wanglab/gogpt-training-data huggingface dataset:
Protein: Follistatin-related protein 3 (Follistatin-like protein 3) (Follistatin-related gene protein) (Q9EQC7)
Organism: Mus musculus (Mouse)
Function: The secreted form is a binding and antagonizing protein for members of the TGF-beta family, such us activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiation. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. The nuclear form is probably involved in transcriptional regulation via interaction with MLLT10 (By similarity).
Subcellular location: Secreted {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Growth/differentiation factor 8
- Inhibin beta A chain
- Growth/differentiation factor 11
- Inhibin beta B chain
Sequence:
MRSGALWPLLWGALVWTVGSVGAVMGSEDSVPGGVCWLQQGREATCSLVLKTRVSREECCASGNINTAWSNFTHPGNKISLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPHCECVPNCEGLPAGFQVCGSDGATYRDECELRTARCRGHPDLRVMYRGRCQKSCAQVVCPRPQSCLVDQTGSAHCVVCRAAPCPVPSNPGQELCGNNNVTYISSCHLRQATCFLGRSIGVRHPGICTGGPKVPAEEEENFV
Protein: Uncharacterized protein C6orf15 homolog (Extracellular matrix protein with prion homology) (Emprin) (Protein STG) (Q8BM15)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}.
Interaction partners:
- RNA polymerase-associated protein LEO1
- DNA-directed RNA polymerase II subunit RPB2
- FACT complex subunit SPT16
- Transcription elongation factor SPT6
- DNA-directed RNA polymerase II subunit RPB4
- Transcription elongation factor SPT4-A
- RNA polymerase-associated protein RTF1 homolog
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MQSHAGGSRAPLGLLLICLCLPGLFARSTGAPEEKASPHSGQPSFTSLLNPGQPQPKPDPVNNELLGVLPRLSESPQDGALPEGGSEVPNGPPFWGPPPMESWPSEDPQQGMAAVAEDQLEQMLPEALPYLSRGGRLPEASSARLRQPSLAASYPQDSEAGLQPGSSSLETEAEAFARSPFWFLIHKLLPGSSGRILRPGTSWGSGGAGTGWGTRPMPYPSGIWGSNGLVSGTSLGGRGPYPVRIWGRNGWYPLRILGGNGRYPPVGTWGGYGQYPPVGTWGGYGQYPPVGPWGGYGQYPPVGTWGANCQYPAGSRRPNCRYPAGSWGTKGQNRLPPGAKRPGSSGITP
Protein: Amyloid-beta A4 protein (O35463)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU367156}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU367156}. Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}.
Interaction partners:
Sequence:
TRPGSGLTNIKTEEISEVKMDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTS
Protein: Putative exonuclease GOR (EC 3.1.-.-) (Antigen GOR homolog) (RNA exonuclease 1 homolog-like 1) (Q8IX06)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11472404}. Nucleus {ECO:0000305|PubMed:11472404}.
Interaction partners:
Sequence:
MLRATAPCWFPPGYPEAKKVAEEAALEASRHLGGEQSQAGAPEGSKMLRATAPCWFRPGYPEAKKVAKEAAPEASRHLGAEQSPAGAPEGSKMLRATAPCWFPPGYPEAKKVAEEAALEAPEFPLPSHQPAQSFGLWVPQMHKQASAFVDIQAEPQNRGPAVPPAWPKMVTESCYFPAQRGSACRLPAAPRLTERPSGVRISAPRKRKTIAHSSSPCLVTGYTDAKRTRVASSSQRSRGSKVGRQPGKTRNRSGMACKTTATTSSKRIVRRASLPSLSLKKPIILRSSGCQVPTVLRRGYLQLFTEECLKFCASKQEAEEKALNEEKVAYDCSPNKNRYLNVVLNTLKRLKGLTPSSMPGLSRAALYSRLQEFLLTQDQLKENGYPFPHPERPGGAVLFTGQGKGPGDSSCRVCCRCGTEYLVSSSGRCVRDQLCYYHWGRVRSSQVAGGRVSQYTCCAAAPGSVGCQVAKQHVRDGRKESLDGFVETFKKELSRDAYPGIYALDCEMCYTTHGLELTRVTVVDADMRVVYDTFVKPDNEIVDYNTRFSGVTEADVAKTSITLPQVQAILLSFFSAQTILIGHSLESDLLALKLIHSTVVDTAVLFPHYLGFPYKRSLRNLAADYLAQIIQDSQDGHNSSEDASACLQLVMWKVRQRAQIQPRHRSASPAALACP
Protein: High mobility group B protein 1 (High mobility group protein A) (AtHMGalpha) (HMG alpha) (Nucleosome/chromatin assembly factor group D 01) (Nucleosome/chromatin assembly factor group D 1) (O49595)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds preferentially double-stranded DNA. Modulates general plant growth and stress tolerance. Confers sensitivity to salt and genotoxic (methyl methanesulfonate, MMS) stresses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:17114349, ECO:0000269|PubMed:18822296}. Note=Displays a highly dynamic speckle distribution pattern in interphase chromatin but does not associate with mitotic chromosomes.
