLDLSGVQAEAAAESEPPAKRQHRDISPISEDSTPASSTSTSSTRSSSSSRYDDVSEAEEAPPEPEPEQPQQQQQEEKKEDGQDQVKSPGPVELEAQEPAQPQKQKEVVDQEIETEDEPSSDTVICVADINPYGSGSNIDDFVMDPDAPPNAIITEVVTIPAPLHLKGTQQLGLPLAAPPPPPPPPAAEQVPETPASPTDDGEEPPAVYLSPYIRSRYMQESTPGLPTRLAPRDPRQRNMPPPAVVLPIQTVLSANVEAISDDSSETSSSDDDEEEEEDEDDALTMEHDNTSRETVITTGDPLMQKIDISENPDKIYFIRREDGTVHRGQVLQSRTTENAAAPDEYYVHYVGLNRRLDGWVGRHRISDNADDLGGITVLPAPPLAPDQPSTSREMLAQQAAAAAAASSERQKRAANKDYYLSYCENSRYDYSDRKMTRYQKRRYDEINHVQKSHAELTATQAALEKEHESITKIKYIDKLQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKTRCAPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTSKTIQDHLQLPQFKQPKLTIDTDYLVWSPQTAAAVVRAPGNSG
|
Histone acetyltransferase that plays a direct role in the specific histone acetylation associated with dosage compensation as part of the male-specific lethal (MSL) complex. Dosage compensation ensures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes. May be directly involved in the acetylation of histone 4 at 'Lys-16' on the X chromosome of males where it is recruited by the MSL complex. As part of the nonspecific lethal (NLS) complex may associate with promoters of X chromosomal as well as autosomal genes and positively regulate their transcription through chromatin modification.
|
O02194
|
PSN_DROME
|
Presenilin homolog (DmPS) (EC 3.4.23.-) (dPS)
|
MAAVNLQASCSSGLASEDDANVGSQIGAAERLERPPRRQQQRNNYGSSNQDQPDAAILAVPNVVMREPCGSRPSRLTGGGGGSGGPPTNEMEEEQGLKYGAQHVIKLFVPVSLCMLVVVATINSISFYNSTDVYLLYTPFHEQSPEPSVKFWSALANSLILMSVVVVMTFLLIVLYKKRCYRIIHGWLILSSFMLLFIFTYLYLEELLRAYNIPMDYPTALLIMWNFGVVGMMSIHWQGPLRLQQGYLIFVAALMALVFIKYLPEWTAWAVLAAISIWDLIAVLSPRGPLRILVETAQERNEQIFPALIYSSTVVYALVNTVTPQQSQATASSSPSSSNSTTTTRATQNSLASPEAAAASGQRTGNSHPRQNQRDDGSVLATEGMPLVTFKSNLRGNAEAAGFTQEWSANLSERVARRQIEVQSTQSGNAQRSNEYRTVTAPDQNHPDGQEERGIKLGLGDFIFYSVLVGKASSYGDWTTTIACFVAILIGLCLTLLLLAIWRKALPALPISITFGLIFCFATSAVVKPFMEDLSAKQVFI
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Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptor. Required for S3 cleavage of Notch, which releases activated Notch protein from the cell membrane. Involved in the patterning of the optic lobes.
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O02213
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SER2_CAEEL
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Tyramine receptor Ser-2
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MFRNYTDSVQEMVLRAIDSIRDSVINASSAVSTTTLPPLDIPMTSMKPPSIIPTVELVLGTITYLVIIAMTVVGNTLVVVAVFSYRPLKKVQNYFLVSLAASDLAVAIFVMPLHVVTFLAGGKWLLGVTVCQFFTTADILLCTSSILNLCAIALDRYWAIHNPINYAQKRTTKFVCIVIVIVWILSMLISVPPIIGWNNWQENMMEDSCGLSTEKAFVVFSAAGSFFLPLLVMVVVYVKIFISARQRIRTNRGRSALMRIQNAEGDDDYRKMSIKRASVESARTSSRVGEKTPLVIADGQTTVTTLAAHSTDGGSLPKDETTKHMKYHNNGSCKVKVKDVKEDEGNPNPTAVLRKREKISVAKEKRAAKTIAVIIFVFSFCWLPFFVAYVIRPFCETCKLHAKVEQAFTWLGYINSSLNPFLYGILNLEFRRAFKKILCPKAVLEQRRRRMSAQP
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G-protein coupled receptor for tyramine, a known neurotransmitter and neuromodulator and direct precursor of octopamine. The rank order of potency is tyramine > octopamine > dopamine > serotonin > epinephrine = norepinephrine.
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O02217
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P2R31_CAEEL
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Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1 (Regulator of spindle assembly protein 1) (Serine/threonine-protein phosphatase 2A 72kDa regulatory subunit rsa-1) (Serine/threonine-protein phosphatase 2A regulatory subunit B'' rsa-1)
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MPTDEPSKRKSILPTIPTSLMLKKSNEALSDFERTFNDRVMDIFAENRRIDVEEFKKNAECFLNIIRSNKIDLNWGEGGESRYVTITRLMKILKTSPQSIKDLLPHNTVSNFVKITNYNLTIDITLLEELVRTVIHAEESYIKLLPFSENSTEISSYSLQDFVATHFIPIMIEEPENPVYYTAYAVGTIFFLLGARRRDCVYLKDLLASTLLLQLEECIHAENHCLSPPKIDVFTVAQFRTTLSEFRFLDSQRKGLLAPADLKFFRDGIFNEVFTKRIFEISITYEDGRIDFKAFVDFVTALKFRHTTASAKYHFEILDLKDDGLLDEEEIRSISSFQLQNLPDYVPEDNSVNPEVATAELRDMMRLNQNGITLEEFLANRMNSTFAGFLSNSDDYMKYERREQ
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Regulatory subunit of phosphatase let-92 which recruits let-92/paa-1 complex to the centrosomes, thereby regulating microtubule outgrowth from centrosomes and mitotic spindle assembly ensuring the stability of kinetochore microtubules.
