wanglab/gogpt-training-data huggingface dataset:
Protein: Pregnancy-specific beta-1-glycoprotein 5 (PS-beta-G-5) (PSBG-5) (Pregnancy-specific glycoprotein 5) (Fetal liver non-specific cross-reactive antigen 3) (FL-NCA-3) (Q15238)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pregnancy-specific beta-1-glycoprotein 1
- Pregnancy-specific beta-1-glycoprotein 2
- Pregnancy-specific beta-1-glycoprotein 4
- Pregnancy-specific beta-1-glycoprotein 6
- Pregnancy-specific beta-1-glycoprotein 3
Sequence:
MGPLSAPPCTQHITWKGLLLTASLLNFWNLPITAQVTIEALPPKVSEGKDVLLLVHNLPQNLAGYIWYKGQLMDLYHYITSYVVDGQINIYGPAYTGRETVYSNASLLIQNVTREDAGSYTLHIIKRGDRTRGVTGYFTFNLYLKLPKPYITINNSKPRENKDVLAFTCEPKSENYTYIWWLNGQSLPVSPRVKRPIENRILILPSVTRNETGPYECEIRDRDGGMRSDPVTLNVLYGPDLPSIYPSFTYYRSGENLYLSCFAESNPPAEYFWTINGKFQQSGQKLSIPQITTKHRGLYTCSVRNSATGKESSKSMTVEVSAPSGIGRLPLLNPI
Protein: Glycine receptor subunit alpha-1 (Glycine receptor 48 kDa subunit) (Glycine receptor strychnine-binding subunit) (P23415)
Organism: Homo sapiens (Human)
Function: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine. Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol. Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q64018}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64018}. Synapse {ECO:0000250|UniProtKB:Q64018}. Perikaryon {ECO:0000250|UniProtKB:Q64018}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q64018}. Cell membrane {ECO:0000269|PubMed:14551753, ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:2155780, ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:22973015, ECO:0000269|PubMed:24108130, ECO:0000269|PubMed:25445488, ECO:0000269|PubMed:25730860, ECO:0000269|PubMed:25973519, ECO:0000269|PubMed:7920629, ECO:0000269|PubMed:7925268, ECO:0000269|PubMed:9009272}; Multi-pass membrane protein {ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860, ECO:0000305|PubMed:2155780}.
Interaction partners:
- Sodium- and chloride-dependent glycine transporter 2
- Gephyrin
- Rho guanine nucleotide exchange factor 9
- Glycine receptor subunit beta
- Dihydropyrimidinase-related protein 5
- Glycine--tRNA ligase
Sequence:
MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ
Protein: Sulfate transport system permease protein CysW (P0AEB0)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Sulfate adenylyltransferase subunit 2
- Thiosulfate-binding protein
- Sulfate transport system permease protein CysT
- Sulfate-binding protein
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate adenylyltransferase subunit 1
