wanglab/gogpt-training-data huggingface dataset:
Protein: Malate dehydrogenase (EC 1.1.1.37) (V9HWF2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRREGMERKDLLKANVKIFKSQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKAQIALKLGVTANDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFVTTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKESAFEFLSSA
Protein: Ubiquitin-activating enzyme E1 1 (EC 6.2.1.45) (Poly(A)+ RNA transport protein 3) (O94609)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 15
- Polyubiquitin
- Ubiquitin-conjugating enzyme E2 4
- Ubiquitin-ribosomal protein eS31A fusion protein
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-ribosomal protein eS31B fusion protein
- Ubiquitin-ribosomal protein eL40B fusion protein
- Ubiquitin-ribosomal protein eL40A fusion protein
- Ubiquitin-conjugating enzyme E2 2
- Ubiquitin-conjugating enzyme E2 1
Sequence:
MSNNMNIDQTDQNTIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKSVTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVDELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIFCDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFTEVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKISFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPRNDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGGAVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQIAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTDMDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERVGPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLGTKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLFEGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSFEECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLSFDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKSGIKIQVNENEEAPETAANKDKQELKSIADSLPPPSSLVGFRLTPAEFEKDDDSNHHIDFITAASNLRAMNYDITPADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKNGFFNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQKEEGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPFRKHLVLEICCDDANGEDVEVPFICIKL
Protein: ATP synthase subunit delta, mitochondrial (F-ATPase delta subunit) (Q9P6R6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP synthase subunit J
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit alpha
- ATP synthase subunit d
- ATP synthase subunit a
- ATP synthase subunit gamma, mitochondrial
- Putative ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit 5, mitochondrial
Sequence:
MFRLSNYMLRKSQFPQGLVRAPFGIRGYAQAVQKNEKLVLSMALPYQTIYEKVPVTQVDIPAEDGEMGILKDHVPMIQCLKPGVISVTDESSNKSKYFISGGFAVQQPSNELSITVPEAYKLEDFSSSVANQLLEKHKAEMNSSDEGVAAEAAVRVSVLESLVRALK
Protein: Bestrophin-3 (Vitelliform macular dystrophy 2-like protein 3) (Q6H1V1)
Organism: Mus musculus (Mouse)
Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate (By similarity).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:18414923}. Note=Localized also in punctate structures in the cytosolic compartment. {ECO:0000269|PubMed:18414923}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:18414923}. Note=Localized also in punctate structures in the cytosolic compartment. {ECO:0000269|PubMed:18414923}.
Interaction partners:
Sequence:
MTVTYSSKVANATFFGFHRLLLKWRGSIYKLLYREFIVFAVLYTAISLVYRLLLTGAQKRYFEKLSIYCDRYAEQIPVTFVLGFYVTLVVNRWWNQFVNLPWPDRLMLLISSSVHGSDQHGRLLRRTLMRYVNLTSLLIFRSVSTAVYKRFPTMDHVVEAGFMTADERKLFDHLKSPHLKYWVPFIWFGNLATKARNEGRIRDSVDLQSLMTEMNRYRSWCSLLFGYDWVGIPLVYTQVVTLAVYTFFFACLIGRQFLDPTKGYVGHDLDLYVPIFTLLQFFFYAGWLKVAEQLINPFGEDDDDFETNWCIDRNLQVSLLAVDEMHMSLPKMKKDIYWDDSAARPPYTLAAADYCIPSFLGSTIQMGLSGSNFPAEDWLWNYEKHGNRHSVMRRVKRFLSTHEHPGSPRRRRSFGRQASDSSMFLPPSPARDLLDVPSRNPHRGSPTRKQSRSQEGSPKLHSSMGELSTIRETSRTSTLQSLSPQSSVRSSPTKMPQVPEVLITAAEAPAFSADSHQHDSTTSILSLEFTGVQPSGTEQQVEPSGTPPGDPNPQTTSASTERDLFKFEEDLEDDRFPKRWSLPEFLESRHTSLGNLGPDPVSPRDALLLPDTETPSETNGIHPGAGSALAPDILYLMESLDKETDILEFNNEHTGESPKGTPQRPRTWF
Protein: Type I HSP40 co-chaperone (A0A1D8PSQ3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Heat shock protein SSA2
- Chaperone ATPase
- Heat shock protein HSP70
- Hsp90 cochaperone
- Type II HSP40 co-chaperone
- Heat shock protein homolog SSE1
- Ssz1p
- Endoplasmic reticulum chaperone BIP
- Hsp70 chaperone Ssb
- Aha1p
Sequence:
MVKDTKFYDALGVSPNASDAELKKAYRKAALKYHPDKNPSPEAAEKFKELSHAYEILSDDQKREIYDQYGEEGLSGQGAGGFGMNADDIFAQFFGGGFHGGPQRPSRGKDIKHSIACSLEELYKGKTVKLALNKTVLCGECKGRGGAEGKVAQCPDCHGNGMKFVTKQMGPMIQRFQTVCDKCQGTGDLIDPKDRCKKCNGKKTESERKILEVHVKPGMKDGDHITFAGEGDQTPGVTPGDVVFIISQKPHPVFQRKGNDLLIEQEIELATALAGGEIAFKHISGDWVRIEIPAGEVIAPGSIKMVEGFGMPVRTHKGNLIIHFNVKFPENNFADEESLKKLASLLPKPKEVKIPADADVDDCTMVPAKLEQSNPYESDEEAHGGPGVQCASQ
Protein: Age-related maculopathy susceptibility protein 2 (P0C7Q2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16174643, ECO:0000269|PubMed:19255159}.
