wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-prolyl cis-trans isomerase CPR4 (PPIase CPR4) (EC 5.2.1.8) (Rotamase) (P25334)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YFR018C
- Peptidyl-prolyl cis-trans isomerase ESS1
- Peptidyl-prolyl cis-trans isomerase CYP7
Sequence:
MWLKSLLLCLYSLVLCQVHAAPSSGKQITSKDVDLQKKYEPSPPATHRGIITIEYFDPVSKSMKEADLTFELYGTVVPKTVNNFAMLAHGVKAVIEGKDPNDIHTYSYRKTKINKVYPNKYIQGGVVAPDVGPFTVYGPKFDDENFYLKHDRPERLAMAYFGPDSNTSEFIITTKADGNEELDGKSVVFGQITSGLDQLMDAIQYTETDEYGKPQHELRFLYFVLEILKISNILDLHAAYTEKVEKFRNGDVSVGSTLENIFRNDKAYTPLTTSTGTTAYDLNHPISRALMCLTVLGLCFIAYKGMHEKPHTVSLRHK
Protein: Otolin-1 (Q4ZJM7)
Organism: Mus musculus (Mouse)
Function: Collagen-like protein specifically expressed in the inner ear, which provides an organic scaffold for otoconia, a calcium carbonate structure in the saccule and utricle of the ear. Acts as a scaffold for biomineralization: sequesters calcium and forms interconnecting fibrils between otoconia that are incorporated into the calcium crystal structure. Together with OC90, modulates calcite crystal morphology and growth kinetics.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20856818}. Note=Localized in both the surrounding otoconial matrix and otoconia. {ECO:0000269|PubMed:20856818}.
Interaction partners:
- Otoconin-90
- Otogelin-like protein
- Alpha-tectorin
- Otogelin
Sequence:
MWIFSSLCAVLTILAMDDVATEAKTTPYTKFTKKSEGKEMLKGLKPSSGFFLDGEETVHTETAAMAEPTTGSPALAMAESTAGPSASATTRLLPFESFSLDTTGFVLNCCHCCSFVTGQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGAKGEKGGVGEKGYRGDLGERGEKGQKGEKGMEGEKGSRGDVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAFSALLSKPFPPPNVPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVTVRGRPARISLVARNRKQFKSRETLYGQQVDQASLLLILKLSAGDQVWLEVSKDWNGLYVGPEDDSIFSGFLLYPEETFSKSP
Protein: Type I restriction enzyme S protein (HsdS) (O25519)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- site-specific DNA-methyltransferase
- Type I restriction enzyme endonuclease subunit
- Restriction endonuclease subunit S
- Uncharacterized protein
- site-specific DNA-methyltransferase
Sequence:
MFCFENLNIQNDIKSKSFGGIVKSISMNDLQQITIPIPPLEIQQEIVKILDAFTELNTELNTELKARKKQYEYYQNMLLDFNDINQNHKDAKIKTYPKRLKTLLHTLAPKGVEFRKLGEVCESTNKKTLKISEVSEVKNKGMYPVINSGRDLYGYYHDFNNDGENITIASRGEYAGFINYFNEKFFAGGLCYPYKVKDTNELLTKFLYFYLKTNEIQIMENLVFRGSIPALNKADIETLTIPIPPLEIQQEIVKILDQFSALTTDLLAGIPAEIKARKKQYEYYREKLLTFKPLQNKE
