wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-related protein Rap1 (EC 3.6.5.2) (Rap1 GTPase) (Ras-like protein 3) (P08645)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in photoreceptor cell determination.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Exchange protein directly activated by cAMP, isoform E
- Raf homolog serine/threonine-protein kinase Raf
- Rap GTPase activating protein 1, isoform H
- Canoe, isoform E
- Dizzy isoform AII
- Ral guanine nucleotide dissociation stimulator-like, isoform E
- LD06925p
- Rhea, isoform B
- 14-3-3 protein zeta
- non-specific serine/threonine protein kinase
Sequence:
MREYKIVVLGSGGVGKSALTVQFVQCIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVYSITAQSTFNDLQDLREQILRVKDTDDVPMVLVGNKCDLEEERVVGKELGKNLATQFNCAFMETSAKAKVNVNDIFYDLVRQINKKSPEKKQKKPKKSLCVLL
Protein: Laccase abr2 (EC 1.10.3.-) (Conidial pigment biosynthesis oxidase abr2) (E9RBR0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Laccase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall. The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA. The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening. 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone. The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN. 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone. Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN. Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin. DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize. DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins. DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses. DHN-melanin protects also conidia against amoeba predation.
Subcellular location: Cell surface {ECO:0000269|PubMed:26972005}.
Interaction partners:
- Conidial pigment polyketide synthase alb1
- Hydroxynaphthalene reductase arp2
- Scytalone dehydratase arp1
- Heptaketide hydrolyase ayg1
Sequence:
MWYQSASLLGVAAVAQAATVHYSLDLTWETGSPNGVSREMIFVNGQFPGPAIILNEGDEAIIDVTNHLPFNTSIHFHGIEQKNTPWADGVVGLSQWAIQPGQSYTYQWRADTYGTYWYHAHDKAEIMDGLYGPVHIRPRPNRDSPFSMISDDPADIRAMKQAERNGKLVMLSDWDHLTGQEYMKAMEETGYDIFCSDSVLINGRGSVFCHDPEELTQMVPPPELAILNSSLTDKGCLPFVPPIQGNWEHHPDKVPPGLNEGCHPSTTQETIFTVDAAHQWASFHFISAASLKVLVVSIDEHPMYVYEVDGRYIEPQLAHSVKLYNGERYSVMVKLDKEPANYKMRAANDGGNQIVSGFATVTYEGGETSQRPSQPYIDYGSRNTSADVIPLDTNHLPPYPAISPASEPDDFHILMLGRTNSSWEWSLDGAAFLPSNLAALPPAILSPQAPEFADALKITTRNDTWVDIVFQLVVSETTPIQPPHPLHKHSNKGFLLGTGHGKFNWTSIKEAKEASPESFLETPVYRDTFTTSPQGETWTAIRYHVENPGPFLLHCHMTTHLQSGMGLILMDGVDVWPEVYADMITPM
Protein: Transporter (A1ZBC7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTQLEISKKSEKPAEKPAEQWGNGLEFLFSCISLSVGLGNIWRFPYIAFQNGGGTFVIPYLIALLVIGRPVYYLEISLGQFTGRGVVKAFDMAPLLKGVALGQVLATAASITYYSSIMALTLRFWLASFGSELPWSRCWESWGTDCHDGNAQNSSGKMSPAQLYFEREILHEVPNIDNGLSLPNWQLVACLAIAWLVIGGVLIRGIKSSGKAAYFLGVFPYVVLLILLLRAVTLPGAIDGIIYFFKPQWRELLNPLVWYAAVTQVFFSLAICFGTLITYASYNNFNRNVYNDIVIITTMDSCSSIIAGCITFGILGNLARETGNPDIGSVVKGGAGLAFISYPEAIAKFEYVPQMFAVLFFLMLFVLGIGSTVGMGSCILRVIRDQFGLRSPPIWKLASGLTVLGFSVSIVYMTPGGQFILNLVDFYGVSFTALILAIGELVAVAWIYGVNRFCEDIKFMMGIETGWYWRLCWRFITPGLMTAVLIYMLLDMSALEYKGVGYPTLAHVFGCFLATLGLIQLPGWAIYAIYKKRGHNGSFWQRIRAACKPSDTWGPANVQLDATI
Protein: Acetone carboxylase beta subunit (EC 6.4.1.6) (Q8RM04)
Organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Function: Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.