Interaction partners:
- Complement factor H
- Pleckstrin homology domain-containing family A member 1
- Hemicentin-1
- Complement factor B
- Serine protease HTRA1
- Complement C2
- Hepatic triacylglycerol lipase
Sequence:
MLRLYPGPMVTEAEGKGGPEMASLSSSVVPVSFISTLRESVLDPGVGGEGASDKQRSKLSLSHSMIPAAKIHTELCLPAFFSPAGTQRRFQQPQHHLTLSIIHTAAR
Protein: Transmembrane protein 71 (E5RJJ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYRISQLMSTPVASSSRLEREYAGELSPTCIFPSFTCDSLDGYHSFECGSIDPLTGSHYTCRRSPRLLTNGYYIWTEDSFLCDKDGNITLNPSQTSVMYKENLVRIFRKKKRICHSFSSLFNLSTSKSWLHGSIFGDINSSPSEDNWLKGTRRLDTDHCNGNADDLDCSSLTDDWESGKMNAESVITSSSSHIISQPPGGNSHSLSLQSQLTASERFQENSSDHSETRLLQEVFFQAILLAVCLIISACARWFMGEILASVFTCSLMITVACLSKFDNHLGMPSMNVLHLNIWKLSNLQSTWNQVFYWKGVSE
Protein: Erythroferrone (Complement C1q tumor necrosis factor-related protein 15) (Myonectin) (Q6PGN1)
Organism: Mus musculus (Mouse)
Function: Iron-regulatory hormone that acts as an erythroid regulator after hemorrhage: produced by erythroblasts following blood loss and mediates suppression of hepcidin (HAMP) expression in the liver, thereby promoting increased iron absorption and mobilization from stores. Promotes lipid uptake into adipocytes and hepatocytes via transcriptional up-regulation of genes involved in fatty acid uptake.
Subcellular location: Secreted {ECO:0000269|PubMed:22351773, ECO:0000269|PubMed:24880340, ECO:0000269|PubMed:32602701, ECO:0000269|PubMed:34002695}. Note=Secreted when glycosylated at Asn-229 and Asn-281 (PubMed:32602701). Hydroxylation promotes secretion (PubMed:32602701). {ECO:0000269|PubMed:32602701}.
Interaction partners:
- Hepcidin
- Hepcidin-2
- Transmembrane protease serine 6
- Transferrin receptor protein 2
- Erythropoietin
- Hemojuvelin
Sequence:
MASTRRPVGARTLLACASLLAAMGLGVPESAEPVGTHARPQPPGAELPAPPANSPPEPTIAHAHSVDPRDAWMLFVKQSDKGINSKRRSKARRLKLGLPGPPGPPGPQGPPGPFIPSEVLLKEFQLLLKGAVRQRESHLEHCTRDLTTPASGSPSRVPAAQELDSQDPGALLALLAATLAQGPRAPRVEAAFHCRLRRDVQVDRRALHELGIYYLPEVEGAFHRGPGLNLTSGQYTAPVAGFYALAATLHVALTEQPRKGPTRPRDRLRLLICIQSLCQHNASLETVMGLENSSELFTISVNGVLYLQAGHYTSVFLDNASGSSLTVRSGSHFSAILLGL
Protein: U3 small nucleolar RNA-associated protein 8 (U3 snoRNA-associated protein 8) (U three protein 8) (U3 protein 8 required for transcription) (t-UTP8) (P53276)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA. Also has a role in nuclear tRNA export. It acts between the steps of tRNA maturation/aminoacylation and its subsequent translocation out of the nucleus. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:12794079, ECO:0000269|PubMed:15489292}. Note=Associated with ribosomal chromatin, even in the absence of transcription.
