wanglab/gogpt-training-data huggingface dataset:
Protein: Catenin alpha-2 (Alpha N-catenin) (Alpha-catenin-related protein) (P26232)
Organism: Homo sapiens (Human)
Function: May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system (By similarity). Required for proper regulation of cortical neuronal migration and neurite growth. It acts as negative regulator of Arp2/3 complex activity and Arp2/3-mediated actin polymerization. It thereby suppresses excessive actin branching which would impair neurite growth and stability. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q61301}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q61301}; Cytoplasmic side {ECO:0000250|UniProtKB:Q61301}. Cytoplasm {ECO:0000269|PubMed:16182284}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q61301}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q61301}. Cell projection, axon {ECO:0000250|UniProtKB:Q61301}. Nucleus {ECO:0000269|PubMed:16182284}.
Interaction partners:
- Catenin beta-1
- Catenin alpha-1
- Cadherin-1
- Vinculin
- Afadin
- Tight junction protein 1
- Catenin alpha-3
- Cadherin-2
- Cadherin-17
- Cadherin-8
Sequence:
MTSATSPIILKWDPKSLEIRTLTVERLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGEQIAKESQDLKEELVAAVEDVRKQGETMRIASSEFADDPCSSVKRGTMVRAARALLSAVTRLLILADMADVMRLLSHLKIVEEALEAVKNATNEQDLANRFKEFGKEMVKLNYVAARRQQELKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGISNAAQATSPTDEAKGHTGIGELAAALNEFDNKIILDPMTFSEARFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMNNTGRKEKGDPLNIAIDKMTKKTRDLRRQLRKAVMDHISDSFLETNVPLLVLIEAAKSGNEKEVKEYAQVFREHANKLVEVANLACSISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLTEAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAEMENYEAGVYTEKVLEATKLLSETVMPRFAEQVEVAIEALSANVPQPFEENEFIDASRLVYDGVRDIRKAVLMIRTPEELEDDSDFEQEDYDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEEKAKIAEQVEIFHQEKSKLDAEVAKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVINAAKKIAEAGSRMDKLARAVADQCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELIVSGTGVQSTFTTFYEVDCDVIDGGRASQLSTHLPTCAEGAPIGSGSSDSSMLDSATSLIQAAKNLMNAVVLTVKASYVASTKYQKVYGTAAVNSPVVSWKMKAPEKKPLVKREKPEEFQTRVRRGSQKKHISPVQALSEFKAMDSF
Protein: Cyclic GMP-AMP synthase (F1QCP4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Interferon regulatory factor 3
- Serine/threonine-protein kinase TBK1
- Stimulator of interferon genes protein
- Interferon
- Mitochondrial antiviral-signaling protein
- Toll-like receptor 9
- Interferon-induced with helicase C domain 1.
Sequence:
MSSHRRPGCVSPTRPDEQPKAKARAKTSGKNEAQKKDKDVYVCESEAKLQETPSLKRGRSKKQKDDASKGDCKSLDNSESKSEEKHGDISKAGSVHKKTGENDRQDSAKDKLKSKRKTAPLDCESEGKNQQTANGKSGEKTALKRPSKKEKDHPNLDREATPENSESKLEQKPIASSSRNKSAPKKGFPGAKNACDASPAVSARSPDCKLKSTEKTAVKDALGDVLKATLDKLTIKKSERSKASRCVNEITEKVIAHLKQDTTWCADIERLRTGSYYENLKICEPDEFDVMLTVPVERVDIQNFDEAGAFYSIALKRHPNKHPLDKFLNEDKTIQASEMLSEFRDGVKKAVEKATDLPYKIKIQRKKPKCPAVTLEVTEGRKNISVDFVLGLKVHRASWPELTKDGFRVEHWLGRKVKSTMKRQPFYLVPKYEGIGNAEHDGVVARDSWRISFSHIEKEILKSHGHTKTCCEGREQKCCRKECLKLLKYLLQQLKNDESKSNKMSSFCSYHAKTTLLQACASRGTDIEWAYSELANCFQQLLEDFVKHLKNHQLPNFFIPSHNLLHHVSTSNCDFLAKEIEFQLNNTFPIFS
Protein: Phosphoserine phosphatase (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (A0QJI1)
Organism: Mycobacterium avium (strain 104)
Function: Catalyzes the dephosphorylation of phosphoserine (P-Ser).