Protein: E1 ubiquitin-activating enzyme (EC 6.2.1.45) (Ubiquitin-activating enzyme E1) (A0A0B4KF46)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGNSAAAGGDIDESLYSRQLYVLGHDAMRRMANSDILLSGLGGLGLEIAKNVILGGVKSITLHDTATCGLHDLSSQFYLTEADIGKNRAEASCAQLAELNNYVRTVSHTGPLTEEFLRKFRVVVLTNSDGEEQQRIAKFAHENGIALIIAETRGLFAKVFCDFGESFTIYDQDGTQPISTMIASITHDAQGVVTCLDETRHGFNDGDYVTFSEVQGMQELNGCQPLKITVLGPYTFSIGDTSKFGEYKSGGVATQVKMPKTISFKPLAQATEEPEFLISDFAKLDSPATLHVAFNALSCYRKAHNGALPRPWNEEDANSFLEVVRASSNAEVDEKLVLQFAKICSGNTCPLDAAVGGIVAQEVLKACSGKFTPIYQWLYFDALECLPTEGVEEADAQPVGSRYDSQIAIFGKKFQEKLADSKWFIVGAGAIGCELLKNFGMLGLGTGNGQIFVTDMDLIEKSNLNRQFLFRPHDVQKPKSMTAADAIKRMNPEVNVTAYELRVGAETEKVFSEDFFGKLDGVANALDNVDARIYMDRKCIFNRIPLVETGTLGTLGNVQVIVPFATESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDAFEGVFKQSAENAAQYIADPQFTERIAKLPGIQPLEILDSIKKALIDDKPKSFAHCVEWARLYWEDQYVNQIKQLLFNFPPDQITSSGQPFWSGPKRCPDPLVFDVNDPMHLDFIYAAANLRAEVYGIEQVRNRETIAELVQKVKVPEFKPRSGVKIETNEAAAAASANNFDDGELDQDRVDKIISELLKNADKSSKITPLEFEKDDDSNLHMDFIVACSNLRAANYKIPPADRHKSKLIAGKIIPAIATTTSVLSGLAVLEVIKLIVGHRDLVKFKNGFANLALPFMAFSEPLPAAKNTYYGKEWTLWDRFEVTGELSLQEFLNYFEENEKLKITMLSQGVSMLYSFFMPKAKCSERLPLPMSEVVRRVSKRRLEPHERSLVFEICCNDVDGEDVEVPYVRYTLP
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (H0Z871)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPGIVVFRRRWSVGSDDLVLPAVFLFLLHTTWFVILSVVLFGLVYNPNETCSLNLVDHGRGYLGILLSCMIAELAIIWLSMRGSILYTEPRDSMQYVLYVRLAILVIEFVYAIVGIVWLTQYYTSCNDITAKSVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQASSWTRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNAQEMQRYREVCYYMLFALAAYGWPIYLMRKPTCGLCRLARSCSCCCLCPSRPRYAPGVTIEEDNCCGCNAIAIRRHFLDENMTSVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHHGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPSLKCFAYSPPGGLLRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEEPEENSVTSNRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEDPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQSQPLPSCPSVQIGTGAIPADRRNSSTKSKSHSEISLEGFYETKPLSPVQKDPVELLLLDTKERLSVELQDRRAPLATMESLSDNESIYSFDSRRSSGFRSIRGSPSLHAVMEKDETHCFYIDPVIPEENPSLSSRTELLAADSLSKHSQETQPPENVLNSGGTTPQRRCSAEGTGSDGERASSSPREEPPLHNGRLADVPSPQVLEFAEFIDSLFNLDSKSSSFQDIYCMMVSDSSSDFAEMPKSVSDQEILLRAQYEPNLVPKPPRLFAGSTDPSSGISVSPSFPLSSSGELMDITPTGVSSQECLATDKIRTSTPSGHVTSPAKQDDLMISAL
Protein: 4-coumarate--CoA ligase 1 (4CL 1) (Os4CL1) (EC 6.2.1.12) ((E)-ferulate--CoA ligase) (EC 6.2.1.34) (4-coumaroyl-CoA synthase 1) (P17814)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the phenylpropanoid metabolism by mediating the activation of a number of hydroxycinnamates for the biosynthesis of monolignols and other phenolic secondary metabolites. Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate. Is more efficient with substrates in the following order: ferulate > 4-coumarate > cinnamate > caffeate. Cannot convert sinapate to its corresponding CoA ester. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity).
Interaction partners:
- Phenylalanine ammonia-lyase
- tricin synthase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Aldehyde dehydrogenase 1
- Os06g0592400 protein
- Trans-cinnamate 4-monooxygenase
- Phenylalanine ammonia-lyase.