Interaction partners:
- Acetone carboxylase alpha subunit
- Acetone carboxylase gamma subunit
- Hydantoinase B/oxoprolinase
- Acetone carboxylase gamma subunit
Sequence:
MNVPVGHLRNVQVLGIDAGGTMTDTFFVDQDGDFVVGKAQSTPQNEALGLIASSEDGLANWGMSLHEALAQLQTGVYSGTAMLNRVVQRKGLKCGLIVNRGMEDFHRMGRAVQSHLGYAYEDRIHLNTHRYDPPLVPRHLTRGVVERTDMIGTQVIPLREDTARDAARDLIAADAEGIVISLLHSYKNPENERRVRDIVLEEVEKSGKKIPVFASADYYPVRKETHRTNTTILEGYAAEPSRQTLSKISNAFKERGTKFDFRVMATHGGTISWKAKELARTIVSGPIGGVIGAKYLGEVLGYKNIACSDIGGTSFDVALITQGEMTIKNDPDMARLVLSLPLVAMDSVGAGAGSFIRLDPYTRAIKLGPDSAGYRVGVCWKESGIETVTISDCHMVLGYLNPDNFLGGAVKLDRQRSVDAIKAQIADPLGLSVEDAAAGVIELLDSDLRDYLRSMISGKGYSPASFVCFSYGGAGPVHTYGYTEGLGFEDVIVPAWAAGFSAFGCAAADFEYRYDKSLDINMPTETPDTDKEKAAATLQAAWEELTKNVLEEFKLNGYSADQVTLQPGYRMQYRGQLNDLEIESPLAQAHTAADWDQLTDAFNATYGRVYAASARSPELGYSVTGAIMRGMVPIPKPKIPKEPEEGETPPESAKIGTRKFYRKKRWVDAQLYHMESLRPGNRVMGPAVIESDATTFVVPDGFETWLDGHRLFHLREV
Protein: Choline/ethanolamine kinase (Choline kinase beta) (CK) (CKB) (EC 2.7.1.32) (Choline kinase-like protein) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (Ethanolamine kinase beta) (EKB) (choline/ethanolamine kinase beta) (CKEKB) (Q9Y259)
Organism: Homo sapiens (Human)
Function: Has a key role in phospholipid metabolism, and catalyzes the first step of phosphatidylethanolamine and phosphatidylcholine biosynthesis.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline-phosphate cytidylyltransferase B
- Choline-phosphate cytidylyltransferase A
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Glycerophosphocholine phosphodiesterase GPCPD1
- Tachykinin-4
- Phosphoethanolamine/phosphocholine phosphatase
- Ethanolamine-phosphate phospho-lyase
- Choline O-acetyltransferase
- Acetylcholinesterase
Sequence:
MAAEATAVAGSGAVGGCLAKDGLQQSKCPDTTPKRRRASSLSRDAERRAYQWCREYLGGAWRRVQPEELRVYPVSGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYIPSRPLKTQELREPVLSAAIATKMAQFHGMEMPFTKEPHWLFGTMERYLKQIQDLPPTGLPEMNLLEMYSLKDEMGNLRKLLESTPSPVVFCHNDIQEGNILLLSEPENADSLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTHEEWPFYKARPTDYPTQEQQLHFIRHYLAEAKKGETLSQEEQRKLEEDLLVEVSRYALASHFFWGLWSILQASMSTIEFGYLDYAQSRFQFYFQQKGQLTSVHSSS
Protein: Gustatory and pheromone receptor 39a, isoform D (P58958)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Plays a role in sustaining courtship behavior in males, possibly through the reception of a stimulating arrestant pheromone.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKRNAFEELRVQLRTLKWLGVLRFTIDFNKCLVRENASEERSAWLYLIGVVGITCSLIVYSTYFPSHFIMGKHNTTGNCYALINIRSCSIVTMLIYTQLYIQRFRFVALLQSILRFNQISGSHREEGRFAFYYYTHLSLLIICMLNYAYGYWTAGVRLTTIPIYLLQYGFSYLFLGQVVVLFACIQQILLSILKYYNQVVLKNIKSSKESREFYYNFCKYNQVIWLSYTEINHCFGLLLLLVTGLILLITPSGPFYLVSTIFEGRFRQNWQFSLMSFTAILWSLPWIVLLVLAMGRNDVQKEANKTAKMLTKVPRTGTGLDRMIEKFLLKNLRQKPILTAYGFFALDKSTLFKLFTAIFTYMVILVQFKEMENSTKSINKF