Interaction partners:
Sequence:
MNSPPKVSVLITVTGVDQPGVTATLFEVLSGHGVELLNVEQVVIRHRLTLGVLVCCPADVADGPALRHDVEAAIRKVGLDVSIERSDDVPIIREPSTHTIFVLGRPITAAAFGAVAREVAALGVNIDLIRGVSDYPVIGLELRVSVPPGADGALRTALNRVSSEEHVDVAVEDYTLERRAKRLIVFDVDSTLVQGEVIEMLAAKAGAEGQVAAITDAAMRGELDFAQSLQQRVATLAGLPATVIDEVAGQLELMPGARTTLRTLRRLGYACGVVSGGFRRIIEPLAEELMLDYVAANELEIVDGTLTGRVVGPIIDRAGKATALREFAQRAGVPMAQTVAVGDGANDIDMLAAAGLGIAFNAKPALREVADASLSHPYLDTVLFLLGVTRGEIEAADAIDGEVRRVEIPPE
Protein: Proline-rich transmembrane protein 2 (Dispanin subfamily B member 3) (DSPB3) (Q7Z6L0)
Organism: Homo sapiens (Human)
Function: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22101681, ECO:0000269|PubMed:25915028, ECO:0000269|PubMed:27172900}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Presynaptic cell membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Synapse {ECO:0000250|UniProtKB:E9PUL5}. Cell projection, axon {ECO:0000269|PubMed:22832103}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D3ZFB6}. Postsynaptic density membrane {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:D3ZFB6}.
Interaction partners:
- Synaptosomal-associated protein 25
- Probable thioesterase PNKD
- Sodium channel protein type 2 subunit alpha
- Synaptotagmin-1
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- Sodium channel protein type 1 subunit alpha
- Potassium voltage-gated channel subfamily KQT member 2
- Sodium/potassium-transporting ATPase subunit alpha-2
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Sequence:
MAASSSEISEMKGVEESPKVPGEGPGHSEAETGPPQVLAGVPDQPEAPQPGPNTTAAPVDSGPKAGLAPETTETPAGASETAQATDLSLSPGGESKANCSPEDPCQETVSKPEVSKEATADQGSRLESAAPPEPAPEPAPQPDPRPDSQPTPKPALQPELPTQEDPTPEILSESVGEKQENGAVVPLQAGDGEEGPAPEPHSPPSKKSPPANGAPPRVLQQLVEEDRMRRAHSGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK
Protein: VASt domain-containing protein (Q381J9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Calcium channel protein, putative
- Uncharacterized protein
- Phospholipid/glycerol acyltransferase domain-containing protein
- Zinc finger, MYND-type containing 10
Sequence:
MSGEIRYASGASAQALFDKQQYTMGISRNMFSPHDKVKEKKCMIPPALMKGVTVAKLWDAIFSDKAEFLQRYHGSRKETNLELSKWEYAPDMASGFRTLTFQCTVDLPRGPVDTTLNQAHRFAYTSSTSGGITLVYHVSSQTPNVPMGTTFRTEALLEITAPSEDADITLAVYGGCKKMSMGFAAIQYMANPRAIKEMTRAYQQMLEMISKDLTGDVLCVQTSDVSEGTYSAKETSVSEPSASEEVGQSSTLFQGLLLVLALVVAVSLLWHLAGLQNIGRMTSLLSARVNDQTMNSAPHPSSLADALNMGSSADTKTARPSLTQDKALHHAARDVHIQSLRQRWLEQRDRIVALEASLDKLWSFFFMQLLIIMFIVVKLFMSPS
Protein: Uncharacterized protein (O44135)
Organism: Caenorhabditis elegans
Interaction partners:
- Nematode Specific Peptide family, group D
- PDZ domain-containing protein
- BAR domain-containing protein
- Uncharacterized protein
- Uncharacterized protein C27D6.3
- Major sperm protein
- Regulator of microtubule dynamics protein 1
- BAR domain-containing protein
- non-specific serine/threonine protein kinase
- PDZ domain-containing protein
Sequence:
MADDNVSFTDAGDPTPGAKPQGGSSAMLDLLGTLNKKEDKKKKDKKGKKGKKSKGKSKTKKVRKTDKFESQNFLFRIEGTIFCAGIVVGLVVLLVFVAVAIFFSVKSGGNMVHYIHPWWGGLEESSSN
Protein: Ankyrin repeat domain-containing protein 53 (Q8N9V6)
Organism: Homo sapiens (Human)
Function: Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26820536}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26820536}. Note=Localizes at the spindle around the centrosome at prophase and prometaphase and at the spindle poles at metaphase and anaphase (PubMed:26820536). {ECO:0000269|PubMed:26820536}.