Interaction partners:
- U3 small nucleolar RNA-associated protein 20
- U3 small nucleolar RNA-associated protein 6
- Essential nuclear protein 1
- Nucleolar protein 58
- Periodic tryptophan protein 2
- RNA cytidine acetyltransferase
- U3 small nucleolar RNA-associated protein 13
- U3 small nucleolar RNA-associated protein 18
- Nucleolar complex protein 14
- U3 small nucleolar RNA-associated protein 5
Sequence:
MPSLSQPFRLATLPKIASLSNFSLQADYVQVADGTFNESTNNITLGISGSSISQYIINPTPKLTFDYPIPSTNIITACNAEKGQANIDGNIEASTDDEANNEKTINTQKKRNVEIWAFGLMVNKGNYTLNVITKALEDTTDTSNDHLSESDIDNKAYTGSDEFLSQYKIKAKAKVMSIKIDTKNSLVIAILQNGLIEIFDFKLTLLHSFDISYDNLKYAKWFTENGTEYVFVLCPLQDDKVCYKLLELTDCGSGESSPIKELSSTIIEGFSFENSKLCYQFGKLYKLNQGKIYIYSLPHCQLQQVIEFPMVDKLSPGDDLISFQPVSVNRVLLTVNNVIYLLDLLHCSTLSQRELTHVKTFQLLKSAVINSEKSHNSKTIAIGISTKNGPNPTSSLEIINIDVGTNTLKDSLGKSFQVGNNDSSVILKPLFDDKDINDKRVKCNDVSGDSSVPVLHCNEVIEKLSALQDNDITSFDDIFFKELKIKEEHYTEKDRYISDPGFLNKVLDLIFGKFSGNDYPKTLTFLLTHPLFPLSRTRNLLSLLRDQPRLFKQAIVTCPNLPLNELLEELFSIRNRELLLDISFRILQDFTRDSIKQEMKKLSKLDVQNFIEFITSGGEDSSPECFNPSQSTQLFQLLSLVLDSIGLFSLEGALLENLTLYIDKQVEIAERNTELWNLIDTKGFQHGFASSTFDNGTSQKRALPTYTMEYLDI
Protein: RNA pseudouridylate synthase domain-containing protein 1 (Ribosomal large subunit pseudouridine synthase C-like protein) (Q9UJJ7)
Organism: Homo sapiens (Human)
Interaction partners:
- tRNA pseudouridine synthase-like 1
- Pseudouridylate synthase PUS7L
- Pseudouridylate synthase 7 homolog
- Mitochondrial mRNA pseudouridine synthase RPUSD3
- tRNA pseudouridine
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- Pseudouridylate synthase 1 homolog
- tRNA pseudouridine synthase Pus10
- Mitochondrial assembly of ribosomal large subunit protein 1
- Pseudouridylate synthase TRUB2, mitochondrial
Sequence:
MEPGSVENLSIVYRSRDFLVVNKHWDVRIDSKAWRETLTLQKQLRYRFPELADPDTCYGFRFCHQLDFSTSGALCVALNKAAAGSAYRCFKERRVTKAYLALLRGHIQESRVTISHAIGRNSTEGRAHTMCIEGSQGCENPKPSLTDLVVLEHGLYAGDPVSKVLLKPLTGRTHQLRVHCSALGHPVVGDLTYGEVSGREDRPFRMMLHAFYLRIPTDTECVEVCTPDPFLPSLDACWSPHTLLQSLDQLVQALRATPDPDPEDRGPRPGSPSALLPGPGRPPPPPTKPPETEAQRGPCLQWLSEWTLEPDS
Protein: Gastric triacylglycerol lipase (GL) (Gastric lipase) (EC 3.1.1.3) (P80035)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol. Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:1568562}.
Interaction partners:
- Triacylglycerol lipase
- PLAT domain-containing protein.
- Lipase G, endothelial type.
- Carboxyl ester lipase
- Lipoprotein lipase
- Monoglyceride lipase.
- Patatin like phospholipase domain containing 3.