- Adenylyl-sulfate kinase
- Sulfite reductase hemoprotein beta-component
- Phosphoadenosine 5'-phosphosulfate reductase
- Cysteine synthase B
Sequence:
MAEVTQLKRYDARPINWGKWFLIGIGMLVSAFILLVPMIYIFVQAFSKGLMPVLQNLADPDMLHAIWLTVMIALIAVPVNLVFGILLAWLVTRFNFPGRQLLLTLLDIPFAVSPVVAGLVYLLFYGSNGPLGGWLDEHNLQIMFSWPGMVLVTIFVTCPFVVRELVPVMLSQGSQEDEAAILLGASGWQMFRRVTLPNIRWALLYGVVLTNARAIGEFGAVSVVSGSIRGETLSLPLQIELLEQDYNTVGSFTAAALLTLMAIITLFLKSMLQWRLENQEKRAQQEEHHEH
Protein: Axonemal dynein heavy chain (O08827)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
LVITPLTDRCYLCLMGALQLDLGGAPAGPAGTGKTETTKDLAKALAIQCVVFNCSDGLDYKMMGRFFSGLAQSGAWCCFDEFNRIDIEVLSVIAQQLITIRNAKAAKLSRFMFEGREIKLVMTCAAFITMNPGYAGRTELPDNLKALFRPMAMMVPNYALIAEVILYSEGFESSKILARKMTQMYKLCSEQLSQQDHYDFGFRA
Protein: Uncharacterized protein (Q388V5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVFWGKLIMFPPVARRVVPRFAVVCPRGTATRYHCGPSKGGVTQGNGHRLGSTNTSSKGETSVVLNSTSVAVRRFLREQQKVSVRWWESPGRVDALLTLFLDRSHSGELHPLLAVEVTKRLGYAVGPEGCGWAIRCGHSGGSIILLTERLLTPLIPLVATHSAVRPLLPVIVEWLLSVANMPMQIVVGHVALYVNNLSEMSLEDMSRHEWPSLEFLLHNFARQSLHISDEAVKQEVNDVICKMVALFGLWGQRHPAETGQSRSCCSASINPVTDSLEKCFFWRGEAPLLIHGSVRTAYARFYNDWFDTSPRSTGGPATNSPSLSVFVGDDDKLRRVLLRLSVDSRVGVGSNEERDMTSAPVVPVEVKLKLDEPSVILRCIVPLAEFVSQVLDTGIGTLLPLSFGSIQTIIYNAISELQRLQGQSAEHHYALLPHKPRVHALKDLCERLLSDIKEKMQKGQRPSRGSVGDYVCFPGETPQQQLQVLHFFYRAARHLVRAVMVEKKASLMEEGCEGSVLLAGGTVASRNDVATLLRNVAFRVLETSLLRYYNALDECSSHSSVWRSLGDNGEITAAISDIEHHAGGHSPLFTARHVLQHPFQQDVIAVVEGLRLVAIQALVLHSQQCVNWLKGRAYSNTAANAFFGVWERTKVGGSSLTNHNQSGREGTESGKFDIQRMMRHRLLWTMLLLHHEYCSCCDPGGREQEAHWQAPTNCMVLRSLLDMLVPDPTCTEFSAFGWSYPLGCDGQNLSLQTGGSGDSELWKRHVVYPPAHRSFSGDASRWDLLDELSPTRDSSRKWLWLGTTGSVREACAIVNPTGDTASRFVGYLLPWSTVAKSRHPLRFYDESGQSAAAAASFDAAVGTLVRGKNSKMPLRLVGVQEEVAFFRDMEHTSELLLCPGILVTNPWTQSKDRVKNSDRNVPDNMEGFLDNEVYDFLD
Protein: Ubiquitin thioesterase ZRANB1 (EC 3.4.19.12) (TRAF-binding domain-containing protein) (hTrabid) (Zinc finger Ran-binding domain-containing protein 1) (Q9UGI0)
Organism: Homo sapiens (Human)
Function: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin. Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones. Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription. Acts as a regulator of autophagy by mediating deubiquitination of PIK3C3/VPS34, thereby promoting autophagosome maturation. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:25752577}. Nucleus {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:25752577}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:25752577}.