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
Sequence:
MGSMEQQQPESAAPATEASPEIIFRSKLQDIAITNTLPLHRYCFERLPEVAARPCLIDGATGGVLTYADVDRLSRRLAAALRRAPLGLRRGGVVMSLLRNSPEFVLSFFAASRVGAAVTTANPMSTPHEIESQLAAAGATVVITESMAADKLPSHSHGALTVVLIDERRDGCLHFWDDLMSEDEASPLAGDEDDEKVFDPDDVVALPYSSGTTGLPKGVMLTHRSLSTSVAQQVDGENPNIGLHAGDVILCALPMFHIYSLNTIMMCGLRVGAAIVVMRRFDLAAMMDLVERHRVTIAPLVPPIVVAVAKSEAAAARDLSSVRMVLSGAAPMGKDIEDAFMAKLPGAVLGQGYGMTEAGPVLSMCLAFAKEPFKVKSGACGTVVRNAELKIIDPDTGKSLGRNLPGEICIRGQQIMKGYLNNPEATKNTIDAEGWLHTGDIGYVDDDDEIFIVDRLKEIIKYRGFQVAPAELEALLITHPSIADAAVVGKQIEPEIGEIPVAFVAKTEGSELSEDDVKQFVAKEVIYYKKIREVFFVDKIPKAPSGKILRKELRKQLQHLQQEA
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp) (Malate dehydrogenase [quinone] flavoprotein subunit) (EC 1.1.5.-) (Q0QF01)
Organism: Sus scrofa (Pig)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (Probable). Can act as a tumor suppressor (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17480203}; Peripheral membrane protein {ECO:0000269|PubMed:17480203}; Matrix side {ECO:0000269|PubMed:17480203}.
Interaction partners:
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- NADH dehydrogenase flavoprotein 1
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH:ubiquinone oxidoreductase core subunit S7
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MSGVRAVSRLLRARRLALTWAQPAASPIGARSFHFTVDGNKRSSAKVSDAISTQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSDWLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGKIYQRAFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIEDGSIHRIRARNTVVATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLEFVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHLPPEQLAVRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQVLRHVNGQDQVVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIAESCRPGDKVPSIKPNAGEESVMNLDKLRFANGTIRTSELRLSMQKSMQSHAAVFRVGSVLQEGCEKILRLYGDLQHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDFKERVDEYDYSKPIQGQQKKPFQEHWRKHTLSYVDVKTGKVSLEYRPVIDKTLNEADCATVPPAIRSY
Protein: Aspartate-rich protein 1 (Q6PGQ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGNILTCCINSHCGWPRGKDAPCYESDTDIYETVAAATSESTTVEPGKLDVGATEGQDLQHISNQKMPTGPPEDRLSLKFLPSSEEDNDDAKILPSPVQGSSEDNLSLVCLPRSEDDDCDDDDDDDAQILPSRVQGGCYRFDSSSCSSEDNLSLVCLPRSEDDDCDDDDDDAQILPSPVQACSEDSLFLRCSLRHKDEEEEDDDDIHITARIESDLTLESLSDEEIHPG