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O02219
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AHA1_CAEEL
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Aryl hydrocarbon receptor nuclear translocator homolog (ARNT) (AHR-associated protein)
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MAQDIFMDPWQSATSFAMEDEDMGMPSGKYARMEDEMGENKERFARENHSEIERRRRNKMTHYINELAEMVPQCASLGRKPDKLTILRMAVSHMKGIRGHTAQDETSYKPSFLTDQELKHLILEAANGFLFVVCCQTGKVLYVADSITPVLNLKQEDWLQRNLNELIHPDDQDKIRDQLCGSEVSVNKVLDLKSGSVKREGASTRVHMSCRRGFICRMRVGALEPLHRLRNRRPLFQHAGQNYVVMHCTGYIKNAPPQGINAPASSCLVAIARLQVASMPVCADPTSTNQFSVRVSEDGKMTFIDARVSDLIGLSSDQLIGRYWWNLAHPADEKTLQDSFVALLSDQPMRINIRVRTSTDYIPCTVSAYKFMNPYSEQFEYVVATHQIAPQEDINNWVTAPTVPQPQASEFGELGGAPSAVDYGQSSSGGWRPEAQGAPQAQWQWDPMNGYNQ
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Transcription factor. Efficient DNA binding requires dimerization with another bHLH protein, such as cky-1 or ahr-1. Regulates transcription of target genes, probably acting in complex with cky-1. Has a role in cellular differentiation. Required for pharyngeal development. In collaboration with ahr-1 it is involved in RMEL/R and SDQR neuron cell migration. Acts in the cellular response to hypoxia. Involved in aggregation behavior by regulating soluble guanylate cyclase gene expression in the URX neurons.
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O02228
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SC5A7_CAEEL
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High-affinity choline transporter 1
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MADLLGIVAIVFFYVLILVVGIWAGRKSKSSKELESEAGAATEEVMLAGRNIGTLVGIFTMTATWVGGAYINGTAEALYNGGLLGCQAPVGYAISLVMGGLLFAKKMREEGYITMLDPFQHKYGQRIGGLMYVPALLGETFWTAAILSALGATLSVILGIDMNASVTLSACIAVFYTFTGGYYAVAYTDVVQLFCIFVGLWVCVPAAMVHDGAKDISRNAGDWIGEIGGFKETSLWIDCMLLLVFGGIPWQVYFQRVLSSKTAHGAQTLSFVAGVGCILMAIPPALIGAIARNTDWRMTDYSPWNNGTKVESIPPDKRNMVVPLVFQYLTPRWVAFIGLGAVSAAVMSSADSSVLSAASMFAHNIWKLTIRPHASEKEVIIVMRIAIICVGIMATIMALTIQSIYGLWYLCADLVYVILFPQLLCVVYMPRSNTYGSLAGYAVGLVLRLIGGEPLVSLPAFFHYPMYTDGVQYFPFRTTAMLSSMATIYIVSIQSEKLFKSGRLSPEWDVMGCVVNIPIDHVPLPSDVSFAVSSETLNMKAPNGTPAPVHPNQQPSDENTLLHPYSDQSYYSTNSN
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Imports choline from the extracellular space to the neuron with high affinity. Choline uptake is the rate-limiting step in acetylcholine synthesis. Sodium ion and chloride ion dependent.
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O02274
|
ZTF11_CAEEL
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Zinc finger protein ztf-11
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MSSISNNPDFSSIDPAVLMSLLMKSSGSLPTPPDTHSDGSESPDSTASDSSDKKRRRKPESKDIVRVAEEAEAAAATCSSIPSSSDTKENETEEDQNMTCDTTTNNAQKPTEQTATSADVVTSSVPSGLEGVPSFLFSQFMAPSFQKQLEIFTSGNMMSATHSDTSPSDVDSVLDGGVVTAEETSSSKSPMMTSSDTPKTPLTASSPPHSSGSESRVMSPITHTNISDELSISTTPTVAFTPNGSIPSPGTGYSWSIRREGKLACPTPGCDGSGHQTGLYTHHRSLSGCPRRPDKTVIQMLALRQDTVLRCTTAGCSGKGHVNGNRTSHRSLSGCPIAHQEKLARKGIKTTPQRTKTPIKGISISDECPLDLTLSGLPAGLSAQQLLAAAQAGLIPSSQMMDALFQQFSQTQPLATLEEESKKENEMEVDVETTSDDIPTLIKEEEEVKCESPVPSVIPEIQSTPSRPVAAPVAPGSAEKSSPTSQMLLQMPGFSEALLKMTAPQVPFPQYSPQAALFGNQSALLAQIMLTQLQMQQGF
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Transcriptional repressor which promotes neuronal differentiation during embryonic and postembryonic neurogenesis. Together with components of the MuvB corepressor complex, negatively regulates the expression of non-neuronal genes during neurogenesis. Required for the generation of postembryonic neurons from epidermal cells.
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O02298
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GCY35_CAEEL
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Soluble guanylate cyclase gcy-35 (EC 4.6.1.2)
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MFGWIHESFRQLVTRKYGKDIWEKIVHMSKFELGTESEIAHYYNDDETLRLVNSMANVIGIPIEEIWEAYGGFLIQFTMETGWDELLRAMAPDLEGFLDSLDSLHYFIDHVVYKTKLRGPSFRCDVQADGTLLLHYYSKRSGLYPIVKGVVREVARRIYDTEVVMKVQERKQEHLDAFVTEHVVFVITQIENANSTQPKSISSKADSQIDLSTGIYEISSSDFSLAFPYHICFDPDLFVEHFGNFIKKTFPNAMRQETRVTDLLELVHPEVPFSYESIKYYKNSLFVFRLKGLGDIVHNANDEAKTVLLKGSMVFIDEGKYILYMCSVNVTTVRELIERNLHLSDMQRHDGTRDVIMLNQSRMSQVELNRTLEETTKKLKKMAQELEIEKQKTDELLCELMPASVADSLRSGKAMDAKEFADCTLLFTDIVTFTNICAMCTPYDVVTLLNDLYLRFDRLVGLHDAYKVETIGDAYMIVGGVPERCENHAERVLNISIGMLMESKLVLSPITHKPIKIRLGVHCGPVVAGVVGIKMPRYCLFGDTVNVANKMESNGIQCKIHVSETGKLNGLKANPSYVFIDRGNTEIRGKGMMYTYFLERNDRKSVWELCSRPRSGEQTIDGYMELHDQSIYQEEGGQQENLTVENGNSAQNNHNNNNNTHHSGRKLMNGSSVDPGSHHIRSPTCTIS
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Plays a central role in social feeding behavior and oxygen sensation by synthesizing 3',5'-cyclic guanosine monophosphate (cGMP) from GTP. Oxygen, which binds to its heme-binding sites, probably regulates social behavior by modulating its activity. cGMP is a common second messenger in sensory transduction and is implicated in oxygen sensation. Indeed, C.elegans exhibits a strong behavioral preference for 5-12% oxygen, avoiding higher and lower oxygen levels a higher level of oxygen inducing a naturally polymorphic social feeding behavior. Involved in avoidance of hyperoxia and for oxygen-induced aggregation and bordering, probably by mediating oxygen-sensing in URX, AQR and PQR sensory neurons.