Interaction partners:
- Polyubiquitin-C
- TNF receptor-associated factor 6
- Ubiquitin-ribosomal protein eS31 fusion protein
- Adenomatous polyposis coli protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- E3 ubiquitin-protein ligase HECTD1
- Striatin-interacting protein 1
- OTU domain-containing protein 3
Sequence:
MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSVCTYENWAKAKRCVVCDHPRPNNIEAIELAETEEASSIINEQDRARWRGSCSSGNSQRRSPPATKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE
Protein: Dachshund, isoform A (Q9VJK6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDSVTSEQSENNNNKAGAINNNINSGIERAAGNMNTTAMLMHHQQQQQAAAAAAAAAAQQQQQQHNGRDGSNSSRGANEDRPNGRSSHTGRGSSCSPASSPSRHPSAVSPVSSLNHSMMQQMQQQQQQQQQQQQQQQHHQLSPPPHGMPSGNGLPTGLPPRMPHGLPPHSLGLLNSLQMMHHASPLELMAAAHHHVPPRSYNSPPPISTSDPSANECKLVEYRGQKVAAFIISNETMLCLPQAFELFLKHLVGGLHTVYTKLKRLDIVPLVCNVEQVRILRGLGAIQPGVNRCKLLCCKDFDILYRDCTTASNSLQFRSSRPGRPPKRGPVGLSLPPTHLSQHPQLKKHRLDNGDYAYENGHISDMKSPLLANGYNPPPINHMAFMQMNAHHPGAAALMSPGMPPHGLHARPESQMLKAAAQNAGMSAANMDALARSGIWENCRAAYEDIVKHLERLREERTDERQQAMGVGGAVVDRVGNVMVAEHKPRDLSSRNCSPTRQSPVLNLSKSGGNTDHGGSNCDAGSERSDCHSVAGSPARGGSRSLDEGSRSGVGGGVASHVGGGIIGVEDDEEEEENLSDENQSEVDERCLAKDDEDLSDTERDNLSTGSAAAAAAAAAAAAHQLHQHAASHHHQTVGLSHLGVVPPHQRGSPSSAEAAAAALQHQRALNYSQLAAAAAVANGAAVGGGAVANGPTGGGGALTPNEALLAANDAAALAGGLALGPLGIDAHAAVPASSTETLLRNIQSLLKVAADNARQQERQISYEKAELKMDVLREREVKDSLERQLVDERKLRVLYQKRFRRERKIRIRYQQQLGGGSGAVKGSPNANGSGGGGSGSACSESEACGGGGGDAKCNNNNNNNNNNNNSNSSSHGGDVETMKENDAGSEKSDKSLASNSSCDVTAGHSAGSVSGSISAGLNCPDSPTHFKREPSSDHEGSVERQPRSSAASLAAHDEDNTKRCGSRDRDERPPSGSAASVAAEGSLAAAAAAAAAAAAAAASNGKGPWSYPGIDLMATGAFWQNYSESLAQELEMERKSRAANAERDVKSPLSERPTAYYKNSVLFGSAN
Protein: 4-coumarate--CoA ligase 3 (4CL 3) (EC 6.2.1.12) ((E)-ferulate--CoA ligase) (EC 6.2.1.34) (4-coumarate--CoA ligase isoform 3) (At4CL3) (4-coumaroyl-CoA synthase 3) (Q9S777)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Produces CoA thioesters of a variety of hydroxy- and methoxy-substituted cinnamic acids, which are used to synthesize several phenylpropanoid-derived compounds, including anthocyanins, flavonoids, isoflavonoids, coumarins, lignin, suberin and wall-bound phenolics. 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 thioesters (By similarity).