Protein: Uncharacterized protein C57A7.06 (P87137)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent RNA helicase dbp4
- Probable nucleolar complex protein 14
- Ribosome biogenesis protein bms1
- U3 small nucleolar ribonucleoprotein protein mpp10
- Uncharacterized protein C3B8.09
- Putative ATP-dependent RNA helicase PB1A10.06c
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar RNA-associated protein 22
- Protein sof1
- Uncharacterized protein C18B11.06
Sequence:
MARKGKVNTLPQPQGKHQRKGKKQLENKILHSYEEESAGFDSEELEDNDEQGYSFGVNSEDDEEIDSDEAFDEEDEKRFADWSFNASKSGKSNKDHKNLNNTKEISLNEEDDSDDSVNSDKLENEGSVGSSIDENELVDLDTLLDNDQPEKNESNTASTIRPPWIGNNDHATDKENLLESDASSSNDSESELTDSADNMNESDSESEIESSDSDHDDGENSDSKLDNLRNYIVSLNQKRKKDEADAESVLSSDDNDSIEEISIKKVKYDPHETNKESEYNLIGSSEKTIDITDLLDSIPMNEQLKVSLKPLVSESSSISSKKLDAPLAKSIQDRLERQAAYEQTKNDLEKWKPIVADNRKSDQLIFPMNETARPVPSNNGLASSFEPRTESERKMHQALLDAGLENESALKKQEELALNKLSVEEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNRKEKEMALIPKSEEDLENERIKSEEARALERMTQRHKNTSSWTRKMLERASHGEGTREAVNEQIRKGDELMQRIHGKEISEMDGEDVSEFSDSDYDTNEQVSTAFEKIRNEEEPKLKGVLGMKFMRDASNRQKALVQDEMQAFEDELAGVPNEDDTSQKGEDGVPGVLIGNNTGRRSFKPSEEAAKLSLPSRKNPFVSDSAVLKVNKPEMKEGQKKAEARKKKESPLEATEETNPWLQVPDQRTSSAKKLDKNSSKADKKNHKLKMDKVASLQELVEEPKVQPDLIFEEKAFESASEAESDVDVSVPMLKPTKGRLSIKQRELVAKAFAGDDVVAEFEKDKEDWVQEDAPKEEDHSLPGWGSWGGVGVKQRKTKPKVKKIAGLDPSKRKDSKLKHVIINEKRNKKAAKLTADSVPFPFESREQYERSLNLPMGPEWTTRASHHKAVAPRVVTKRGKVINPIKAPN
Protein: Uncharacterized protein YJL016W (P47072)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Dilute domain-containing protein YPR089W
- Uncharacterized protein JIP4
- Myosin tail region-interacting protein MTI1
- Serine/threonine-protein kinase PTK1/STK1
- Suppressor of lethality of KEX2 GAS1 double null mutant protein 1
- Probable pseudouridine-5'-phosphatase YKL033W-A
Sequence:
MGILDSLKKPVNIKSSLPKFSRSATSINLSSHPVSSRSFLELPPELFSITKPIFKLLQAHANKIYFQSSDAEAVWNVKDSSGHVFEAESISLLGSHIIITNSSVQVADVAIIDSPSNINQCEISSVGEFLQFNNGQLSITCNDFGLLEKFKRLCMISIFEFISIYKALTGTVISSYGLRMSDMHIILNSPFNFKDWCEVYLDGQGWVKVWCHIDKVSKTNNSKSSSDNDAKGKYQIRFYRDDKSTSSKNCVFFIPDNEYVQDIFFYNINAAEPSKNMNDFFQGLQMIKLVGNVRFCSDTDFNDVVDSGSIYSSANNGSGDSSSTALNNESPNTTPKSRTFFSPKGHRRNSSHVSSLTSRSTKKPITNFTTRTNGLLIRPLPHHGVHHLEAMIRFIIPLMDCARLYGRPVQFKTERTDINSLMFGLPKLPSVDYFAEEEIAHLMTQEFNPLKEKDTDDTMALTMSRFSSYLQERMTKVSKRNTELNFRTFSDVMGMYNTTRDHSKLNCMSDKDNSVKEFSLSDKSNVSSETTNMMNQLQVNAHEYKSSMCERPIVASTSPIA