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O02324
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FABP8_CAEEL
|
Fatty acid-binding protein homolog 8
|
MVSMKEFIGRWKLVHSENFEEYLKEIGVGLLIRKAASLTSPTLEIKLDGDTWHFNQYSTFKNNKLAFKIREKFVEIAPDERSYNTLVTFENGKFISHQDKIKENHHSSVFTTWLENGKLLQTYQSGSVICRREFVKE
|
Lysosomal lipid chaperone which binds to a wide range of unsaturated fatty acids, including high affinity binding to oleic acid and oleoylethanolamide, to transport them into the nucleus. As part of a lysosome-to-nucleus retrograde lipid signaling pathway, translocates into the nucleus where it activates the transcription of genes promoting longevity and activation of mitochondrial beta oxidation.
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O02326
|
CFI1_CAEEL
|
AT-rich interactive domain-containing protein cfi-1 (ARID domain-containing protein CFI-1)
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MSVRIDEPQLFVSMSKEPTQETVNVGGHHDDSSSNCDERVDDQTEEQKSPPASPDLTANLNVFDLESRQKVVQRLLNSQLNLSNLRAPLNLPPIFQALQGPFSIQQQLLGLASGLTAISPGLDDYDEENTNQGEPEDLTLGGFRKETSVKSEEPSESGINASGPAWSYEEQFKQLYELSDDVKRKEWLDDWLNFMHRIGKPVTRIPIMAKQVLDLYELYRLVVQHGGLVEIINKKLWREITKGLNLPSSITSAAFTLRTQYQKYLYDYECEKEKLSNQSDLQQAIDGNRREAPGRRTAPSFPLPFQLPHAASAAATMLNNQLNGLGMRNDLLDDENTLSLQASGLFGTSYGAEQMAILEAHQRNLERAQRAVQQQVARQSLGLTACSNGNGGNIHNSGRESTSSNDSDIPAKRPKLENDVKTNGASSMRISTKHSDNSKTSMSVSMEINGITYQGVLFALDETVSES
|
Transcription factor. Regulates neuronal subtype identity. Involved in motor neuron fate determination and maintenance, acting as a transcriptional repressor to counteract gene activation by transcription factor unc-3 in a subset of motor neurons. Probably acts by binding to specific promoter elements. Promotes differentiation of URA sensory neurons and prevents them from expressing male-specific CEM neuronal features. Promotes differentiation of AVD and PVC interneurons and their glutamate receptor expression.
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O02365
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IFA2_CAEEL
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Intermediate filament protein ifa-2 (Cel IF A2) (Intermediate filament protein A2) (IF-A2)
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MTDPDSYRSSITSRPSFNRTVTSSSQNYGAPGSGNRVLKIVTETHSSSVSSGLSPYGQNAASTIRDNREREKKEIMELNDRLASYIEKVRFLDAQNRKLDADLKMLQGRFGKSTGSVKVMYEMEITTATNVVKQTGKDHGETEKEIRKLQDQLDELRKKFEEAQRGRAEDRLKIDDLLVTLSNLEAEINLLKRRIALLEEEVARLKKENFRLTSELQRVRIELDQETLLRIDNQNKVKTILEEIDFMKRGFETELKELQAQAARDTTSENREYFKNELANAMRDIRAEYDQIMNGNRNDMESWYQLRVQEINTQSNRQNAENNYQKEEVKRLRNQTSELRQKLSDLESRNLLLEKQIEDLNYQLEDDQRSYEAALNDKDAQIRKLREECQALMVELQMLLDTKQTLDGELKVYRQMLEGNSEGNGLRQLVEKVVRTSAINEEADTETMRVVKGEHSSRTSYQRSAKGNVAIKETSPEGKFVILENTHRAKEEPLGDWKLKRKIDGKREIVFTFPSDYILHPFQSVKIFARGQGIANPPEVLIFEGDETFGVGANVQTILYNNKGEERATHIQRQSQQTTSS
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Cytoplasmic intermediate filaments provide mechanical strength to cells. Essential protein, involved in attachment structures in epidermal cells that connect muscles to the external cuticle. Probably acts by forming hypodermal hemidesmosome complexes that help mediate muscle-cuticle force transduction. Although expressed during embryogenesis, it is not required for embryonic development of muscle-cuticle linkages nor for the localization of other proteins to the hemidesmosomes in embryos.
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O02372
|
OB76A_DROME
|
General odorant-binding protein lush
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MKHWKRRSSAVFAIVLQVLVLLLPDPAVAMTMEQFLTSLDMIRSGCAPKFKLKTEDLDRLRVGDFNFPPSQDLMCYTKCVSLMAGTVNKKGEFNAPKALAQLPHLVPPEMMEMSRKSVEACRDTHKQFKESCERVYQTAKCFSENADGQFMWP
|
Odorant-binding protein required for olfactory behavior and for activity of pheromone-sensitive neurons. Binds to alcohols and mediates avoidance behavior to high concentrations of alcohols, the alcohol-binding possibly resulting in activation of receptors on T2B neurons, the activation of these receptors inhibiting these neurons. Acts in concert with Snmp and lush to capture cVA molecules on the surface of Or67d expressing olfactory dendrites and facilitate their transfer to the odorant-receptor Orco complex. Required for cVA response, probably by binding to VA. May act by serving as an adapter that bridges the presence of gaseous pheromone molecules, cVA, to activation of specific neuronal receptors expressed on T1 olfactory neurons, possibly via a specific conformational change induced by cVA that in turn activates T1 receptors. T1 neurons are excited by the pheromone VA, while T2 neurons are inhibited by alcohols. Also binds to phthalates.