Interaction partners:
Sequence:
MASAGSTARRAGSGSWHSERGEGRGARPQPTPSGSMQQANKVSLKATWTDAESKQPSQPLPDLADHLSAQATALARPRRPASLTPPRADPSPSKESDQTAIDQTAIGSYYQLFAAAVGNVEWLRFCLNQSLREIPTDDKGFTAIHFAAQWGKLACLQVLVEEYKFPVDLLTNNSQTPLHLVIHRDNTTVALPCIYYLLEKGADLNAQTCNGSTPLHLAARDGLLDCVKVLVQSGANVHAQDAMGYKPIDFCKIWNHRACARFLKDAMWKKDKKDFAREMTKMKMFKSQLTLMEHNYLIEYQKEHKILREAAIRKWLHGKLHPGHSLVSNTKQARATALSKTPEQRESQRSRSFHPSVDARLQCIPQPTEMPKPIYRKPTVKRPTMWNVSNNPARPPTTQISHSQGIRLGVHPDPTPEHDFSSFLEVRPDGHGGARLHTVDGHWVAPVPRLPFEVLLRMLYPRVWPYRMKVPQGFYPISMREVPRKRHLGDNTFWTDTLAMNLRDTFDEAFLAAVRSHQGLPTLPSPQTNP
Protein: Arginine--tRNA ligase (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (Q54869)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MNTKELIASELSSIIDSLDQEAILKLLETPKNSEMGDIAFPAFSLAKVERKAPQMIAAELAEKMNSQAFEKVVATGPYVNFFLDKSAISAQVLQAVTTEKEHYADQNIGKQENVVIDMSSPNIAKPFSIGHLRSTVIGDSLSHIFQKIGYQTVKVNHLGDWGKQFGMLIVAYKKWGDEEAVKAHPIDELLKLYVRINAEAENDPSLDEEAREWFRKLENGDEEALALWQWFRDESLVEFNRLYNELKVEFDSYNGEAFYNDKMDAVVDILSEKGLLLESEGAQVVNLEKYGIEHPALIKKSDGATLYITRDLAAALYRKNEYQFAKSIYVVGQEQSAHFKQLKAVLQEMGYDWSDDITHVPFGLVTKEGKKLSTRKGNVILLEPTVAEAVSRAKVQIEAKNPELENKDQVAHAVGIGAIKFYDLKTDRTNGYDFDLEAMVSFEGETGPYVQYAYARIQSILRKADFKPETAGNYSLNDTESWEIIKLIQDFPRIINRAADNFEPSIIAKFAISLAQSFNKYYAHTRILDESPERDSRLALSYATAVVLKEALRLLGVEAPEKM
Protein: Cytochrome b (EC 7.1.1.8) (Complex III subunit 3) (Complex III subunit CYTB) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Cytochrome b-c1 complex subunit CYTB) (Ubiquinol-cytochrome c oxidoreductase complex cytochrome b subunit) (P00163)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome b is a catalytic core subunit containing 2 b-type hemes BL and BH topographically segregated in the quinone reduction (Qi) and quinol oxidation (Q0) sites on opposite sides of the membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:8031140}; Multi-pass membrane protein {ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:8031140}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 7, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 12, mitochondrial
Sequence:
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYFAYFLIIVPVISTIENVLFYIGRVNK