Interaction partners:
- High mobility group B protein 12
- Putative high mobility group B protein 11
- Pentatricopeptide repeat-containing protein At3g26630
- WD repeat-containing protein LWD2
- General transcription factor IIH subunit 2
- Transcription initiation factor TFIID subunit
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH8
- Actin-related protein 9
- RuvB-like protein 1
Sequence:
MKTAKGKDKVKTTKEALKPVDDRKVGKRKAPAEKPTKRETRKEKKAKKDPNKPKRAPSAFFVFLEDFRVTFKKENPNVKAVSAVGKAGGQKWKSMSQAEKAPYEEKAAKRKAEYEKQMDAYNKNLEEGSDESEKSRSEINDEDEASGEEELLEKEAAGDDEEEEEEEDDDDDDDEEED
Protein: Effector protein SifA (SPI-2 type III secretion system effector SifA) (Secreted effector protein) (A0A0D6GID3)
Organism: Salmonella typhimurium
Interaction partners:
Sequence:
MPITIGNGFLKSEILTNSPRNTKEAWWKVLWEKIKDFFFSTGKAKADRCLHEMLFAERAPTRERLTEIFFELKELACASQRDRFQVHNPHENDATIILRIMDQNEENELLRITQNTDTFSCEVMGNLYFLMKDRPDILKSHPQMTAMIKRRYSEIVDYPLPSTLCLNPAGAPILSVPLDNIEGYLYTELRKGHLDGWKAQEKATYLAAKIQSGIEKTTRILHHANISESTQQNAFLETMAMCGLKQLEIPPPHTHIPIEKMVKEVLLADKTFQAFLVTDPSTSQSMLAEIVEAISDQVFHAIFRIDPQAIQKMAEEQLTTLHVRSEQQSGCLCCFL
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial (Pyruvate dehydrogenase kinase) (EC 2.7.11.2) (Q9P6P9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Probable pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Sequence:
MSVLGKTLQEKVNLLAQYPQTGLSLKQLVYFGKNPTPGTLFRAGLFLRDELPIRLARRIQDLQNLSPMLRSMKRISSVKAAYGRSMEEIIELKGVELPKCLPKHARYHNAPKWRSSLMDSEILHNPSLANTHLDSSKGRYFETDFSDQDNGVDCNWPESLLKFNSNFAYLLNTIRTRHDNVAVEIALDIQEYRRKTNQIDNSIQIFLDRFYMSRIGIRMLLGQYIALVSEPPRENYVGVISTRANIYQIIEGAAENAKYICRLAYGLFEAPEIQIICDPSLEMMYVESHLNHAVFEILKNSLRATVEFHGVDSDFFPPIKVIVAKGQEDITIKISDEGGGISRRNIPLVWSYMFTTASPTLTDDPHDIVSANSTTPMAGFGFGLPLARLYTRYFGGDLELISMEGYGTDVYIHLNRLCESAEPLQ
Protein: T17B22.17 protein (Tudor/PWWP/MBT superfamily protein) (Q9M9N3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASPGSGAVDWTVGSIVWVRRRNGSWWPGRILGQEDLDSTHITSPRSGTPVKLLGREDASVDWYNLEKSKRVKPFRCGDFDECIERVESSQAMIIKKREKYARREDAILHALELEKEMLKREGKLVPEKARDDSLDATKERMAIVRVQDTSNGTRESTDYLRTNHVGDVMHLLRDKEEDQPSCEDEAVPRMRGLQDFGLRTASSKRKISCSNGPDTSFKYLARSNSSASSSGDHSMERPIYTLGKEKTKSRAEAKRTKYMFTPSESNDVSDLHENLLSHRDAMHSSFAGGDTRYSDYDPPNFLEDMESDYSESETDSSDMEEDTDDDIPLLSGAGRHSERRNTFSRHTSGEDESTSSEEDHYESSISGDSSYLYSQNPNNEASTVSNWQHKGKRNFRTLPRRSARKRKLHRNRLEDGRYCEYKRRAFGQKPMGYGLDFNGINDMSDGTDDTDPNERQFGDRMIVPGDDYQLSNVVASRCKNIYSHDMLDWDDDPWEGRIGMKKRGEEKLEGLGQEFDVSERHFGRKTYSSLMDVDLEVRGSYQKGPVPIVSLMSKLNGRAIIGHPVEVEVLADGSSESYIQTIDYFGNETTYQDKTFLLPSAWKTARRSNSRVPRLQPFSSSVEADDDATYDYSLADQGRKPLVKKLGLGHFSNDDNSVRRNSSLRIPRPPAERKQQHQQQQKKLLKNTNATASQKTRALSSFSGEQGHNGMKASRDRTHELSNRRVLPGPPTVACIPVKLVYSRLLEKINRPPSKPTAKAFNERRRVQ
Protein: Secreted aspartic protease 4 (ACP 4) (Aspartate protease 4) (EC 3.4.23.24) (Candidapepsin-4) (Q5A8N2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Activates host systemic immunity. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0CY27}.
Interaction partners:
- Hyphal wall protein 1
- Agglutinin-like protein 3
- Secreted aspartic protease 5
- Hyphally regulated cell wall protein 1
Sequence:
MFLQNILSVLAFALLIDAAPVKRSTGFVTLDFNVKRSLVDPKDPTVEVKRSPLFLDIEPTEIPVDDTGRNDVGKRGPVAVKLDNEIITYSADITIGSNNQKLSVIVDTGSSDLWVPDSNAVCIPKWPGDRGDFCKNNGSYSPAASSTSKNLNTPFEIKYADGSVAQGNLYQDTVGIGGVSVRDQLFANVRSTSAHKGILGIGFQSNEATRTPYDNLPITLKKQGIISKNAYSLFLNSPEASSGQIIFGGIDKAKYSGSLVDLPITSDRTLSVGLRSVNVMGQNVNVNAGVLLDSGTTISYFTPNIARSIIYALGGQVHYDSSGNEAYVADCKTSGTVDFQFDRNLKISVPASEFLYQLYYTNGEPYPKCEIRVRESEDNILGDNFMRSAYIVYDLDDRKISMAQVKYTSQSNIVAIN
Protein: CDC48-associated ubiquitin-like/zinc finger protein 1 (CDC48-associated UBL/Zn-finger protein 1) (P53899)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Promotes efficient arsenite-induced clearance of stress granules (SGs). May have a role in the ubiquitin-proteasome system (UPS) protecting cells from metalloid-induced proteotoxicity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cell division control protein 48
- AN1-type zinc finger protein TMC1
- Nuclear protein localization protein 4
- UBX domain-containing protein 1
- 26S proteasome regulatory subunit RPN8
- 26S proteasome regulatory subunit RPN2
- 13 kDa ribonucleoprotein-associated protein
Sequence:
MSAAIEKETGMLDVGKHCAYCRQLDFLPFHCSFCNEDFCSNHRLKEDHHCRWLLEHEEVHKTEKSPSKSRDGSSSNDEAYFKSLLPERASVRIQRVSETREPLRGSNTAKVSSTLNSKTLDKIFKFFQRNEKRKSNNKSKKNFGSSSNKIIQLANLKKIAKGDPKIPMQNRIYIWCYLVDGDETDIAKEDTRMPLYINKMWPVGRAMDYLSIQLNVKSSTLTNSSSNDKFQLCKLKEGKQVSFYNIGASLRVTNEIKDLDTLYLVHNNADEKSN
Protein: Protein TESPA1 (Thymocyte-expressed positive selection-associated protein 1) (A2RU30)
Organism: Homo sapiens (Human)
Function: Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23501103}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23501103}. Note=May localize to mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000269|PubMed:23501103}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Growth factor receptor-bound protein 2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- COP9 signalosome complex subunit 9
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 7b
Sequence:
MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDVPDPEPSSLDDVFQEGNPINKIEDWLQDCGYSEEGFSEEAGQFIYNGFCSHGTSFEDDLTLGAEATLLAANGKLFSRSFLETARPCQLLDLGCSLASSSMTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSRIPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASRFKQVQTLAVTADAFFCLYSYVSKTPVQKFTPSHMFWNCNHPTDVPSIRILSREPEPQSPRDRLRKAISKMCLYTCPRDRPPPPHNTPKRNSLDQVVLEVMDKVKEEKQFLQQDSDLGQFSQEDPVPPAEGKKLPTSPYPCVFCCEEETQQRMSTVLAPSQTLDSNPKVPCCTHSLPIEDPQWSTDPAQIRRELCSLPATNTETHPAKDETFWKRKSRARKSLFQKNLMGRKVKSLDLSITQQKWKQSVDRPELRRSLSQQPQDTFDLEEVQSNSEEEQSQSRWPSRPRHPHHHQTFAGKDS
Protein: Small ribosomal subunit protein uS7m (28S ribosomal protein S7, mitochondrial) (MRP-S7) (S7mt) (Q3T040)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11402041, ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein uS2m
Sequence:
MAAPTAKVSRGWSGLALGVRIAVLRLPGLTQVRWSRYGPEYQDPQIDKEYYRKPLAQLTEEETYERELRKTQVIKAAPATKTSSVFEDPVISKFTNMMMKGGNKILARSLMTQTLEAVKRKQFEKYHAASAEEQATVERNPYTIFHQALKNCEPVIGLVPILKGGHFYQVPVPLAERRRRFLAMKWMITECREKKPRRMLMPEKLSQELLEAFCNRGPVIKRKHDMHKMAEANRALAHYRWW
Protein: Nuclear distribution C, dynein complex regulator (A0A0A0MSU9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISNYRNGSELVCFNSGVGCFLIGCDWAFTVLVNTFFSFLRRKTDFFIGGEEGMAEKLITQTFSHHNQLAQKTRREKRARQEAERREKAERAARLAKEAKSETSGPQIKELTDEEAERLQLEIDQKKDAENHEAQLKNGSLDSPGKQDTEEDEEEDEKDKGKLKPNLGNGADLPNYRWTQTLSELD
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (G8B5I4)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Phosphoglycerate mutase
- Glyceraldehyde-3-phosphate dehydrogenase
- phosphopyruvate hydratase
- phosphopyruvate hydratase
- Glucose-6-phosphate isomerase
- Phosphoglycerate mutase
- mRNA 3'-end-processing protein RNA14
- Pyruvate decarboxylase
Sequence:
MSLSNKLSVKDLDVAGKRVFIRVDFNVPLDGKTITNNQRIVAALPTIKYVEEHKPKAIILASHLGRPNGEKNDKYSLKPVATELEKLLGKKVTFLDDCVGSEVEKAVNSASNGEIFLLENLRFHAEEEGSSKDKDGKKIKADPEAVKKFRDQLSSLADVYVNDAFGTAHRAHSSMVGVEVPQRAAGFLMSKELEYFAKALENPARPFLAILGGAKVSDKIKLIDNLLDKVDLLIIGGGMTFTFKKVLDNMSIGDSLFDEDGAKNVNDLVAKAKKNNVEIILPVDFVTADKFDKDAKVGEADDKEGIPENWMGLDCGPKSRELFDDAVAKAKTIVWNGPPGVFEFDNFAGGTKNLLDAVVKSAENGNIVIIGGGDTATVAKKYNAVDKLSHVSTGGGASLELLEGKELPGVVALSNKN
Protein: Pentatricopeptide repeat-containing protein 2, mitochondrial (Q8R3K3)
Organism: Mus musculus (Mouse)
Function: Involved in mitochondrial RNA maturation and mitochondrial respiratory chain function.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18729827}.
Interaction partners:
- Pentatricopeptide repeat-containing protein 1
- Small ribosomal subunit protein mS39
- Leucine-rich PPR motif-containing protein, mitochondrial
- Mitochondrial ribonuclease P catalytic subunit
Sequence:
MATVFRPLERLRVPRPSLHPGVTGSGSACCRCTLGAKRYLLTDNIVKLKEFQHKKIAIAYNLPGTKEIYFRNLEEKLTQNKLILKEELKTLLYLCQSLEDVQLAKAVIYRYHAENKNFTLGEYKFGPVFMRLCYELDLEDSAVELVRDKHLQGFFLDSTSFNILMDMLFTKGKYERALQVLIEMKNQDVRFSKETYILAFAICYKLNTLESLKICTTLREEALIKGDIICRRAYCFVVALALNKNQLKNAVSIFSQIVNPESIVCINLNILIHIQSNMLESLLKILEDSLDTNLSKFVRRHTFSEEVLAKVREKLKDSPALIARFDEVYGKLHVNGQITVHSLDALLCHVPRDKRSNLLLLKKRAVSHRTLQPLSRSLLTE
Protein: Probable transcriptional repressor TraM (P55408)
Organism: Sinorhizobium fredii (strain NBRC 101917 / NGR234)
Function: Acts to antagonize TraR-dependent activation.
Interaction partners:
Sequence:
MNDMGSSEVNDENKEKEARYSVMTKSELEALAVSAIREHRRLLWADQAVYEEWLRASDDPSISGPVLQTLQDEYVARQKRSEAQQEELSDILDALGFVPDVPFDDDN
Protein: SNAD (C8V7G9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Polo-like kinase
Sequence:
MADTTSHDTVGASTLAAPYFSPSSPSPSEHPPIDSPDRLPSPVSSPGARSPSGSPPSHREASLERAALELDARLAQYTVDFSQFPSTHADDGIDEQQEIEDEPDKLSAVGGPEDFTANLERYLLGEDDSINQDIDDEDKDQGQPQEESKRETEPLQPHDKPARPDSGQSNQPAVEDEAELGEYSEFGPPDDMSTPSHFLRRNVAPTKDTTHLEDIEENPNDELSPAATPTVRKFKSQTNQDVKQADKDLRRQIAELTQAVKERDEQLERNRNRVIEAASAGEEVTHLRAELQRKTALLEDMQESHAERVIARRSSLNASDFRALQKQIADMQKDLNSRSSHADIDTERLETISLLRQQLSLTQEQLEKRNAVLDDTLASLKQVTASKEQQLHEKDAEIDRLRSQVDAQRAEIERLETDVAEAHREYRALEDQMVLLETKNRPLEEKNSTLEADLNRAQSQVTAQENALKAMAADLPTDTPGGTYSEILELIKDLGQPNTNRSTRPRDGSDQDHDLEQIYEELSKLRTESSERAATNKNLEAQLSRAHDQAAESQLLIQSIEAENNRLVRNTEELKSKLDKTFNELNRLRTEHSEAQETITRLQESQQAQAQAQIQQPSPPSTPHANPNTTSLSALEANHKAQIANLKTAHATALSTLRSAHADSTRKLRAFLSAAEARETELRSLLEQEKEIHRNDEEEKDAEIQRLNSVIASKDETAAAMDLRIAKSVEKREREWERRVELLLKERERMGKALLWSWGEKEHPTKKAKGSISGSGKTAEVSSCETDKENVDDGRRHGQGQPYRYKYVKKT
Protein: Cullin-associated NEDD8-dissociated protein 1, N-terminal part (Cullin-associated and neddylation-dissociated protein 1, N-terminal part) (C8VP82)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor when interacting with candA-C (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21119001}. Note=Requires candA-C for nuclear localization.
Interaction partners:
- Cullin-associated NEDD8-dissociated protein 1, C-terminal part
- JmjC domain-containing histone demethylation protein 1
- Ubiquitin ligase subunit CulD, putative
- RING-box protein 1
- SCF ubiquitin ligase subunit CulC, putative
- Cullin-1
- DNA damage-binding protein 1
- Ubiquitin-like domain-containing protein
Sequence:
MGDRHTIQQNLNGLLSKLNDPDPDMRYMSLNDLYGILSNPCSSYLAHDQASATRLAEGLLKALDDQHGDVQNQALKCLGPLVARLPLEGLRTLLERLSNLTTSQTIDTSVPNTALRVIVTALPRPQPNQAPSPDANMAYSAVSEVLIPRLIGPGPHKRRGSVTKGMLEKDPAKGFSSDAIDVLIQVASCFGALLQESELTALEKAVMSIIDNDTAGTVVTKRALAAISALVVYFSDEQFGILVSELVERFNSPQLSTVHRRHLIAAVGCLARTVPAKFGPHLSTLAPFIFSAVGEDNLEVSHVLHYLCTSASNVYSSRNKPKIYHQYRQLPKEKLITGM
Protein: At3g12870 (MJM20.1 protein) (Transmembrane protein) (Q9LDH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASDQSTNPPIMEAKTRHPLHQIADTPTHKLLLKQWLKEEELILSRVSHKESQIDSVRREITQLYIFFFLFHSISLLLLFHASSSSSSSASSSACKRSWIPSLCALLSSLGIIWAVRYKSEVESHLEKLLEREKEDAKLLRKCVEELKKKGIEFDLLKEVDALRRAKSLRVESKPVKKWSARDFVTLFFFSVSCLVLAMIRLILCD
Protein: Thromboxane-A synthase (TS) (TXA synthase) (TXS) (EC 5.3.99.5) (Cytochrome P450 5A1) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (P36423)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation. Cleaves also PGH2 to 12-hydroxy-heptadecatrienoicacid (12-HHT) and malondialdehyde, which is known to act as a mediator of DNA damage. 12-HHT and malondialdehyde are formed stoichiometrically in the same amounts as TXA2. Additionally, displays dehydratase activity, toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) producing 15-KETE and 15-HETE.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P24557}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Prostacyclin synthase
- Prostaglandin G/H synthase 1
- Prostaglandin E synthase
- Prostaglandin E synthase 2
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Prostaglandin E synthase 3
- Prostaglandin G/H synthase 2
- Prostamide/prostaglandin F synthase
Sequence:
MEVLGLLKFEVSGTIVTVTLLVALLALLKWYSMSAFSRLEKLGIRHPKPSPFVGNLMFFRQGFWESQLELRERYGPLCGYYLGRRMHVVISEPDMIKQVLVENFSNFSNRMASGLEPKMVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFLQMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSALGPKNGVYIKIVSR
Protein: Secreted frizzled-related protein 5 (sFRP-5) (Frizzled-related protein 1b) (FRP-1b) (Secreted apoptosis-related protein 3) (SARP-3) (Q5T4F7)
Organism: Homo sapiens (Human)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP5 may be involved in determining the polarity of photoreceptor, and perhaps, other cells in the retina.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protein Wnt-11
- Protein Wnt-8b
- Protein Wnt-5a
- Protein Wnt-3a
- Protein Wnt-5b
- Protein Wnt-10b
- Protein Wnt-2
- Protein Wnt-2b
- Ankyrin repeat domain-containing protein 42
- Protein Wnt-7b
Sequence:
MRAAAAGGGVRTAALALLLGALHWAPARCEEYDYYGWQAEPLHGRSYSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRSLCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPATAPPVTKICAQCEMEHSADGLMEQMCSSDFVVKMRIKEIKIENGDRKLIGAQKKKKLLKPGPLKRKDTKRLVLHMKNGAGCPCPQLDSLAGSFLVMGRKVDGQLLLMAVYRWDKKNKEMKFAVKFMFSYPCSLYYPFFYGAAEPH
Protein: 5-hydroxytryptamine receptor 3E (5-HT3-E) (5-HT3E) (Serotonin receptor 3E) (A5X5Y0)
Organism: Homo sapiens (Human)
Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:17392525}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:19012743}; Multi-pass membrane protein {ECO:0000255}. Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. {ECO:0000269|PubMed:17392525}.
Interaction partners:
- 5-hydroxytryptamine receptor 3A
- 5-hydroxytryptamine receptor 3C
- 5-hydroxytryptamine receptor 3D
- 5-hydroxytryptamine receptor 3B
- Glutamate receptor 3
Sequence:
MEGSWFHRKRFSFYLLLGFLLQGRGVTFTINCSGFGQHGADPTALNSVFNRKPFRPVTNISVPTQVNISFAMSAILDVNEQLHLLSSFLWLEMVWDNPFISWNPEECEGITKMSMAAKNLWLPDIFIIELMDVDKTPKGLTAYVSNEGRIRYKKPMKVDSICNLDIFYFPFDQQNCTLTFSSFLYTVDSMLLDMEKEVWEITDASRNILQTHGEWELLGLSKATAKLSRGGNLYDQIVFYVAIRRRPSLYVINLLVPSGFLVAIDALSFYLPVKSGNRVPFKITLLLGYNVFLLMMSDLLPTSGTPLIGVYFALCLSLMVGSLLETIFITHLLHVATTQPPPLPRWLHSLLLHCNSPGRCCPTAPQKENKGPGLTPTHLPGVKEPEVSAGQMPGPAEAELTGGSEWTRAQREHEAQKQHSVELWLQFSHAMDAMLFRLYLLFMASSIITVICLWNT