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O02373
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UGDH_DROME
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UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) (Protein sugarless) (Protein suppenkasper)
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MKVCCIGAGYVGGPTCAVMALKCPDIVITLVDKSSERIAQWNSDKLPIYEPGLDEVVKKCRNVNLFFSTDIETAIKEADLIFISVNTPTKTCGNGKGRAADLKYVESAARMIAEIAQSNKIVVEKSTVPVRAAESIMHILRANQKPGIHYDILSNPEFLAEGTAINDLLNADRVLIGGEETPEGHQAVEKLSWIYEHWIPKQNILTTNTWSSELSKLAANAFLAQRISSINSLSAVCEATGADVSEVARAVGLDSRIGSKFLQASVGFGGSCFQKDILNLIYICENLNLPEVAAYWQQVIDMNEYQKRRFSQKIIESLFNTVSDKRIAILGFAFKKNTGDTRETAAITVCQTLLEEGAALDIYDPKVEPEQIIDDLTHPSVTESPEKVKKAVQIHSDPYSAVRATHALVICTEWDEFVDLDFKRIYQSMMKPAYIFDGRKILDHERLQQIGFHVQTIGKKYQRTGLLRSWGIVPQL
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Involved in the biosynthesis of glycosaminoglycans hyaluronan, chondroitin sulfate and heparan sulfate. Required for wingless signaling in different tissues.
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O02482
|
UNC37_CAEEL
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Transcription factor unc-37 (Uncoordinated protein 37)
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MKASYLETLDRIKDEHAEMSKHVNQQRSDIEKVALEKENMNRSYMTYAEVSNTLRSDLRKAEEINKRLQEFIMQSLAPQLSQDNQANCLAALEAFKTASPRENGNGAPALPPGFPPGAAGMLGMMPNMPFGMSPAMSQLFNQFASPHVNGGDGAGGSSGGASEAKKAKLEDPDDGELEIDVTNDDHPSTASNGGAANKNGRDSTNSVASSGASTPSIASNSRARQQQQPLAGLQGLEQMNFLAGFNPNLLRQASAAGGFNFLNDPHAQARLAAAIGQIGSRPAYSFKIVDGGVPTPTSFPPDAQKGPGIPTGLKKKMELNHGEVVCAATISRDNSRVYTGGKGCVKIWDVKESDISGATVVNRPPIASLDCLKENYIRSCKLFEDGNTLLIGGEASTVALWDLTTETKTLDLETDSQACYALAMSPDEKLLFACLADGNILIYDIHNKVKVGTLPGHQDGASCLDLSKDGTKLWSGGLDNSVRCWDLAQRKEVAKHDFASQVFSLGCCPNDEWVAVGMENNYVEVLSTTGKEKYQLTQHESCVLSLKFAHSGKFFISTGKDNALNAWRTPYGASLFQLKENSSVLSCDISFDDSLIVTGSGEKKATLYAVEY
|
Transcriptional corepressor that functions with the neural specificity gene unc-4 to govern motor neuron identity. In concert with unc-4, represses the expression of VB-specific genes such as ceh-12, thereby preventing the adoption of VB motor neuron fate. May function with transcription factor mls-1 to promote uterine muscle specification and formation.
|
O02495
|
SYB1_CAEEL
|
Synaptobrevin-1 (Synaptobrevin-related protein 1)
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MDAQGDAGAQGGSQGGPRPSNKRLQQTQAQVDEVVGIMKVNVEKVLERDQKLSQLDDRADALQEGASQFEKSAATLKRKYWWKNIKMMIIMCAIVVILIIIIVLWAGGK
|
Involved in the targeting and/or fusion of transport vesicles to their target membrane. Acts in neuronal exocytosis of synaptic transmission. Likely to have a role in cholinergic transmisson. Required for viability, coordinated movement and M3 pharynx motor neuron function.
|
O02604
|
DRTS_PLAVI
|
Bifunctional dihydrofolate reductase-thymidylate synthase (DHFR-TS) [Includes: Dihydrofolate reductase (EC 1.5.1.3); Thymidylate synthase (EC 2.1.1.45)]
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MEDLSDVFDIYAICACCKVAPTSEGTKNEPFSPRTFRGLGNKGTLPWKCNSVDMKYFSSVTTYVDESKYEKLKWKRERYLRMEASQGGGDNTSGGDNTHGGDNADKLQNVVVMGRSSWESIPKQYKPLPNRINVVLSKTLTKEDVKEKVFIIDSIDDLLLLLKKLKYYKCFIIGGAQVYRECLSRNLIKQIYFTRINGAYPCDVFFPEFDESQFRVTSVSEVYNSKGTTLDFLVYSKVGGGVDGGASNGSTATALRRTAMRSTAMRRNVAPRTAAPPMGPHSRANGERAPPRARARRTTPRQRKTTSCTSALTTKWGRKTRSTCKILKFTTASRLMQHPEYQYLGIIYDIIMNGNKQGDRTGVGVMSNFGYMMKFNLSEYFPLLTTKKLFLRGIIEELLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFHREVNDLGPIYGFQWRHFGAEYTNMHDNYEDKGVDQLKNVIHLIKNEPTSRRIILCAWNVKDLDQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSIFTHMIAQVCNLQPAQFIHILGNAHVYNNHVDSLKVQLNRIPYPFPTLKLNPEVKNIEDFTISDFTIENYVHHDKITMEMAA
|
Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
|
O02626
|
MADD_CAEEL
|
MAP kinase-activating death domain protein (Aboc, expulsion defective protein 3) (Regulator of presynaptic activity aex-3)
|
MNDKEKEICPRLIDFLVVVGKRNRTRGASQSSPDATTDTTVTYPEILRRYPTDDHKDFILPTDVTVFCQPEGCTTTSARLRKNARNDPQFFVFMLTEKDSAKVRYGICLNFYQSFDRRSTPKDEIKKVPDDAHHKKRDSHVSLTSLCFISHHPFVSIFHQVLLLLKRIIDSSNHRAAQRTGLKDVVWAILTGHYNEPIVPEVMKEIKEIETWILMLLSSPVPVPGKTKVQIEVMPMDLSQVFEFALPDHTRFTLIDFPLHIPFEILGIDMALRVLTAAMLEFKIVIQSRNYNAVSMCILSIVALLYPLEYMFPVIPLLPAYMPSAEQLLLAPTPFLIGVPSSFFHHRKIRELPSDVILVDLDTNCLQVPDDLYIPDLPEPDATHLKERLKNAINKMTTMTVDNETSVTDADFGIDIDSVDVACRVAMVQFFNSANVFGNFSEHTRTLRLYPRPVVSLQTDSFLRSRPQCTQLITDLCRTQAVEYFAECCLCPKNETFVRVQAGIESAEQVGDKPKWFSESLMPVHFMVYPNNSTLDSAIRVYNAEIDNDDYEDDSATSTENSNSIDDLVFDENQVTDAGGEVTKPLAEVNYIYKEPMTLELPQSESVVSIDSSLSSGRSSPDSSLSTSAVDSEADFARLADNLALKSNSQGAFSFDHGSDSEYESTPVSQRRKTIHNPGSDASDTPTSRGSIKSGLRMKGLTTLTDSGEKVLGPSLMNAINGYAEKSQSVFSQVINKTAPKAQALKERTMKPLANRIEQSQHIVRSKTQPNPTSQQTANQQSKNQQTVKEFCDQALVGQSVGMFSAPKLKRLMEDESLRELVCSKLNLGLEVKLSEDEYVKEVQLTKGQFKAYVKILKACLEGIEVSFNTPGCCGFASVFHVLEIAHTHYWAMGGGEVITPSSSAPSTMTTPSEHSNDILKESRPKLPASTIDLRTPTKPLGQNVTPTSTNNHEIAQSTRSPALPPPVPPREAPPIPKRNPPPLGAPPKVPEGARAPPPLPPRPKVKTTAVDETPQNLVPNNQPAQPSSPSFLADADEQTKPLLKPAPPTTLPVGKQEPCKVLPTPNEPVRHYIYQELILAVQHQIWQNLQFWENAFVDLVAQEREIVGMDQEPSEMIDRYSALNDSEKKRLELEEDRLLSTLLHNMTAYMIMCGTGQKALQQKVRRLLGKAHIGLVCSKEINKLLDELPSTQGNFIPLKPLGSRLVQKQSFTVCPGQSSDGQMMFMEVCDDAVVLRSITGAATERWWYERLVNITYSPKTKILCLWRRHDDKVHMHKFHTKKCRELYQCMKAAMERAAARGKVNVEGRALGGEFPVHDTETNQGGLLQVRCDGVAVIFAHNQIFIGLSNIKKCNTFGGNVFLLEEFDRKKGEIIQRRYFSQMADQICYAVLCVFSLAAAGHKKEEHSK
|
Guanyl-nucleotide exchange factor that regulates small GTPases (By similarity). Converts GDP-bound inactive form of rab-3 and cab-1 to the GTP-bound active forms. Regulator of presynaptic activity that interacts with rab-3 to regulate synaptic vesicle release. Is also a regulator of the cab-1 synaptic transmission pathway. Probably by converting rab-3 to its GTP-bound active form, plays a role in the recruitment of endophilin unc-57 to synaptic vesicles. Probably by activating rab-3 and thus regulating the trafficking of dense-core vesicles, plays a role in AVG neuron-mediated formation of the right axon tract of the ventral nerve cord. Regulates anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP). Probably by regulating DMP, required for fatty acid uptake by intestinal cells.
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O02655
|
DCAM_CAEEL
|
S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain]
|
MSATSATNFAVQTHPVKAPDEEYFFEGAEKLLELWFCSSTQNETRSLRIIPREEIDAMLDIARCKILHSKHNESIDSYVLSESSLFISDNRVILKTCGTTRLLAALPVIMQLAGAYAGLDQVQSVYYSRKNFLRPDLQPSLHKNFDAEVEYLDSFFVDGHAYCLGSLKQDRWYLYTFHREVEFPAHKQPDHTLEILMSDLDEEVLHKFTKDYAVDGNDCFMRAGIDKIIPAGADVHDELFDPCGYSMNAYMNDTDQYATIHVTPEKAFSFASFETNQDLVCLYSQTRKVLQCFRPNKILMTVFANDISEKGKDAQQQLWDRELPGYRRTNVQFVRLETETLVYAHFVRKASTGQDSSSSDEDDGERSD
|
Essential for biosynthesis of the polyamines spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
|
O02658
|
GLC7C_CAEEL
|
Serine/threonine-protein phosphatase PP1-gamma (EC 3.1.3.16) (CeGLC-7-gamma) (Glc seven-like phosphatase 3)
|
MTAPMDVDNLMSRLLNVGMSGGRLTTSVNEQELQTCCAVAKSVFASQASLLEVEPPIIVCGDIHGQYSDLLRIFDKNGFPPDVNFLFLGDYVDRGRQNIETICLMLCFKIKYPENFFMLRGNHECPAINRVYGFYEECNRRYKSTRLWSIFQDTFNWMPLCGLIGSRILCMHGGLSPHLQTLDQLRQLPRPQDPPNPSIGIDLLWADPDQWVKGWQANTRGVSYVFGQDVVADVCSRLDIDLVARAHQVVQDGYEFFASKKMVTIFSAPHYCGQFDNSAATMKVDENMVCTFVMYKPTPKSMRRG
|
Probable phosphatase which plays a redundant role with gsp-4 in spermatogenesis by regulating sister chromatid segregation during meiosis. In addition, involved in sperm motility by controlling the dynamic disassembly of major sperm proteins (MSP) in the spermatozoan pseudopodium.
|
O02662
|
ADRB3_CANLF
|
Beta-3 adrenergic receptor (Beta-3 adrenoreceptor) (Beta-3 adrenoceptor)
|
MAPWPHGNGSVASWPAAPTPTPDAANTSGLPGAPWAVALAGALLALEVLATVGGNLLVIVAIARTPRLQTMTNVFVTSLATADLVVGLLVVPPGATLALTGRWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRRARAAVVLVWVVSAAVSFAPIMSKWWRVGADAEAQRCHSNPHCCAFASNIPYALLSSSVSFYLPLLVMLFVYARVFLVATRQLRLLRRELGRFPPAESPPAASRSRSPGPARRCASPAAVPSDRLRPARLLPLREHRALRTLGLIVGTFTLCWLPFFVANVMRALGGPSLVPSPALLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCRREEHRAAASPPGDPSAAPAALTSPAESSRCQALDGASWGIS
|
Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.