Protein: Protein interacting with PRKCA 1 (F6VY12)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTA
Protein: Host cell factor C1 (A6NEM2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASAVSPANLPAVLLQPRWKRVVGWSGPVPRPRHGHRAVAIKELIVVFGGGNEGIVDELHVYNTATNQWFIPAVRGDIPPGCAAYGFVCDGTRLLVFGGMVEYGKYSNDLYELQASRWEWKRLKAKTPKNGPPPCPRLGHSFSLVGNKCYLFGGLANDSEDPKNNIPRYLNDLYILELRPGSGVVAWDIPITYGVLPPPRESHTAVVYTEKDNKKSKLVIYGGMSGCRLGDLWTLDIDTLTWNKPSLSGVAPLPRSLHSATTIGNKMYVFGGWVPLVMDDVKVATHEKEWKCTNTLACLNLDTMAWETILMDTLEDNIPRARAGHCAVAINTRLYIWSGRDGYRKAWNNQVCCKDLWYLETEKPPPPARVQLVRANTNSLEVSWGAVATADSYLLQLQKYDIPATAATATSPTPNPVPSVPANPPKSPAPAAAAPAVQPLTQVGITLLPQAAPAPPTTTTIQVLPTVPGSSISVPTAARTQGVPAVLKVTGPQATTGTPLVTMRPASQAGKAPVTVTSLPAGVRMVVPTQSAQGTVIGSSPQMSGMAALAAAAAATQKIPPSSAPTVLSVPAGTTIVKTMAVTPGTTTLPATVKVASSPVMVSNPATRMLKTAAAQVGTSVSSATNTSTRPIITVHKSGTVTVAQQAQVVTTVVGGVTKTITLVKSPISVPGGSALISNLGKVMSVVQTKPVQTSAVTGQASTGPVTQIIQTKGPLPAGTILKLVTSADGKPTTIITTTQASGAGTKPTILGISSVSPSTTKPGTTTIIKTIPMSAIITQAGATGVTSSPGIKSPITIITTKVMTSGTGAPAKIITAVPKIATGHGQQGVTQVVLKGAPGQPGTILRTVPMGGVRLVTPVTVSAVKPAVTTLVVKGTTGVTTLGTVTGTVSTSLAGAGGHSTSASLATPITTLGTIATLSSQVINPTAITVSAAQTTLTAAGGLTTPTITMQPVSQPTQVTLITAPSGVEAQPVHDLPVSILASPTTEQPTATVTIADSGQGDVQPGTVTLVCSNPPCETHETGTTNTATTTVVANLGGHPQPTQVQFVCDRQEAAASLVTSTVGQQNGSVVRVCSNPPCETHETGTTNTATTATSNMAGQHGCSNPPCETHETGTTNTATTAMSSVGANHQRDARRACAAGTPAVIRISVATGALEAAQGSKSQCQTRQTSATSTTMTVMATGAPCSAGPLLGPSMAREPGGRSPAFVQLAPLSSKVRLSSPSIKDLPAGRHSHAVSTAAMTRSSVGAGEPRMAPVCESLQGGSPSTTVTVTALEALLCPSATVTQVCSNPPCETHETGTTNTATTSNAGSAQRVCSNPPCETHETGTTHTATTATSNGGTGQPEGGQQPPAGRPCETHQTTSTGTTMSVSVGALLPDATSSHRTVESGLEVAAAPSVTPQAGTALLAPFPTQRVCSNPPCETHETGTTHTATTVTSNMSSNQDPPPAASDQGEVESTQGDSVNITSSSAITTTVSSTLTRAVTTVTQSTPVPGPSVPKISSMTETAPRALTTEVPIPAKITVTIANTETSDMPFSAVDILQPPEELQVSPGPRQQLPPRQLLQSASTALMGESAEVLSASQTPELPAAVDLSSTGEPSSGQESAGSAVVATVVVQPPPPTQSEVDQLSLPQELMAEAQAGTTTLMVTGLTPEELAVTAAAEAAAQAAATEEAQALAIQAVLQAAQQAVMAGTGEPMDTSEAAATVTQAELGHLSAEGQEGQATTIPIVLTQQELAALVQQQQLQEAQAQQQHHHLPTEALAPADSLNDPAIESNCLNELAGTVPSTVALLPSTATESLAPSNTFVAPQPVVVASPAKLQAAATLTEVANGIESLGVKPDLPPPPSKAPMKKENQWFDVGVIKGTNVMVTHYFLPPDDAVPSDDDLGTVPDYNQLKKQELQPGTAYKFRVAGINACGRGPFSEISAFKTCLPGFPGAPCAIKISKSPDGAHLTWEPPSVTSGKIIEYSVYLAIQSSQAGGELKSSTPAQLAFMRVYCGPSPSCLVQSSSLSNAHIDYTTKPAIIFRIAARNEKGYGPATQVRWLQETSKDSSGTKPANKRPMSSPEMKSAPKKSKADGQ