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Chalcone synthase
- Cytochrome P450 84A1
- Flavone 3'-O-methyltransferase 1
- Phenylalanine ammonia-lyase 1
- F5F19.5 protein
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 4
Sequence:
MITAALHEPQIHKPTDTSVVSDDVLPHSPPTPRIFRSKLPDIDIPNHLPLHTYCFEKLSSVSDKPCLIVGSTGKSYTYGETHLICRRVASGLYKLGIRKGDVIMILLQNSAEFVFSFMGASMIGAVSTTANPFYTSQELYKQLKSSGAKLIITHSQYVDKLKNLGENLTLITTDEPTPENCLPFSTLITDDETNPFQETVDIGGDDAAALPFSSGTTGLPKGVVLTHKSLITSVAQQVDGDNPNLYLKSNDVILCVLPLFHIYSLNSVLLNSLRSGATVLLMHKFEIGALLDLIQRHRVTIAALVPPLVIALAKNPTVNSYDLSSVRFVLSGAAPLGKELQDSLRRRLPQAILGQGYGMTEAGPVLSMSLGFAKEPIPTKSGSCGTVVRNAELKVVHLETRLSLGYNQPGEICIRGQQIMKEYLNDPEATSATIDEEGWLHTGDIGYVDEDDEIFIVDRLKEVIKFKGFQVPPAELESLLINHHSIADAAVVPQNDEVAGEVPVAFVVRSNGNDITEEDVKEYVAKQVVFYKRLHKVFFVASIPKSPSGKILRKDLKAKLC
Protein: V-type ATP synthase subunit E (V-ATPase subunit E) (P74901)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Interaction partners:
Sequence:
MSKLEAILSQEVEAEIQALLQEAEAKAEAVKREAEEKAKALLQARERALEAQYRAALRRAESAGELLVATARTQARGEVLEEVRRRVREALEALPQKPEWPEVVRKLALEALEALPGAKALVANPEDLPHLEALARERGVELQAEPALRLGVRAVGAEGKTQVENSLLARLDRAWDALSSKVAQALWG
Protein: DPR1 (Q8T603)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSLPSRANFGLLNWLIGWLLLLSMVLLRGYNAALAPTPPTTSTTTISPSNLLPYFDFDVPRNLTVTVGQTGFLHCRVERLGDKDVSWIRKRDLHILTAGGTTYTSDQRFQVLRPDGSANWTLQIKYPQPRDSGVYECQINTEPKMSLSYTFNVVELKAEIFGPSDLMVKTGSDINLTCKIMQGPHELGNIFWYKGSEMLDGKGENEIDSSMARIRVEDDWTDGLTSRLKIKRAMPGDTGNYTCVPTVAKTSSVYVHVIIGEHPAAMQHNSSSNSNSFYCGICCMLLSIVSCCLQHFYETGCGYLHAAAAVAKSAGLGPPKRATLTTSETGISAAEVASAAGASAAVASTLATCNMLRERPAAIRCLS
Protein: Rho GTPase activating protein 32 (A0A8I5Y6H2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKSSIHSEEDDFVPELHRNVHPRERPDWEETLSAMARGADVPEIPGDLTLKSCGSTASMKVKHVKKLPFTKGHFPKMAECAHFHYENVEFGSIQLSLSEEQNEIMKNGCESKELVYLVQIACQGKSWIVKRSYEDFRVLDKHLHLCIYDRRFSQLSELPRSDILKDSPESVTQMLAAYLSRLSTIAGNKINCGPALTWMEIDNKGNHLLVHEESSINTPAVGAAHVIKRYTARAPDELTLEVGDIVSVIDMPPKVLSTWWRGKHGFQVGLFPGHCVELINQKVPQSVTNSVPKPVSKKHGKLITFLRTFMKSRPTKQKLKQRGILKERVFGCDLGEHLLNSGFEVPQVLQSCTAFIERYGIVDGIYRLSGVASNIQRLRHEFDSEHVPDLTKEPYVQDIHSVGSLCKLYFRELPNPLLTYQLYEKFSDAVSAATDEERLIKIHDVIQQLPPPHYRTLEFLMRHLSLLADYCSITNMHAKNLAIVWAPNLLRSKQIESACFSGTAAFMEVRIQSVVVEFILNHVDVLFSGKISAVMQEGAASLTRPKSLLVSSPSTKLLTLEEAQARTQAQVNSPIVTENKYIEVGEGPAALQGKFHTIIEFPLERKRPQNKMKKSPVGSWRSFFNLGKSSSVSKRKLQRNESEPSEMKAMALKGGRAEGTLRSAKSEESLTSLHAVDGDSKLFRPRRPRSSSDALSASFNGEVLGNRCNSYDNLPHDNESEEEVGLLHIPALVSPHSAEDVDLSPPDIGVASLDFDPMSFQCSPPKAESECLESGASFLDSLGFTRDKLGASKKDVEAGGSQSQTPGSTASSEPVSPVQEKLSPFFTLDLSPTEDKSSKPSSFTEKVVYAFSPKIGRKLSKSPSMNISEPISVTLPPRVSEVIGTVSNTVSQNASPPSWDKSVEERDVINRSPTQLGKMKPGEREAQERCEPEAQPQEQGAAEEVELPGTEERPVSSSQSKAVPSGQSQTGAVTHDPPQDPVPVSSVSLIPPPPPPKNVARMLALALAESAQQASTQTLKRPGPSQAGCTSYGDMAVATSEEKLPSSYSSVTLDKTYFQTDRPAEQFHLQINGLGNCDQPLPETAAMGGPTHPNTTDSGEQLHQVDLIGNSLHRNHLSGDPEKARSTSAPLADSEKSDGHGSFPEDHAGKTSVSTVSFVGQGQSPLHFSSGDQPLSYLGTSMDKPHHSSELTEKSPMPSTLPRDKAHPLSGSPEENTSTATMAYMMTTPPRAETSTREASRAMAEQPTAADFVAATLQRAHRTNRPLPPPPSQRPTEQPPGVGQVQEAPSIGVNNSHKVQGAAPAPERPPEPRAMADPAPIFVSDGSAAAQCPMAISAAQPGLPEKVRESSRAPPLHLRAETFPGHSCGFAAPVPPTRTVESKMAAAMHSSAAEANNSSNYHSFVPSSASADDVLPLPPPIAQPKHASQKIAYSSFARPDVTTEPFGPENCLHFNMTPNCQFRPQSVPPHHNKLEPHQVYGTRSEPPASMGPRYNTYVAPGRSMSGHHSKPCSRVEYVSSLGSSVRNPCCPEDILPYPTIRRVQSLHAPPPSMIRSVPISRTEVPPDDEPAYCPRPVYQYKPYQSSQARSDYHVTQLQPYFENGRVHYRYSPYSSSSSSYYSPDGALCDVDAYGTVQLRPLHRLSNRDFAFYNPRLQGKNAYNYAALPPRPRASATGYFSSNDHNVVNMPPTADVKHTYTSWDLEDMEKYRMQSIRRESRARQKVKGPIMSQYDNMAPAVQDDLGGIYVIHLRSKSDPGKTGLLSVAEGKEGRHPAKAVSPEGDERFYRKHPESEFDRAHHHGGYGSQQVEKPSLPQKQSSLRNRKLHDMGCSLPEHRAHQEASHRQLCESKNGPPYPQGAGQLDYGSKGMPDASEPNSYHNSGKYVTSGQESLRLNHKEVRLSKDVDRPRARQPPAPEKHSRDCYKEEEHFTQSVVPPPKPERSHSLKLHHTQNLERDPSMLYPYQTHSKRQSSVTVVSQYDNLEDYHSLPQHQRGGFGGGGMGAYVPSGFVHPQSRTYATALGQGAFLPTELSLPHPDTQIHAE
Protein: Inactive lipoate--protein ligase 2 (Q8I2S0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: In the mitochondrion and together with LipL1, involved in the lipoylation of the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha -ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction. Although its role is unclear, it may catalyze the transfer of lipoyl groups from lipoyl-AMP to BCDH and KDH or act as an effector protein.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18069893}. Plastid, apicoplast {ECO:0000269|PubMed:18069893}. Note=Predominantly localizes to the mitochondrion. {ECO:0000269|PubMed:18069893}.