Protein: Msh3 protein (Q5BJY1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
TNLSDSERVMIITGPNMGGKSSYIKQVALVVIMAQIGSYVPAEEATIGIVDGIFTRRGAADNIYKGRSTFMEELTDTAEIIQKATQRSLVILDELGRGTSTHDGIAIAYATLEYFIRDVKSLTLFVTHYPPVCELEKRYPEQVGNYHMGFLVNEDGSKQDSGDMEQMPDSVTFLYQITRGIAARSYGLNVAKLADVPREILQKAAHKSKELEGLVNLRRKRLEYFIDLWTTHSVKDLHTRAAELEIQEIQTSPHNEMKTTLLELK
Protein: Protoporphyrinogen oxidase 2, chloroplastic/mitochondrial (PPO2) (EC 1.3.3.4) (Protein MATERNAL EFFECT EMBRYO ARREST 61) (Q8S9J1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular location: Plastid, chloroplast. Mitochondrion {ECO:0000269|PubMed:21841088}.
Interaction partners:
- Ferrochelatase-1, chloroplastic/mitochondrial
- Uroporphyrinogen decarboxylase 2, chloroplastic
- Ferrochelatase-2, chloroplastic
- Uroporphyrinogen decarboxylase 1, chloroplastic
- Coproporphyrinogen-III oxidase 1, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- Magnesium-chelatase subunit ChlD, chloroplastic
- Coproporphyrinogen-III oxidase 2, chloroplastic
- Magnesium-chelatase subunit ChlI-2, chloroplastic
- Magnesium-chelatase subunit ChlI-1, chloroplastic
Sequence:
MASGAVADHQIEAVSGKRVAVVGAGVSGLAAAYKLKSRGLNVTVFEADGRVGGKLRSVMQNGLIWDEGANTMTEAEPEVGSLLDDLGLREKQQFPISQKKRYIVRNGVPVMLPTNPIELVTSSVLSTQSKFQILLEPFLWKKKSSKVSDASAEESVSEFFQRHFGQEVVDYLIDPFVGGTSAADPDSLSMKHSFPDLWNVEKSFGSIIVGAIRTKFAAKGGKSRDTKSSPGTKKGSRGSFSFKGGMQILPDTLCKSLSHDEINLDSKVLSLSYNSGSRQENWSLSCVSHNETQRQNPHYDAVIMTAPLCNVKEMKVMKGGQPFQLNFLPEINYMPLSVLITTFTKEKVKRPLEGFGVLIPSKEQKHGFKTLGTLFSSMMFPDRSPSDVHLYTTFIGGSRNQELAKASTDELKQVVTSDLQRLLGVEGEPVSVNHYYWRKAFPLYDSSYDSVMEAIDKMENDLPGFFYAGNHRGGLSVGKSIASGCKAADLVISYLESCSNDKKPNDSL
Protein: Exonuclease V (X6RCY3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAETREEETVSAEASGFSDLSDSEFLEFLDLEDAQESKALVNMPGPSSESLGKDDKPISLQNWKRGLDILSPMERFHLKYLYVTDLATQNWCELQTAYGKELPGFLAPEKAAVLDTGASIHLARELELHDLVTVPVTTKEDAWAIKFLNILLLIPTLQSEGHIREFPVFGEGEGVLLVGVIDELHYTAKGELELAELKTRRRPMLPLEAQKKKDCFQVSLYKYIFDAMVQGKVTPASLIHHTKLCLE
Protein: Immunoglobulin superfamily containing leucine-rich repeat protein 2 (Leucine-rich repeat domain and immunoglobulin domain-containing axon extension protein) (Q5RKR3)
Organism: Mus musculus (Mouse)
Function: Required for axon extension during neural development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19755105}; Single-pass membrane protein {ECO:0000269|PubMed:19755105}.