Protein: NAD-capped RNA hydrolase (DeNADding enzyme) (EC 3.6.1.-) (Probable NADH pyrophosphatase) (EC 3.6.1.22) (Q9Y7J0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Mediates the hydrolysis of some nucleoside diphosphate derivatives (By similarity).
Interaction partners:
- Putative glutamine-dependent NAD
- Probable nicotinate phosphoribosyltransferase
- Uncharacterized protein C24B11.05
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- NAD-dependent protein deacetylase hst2
- NAD-dependent histone deacetylase sir2
- NAD-dependent protein deacetylase hst4
- Uncharacterized kinase C24B10.02c
- IMP-specific 5'-nucleotidase 1
- Uncharacterized kinase C3H5.11
Sequence:
MQGFKIARHFELPTAPSQFFAGSSLNRLSFLRSNREFLNKAFYDHTTRFLPFCDLNPALLVKDDKLVTLSYPQISKYFTFSPFEHTDKQIAERFSKGESLPVLVYMGNEERNGPTDNWSQHNVFAIDITGIDELQQSIRDNGGTFVNLRSIFTEQYQLSASDSGACAFARSILDWISRYRFCPGCGKRNIPTMGGTKLVCSDVLLNDDSNCPSKKGINNYQYPRTDPCVIMVILSHDMQHILLGRALRHPKGLYACLAGFLEPGESLEEAVVRETYEESGVDVEKVLYYASQPWPFPQSLMLACFGIARKNAKIQRDKDLELEDVRFFSREEVLRSLEWDAKDGPAPILFPPKLSIARNLIQAFAYDDWTNSQVKM
Protein: LD21953p (Rab35, isoform A) (Rab35, isoform B) (Rab35, isoform D) (Q9W5X0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
- EG:86E4.5 protein
- Centaurin beta 1A
- TBC1 domain family member whacked
- Rab GDP dissociation inhibitor
- Anaphase-promoting complex subunit 10
- Guanine nucleotide exchange factor MSS4 homolog
- Uncharacterized protein, isoform A
- Tumor suppressor protein 101
- TBC1 domain family member 13
Sequence:
MARGFDHLFKLLIIGDSGVGKSSLLIRFSDDTFSGSYITTIGVDFKIRTVDIEGMRVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTNGESFANVRRWLEEIQNNCDVVKKVLVGNKNDDPDRKVVITEDAQRFAKQMDIELFETSAKDNINVENMFLSITRQVLDHKLRTSPNEQQKDTLHLKPNPKGSKGGKCCR
Protein: 4-aminobenzoate N-oxygenase (EC 1.14.99.68) (N-oxygenase) (Non-heme di-iron N-oxygenase) (p-aminobenzoate oxygenase) (Q70KH9)
Organism: Streptomyces thioluteus
Function: Involved in the biosynthesis of the polyketide antibiotic aureothin. Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit. Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound.