|
O02671
|
LEPR_PIG
|
Leptin receptor (LEP-R) (OB receptor) (OB-R) (CD antigen CD295)
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MTCPKFSVALLHWEFIYVITAFDLAYPITPWKFKLSCMPPNTTYDFLLPAGISKNTSTLNGHDEAVVETELNSSGTYLSNLSSKTTFHCCFWSEEDKNCSVHADNIAGKAFVSAVNSLVFQQTGANWNIQCWMKEDLKLFICYMESLFKNPFKNYDLKVHLLYVLLEVLEGSPLLPQKGSFQSVQCNCSARECCECHVPVSAAKLNYTLLMYLKITSGGAVFHSPLMSVQPINVVKPDPPLGLHMEITDTGNLKISWSSPTLVPFQLQYQVKYSENSTTNMREADEIVSDTSLLVDSVLPGSSYEVQVRGKRLDGPGIWSDWSTPFTFTTQDVIYFPPKILTSVGSNISFHCIYKNENKIVSSKKIVWWMNLAEKIPQSQYDVVGDHVSKVTFPNMNATKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTNAIQSLVGSTLQLRYHRSSLYCSDVPSVHPISEPKDCQLQRDGFYECIFQPIFLLSGYTMWIRINHPLGSLDSPPTCVIPDSVVKPLPPSSVKAEITAKIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKIYEVYDTKLKSTSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSTPAYTVVTDVKVPIRGPEFWRIINEDATKKERNITLLWKPLMKNDSLCSVRSYVVKHHTSRHGTWSEDVGNHTKLTFLWTEQAHSVTVLAVNSIGASSANFNLTFSWPMSKVNIVQSLSAYPLNSSCVGLSWLLSPSDYNLMYFILEWKILNEDHEIKWLRIPSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDGEKHRNDAGLYVIVPIIISSSILLLGTLLMSHQRMKKLFWEDVPNPKNCSWAQGLNFQKPETFEHLFIKHTESVTFGPLLLEPETISEDISVDTSWKNKDEMVPPTTVSLLLTTPDLEKSSICISDQRSSAHFSEAESMEITREDENRRQPSIKYATLLSSPKSGETEQEQELVSSLVSRCFSSSNSLPKESFSNSSWEIETQAFFILSDQHPNMTSPHLSFSEGLDELMKFEGNFPKEHNDERSVYYLGVTSIKKRESDVFLTDESRVRCPFPAHCLFADIKILQESCSHLVENNFNLGTSGQKTFVSYMPQFQTCSTQTQKIMENKMYDLTV
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Receptor for hormone LEP/leptin (By similarity). On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity (By similarity). Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis. Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T-cells. Leptin increases Th1 and suppresses Th2 cytokine production (By similarity).
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O02691
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HCD2_BOVIN
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3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-estradiol 17-dehydrogenase) (EC 1.1.1.62) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+))) (EC 1.1.1.239) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (3alpha(or 20beta)-hydroxysteroid dehydrogenase) (EC 1.1.1.53) (7-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.159) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH)
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MAAACRSVKGLVALITGGASGLGLATAERLVGQGATAVLLDLPNSDGETQAKKLGKSCAFAPADVTSEKDVQAALTLAREKFGRVDVAVNCAGIAVASKTYNLKKSQAHTLEDFQRVINVNLIGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPMGIRVMTIAPGLFGTPLLTTLPDKVRNFLASQVPFPSRLGDPAEYAHLVQAIIENSFLNGEVIRLDGAIRMQP
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Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism. Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA. Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway. Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids. Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel. Has phospholipase C-like activity toward cardiolipin and its oxidized species. Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis. By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). Essential for structural and functional integrity of mitochondria. In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
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O02695
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PTPR2_MACNE
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Receptor-type tyrosine-protein phosphatase N2 (R-PTP-N2) (EC 3.1.3.-) (EC 3.1.3.48) (M1851) [Cleaved into: IA-2beta60]
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MALPLLLLLLLLLPPRVLPAAPSSVPHGRQLPGRLGCLLEEGLCGASEACVNDGVFGRCQKVPAMDFYRYEVSPVALQRLRVALQKLSGTGFTWQDDYTQYVMDQELADLPKTYLRHPEASGPARPSKHSIGSERRYSQEGGAALAKAFRRHLPFLEALSQAPASDALARTRMAQDRPRAEGDDRFSKSILTYVAHTSVLTYPPGPQAQLPEDLLPRTLSQLQPDELSPKVDSSVERHHLMAALSAYAAQRPPAPPGKGSLEPQYLLRAPSRMPRPLLSPAVPQKWPSPLGDPEDPPSTGEGARIHTLLKDLQRQPAEARGLSDLELDSMAELMAGLMQGMDHRGALGGPGKAALGESGEQADGPKAALRGESFPDDGVQDDDDRLYQEVHRLSATLGGLLQDHGSRLSPGALPFAKPLKMERKKSERPEASLSSEEETAGVENVKSQTYSKDLLGQQPHSEPGAGAFGELQNQMPGPSEEEQSLPAGAQEALGDGLQLEVKPSEEEARGYIVTDRDPLRPEEGRQLVEDVARLLQMPSSTFADVEVLGPAVTFKVGANVQNVTTADVEKATVDNKDKLEETSGLKILQTGVGSKSKLKFLPPQAEQEDSTKFIALTLVSLACILGVLLASGLIYCLRHSSQHRLKEKLSGLGRDPGADATAAYQELCRQRMATRPPDRPEGPHTSRISSVSSQFSDGPMPSPSARSSASSWSEEPVQSNMDISTGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQKEENVPKNRSLAVLTYDHSRVLLKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLTENGVRQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWYDRGVPSSSRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAILKALPQ
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Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH). Required to maintain normal levels of renin expression and renin release. May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization. Has phosphatidylinositol phosphatase activity the PIPase activity is involved in its ability to regulate insulin secretion. Can dephosphorylate phosphatidylinositol 4,5-biphosphate, phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate. Regulates PI(4,5)P2 level in the plasma membrane and localization of cofilin at the plasma membrane and thus is indirectly involved in regulation of actin dynamics related to cell migration and metastasis upon hydrolyzation of PI(4,5)P2 cofilin is released from the plasma membrane and acts in the cytoplasm in severing F-actin filaments.