Interaction partners:
Sequence:
MGPFGALCLAWALLGVVRACPEPCACVDKYAHQFADCAYKELREVPEGLPANVTTLSLSANKITVLRRGAFVNVTQVTSLWLAHSEVRTVESGALAVLSQLKNLDLSHNLISNFPWSDLRNLSALQLLKMNHNRLGSLPRDALGALPDLRSLRINNNRLRTLEPGTFDALSALSHLQLYHNPFHCSCGLVWLQAWAASTRVSLPEPDSIACASPPELQGVPVHRLPALPCAPPSVRLSAEPPPEAPGTPLRAGLAFMLHCVAEGHPTPRLQWQLQIPGGTVVLVPPVLSKEEDGGDKVEDGEGDGDEDLPTQTEAPTPTPAPAWPAPPATPRFLALANGSLLVPLLSAKEAGIYTCRAHNELGTNSTSLRVTVAAAGPPKHAPGTGEEPDAQVPTSERKATTKGRSNSVLPFKPEGKTKGQGLARVSVLGEIEAELEETDEGEQMEGQIPADPMGEKHCGHGDPSRYVSNHAFNQSSDLKPHVFELGVIALDVAEREARVQLTPLAARWGPGPDGASGARRPGRRPLRLLYLCPAGGGTAVQWSRVEEGVNAYWFRGLRPGTNYSVCLALAGEACHVQVVFSTKKELPSLLVIVTVSVFLLVLATVPLLGAACCHLLAKHPGKPYRLILRPQAPDPMEKRIAADFDPRASYLESEKSYPARGEAGGEEPEEVPEEGLDEDVEQGDPSGDLQREESLAGCSLVESQSKANQEEFEAGSEYSDRLPLGAEAVNIAQEINGNYRQTAG
Protein: Receptor-type guanylate cyclase gcy-1 (EC 4.6.1.2) (Q09435)
Organism: Caenorhabditis elegans
Function: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Involved in the sensing of K+ gradient by the ASE right (ASER) sensory neuron.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Bis
- Inosine triphosphate pyrophosphatase
- GTP cyclohydrolase 1
- Probable 3',5'-cyclic phosphodiesterase pde-5
- Probable 3',5'-cyclic phosphodiesterase pde-2
- Probable 3',5'-cyclic phosphodiesterase pde-3
- Probable 3',5'-cyclic phosphodiesterase pde-1
Sequence:
MQIFTILLLFNIFPSIFVQNLPDTTVAPRTKRTIKIGIAAAQRIQTSSIGWSVCGGAVPLAIERLKEMGFVKDFDFEYIVDYTECDLGSVVRAGMEFIKTHKVDVIIGPPCAQALRLMSFLAENYKKPVLGWGFVSDTDLSDVIRFPHLTTVIPNSLMLGYAASKMLTTFHWNRVALLYYFSDVKYCSGVMNDIEATFNDPSTPNVNIVIKAEIYLNDNETTDNVFQTVKSRARIILWCTQTSVEKRDYLIKIATHDMIGDEYVHIMLSMRNVAFGTQTSLGKPTFSQSGLTPIWESFTEGTDGFEKMAKQAATRMFVLDVNSEVADKKYLEYMQKNIIKAVQSPPMNCSTVECMTANTTIMGGYARHLFDVVYLYGIALTHTNSTDPAVYGDVDVLVHQFVTSFQGMTGHVVISPNLTRMPIFQLYGLNSDYDQVALVDFTYTNSVMVPNVTLFYKDEGGAVWSYYGHSRPLDIPICGFLGKSCPVSFWEQYKILIFVAIAVIVLMVLIMIIGCLCVISGKRAERARINAEWQVPFAKLIESEKQVRGKGASRRSLQSAPSISTGHSGVTTVSDFCENYTMMMYEKEMVLTAKYQYTHLTKADKERFVKMRKLDHENINRFIGLSIDSAHFISVTKLCSRGSLQDILSRGNFSMDYFFMFCIIRDVAKGLEYLHKTFLRLHGNLRSATCLVNDSWQVKLAEYGMDNLVEEQTPPKKRLLWVAPEVLRGSLSVSQMEPSADIYSFAIIASEILTKKEAWDILDRKEDCEEIVYNVKKGGLFPIRPEIITDIHDVNPALIALVKDCWAEVPEDRPTAENICSQMKGLVSKQKTNLMDHVFNMLEEYTSTLEEEIEERTKELTLEKKKADILLSRMLPKQVAERLKAGQTVEPEGFDSVTVFFSDVVKFTILASKCSPFQTVNLLNDLYSNFDTIIEQHGVYKVESIGDGYLCVSGLPTRNGYAHIKQIVDMSLKFMEYCKSFNIPHLPRENVELRIGVNSGPCVAGVVGLSMPRYCLFGDTVNTASRMESNGKPSLIHLTNDAHSLLTTHYPNQYETSSRGEVIIKGKGVMETFWVHGRFGEMEPTELRSISNRSTPPVTNDRWIPNPSSSHGSRPSSVYDPLQGHQKFKMDTLKVAN
Protein: NAD(+) ADP-ribosyltransferase (EC 2.4.2.30) (B1WC20)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAPRRRRSGCGRRVLNEAKRVDNGNRATDDSPPGKKVRTCQKKGPAAGGEDTDRTKGKQDSVKTLLVKGRAPVDPECTSKVGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQQNFSVWMRWGRGKGFMMD
Protein: Uncharacterized protein P4H10.19c (Q9P7D0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glucosidase 2 subunit alpha
- Endoplasmic reticulum chaperone BiP
Sequence:
MQTLLFYFFFINLIFAHDLNVKTYKPCTIPSVFSEQFTSEDITTWRSRWRAPVNKDLGVWDLVEAPGSHLRDEYGLITLKSNKPHILISNLENPTTRQSSSVPIVLSFQVKPTKPWTCGHAYVSLVHQSNPKNVSKEPPSVIRFGVKKCGMFDYISLSIISYDGKVSCHLYDAPPSGLVEGRTSMYTLLLQNTTVVIRRDQSVVYTGDVGTNFFHSPTKWITHSNVSNGYYTSRNIMSFLLSNNTNTSSYPFSVNGVELDVWNENAGVFINNIYFGFSLSDAMKFENETFIAKKILENSPCPNQPSIQPFGILMMLVSTIYGNFKNLYNCIKRNTIGYIYNSIYDFWITEGMLFPMRNMDIFKITAISIGLSIPVFLWLLK
Protein: Syntaxin-52 (AtSYP52) (Q94KK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vesicle trafficking protein that functions in the secretory pathway.
Subcellular location: Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein. Prevacuolar compartment membrane; Single-pass type IV membrane protein.