Interaction partners:
Sequence:
MREEQPHLATTWAARGWVEEEGIGSATLGRLVRAWPRRAAVVNKADILDEWADYDTLVPDYPLEIVPFAEHPLFLAAEPHQRQRVLTGMWIGYNERVIATEQLIAEPAFDLVMHGVFPGSDDPLIRKSVQQAIVDESFHTYMHMLAIDRTRELRKISERPPQPELVTYRRLRRVLADMPEQWERDIAVLVWGAVAETCINALLALLARDATIQPMHSLITTLHLRDETAHGSIVVEVVRELYARMNEQQRRALVRCLPIALEAFAEQDLSALLLELNAAGIRGAEEIVGDLRSTAGGTRLVRDFSGARKMVEQLGLDDAVDFDFPERPDWSPHTPR
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (Q0PIT9)
Organism: Sus scrofa (Pig)
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}.
Interaction partners:
- Pyridoxine-5'-phosphate oxidase
- ATP-dependent
- Intercellular adhesion molecule 5
- m7GpppN-mRNA hydrolase
- Probable ATP-dependent RNA helicase DDX6
Sequence:
MSGLRALLGLGLPVAGSRLPRVRVQAGACRARPTWWGPQRLISGGRGDVEGMASSAVKYLSQEEAQAVDQELFNEYQFSVDQLMELAGLSCATAIAKVYPPTSLSRSPPTVLVICGPGNNGGDGLVCARHLKLFGYHPTIYYPKRPNKPLFTALVTQCQKMDIPFLDEMPSEPTLIDELYELVVDAIFGFSFKGEVREPFRSILSVLNGLTVPIASIDIPSGWDVERGNSGGIQPDLLISLTAPKKSAAQFTGRYHYLGGRFVPPALEKKYQLNLPPYPDTECVYRLQ
Protein: Methane monooxygenase component A alpha chain (EC 1.14.13.25) (Methane hydroxylase) (P22869)
Organism: Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Function: Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
Interaction partners:
- Methane monooxygenase component A gamma chain
- Methane monooxygenase component A beta chain
- Methane monooxygenase regulatory protein B
- Methane monooxygenase component C
- Methane monooxygenase component D
- Particulate methane monooxygenase alpha subunit
- Methane monooxygenase, C subunit
- Methanol dehydrogenase protein, large subunit
- Particulate methane monooxygenase beta subunit
- Putative methanol dehydrogenase protein, large subunit
Sequence:
MALSTATKAATDALAANRAPTSVNAQEVHRWLQSFNWDFKNNRTKYATKYKMANETKEQFKLIAKEYARMEAVKDERQFGSLQDALTRLNAGVRVHPKWNETMKVVSNFLEVGEYNAIAATGMLWDSAQAAEQKNGYLAQVLDEIRHTHQCAYVNYYFAKNGQDPAGHNDARRTRTIGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAVTEWAAANGDEITPTVFLSIETDELRHMANGYQTVVSIANDPASAKYLNTDLNNAFWTQQKYFTPVLGMLFEYGSKFKVEPWVKTWNRWVYEDWGGIWIGRLGKYGVESPRSLKDAKQDAYWAHHDLYLLAYALWPTGFFRLALPDQEEMEWFEANYPGWYDHYGKIYEEWRARGCEDPSSGFIPLMWFIENNHPIYIDRVSQVPFCPSLAKGASTLRVHEYNGQMHTFSDQWGERMWLAEPERYECQNIFEQYEGRELSEVIAELHGLRSDGKTLIAQPHVRGDKLWTLDDIKRLNCVFKNPVKAFN
Protein: Anion exchange protein 4 (AE 4) (Anion exchanger 4) (Solute carrier family 4 member 9) (A0A494BA31)
Organism: Mus musculus (Mouse)
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411, ECO:0000305|PubMed:34585968}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the basolateral membrane of the cortical collecting duct (CCD)and submandibular gland (SMG) duct. {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411}.