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O02696
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PI3R5_PIG
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Phosphoinositide 3-kinase regulatory subunit 5 (PI3-kinase regulatory subunit 5) (IB PI3-kinase p101 subunit) (PI3-kinase p101 subunit) (Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit) (PtdIns-3-kinase regulatory subunit) (PtdIns-3-kinase p101) (p101-PI3K)
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MQPGATTCTEDRIQHALERCLHGLSLSRRSTSWSAGLCLNCWSLQELVSRDPGHFLILLEQILQKTREVQEKGTYDLLAPLALLFYSTVLCTPHFPPDSDLLLKAARTYHRFLTWPVPYCSICQELLTFIDAELKAPGISYQRLVRAEQGLSTRSHRSSTVTVLLLNPVEVQAEFLDVADKLSTPGPSPHSAYITLLLHAFQATFGAHCDLSGLHRRLQSKTLAELEAIFTETAEAQELASGIGDAAEARQWLRTKLQAVGEKAGFPGVLDTAKPGKLRTIPIPVARCYTYSWNQDSFDILQEILLKEQELLQPEILDDEEDEDEEDEEEDLDADGHCAERDSVLSTGSAASHASTLSLASSQASGPTLSRQLLTSFVSGLSDGVDSGYMEDIEESAYERPRRPGGHERRGHRRPGQKFNRIYKLFKSTSQMVLRRDSRSLEGSPDSGPPLRRAGSLCSPLDSPTLPPSRAQGSRSLPQPKLSPQLPGWLLAPASRHQRRRPFLSGDEDPKASTLRVVVFGSDRISGKVVRAYSNLRRLENNRPLLTRFFKLQFFYVPVKRSRGTGTPTSPAPRSQTPPLPTDAPRHPGPAELGAAPWEESTNDISHYLGMLDPWYERNVLGLMHLPPEVLCQSLKAEPRPLEGSPAQLPILADMLLYYCRFAARPVLLQVYQTELTFITGEKTTEIFIHSLELGHSAATRAIKASGPGSKRLGIDGDREAVPLTLQIIYSKGAISGRSRWSNMEKLCTSVNLSKACRQQEELDSSTEALTLNLTEVVKRQTPKSKKGFNQISTSQIKVDKVQIIGSNSCPFAVCLDQDERKILQSVIRCEVSPCYKPEKSSLCPPPQRPSYPPAPATPDLCSLLCLPIMTFSGALP
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Regulatory subunit of the PI3K gamma complex. Required for recruitment of the catalytic subunit to the plasma membrane via interaction with beta-gamma G protein dimers. Required for G protein-mediated activation of PIK3CG.
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O02697
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PK3CG_PIG
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Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.137) (EC 2.7.1.153) (EC 2.7.1.154) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K)
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MELENYEQPVVLREDNRRRRRRMKPRSTAASLSSMELIPIEFVLPTSQRNTKTPETALLHVAGHGNVEQMKAQVWLRALETSVSADFYHRLGPDHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKVLHRSPGQIHVVQRHAPSEETLAFQRQLNALIGYDVTDVSNVHDDELEFTRRRLVTPRMAEVAGRDPKLYAMHPWVTSKPLPEYLLKKITNNCVFIVIHRSTTSQTIKVSADDTPGTILQSFFTKMAKKKSLMDIPESQNERDFVLRVCGRDEYLVGETPIKNFQWVRQCLKNGEEIHLVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRTADLTVFVEANIQYGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSGKTSAEMPSPESKGKAQLLYYVNLLLIDHRFLLRHGEYVLHMWQLSGKGEDQGSFNADKLTSRTNPDKENSMSISILLDNYCHPIALPKHRPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKDPKAYPKLFSSVKWGQQEIVAKTYQLLAKREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIDMLQKVTIDIKSLSAEKYDVSSQVISQLKQKLENLQNLNLPQSFRVPYDPGLKAGALVIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLSHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMISETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSLHFQKFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKSEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA
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Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Required for B-lymphocyte development and signaling. Together with other PI3Ks are involved in the oxidative burst produced by neutrophils in response to chemotactic agents. Together with PIK3CD regulate neutrophil extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contribute to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis (By similarity).
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O02703
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BAX_BOVIN
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Apoptosis regulator BAX
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MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGETPELGLEQVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAAEMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG
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Plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.
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O02705
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HS90A_PIG
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Heat shock protein HSP 90-alpha (EC 3.6.4.10)
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MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDSSAAVTEEMPPLEGDDDTSRMEEVD
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Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response.
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O02713
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S22A2_PIG
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Solute carrier family 22 member 2 (Apical organic cation transporter) (Organic cation transporter 2)
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MLTVDDILEHTGEFNFFQKQTFFLLALLSAAFTPIYVGIVFLGFIPDHRCRSPGVAELSQRCGWSLAEELNYTVPGPGPAGQAFPRQCRRYEVDWNQSTLGCVDPLAGLAANSSHLPLGPCRYGWVYDTPGSSIVTEFDLVCANSWLLDLFQSAVNVGFFIGSVGIGYIADRFGRKLCLLLTILINAVSGVLMAISPTYTWMLVFRLIQGLVSKAGWMIGYILITEFVGLSYRRTVGIFYQVAFTFGLLVLAGVAYALPHWRWLQFTVTLPNFCFLFYYWCVPESPRWLISQNKNAKAMSIIKHIAKKNGKSLPASLQSLRPDEEVGEKLKPSFLDLVRTPQIRKHTLILMYNWFTSAVLYQGLVMHMGLAGSNLYLDFFYSALVEFPAALLILLTIDRLGRRHPWAASNVVAGAACLASVFIPEDPHWLRITVLCLGRMGITMAYEMVCLVNAELYPTFIRNLGVLVCSSMCDIGGIITPFLVYRLTDIWHELPLVVFAVVGLIAGGLVLLLPETKGKTLPETIEEAETMRRPRKNKEKIIYLQVKKLDIPPN
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Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics. Functions as a Na(+)-independent, bidirectional uniporter. Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (By similarity). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow. Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters. Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system. Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium. Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN). Mediates the uptake and efflux of quaternary ammonium compound choline. Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine. Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity).
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O02718
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BCL2_BOVIN
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Apoptosis regulator Bcl-2
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MAHAGGTGYDNREIVMKYIHYKLSQRGYEWDAGDAGAAPPGAAPAPGILSSQPGRTPAPSRTSPPPPPAAAAGPAPSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARERFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDSIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKALLSLALVGACITLGAYLGHK
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Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release.
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O02720
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LEP_CANLF
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Leptin (Obesity factor)
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MRCGPLCRFLWLWPYLSCVEAVPIRKVQDDTKTLIKTIVARINDISHTQSVSSKQRVAGLDFIPGLQPVLSLSRMDQTLAIYQQILNSLHSRNVVQISNDLENLRDLLHLLASSKSCPLPRARGLETFESLGGVLEASLYSTEVVALNRLQAALQDMLRRLDLSPGC
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Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (By similarity). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (By similarity). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (By similarity). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (By similarity).