Protein: Protocadherin gamma A12 (Protocadherin gamma subfamily A, 12) (Q91XY7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MIPMQRREDCKGLVFLGVLLGMLWKAGSTQIRYSVPEELEKGSRVGNISKDLGLEPRELEKRGVRIVSRGRAQLFALNPRSGSLVTAGRIDREELCMGSIKCQLNLEILMEDIGKIYGVEIEVRDINDNAPYFRESELEIKMSENAAAGMRFPLPHAWDPDIGKNSLQSYQLSPNAHFSLEVQNGADGNKYPELVLESSLDREEKAAHLLVLTASDAGDPVRTGTARIRVMVVDANDNAPAFARSEYRVSVRENVAVGTQLLLVNATDPDEGANAEVIYSFRYVDDKAAKVFKLDSNLGTISTIGELNHEESGFYEMEVQATDNAGYSARAKVLVTVLDVNDNAPEVAITSLTNSVPENSPQGTLIALLNVNDQDSGENGQVICSIQENLPFKLEKSYGNYYRLVTDAVLDREEVPSYNITMTATDRGSPPLTTETHLALDIADTNDNSPVFLQASYWAYIPENNPRGASIASVTAHDPDSDKNAQVTYSLAEDTHQGVPLSSYVSINSDTGVLYALHSFDYEQFPDLQLQVIARDSGDPPLSSNVSLSLFVLDQNDNVPEILYPTLPTDGSTGVELAPRSAEPGYLVTKVVAVDRDSGQNAWLSYRLLKASEPGLFSVGLHTGEISTARALMDRDALKQNLVVSVQDHGQPPLSATVTLTVAIADSIPDVLADLDNLESPSTSETSGLTLYLVVAVAAVSTVFLVFVLVLLALRLRRWHSLRLLRAGGPGLADVAASHFVGVDGVQAFLQTYSHEVSLTAGSRKSHLIFPQPNYADTLISQESCEKTEPLLPSGDSVFSKDNHALNQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Putative cytoplasmic protein (A0A0F6B9Z0)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Interaction partners:
Sequence:
MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNIIMNTSQFTQSSWARHVQ
Protein: Multiple C2 domain and transmembrane region protein 16 (Q9FJG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable serine/threonine-protein kinase PBL3
- 16 kDa phloem protein 2
- Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 4
Sequence:
MATTRKLVVEVVDAKDLTPKDGHGTSSPYVVLDYYGQRRRTRTIVRDLNPVWNETLEFSLAKRPSHQLFTDVLELDMYHDKNFGQTRRNNFLGRIRLGSDQFVGQGEEALIYYPLEKKSLFNLVQGEIGLRVYYADEKPPPLKPTVAPLETVVEEKTEETKAEGPDESKPPPETNDIPAEVKETVKPPQPPPEESSPAEGPKPDEEASPPLQENATVGGEEPPASESDKNEAEAKPVEEPPQNQPDGEDIVLESEDTMSWASAPRSPLPEVIISRSVSGSIPETKNGPQPLRRSVSETASYTSEISDVSTIERSTFDLVEKMHYVFIRVVKARSLPTSGSPVTKISLSGTMIQSKPARKTSCFEWDQTFAFLRDSPDLSSSPILEISVWDSSTGIETSQFLGGICFDVSEIPLRDPPDSPLAPQWYRLEGGGAHNSDLMLATWTGTQADESFPDAWKTDTAGNVTARAKVYMSSKLWYLRATVIEAQDLLPPQLTAFKEASFQLKAQLGSQVQKTKSAVTRNGAPSWNEDLLFVAAEPFSDQLVFTLEYRTSKGPVTVGMARVPLSAIERRVDDRLVASRWLGLEDPNDEKRGNRSRVHIRLCFDGGYHVMDEAAHVCSDYRPTARQLWKPAVGIVELGIIGCKNLLPMKTVNGKGSTDAYTVAKYGSKWVRTRTVSDSLDPKWNEQYTWKVYDPCTVLTIGVFDSWGVYEVDGGKEATRQDLRIGKVRIRISTLETGKAYRNTYPLLMLVNGGVKKLGEIELAVRFVRTAPPLDFLHVYTQPLLPLMHHIKPLSLFQEDMLRNTAVKILAAHLSRSEPPLRPEIVRYMLDADTHTFSMRKVRANWLRIVNVVAGMVDVVRWVDDTRFWKNPTSTLLVHALVVMLIWFPDLIVPTLAFYLFVIGAWNYRFRSRAALPHFDPRLSLADAADRDELDEEFDVVPSNRPPEMVRLRYDKLRNVGARVQTILGEVAAQGEKMQALVTWRDPRATGIFVGLCFFVALVLYLVPTKMVAMASGFYYFRHPIFRDRKPSPVLNFFRRLPSLSDRLM
Protein: Meltrin, isoform D (EC 3.4.24.-) (Q400M8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLHLHLFLLPLLLLNTCLQQHILQPAEATAFHQSEGEKSKAHPVLEEFSTYTVIRPQVEHGRTKRSLLTTLDATDGLHTPQISLSYTHEGKRVVVDLQRNDLLLPNSHFLRYQNASRGATPGHVVTTFTKTEVDLCHYQGHIRGKPESVVALSTCDGALDGIVIDGRQTYFIHPHIDGRGRLQDDHYLLKQADMHPTNATCGYDNHRDDHSHDYEKADGDNGLGGGIPSLPLRLDGGEFSRTLLRKRRQADDSSQLIRGPYNANKYSSYVELVIVVDNKVYKNFQENTKKVHQYCKGIANIINALYVPLNIFVALVGVVIWNESNEIEFSSDGDLTLRNFLNYRSTKLVLDHPNDNAQLLTKENFAGGVVGKALKGPICTYEYSGGVSMQHSPNPAMVATTMAHEMGHNFGMEHDTSDCHCRDEKCVMAASSTSFIPVNWSSCSIDQLTIAFSRGMNYCLRNKPERLFESPTCGNGFVEPGEQCDCGLPEHCENACCNAQTCMLHSKNATCATGECCDLTTCRPKLAGSACREAENECDLPEYCTGESEYCPADVFRRDTEPCDGGQAYCFHGTCRSHSNQCRTLWGPTGDNSEHCYNKNTEGTRLGNCGYNRLNKTFLRCEEQHVNCGMLHCIHLNERLEFGMESAAVLSHSYISHDRKIVACRTALVDLGLQTTDPGLTPNGAKCGVDKMCVDQRCLPVDAVRQKGMGKPCPEDCNGNGICNSRGHCHCDVGFGGESCSKAGSGGSPDSGPATDPNGSVGFKRFLYVLFFFVLPVVALFWFLYHCYKNGMLTRGKLADNMYVSTSSFSIGSKEDTSPDSSISTTLAHKQTPARTAPPPLPLHTNRQLSGIVTNTAPATITNIHAILPRHKSNPDVVHQLNIPPPSVPKSHSTHEVRPKAATLKPLTLLHSTHSTSNNNNTESLNQNDKSNTNNSTLRRKLDITAPRLNATTNPLALTEGAQFIQSDPARCAKN
Protein: Nucleoporin seh1 (Nuclear pore protein seh1) (Q10099)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular location: Cytoplasm. Nucleus, nuclear pore complex.
Interaction partners:
- Nucleoporin nup107
- Nucleoporin nup189
- Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05
- Protein transport protein sec13
- Nucleoporin nup85
- Uncharacterized WD repeat-containing protein C12G12.01c
- Nucleoporin nup120
- Uncharacterized WD repeat-containing protein C4F8.11
- Nitrogen permease regulator 2 homolog
- Probable nucleoporin C890.06
Sequence:
MDDISATTIQTNHQDLVNDVTYDFYGRRMVSCSADQRVKVYDFNDDTETWAITSEWRAGDASLMRVAWAHPSFGQVLAVCSLDRGVRIYEEQKKNFESKTWVEVAKLMDARSAVLDISFCPFQHGCKLAAVSADATLRIYEAMEPGNLTYWTLMNEIALMPSPPSRNEQPAFCVNWCPSRWREQYIAVGCMNDAYIYKQNSHGKWKKVAELPGHTDLIRDICWAPSMGSSYYLIATACKDGNVRIFKVETLCEEVFQEEEDAGNSMTEDSNFNLNSLKVELIGEYDNHKCQVWRCRFNVTGTILSSSGDDGCVRLWKASYANLFKCISVVSLEKKPEKL
Protein: Exostosin-2 (EC 2.4.1.224) (Exostosin glycosyltransferase 2) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Multiple exostoses protein 2 homolog) (P70428)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10639137}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q93063}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:O77783}. Note=The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized to the Golgi apparatus. If both proteins are individually detected in the endoplasmic reticulum, the formation of the complex promotes their transport to the Golgi. {ECO:0000269|PubMed:10639137}.
Interaction partners:
- Exostosin-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- 1-aminocyclopropane-1-carboxylate synthase-like protein 1
- Heparan sulfate 2-O-sulfotransferase 1
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2
- UDP-glucuronosyltransferase 3A1
Sequence:
MCASVKSNIRGPALIPRMKTKHRIYYVTLFSIVLLGLIATGMFQFWPHSIESSSDGGVEKRSIREVPVVRLPTDSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYPLKKYVDDAGVPVSSAISREYNELLTAISDSDYYTDDINRACLFVPSIDVLNQNPLRIKETAQALAQLSRWDRGTNHLLFNMLPGAPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVFSPLSAEMALPEKAPGPRRYFLLSSQMAIHPEYREELEALQAKHQESVLVLDKCTNLSEGVLSVRKRCHQHQVFDYPQVLQEATFCTVLRGARLGQAVLSDVLQAGCVPVVIADSYILPFSEVLDWKRASVVVPEEKMSDVYSILQNIPQRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYPYAAISYEEWNDPPAVKWASVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVPSLSKLLVVWNNQNKNPPEESLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDDIIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFYHKYFNYLYTYKMPGDIKNWVDTHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAIDGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