Interaction partners:
Sequence:
MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
Protein: Cytidine deaminase (EC 3.5.4.5) (Cytidine aminohydrolase) (Q20628)
Organism: Caenorhabditis elegans
Interaction partners:
- Uridine and thymidine phosphorylase
- Thymidine kinase
- Uridine kinase
- Probable uridine-cytidine kinase
- Purine nucleoside phosphorylase
- Thymidylate kinase
- Probable deoxycytidylate deaminase
- Putative deoxyribose-phosphate aldolase
- Gut esterase 1
- Cytidine deaminase
Sequence:
MAANSLPQDISDVELVHLARAAMKRAHCPYSKFPVGAALLTESGEIVQGCNVENASYGGTICAERSAIVSAVSQGYTKFRAIAVVTELSEPASPCGLCRQFLVEFGDYKVVVGTASNNKILITSTRALLPFAFTPESLDTFEQEKASEAKGLKQDDATEHNVTVVS
Protein: Tetraspanin-21 (Q5WRN1)
Organism: Caenorhabditis elegans
Function: Regulates cell fate specification in the postembryonic mesodermal M lineage and body size, probably by positively modulating BMP-like Sma/Mab signaling at the ligand-receptor level. Promotes ventral fate specification in the M lineage, probably by positively modulating lin-12/Notch signaling.
Subcellular location: Cell membrane {ECO:0000255|RuleBase:RU361218, ECO:0000269|PubMed:25978409}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU361218}. Basolateral cell membrane {ECO:0000269|PubMed:25978409}; Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25978409}; Multi-pass membrane protein {ECO:0000305}. Note=Specifically localizes to the basolateral side of intestinal cells. Localizes to cytoplasmic vesicles in the M mesoblast. {ECO:0000269|PubMed:25978409}.
Interaction partners:
Sequence:
MIDLKSIWNDKRKITYFFLANVCFLISGLSSLIVGVWLYSSKNNFIELTPTSYSALSAAGLCVFTGVTIFIIVAVGYLGVSWSNKSLLYSYIGFVILLILVHGIARITGSLHKEEAKENLRKSMLHNINTTAVVTKIGREIKLSLTWDHLQRELQCCGVDNYTDWHYSVHWPNNLYTPDSCCDPQHFDAENGTENCGKLPDEQSLLYQKGCFPKFSDWLYHHIILVNWVTSILFVVEILLLILSLVVLRVLKNSRHKTRRSHRERDPETTSENMRLNSMDRIADARLETDTVEDGMSINSR
Protein: Inwardly rectifying K+ channel protein (Q8WQ81)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MAYPKMGKPVPPQPSCRSRNFRPGSMRRVRRRAVFKNGDCNVVQKHLQRRRVRFLQDMYTTMVDWQWRWTLLAFALSFILSWLFFALIWWLIIYTHGDLEEPHLPENQEESGWAPCVSAIDGFTSCFLFSIETQHTIGYGVRTTSPECPEAIFMMCFQSIYGVMSSAFMAGIVFAKMTRAKQRAQTLLFSKHAVICQRDGTLSLMFRVGDMRKSHIIGAGVRAQLIRTKSTKEGEVMTQYFTELEIGTDDSGSDLFFIWPMVIEHKIDENSPLYNLNATDMLQDKFEIVVILEGTVESTGQSTQARSSYINTEILWGHRFDPVVLYNKDLQAYEIDYARFNETTQVDTPLCSARELNEIYKIQEGFRTPETTFTMRQLSHNHSDQAS