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O02740
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GUC2F_BOVIN
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Retinal guanylyl cyclase 2 (RETGC-2) (EC 4.6.1.2) (Guanylate cyclase 2F, retinal) (Guanylate cyclase F) (GC-F) (Rod outer segment membrane guanylate cyclase 2) (ROS-GC2)
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MFLAPWPFSHLMLWFVTLGRQRGQHGLASFKLLWCLWLLVLMSLPLQVWAPPYKIGVVGPWTCDPLFSKALPEIAAQLATERINKDPALDLGHSLEYVIFNEDCQASRALSSFISHHQMASGFIGPANPGYCEAASLLGNSWDKGIFSWACVNYELDSKNSHPTFSRTLPSPIRVLLTVMKYFQWAHAGVISSDEDIWVHTAYRVASALRSRGLPVGVVLTTGQDSQSIQKALQQIRQADRIRIIIMCMHSTLIGGETQTHLLEWAHDLQMTDGTYVFVPYDTLLYSLPYKHTPYKVLRNNPKLREAYDAVLTITVESQEKTFYQAFEEAAARGEIPEKLESDQVSPLFGTIYNSIYFIAQAMNNAMKENGWASAASLVQHSRNVQFYGFNQLIRTDANGNGISEYVILDTNWKEWELHSTYTVDMETELLRFGETPIHFPGGRPPRADAQCWFADGRICQGGINPTFALMVCLALLIALLSINGFAYFIRHRINKIQLIKGPNRILLTLEDVTFINPHFGSKRGSHASVSFQITSEVQSGRSPRLSFSSGSLTPATCENSNIAIYEGDWVWLKKFPSGNFGDIKSVESSASDIFEMMKDLRHENINPLVGFFYDSGVFAIVTEFCSRRSLEDILMNQDVKLDWMFKSSLLLDLIKGMKYLHHREFAHGRLKSRNCVVDGRFVLKVTDYGFNDILETLRLSQEEPSAEELLWTAPELLRAPRGSRLRSFAGDVYSFAIIMQEVMVRGTPFCMMDLPAKEIIERIKKPPPVYRPVVPPEHAPPECLQLMKQCWAEAAEQRPTFDEIFNQFKTFNKGKKTNIIDSMLRMLEQYSSNLEDLIQERTEELEIEKQKTEKLLTQMLPPSVAESLKKGCTVEPEGFDLVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPKRNGMRHAAEIANMSLDILSSVGTFKMRHMPEVPVRIRIGLHSGPVVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSHSTVTILRTLGEGYEVELRGRTELKGKGTEETFWLVGKKGFTKPLPVPPPVGKDGQVGHGLQSVEIAAFQRRKQKSSW
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Responsible for the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-asociated proteins to the photoreceptor outer segment membrane (By similarity).
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O02741
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ISG15_BOVIN
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Ubiquitin-like protein ISG15 (Interferon-stimulated gene product 17) (Ubiquitin cross-reactive protein) (BoUCRP)
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MGGDLTVKMLGGQEILVPLRDSMTVSELKQFIAQKINVPAFQQRLAHLDSREVLQEGVPLVLQGLRAGSTVLLVVQNCISILVRNDKGRSSPYEVQLKQTVAELKQQVCQKERVQADQFWLSFEGRPMDDEHPLEEYGLMKGCTVFMNLRLRGG
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Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Exhibits antiviral activity towards both DNA and RNA viruses. The secreted form of ISG15 can: induce natural killer cell proliferation, augment lymphokine-activated-killer (LAK) activity, induce dendritic cell maturation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity (By similarity). The secreted form acts through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine kinases including LYN, HCK and FGR which leads to secretion of IFNG and IL10 the interaction is mediated by ITGAL (By similarity). In response to IFN-tau secreted by the conceptus, may ligate to and regulate proteins involved in the release of prostaglandin F2-alpha (PGF), and thus prevent lysis of the corpus luteum and maintain the pregnancy.
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O02750
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LEP_PANTR
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Leptin (Obesity factor)
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VPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNMIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC
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Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (By similarity). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (By similarity). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 wich promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (By similarity). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (By similarity).
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O02755
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CEBPB_BOVIN
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CCAAT/enhancer-binding protein beta (C/EBP beta)
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MQRLVVWDPVCLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPADRPGPRPPTGELGSIGEHERAIDFSPYLEPLGAPQAPAPTTASDTFEAAPSAPAPVPASSGQHHDFLSDLFSDDYGGKNCKKAAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKATPAAAACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTGENERLQKKVEQLSREVSTLRNLFKTLPEPLLASSGHC
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Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing. During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation. Essential for female reproduction because of a critical role in ovarian follicle development. Restricts osteoclastogenesis: together with NFE2L1 represses expression of DSPP during odontoblast differentiation (By similarity).
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O02766
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CP8B1_RABIT
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7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.14.139) (7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase) (CYPVIIIB1) (Cytochrome P450 8B1) (Sterol 12-alpha-hydroxylase)
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MVLWGLLGALLMVMVGWLCLPGLLRQRRPQEPPLDKGSIPWLGHAMTFRKNMLEFLKHMRSKHGDVFTVQLGGQYFTFVMDPVSFGPILKDGQRKLDFVEYAKGLVLKVFGYQSIEGDHRMIHLASTKHLMGHGLEELNKAMLDSLSLVMLGPEGRSPDASRWHEDGLFHFCYGVMFKAGYLSLFGHTSDKRQDLLQAEEIFIKFRRFDLLFPRFVYSLLGPREWREVGRLQQLFHELLSVKHNPEKDGMSNWIGHMLQYLSEQGVAPAMQDKFNFMMLWASQGNTGPASFWALIYLLKHPEAMRAVKEEATRVLGEPRLEAKQSFTVQLSALQHIPVLDSVMEETLRLGAAPTLYRVVQKDILLKMASGQECLLRQGDIVTLFPYLSVHMDPDIHPEPTTFKYDRFLNPNGSRKVDFYKAGQKIHHYTMPWGSGVSICPGRFFALSEMKLFVLLMVQYFDLELVDPNTPVPPIDPRRWGFGTMQPTHDVRIRYRLKPLE
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A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis. Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR NADPH--hemoprotein reductase).
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