Protein: Probable inactive ATP-dependent zinc metalloprotease FTSHI 3, chloroplastic (AtFTSHI3) (Protein FTSH INACTIVE PROTEASE 3) (Q9M895)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
Subcellular location: Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- AT5g10910/T30N20_180
- Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial
- At5g09480
- Protein TIC 100
- Pentatricopeptide repeat-containing protein At2g15820, chloroplastic
- Probable mitochondrial-processing peptidase subunit alpha-2, chloroplastic/mitochondrial
- Protein TIC 56, chloroplastic
- Protein TIC 20-I, chloroplastic
- Small ribosomal subunit protein bS16m/bS16c
Sequence:
MATFNVLCSNRFRFNGGYSPEKFNRKVSSRSSELNVCVSRIRTQSFSCRRLGGFMEIGETRLGVIRVHGDSRNRFSCNSEIKRLVTGDYGDKETRIGENGRNKGKRRRFSLRLRPRLRLVRMRLGRFDFRASMEDFRYFLKKNLKRVILSTGVALIFGLCYLFLRLTAVPSPSIVPYSDFVTNLRGGSVSKVLLEEGSRRIYYNTDENVEVVDDVHKSETLEDPAIQIDGGTVTEAVTKDDTPRKVRALPPVWKYVTRKVDHDEKFLLSLMREKGITYSSAPQSALMSMRTTLITIISLWIPLTPLMWLLYRQLSASNSPAKKRRSKNPTVGFDDVEGVDSAKDELVEIVSCLQGSINYKKLGARLPRGVLLVGPPGTGKTLLARAVAGEAGVPFFSVSASEFVELFVGRGAARIRDLFNAARKNSPSIIFIDELDAVGGKRGRSFNDERDQTLNQLLTEMDGFESDTKVIVIAATNRPEALDSALCRPGRFSRKVLVAEPDQEGRRKILAIHLRDVPLEEDAFLICDLVASLTPGFVGADLANIVNEAALLAARRGGEAVAREDIMEAIERAKFGINDKEARPRTLGNELSKMFPWMPSLARRNGPDQDGLQGPLGYQTLS
Protein: Coiled-coil domain-containing protein 110 (Cancer/testis antigen 52) (CT52) (Cancer/testis antigen KM-HN-1) (Q8TBZ0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:15447989}.
Interaction partners:
Sequence:
MSPEKQHREEDEVDSVLLSASKILNSSEGVKESGCSDTEYGCIAESENQIQPQSALKVLQQQLESFQALRMQTLQNVSMVQSEISEILNKSIIEVENPQFSSEKNLVFGTRIEKDLPTENQEENLSMEKSHHFEDSKTLHSVEEKLSGDSVNSLPQSVNVPSQIHSEDTLTLRTSTDNLSSNIIIHPSENSDILKNYNNFYRFLPTAPPNVMSQADTVILDKSKITVPFLKHGFCENLDDICHSIKQMKEELQKSHDGEVALTNELQTLQTDPDVHRNGKYDMSPIHQDKMNFIKEENLDGNLNEDIKSKRISELEALVKKLLPFRETVSKFHVHFCRKCKKLSKSEMHRGKKNEKNNKEIPITGKNITDLKFHSRVPRYTLSFLDQTKHEMKDKERQPFLVKQGSIISENEKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKICNQHNDPSKTTYISRREKFHFDNYTHEDTSSPQSRPLASDLKGYFKVKDRTLKHH
Protein: Angiotensin-converting enzyme-related protein (EC 3.4.15.1) (Q9VLJ6)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in the specific maturation or degradation of a number of bioactive peptides. May have a role in the specification of heart progenitors.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:9839949}.