- Diacylglycerol O-acyltransferase 1
- Monoacylglycerol O-acyltransferase 1.
- Patatin like phospholipase domain containing 2.
Sequence:
MWLLLTAASVISTLGTTHGLFGKLHPTNPEVTMNISQMITYWGYPAEEYEVVTEDGYILGIDRIPYGRKNSENIGRRPVAFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFILKKTGQDKLHYVGHSQGTTIGFIAFSTNPKLAKRIKTFYALAPVATVKYTETLLNKLMLVPSFLFKLIFGNKIFYPHHFFDQFLATEVCSRETVDLLCSNALFIICGFDTMNLNMSRLDVYLSHNPAGTSVQNVLHWSQAVKSGKFQAFDWGSPVQNMMHYHQSMPPYYNLTDMHVPIAVWNGGNDLLADPHDVDLLLSKLPNLIYHRKIPPYNHLDFIWAMDAPQAVYNEIVSMMGTDNK
Protein: T-complex protein 1 subunit zeta-2 (TCP-1-zeta-2) (CCT-zeta-2) (Cctz-2) (Q61390)
Organism: Mus musculus (Mouse)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q92526}.
Interaction partners:
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma
- Chaperonin containing TCP1 subunit 8-like 1
- T-complex protein 1 subunit zeta
- Molecular chaperone MKKS
Sequence:
MAAIKIANPGAEVTRSQAALAVNICAARGLQDVLRPTLGPKGALKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASIIAKVAAAQDHVTGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFDVAKTKALEVLDEIKVQKEMKREILLDVARTSLQTKVHAELADILTEAVVDSVLAIRRPGVPIDLFMVEIVEMRHKSETDTQLIRGLVLDHGARHPRMRKQVRDAYILTCNVSLEYEKTEVSSGFFYKTVEEKEKLVKAERKFIEDRVQKIIDLKQKVCAESNKGFVVINQKGIDPVSLEMLAKHNIVALRRAKRRNLERLTLACGGLAVNSFEGLSEECLGHAGLVFEYALGEEKFTFIEDCVNPLSVTLLVKGPNKHTLIQIKDALRDGLRAVKNAIEDGCVVPGAGAVEVAIAEALVNYKHRVQGRVRLGIQAFADALLIIPKVLAQNSGYDLQETLIKIQTKHAESKELLGIDLNTGEPMAAAEAGIWDNYCVKKHLLHSCTVIATNILLVDEIMRAGMSSLRD
Protein: Putative holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4'-phosphopantetheinyl transferase) (G2TRL9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Interaction partners:
- Uncharacterized protein C14G10.01
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15
Sequence:
MGLGIDILKISRISRLIQRSPEWEKNFLKKCLCENEIKKYNLIKSNSSLPRLSEQAKWLAVRWCVKEAVFKALQPNFRVYMSMMEYVRTPTGYPSVVIHDPRFPLSPVMVSVSHEEDLVVANALYLPSMPKT
Protein: Signal recognition particle subunit SRP54 (EC 3.6.5.4) (Signal recognition particle 54 kDa protein) (P61010)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (By similarity). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (By similarity). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (By similarity). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (By similarity). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (By similarity). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA. Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:P61011}. Cytoplasm {ECO:0000250|UniProtKB:P61011}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61011}.
Interaction partners:
- Signal recognition particle subunit SRP72
- Signal recognition particle receptor subunit alpha
- Signal recognition particle 19 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle 9 kDa protein
- Signal recognition particle 14 kDa protein
- Large ribosomal subunit protein uL14
- Ribosomal protein L5.
- Ribosomal protein L35.
- 40S ribosomal protein S30
Sequence:
MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQELDSTDGAKVFSKQPGRIQRVARGSGVSTRDVQELLTQYTKFAQMVKKMGGIKGLFKGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM
Protein: FOS like 1, AP-1 transcription factor subunit (E9PKL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFRDFGEPGPSSGNGGGYGGPAQPPAAAQAAQQKFHLVPSINTMSGSQELQWMVQPHFLGPSSYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQPGGRGAPPSKARAEQAGCGQVQEPEEGTDRLPAGGD
Protein: Golgi-associated kinase 1B (Expressed in nerve and epithelium during development) (Protein FAM198B) (Q6UWH4)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:11256614}; Single-pass type II membrane protein {ECO:0000305|PubMed:11256614}.
Interaction partners:
Sequence:
MTCPDKPGQLINWFICSLCVPRVRKLWSSRRPRTRRNLLLGTACAIYLGFLVSQVGRASLQHGQAAEKGPHRSRDTAEPSFPEIPLDGTLAPPESQGNGSTLQPNVVYITLRSKRSKPANIRGTVKPKRRKKHAVASAAPGQEALVGPSLQPQEAAREADAVAPGYAQGANLVKIGERPWRLVRGPGVRAGGPDFLQPSSRESNIRIYSESAPSWLSKDDIRRMRLLADSAVAGLRPVSSRSGARLLVLEGGAPGAVLRCGPSPCGLLKQPLDMSEVFAFHLDRILGLNRTLPSVSRKAEFIQDGRPCPIILWDASLSSASNDTHSSVKLTWGTYQQLLKQKCWQNGRVPKPESGCTEIHHHEWSKMALFDFLLQIYNRLDTNCCGFRPRKEDACVQNGLRPKCDDQGSAALAHIIQRKHDPRHLVFIDNKGFFDRSEDNLNFKLLEGIKEFPASAVSVLKSQHLRQKLLQSLFLDKVYWESQGGRQGIEKLIDVIEHRAKILITYINAHGVKVLPMNE
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q586M4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MDKAFLISLPLLTMTAAETNPNCSIQDHNNVYIGELVKKLKTAASLPDVNVKKSKKLKIAALLTTDRKKAAFLQALSDLHLSCKRGDDDRALQTLIGLASKAAALAHMAGTSAALTKLATLKKKTDTNAFTTGTNSAQRKRIAVDGAKTGINTGKCTIHSYINAEAPAGADKALSNWQHSLKVVKPDTTAATQGATQAMVCETTNGQCSSSSSGNTAGISSGTLYKTDPAAKQQTGKVKPSATTKEWVFHSDKIAHQAAQLDTELSDALTTYATTTDSCEPYNKLDNNNFILRVYKIAKGDDTATEIPQAERNNIKNIVESSYGKDPTTYEETIWKGVKATPLTKSNSGRPSDTKLDSITTLNDLQQIEAFIEASAAIKQNERSSASTSECKAQIETASACKGKEKKNCNSNCEWEGTEDKGTCKPKNEEEGVKVENDGKTNTNTTGGNSFVINKAPLLLAFLHMGQKLCQTFFLR
Protein: LP08350p (Q8MST7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSEQEFEVKFRQWLDQEGIAREMHSHLRVELIHCFNNTALGQLLSKAAGVQMAQSHALLVSPLAMVLHTLVAEFLHSQNCHFTLSVFCSETPHRSNLPDFRSRPEFRFQTEELQKVVAAILGEKEALADSEFGKLAEAHYEEDLAGQTQCLLMALMRTLVEIRRSVPKQEVEQPVPVSLQDTGCQTEPSACVEARPEVDTTGLYQTEEHELILGADGRSVFVGGRVSQSLHSVEQQLNQLIKNLRHLAKSCAPPVEVISSTKFEDLLMKELRERERLLKAGQAFNPGEPVIKIATGDKEEEHEVTSGRNQKDVVHSNLGPIQVPALDVTIPQLPRLHSEQLASLAVIRQSLEKVQKKSRQPQGRMYVSMERMETLMGDVCGCVQLLSNVLNLSMEQEHSVGMHKGFKWGYREGFAHGHFMGLQEGQKLEQLEQKKWQKERPLPEKRESSVQTESTIPTASIATQTSRKSAHNESVITQTEQKQLKDAGNQASCEPPTFQKSYEQWIHEMLHSSSGQVFLERVELSLNKALELQKVRLNELFQVKLRHQAEMLRLSKRQNSWRTLCKRVERDSQSSAEARDLVQQIFRLLEHYEAHHQQLAEKIQQTELAAEQAARIMPMWADGAAVGSASVNWNTAMSTTLISSGICTPPPAQPAADGALNVGKTHVEQHTYPDLGYPYQLLALAPPGGVPVAGTFVPVTHLPAHLLGASEHPVPLVPVARIYSDPMKTSRRLLSPSSVPADNDSAHRAAGETNAFTFQGGPVSGDLHPTENRNQAPATQGQQFPVPLPVPAPRGPSPSVQSVLPSTASPALPPPDETVPQPGPSQSSIPLKPSMHSVATNTITPVPPKATPLKPVNSKVSEGPSFEEALLSAKSRMLQLEQESDLLEQSFLSYLEKTKSKTSPHKSSEDAARARRIRSSCLREREQVHRTMDGFRDWHRRVRKEDAASVAQLEELRNQRLIPDPILDSKGSSPLWLSELEEGHEQDSYPFTNAITEARNKVLDKIMPVRKEEKKEKQNVKKNWLADLPFQIPEASPKQDRHLTNVKPAVTRSSSNGEMNVLLQRAKDALGLRTPNPLLDSSSSSSSMELPSMGAGRSPSTKFQQSMARMQMLFGGAEAVKPTMPAKTGRPVSAPTAASEPGLCAHLVLPKRPHTAPTLHTINENEPAVHHLDVSTSSSSQSTLPGRSSGEAFEDLVMSAVADGARRRNAESSTEVSYSQAFWKRINL
Protein: Caveolin-1 (P41350)
Organism: Rattus norvegicus (Rat)
Function: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:16358225}; Peripheral membrane protein {ECO:0000269|PubMed:16358225}. Membrane, caveola {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae.
Interaction partners:
- Caveolin-2
- Proto-oncogene tyrosine-protein kinase Src
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Dynamin-2
- Tyrosine-protein kinase Fyn
- Integrin beta-1
- Estrogen receptor
- Nitric oxide synthase 3
- Calmodulin-1
Sequence:
MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADEVNEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSTIFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQEEI
Protein: Histidine-rich calcium-binding protein (Q9WVE4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGFQGPWLHTCLLWATVAILLVPPVVTQELRGAGVGLGNWNNNAGIPGSSEDLSTEFGHHIHRGYQGEKDRGHREEGEEFSREYGHRVQDHRYPGREVGEENVSEEVFRGHVRQLHGHGEHDNEDLGDSAENHLPRQRSHSHEEEDGIVSSEYHGHVPRHAHHGHGEEDDDDDGGEEEERVDVMEDSDDNEHQVHGHQSHSKERDELHHAHSHRHQGHSDDDDDDGVSTEHGHQAHRYQDHEEENDGDSDEDSHTHRVQGREDENDDEDGDSGEYRHHTQDHQGHNEEQDDDDDDDDDDEDKEDSTEHRHQTQGHRKEEDEDESDEDDHHVSRHGRQGYEEEEDDDDDDGDDDSTEHVHQAHRHRDHEHKDDEDDSEEDYHHVPSHGRQSHQNEEEEDEAVSTEHWHQSPRHARHDLGRESEEEVAVKYSHHVASHRPQGHNADREEDSLEEHMNEVPGHHHHRASRGDDEDISTEFGHKAPSHRLQDQDERARQGHREPVQGEIAHQPLQPTGPSSRESRKEGDHSSQEGDEDPEQRQAHSEEEKEEEEEEEEEQEEEKEGGHSLPMSQEDDEEEEKDEKESKVDRAAVSAPLSHHRKQGEEEEEEEEEEEEEILEENLLPFTIIPNPLAGREVAREGSSEEESREVTGQQDAQEYENYQPGSLCGYCSFCNRCTECESCHCDEENMGEHCDQCQHCQFCYLCPLVCDTLCTPGSYVDYFSSSLYQALADMLETPEP
Protein: Benzoate-para-hydroxylase (C8VBT1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MITDFLTPENITPERIALALLGLLAAYYVVPYLQTWRLSDIPAPGLAAWTNFWLLLQTRLGHRFISVDNAHKKYGKLVRIAPRHISIADDAAIQAVYGHGNGFLKSDFYDAFVSIRRGLFNTRDRAEHTRKRKTVSHTFSAKSIGQFEQYIHHNIENLVKQLTRISNLQRNPKNGYATVDALNWFNFVAFDIIGDLAFGAPFGMLDKGQDIAEMRKSPDSPPQYVQAVEVLNRRGEVSATLGCYPALKPFAKYLPDRFFRDGLEAVENLAGIAIACVNERLKPEVMANNTRVDLLARLMEGKDANGNKLGRAELTAEALTQLIAGSDTTSNTSCAILYYCLRTPGVIDKLHKVLDEAIPQDVEVPTHAMVKEIPYLQWVIWETMRIHSTSAMGLPREIPEGNPPVEISGHIFKPGDILSVPTYTIHHSKEIWGADADEFIPERWAPERLTARQKAAFIPFSTGPRACVGRNVAEMELLVICSTVFRMFDWELQQKGPMETREGFLRKPLGLTVGVKRRTIV