Interaction partners:
- VAMP-like protein YKT62
- Vesicle transport v-SNARE 13
- Vesicle transport v-SNARE 11
- Vesicle transport v-SNARE 12
- VAMP-like protein YKT61
- Vesicle transport v-SNARE family protein
- Syntaxin-22
- Syntaxin-21
- Syntaxin-43
- Syntaxin-42
Sequence:
MASSSDPWMREYNEALKLSEDINGMMSERNASGLTGPDAQRRASAIRRKITILGTRLDSLQSLLVKVPGKQHVSEKEMNRRKDMVGNLRSKTNQVASALNMSNFANRDSLFGTDLKPDDAINRVSGMDNQGIVVFQRQVMREQDEGLEKLEETVMSTKHIALAVNEELTLQTRLIDDLDYDVDITDSRLRRVQKSLALMNKSMKSGCSCMSMLLSVLGIVGLALVIWLLVKYL
Protein: Zinc finger protein 57 (Zinc finger protein 424) (Q68EA5)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MDSVVFEDVAVDFTLEEWALLDSAQRDLYRDVMLETFRNLASVDDGTQFKANGSVSLQDMYGQEKSKEQTIPNFTGNNSCAYTLEKNCEGYGTEDHHKNLRNHMVDRFCTHNEGNQYGEAIHQMPDLTLHKKVSAGEKPYECTKCRTVFTHLSSLKRHVKSHCGRKAPPGEECKQACICPSHLHSHGRTDTEEKPYKCQACGQTFQHPRYLSHHVKTHTAEKTYKCEQCRMAFNGFASFTRHVRTHTKDRPYKCQECGRAFIYPSTFQRHMTTHTGEKPYKCQHCGKAFTYPQAFQRHEKTHTGEKPYECKQCGKTFSWSETLRVHMRIHTGDKLYKCEHCGKAFTSSRSFQGHLRTHTGEKPYECKQCGKAFTWSSTFREHVRIHTQEQLYKCEQCGKAFTSSRSFRGHLRTHTGEKPYECKQCGKTFTWSSTFREHVRIHTQEQLHKCEHCGKAFTSSRAFQGHLRMHTGEKPYECKQCGKTFTWSSTLHNHVRMHTGEKPHKCKQCGMSFKWHSSFRNHLRMHTGQKSHECQSYSKAFSCQVILSKTSESTH
Protein: Tetratricopeptide repeat protein 17 (TPR repeat protein 17) (Q96AE7)
Organism: Homo sapiens (Human)
Function: Plays a role in primary ciliogenesis by modulating actin polymerization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24475127}. Cell membrane {ECO:0000269|PubMed:24475127}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24475127}. Note=Colocalized with CATIP at F-actin rich zones and at dynamic plasma membrane protrusions.
Interaction partners:
Sequence:
MAAAVGVRGRYELPPCSGPGWLLSLSALLSVAARGAFATTHWVVTEDGKIQQQVDSPMNLKHPHDLVILMRQEATVNYLKELEKQLVAQKIHIEENEDRDTGLEQRHNKEDPDCIKAKVPLGDLDLYDGTYITLESKDISPEDYIDTESPVPPDPEQPDCTKILELPYSIHAFQHLRGVQERVNLSAPLLPKEDPIFTYLSKRLGRSIDDIGHLIHEGLQKNTSSWVLYNMASFYWRIKNEPYQVVECAMRALHFSSRHNKDIALVNLANVLHRAHFSADAAVVVHAALDDSDFFTSYYTLGNIYAMLGEYNHSVLCYDHALQARPGFEQAIKRKHAVLCQQKLEQKLEAQHRSLQRTLNELKEYQKQHDHYLRQQEILEKHKLIQEEQILRNIIHETQMAKEAQLGNHQICRLVNQQHSLHCQWDQPVRYHRGDIFENVDYVQFGEDSSTSSMMSVNFDVQSNQSDINDSVKSSPVAHSILWIWGRDSDAYRDKQHILWPKRADCTESYPRVPVGGELPTYFLPPENKGLRIHELSSDDYSTEEEAQTPDCSITDFRKSHTLSYLVKELEVRMDLKAKMPDDHARKILLSRINNYTIPEEEIGSFLFHAINKPNAPIWLILNEAGLYWRAVGNSTFAIACLQRALNLAPLQYQDVPLVNLANLLIHYGLHLDATKLLLQALAINSSEPLTFLSLGNAYLALKNISGALEAFRQALKLTTKCPECENSLKLIRCMQFYPFLYNITSSVCSGTVVEESNGSDEMENSDETKMSEEILALVDEFQQAWPLEGFGGALEMKGRRLDLQGIRVLKKGPQDGVARSSCYGDCRSEDDEATEWITFQVKRVKKPKGDHKKTPGKKVETGQIENGHRYQANLEITGPKVASPGPQGKKRDYQRLGWPSPDECLKLRWVELTAIVSTWLAVSSKNIDITEHIDFATPIQQPAMEPLCNGNLPTSMHTLDHLHGVSNRASLHYTGESQLTEVLQNLGKDQYPQQSLEQIGTRIAKVLEKNQTSWVLSSMAALYWRVKGQGKKAIDCLRQALHYAPHQMKDVPLISLANILHNAKLWNDAVIVATMAVEIAPHFAVNHFTLGNVYVAMEEFEKALVWYESTLKLQPEFVPAKNRIQTIQCHLMLKKGRRSP