Interaction partners:
- GH24474p
Sequence:
MGACNITVLLLVIMLWLPHGLSMGNSCSASVLEARRFFELENEQLRRRFHEEFLSGYNYNTNVTEANRQAMIEVYARNAELNKRLAQQIKSSDYVQSEDADIRRQAEHLSKLGASALNADDYLALQNAISSMQTNYATATVCSYTNRSDCSLTLEPHIQERLSHSRDPAELAWYWREWHDKSGTPMRQNFAEYVRLTRKASQLNGHRSYADYWVQFYEDPDFERQLDATFKQLLPFYRQLHGYVRFRLRQHYGPDVMPAEGNIPISLLGNMWGQSWNELLDLFTPYPEKPFVDVKAEMEKQGYTVQKLFELGDQFFQSLGMRALPPSFWNLSVLTRPDDRHVVCHASAWDFYQDSDVRIKMCTEVDSHYFYVVHHELGHIQYYLQYEQQPAVYRGAPNPGFHEAVGDVIALSVMSAKHLKAIGLIENGRLDEKSRINQLFKQALSKIVFLPFGYAVDKYRYAVFRNELDESQWNCGFWQMRSEFGGVEPPVFRTEKDFDPPAKYHIDADVEYLRYFAAHIFQFQFHKALCRKAGQYAPNNSRLTLDNCDIFGSKAAGRSLSQFLSKGNSRHWKEVLEEFTGETEMDPAALLEYFEPLYQWLKQENSRLGVPLGWGPTDKIPSDCCGTFST
Protein: Caveolae-associated protein 2 (Cavin-2) (Phosphatidylserine-binding protein) (Serum deprivation-response protein) (Q66H98)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae. Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells (By similarity). May play a role in targeting PRKCA to caveolae.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O95810}. Membrane, caveola {ECO:0000269|PubMed:9566962}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:9566962}.
Interaction partners:
- Caveolin-1
Sequence:
MGEDAAQAEKFQHPNTDMLQEKPSNPSPMPSSTPSPSLNLGSTEEAIRDNSQVNAVTVHTLLDKLVNMLDAVRENQHNMEQRQINLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVRERLEKQCVQVKRLENNHAQLLRRNHFKVLIFQEESEIPASVFVKEPVPSTAEGKELADENKSLEETLHNVDLSSDDELPGDEEALEDSAEEKMEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTPNHQKASSGKSSPFKVSPLSFGRKKIREGESSAENETKLEEQVQDDHEEGSFTEGLSEASLPSGLLEGSAEDAEKSALRGNNSGVGSNADLTIEEDEEEESVALQQAQQVRYESGYMLNSKEMEESSEKHVQAAVLHVDQTA
Protein: Class V chitinase (AtChiC) (EC 3.2.1.14) (EC 3.2.1.200) (O81862)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Can hydrolyze glycol chitin and chitin oligosaccharides (e.g. N-acetylglucosamine) (GlcNAc)4, (GlcNAc)5 and (GlcNAc)6. Hydrolyzes N-acetylglucosamine oligomers producing dimers from the non-reducing end of the substrates.
Interaction partners:
- Acidic endochitinase
- Beta-hexosaminidase 2
- Beta-hexosaminidase 3
- Beta-hexosaminidase 1
- Basic endochitinase B
- Eukaryotic aspartyl protease family protein
- Cytochrome P450 71B23
- Endochitinase EP3
- Short-chain dehydrogenase/reductase 2b
- Short-chain dehydrogenase reductase 2a
Sequence:
MSSTKLISLIVSITFFLTLQCSMAQTVVKASYWFPASEFPVTDIDSSLFTHLFCAFADLNSQTNQVTVSSANQPKFSTFTQTVQRRNPSVKTLLSIGGGIADKTAYASMASNPTSRKSFIDSSIRVARSYGFHGLDLDWEYPSSATEMTNFGTLLREWRSAVVAEASSSGKPRLLLAAAVFYSNNYYSVLYPVSAVASSLDWVNLMAYDFYGPGWSRVTGPPAALFDPSNAGPSGDAGTRSWIQAGLPAKKAVLGFPYYGYAWRLTNANSHSYYAPTTGAAISPDGSIGYGQIRKFIVDNGATTVYNSTVVGDYCYAGTNWIGYDDNQSIVTKVRYAKQRGLLGYFSWHVGADDNSGLSRAASQAWDATTATTRTIQKV
Protein: Large ribosomal subunit protein eL42 (60S ribosomal protein L36a) (P61485)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P83881}.
Interaction partners:
- Large ribosomal subunit protein eL39
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Large ribosomal subunit protein eL13
- Ribosomal protein S10
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS1
- 60S ribosomal protein L29
- Small ribosomal subunit protein uS7
Sequence:
MVNVPKTRRTYCKKCKKHQPHKVTQYKKGKDSLYAQGKRRYDRKQSGYGGQTKPIFRKKAKTTKKIVLRLECVEPNCRSKRMLAIKRCKHFELGGDKKRKGQVIQF