Interaction partners:
- Lipoyl synthase, apicoplast
- Lipoate--protein ligase 1
- Nodulation protein E
- Enoyl-acyl carrier reductase
- Glycine cleavage system H protein
- Lipoate-protein ligase B
Sequence:
MRIIKCLDQIFRPVLPNVNINNIQKNKKINILYFIDVSKFHVFEQLLLEESLFRISNNTTEGLNNIGFVIVNNTCEEMNESKGNECIFNNKKCVILGISNKIKDHIKDTNYIKENKISLIKRFTGGGTIYINKNSLLVSLILPHKFEKNKKIYPSNITEWSYNYFYNTSKQIYDKTQINNEKNSLNKNHILFNQYFNYYENDYVYKDYDEHNKNIILKKVGGNAQSFARNYFVHHTSYIWTCDYKEMNNILLNPSKQPIYRNKRKHQHFLQSIKLCLHDDIHTPNIFIEKLIKHIKHIINYKNITDQHDYWFFNKINLKNINDHILRNSEHFDDIYVADMNLLQCIFNYYNNSSLFNNMRSTYFLDLEGKKVSDRYYDIPTYFL
Protein: U2 snRNP associated SURP domain containing (H7C4V2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XIEEKETEDVPDDLDGAPIEEELDGAPLEDVDGIPIDATPIDDLDGVPIKSLDDDLDGVPLDATEDSKKNEPIFKVAPSKWEAVDESELEAQAVTTSKWELFDQHEESEEEENQNQEEESEDEEDTQSSKSEEHHLYSNPIKEEMTESKFSKYSEMSEEKRAKLREIELKVMKFQDELESGKRPKKPGQSFQEQVEHYRDKLLQREKEKELERERERDKKDKEKLESRSKDKKEKDECTPTRKERSPSGSRTPKRSRRSRSRSPKKSGKKSRSQSRSPHRSHKKSKKNKH
Protein: Probable fatty oxidation protein FadB (O53872)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative acyltransferase Rv0859
- Probable acetyl-CoA acyltransferase FadA2
- Probable acetyl-CoA acetyltransferase
- Steroid 3-ketoacyl-CoA thiolase FadA6
- Conserved protein
- Probable lipid carrier protein or keto acyl-CoA thiolase Ltp3
- propanoyl-CoA C-acyltransferase
- Probable beta-ketoacyl CoA thiolase FadA3
- Steroid 3-ketoacyl-CoA thiolase
- Possible lipid carrier protein or keto acyl-CoA thiolase
Sequence:
MPDNTIQWDKDADGIVTLTMDDPSGSTNVMNEAYIESMGKAVDRLVAEKDSITGVVVASAKKTFFAGGDVKTMIQARPEDAGDVFNTVETIKRQLRTLETLGKPVVAAINGAALGGGLEIALACHHRIAADVKGSQLGLPEVTLGLLPGGGGVTRTVRMFGIQNAFVSVLAQGTRFKPAKAKEIGLVDELVATVEELVPAAKAWIKEELKANPDGAGVQPWDKKGYKMPGGTPSSPGLAAILPSFPSNLRKQLKGAPMPAPRAILAAAVEGAQVDFDTASRIESRYFASLVTGQVAKNMMQAFFFDLQAINAGGSRPEGIGKTPIKRIGVLGAGMMGAGIAYVSAKAGYEVVLKDVSLEAAAKGKGYSEKLEAKALERGRTTQERSDALLARITPTADAADFKGVDFVIEAVFENQELKHKVFGEIEDIVEPNAILGSNTSTLPITGLATGVKRQEDFIGIHFFSPVDKMPLVEIIKGEKTSDEALARVFDYTLAIGKTPIVVNDSRGFFTSRVIGTFVNEALAMLGEGVEPASIEQAGSQAGYPAPPLQLSDELNLELMHKIAVATRKGVEDAGGTYQPHPAEAVVEKMIELGRSGRLKGAGFYEYADGKRSGLWPGLRETFKSGSSQPPLQDMIDRMLFAEALETQKCLDEGVLTSTADANIGSIMGIGFPPWTGGSAQFIVGYSGPAGTGKAAFVARARELAAAYGDRFLPPESLLS
Protein: Scinderin (SC) (Adseverin) (Q28046)
Organism: Bos taurus (Bovine)
Function: Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+). Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2). Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles (By similarity). Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts (By similarity). Regulates chondrocyte proliferation and differentiation (By similarity). Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, podosome {ECO:0000250|UniProtKB:Q60604}.
Interaction partners:
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
- Gelsolin
- Phosphatidylinositol-4-phosphate 5-kinase type 1 gamma
- PIP5K1A protein
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol-4-phosphate 5-kinase type 1 beta
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- 1-phosphatidylinositol-5-phosphate 4-kinase
Sequence:
MAQGLYHEEFARAGKRAGLQVWRIEKLELVPVPESAYGNFYVGDAYLVLHTTQASRGFTYRLHFWLGKECTQDESTAAAIFTVQMDDYLGGKPVQNRELQGYESTDFVGYFKGGLKYKAGGVASGLNHVLTNDLTAQRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKASQVAIGIRDNERKGRAQLIVVEEGSEPSELTKVLGEKPKLRDGEDDDDIKADITNRKMAKLYMVSDASGSMKVSLVAEENPFSMAMLLSEECFILDHGAAKQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSTNTQIQVLPEGGETPIFKQFFKDWRDRDQSDGFGKVYVTEKVAHVKQIPFDASKLHSSPQMAAQHHVVDDGSGKVQIWRVENNGRVEIDRNSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQGKEPAHLLSLFKDKPLIIYKNGTSKKEGQAPAPPIRLFQVRRNLASITRIMEVDVDANSLNSNDVFVLKLRQNNGYIWIGKGSTQEEEKGAEYVASVLKCKTSTIQEGKEPEEFWNSLGGKKDYQTSPLLESQAEDHPPRLYGCSNKTGRFIIEEVPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKSESLKSAKIYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSRW
Protein: Vinculin (P107B) (P19826)
Organism: Caenorhabditis elegans
Function: Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane. Involved in ovulation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P12003}. Cell membrane {ECO:0000269|PubMed:20385102, ECO:0000269|PubMed:28978740}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell junction {ECO:0000269|PubMed:20385102}. Cell junction, focal adhesion {ECO:0000269|PubMed:20385102}. Note=Cytoplasmic face of adhesion plaques (By similarity). In myoepithelial sheath cells, colocalizes in dense body-like structures with actin thin filaments and pat-3 (PubMed:17326220). In body wall muscles, localizes to integrin adhesion structures (M line and dense bodies) (PubMed:20385102). Requires unc-95 for the localization to nascent muscle attachments during embryogenesis (PubMed:20385102). Co-localizes with sorb-1 at dense bodies (PubMed:28978740). {ECO:0000250|UniProtKB:P12003, ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:20385102, ECO:0000269|PubMed:28978740}.
Interaction partners:
- Paxillin homolog 1
- FERM domain-containing protein
- Alpha-actinin, sarcomeric
- Actin
- Zyxin
- Integrin beta pat-3
- Integrin-linked protein kinase homolog pat-4
- Sorbin and SH3 domain-containing protein 1 homolog
- Paralyzed arrest at two-fold protein 6
- Alpha-catenin-like protein hmp-1
Sequence:
MPVFHTKTIENILEPVAQQLHYVLAMAEKNATSVDEVRHLGTSMPNLDRFASRSALALSRASSRRSIPEYITPDTVRHVVNDDDCPVCQLMMPRGKDGCVSRLVILHEEANDGNAMPDLTGPVGMVSRAVGNLIQVGYDTCDHSDDRILQQDMPPALQRVEGSSKLLEESSYSLKHDPYSVPARKKLIDGARGILQGTSALLLCFDESEVRKIIRVCRKANDYVAVSEVIESMADLQQFVKDISPVLHDVTNDVNLRQQELTHQVHREILIRCMDSIKVIAPILICSMKTSIELGTPHPRQGHAEAIANRNFMSQRMTEEMNEIIRVLQLTTYDEDEWDADNVTVMRKALSAAKSLLTAALDWLADPHARSGAVGEKAIRRICEYADRISARALPEDAQSIKRSIFEITSFTDELCNLRNNGQPDRENLAAQTARRLKDLVGSQNSSGLMGDALQNAQRHGGANPAHTAAGRLEQALRWLDNPGLDDGGLGLQALRLLTADARKLADRLNPQDRNRLLGLCSDIDRLAAQLADLERRGLGNSPEAHQIRNQLKNALRDLGDFMRRVLTDRVVDDFADITTPLKQFVEAVHADPYDPNREQNFVDKSQRLTDHSQSMTTTARLVASCGPSKSKKTVEAILDTAEKVEQLTPQLVNAGRVRLHNPGSEQHFENIHKQYADALHRLRSHVDDAIDTGEFVRASETAMRRYTNHCEGAINGADAHGLVNNSSQIARLGNRVLMTAQNEADNSEEPSFVSRVRNAADQLHNAIPPMVNNAKQIAQNPHDQYAAQNWRGTNDHLLNSVRAVGDAITGVPMSNGRHSSYQESISRASPYNPPPPSSQVIRSVNASPPTAPIIHNKMIIREDIPAPPRPPPPVELSPPPRPPPPPEYDEEEETRAFWERYPLPQASHQPMLAAAHNLHNELKQWSSQENDIVAAAKRMAILMARLSQLVRGEGGTKKDLINCSKAIADSSEEVTRLAVQLARLCTDIKMRTALLQVSERIPTIATQLKVLSTVKATMLGSANVIGPYGQPVEGSEEDDEAMQQLVHNAQNLMQSVKDVVRAAEAASIKIRTNSGLRLRWLRKPMWSNF
Protein: 4-hydroxyproline 2-epimerase (4Hyp 2-epimerase) (4HypE) (EC 5.1.1.8) (Q2T3J4)
Organism: Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)
Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C), albeit with 42-fold lower efficiency. Displays no proline racemase activity.
Interaction partners:
Sequence:
MKHLHIIDSHTGGEPTRVVVSGFPPLGDGPMAERLAALARDHDRYRTACILEPRGSDVLVGALLCEPVSAGAAAGVIFFNNAGYLGMCGHGTIGLVRTLHHMGRIAPGVHRIETPVGDVEATLHDDLSVSVRNVLAYRHAKDVVVEVPGHGSVTGDVAWGGNWFFLVSDHGQRIAGENVAALAAYASAVRAGLERAGVTGRDGAPIDHIELFADDPEHDSRSFVLCPGHAYDRSPCGTGTSAKLACLAADGKLAPGAAWRQASVIGSVFSASYERAESGVVPTIRGSAHLSAEATLLIEDDDPFGWGIVS
Protein: Liprin-alpha 1 (B8QI33)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MMCEVMPTISEAEGPPGGGGSHGSGSPSQPDADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGLLDGNHEQESAPSTNGKRSSDGSLSHEDLAKVLELQEVIDRQAREQSQMKERLASLSSHAAELEEDLDTARKDLIKSEEMNTKLQREVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKSGPLSSGSSAAKEAKLLELTSKLRKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVENAKKQLEETQHDKDQLVVTIEALKAELEQMRLRGPSLHHGRPHLGSVPDFRFSVADGHVDAYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDVDVSDGEDDRDTLLSSVDLLSPSGQADAQTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLAGSSPPGSGRSTPRRVPHSPAREVDRLGVMTLPSDLRKHRRQLPASREEVRDDKTTIKCETSPPSSPRPLRLDRMHKGAPHTVSHEDIRDLRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGPLGKESPGQVGVSETENSSQDALGLSKLGGQAEKNRKLQKKHELLEEARRQGLPFAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLTSPSAPPTSRTTTGNVWLTHEEMETLTATPQTQEDEEGSWAQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRLNYDRKELERKREESQNETRDVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLITGTDRRFDEDDDKSFRRAPSWRKKFRPKDIRGLASGSAETLPANFRVTSSMSSPSMQPKKVQMDGSVSGAQRLDSATVRTYSC