Protein: Aldehyde dehydrogenase, cytosolic 1 (EC 1.2.1.3) (ALDH class 1) (ETA-crystallin) (Q28399)
Organism: Elephantulus edwardii (Cape long-eared elephant shrew)
Function: Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSSSGMPDLPAPLTNIKIQHTKLFINNEWHESVSGKTFPVFNPATEEKICEVEEADKEDVDKAVKAAREAFQMGSPWRTMDASERGQLIYKLADLIERDRLLLATLESINAGKVFASAYLMDLDYCIKALRYCAGWADKIQGRTIPVDGEFFSYTRHEPIGVCGLIFPWNAPMILLACKIGPALCCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKMIQEAAAKSNLKRVTLELGAKNPCIVFADADLDSAVEFAHQGVFTNQGQSCIAASKLFVEEAIYDEFVQRSVERAKKYVFGNPLTPGVNHGPQINKAQHNKIMELIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDDMRIAKEEIFGPVQQIMKFKSLDEVIKRANNTYYGLVAGVFTKDLDKAVTVSSALQAGTVWVNCYLAASAQSPAGGFKMSGHGREMGEYGIHEYTEVKTVTMKISEKNS
Protein: Galanin receptor type 1 (GAL1-R) (GALR-1) (Q62805)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the hormone galanin. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P47211}; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Galanin receptor type 3
- Galanin receptor type 2
- Galanin-like peptide
- Spexin
Sequence:
MELAPVNLSEGNGSDPEPPAEPRPLFGIGVENFITLVVFGLIFAMGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGFIWALSIAMASPVAYYQRLFHRDSNQTFCWEHWPNQLHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHVIHLWAEFGAFPLTPASFFFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCRVCNESPHGDAKEKNRIDTPPSTNCTHV
Protein: NAD-dependent protein deacylase sir-2.2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 2) (Q20480)
Organism: Caenorhabditis elegans
Function: NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues. Plays a role in oxidative stress resistance.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161}. Mitochondrion {ECO:0000269|PubMed:23438705}.
Interaction partners:
- NAD-dependent protein deacetylase sir-2.4
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Purine nucleoside phosphorylase
- Nicotinamide N-methyltransferase
- NAD-capped RNA hydrolase ndx-9
- Nicotinamide N-methyltransferase-like
- NAD
- NAD kinase 2, mitochondrial
Sequence:
MAQKFVPEAAELCENSLKKFISLIGTVDKLLVISGAGISTESGIPDYRSKDVGLYARIAHKPIYFQDYMRSNRCRQRYWSRNFLAWPRFGQAAPNINHYALSKWEASDRFQWLITQNVDGLHLKAGSKMVTELHGSALQVKCTTCDYIESRQTYQDRLDYANPGFKEEHVAPGELAPDGDIILPLGTEKGFQIPECPSCGGLMKTDVTFFGENVNMDKVNFCYEKVNECDGILSLGTSLAVLSGFRFIHHANMKKKPIFIVNIGPTRADHMATMKLDYKISDVLKEM
Protein: Cullin 2 (Q5T2B5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA