wanglab/gogpt-training-data huggingface dataset:
Protein: Cadherin-6 (Kidney cadherin) (K-cadherin) (P55285)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Probable non-functional immunoglobulin heavy variable 3-16
- Immunoglobulin heavy variable 3-43D
- Catenin alpha-1
- Catenin beta-1
- Cadherin-15
- Cadherin-2
- Cadherin-7
- Cadherin-19
- Cadherin-20
- Cadherin-10
Sequence:
MRTYRYFLLLFWVGQPYPTLSTPLSKRTSGFPAKKRALELSGNSKNELNRSKRSWMWNQFFLLEEYTGSDYQYVGKLHSDQDRGDGSLKYILSGDGAGDLFIINENTGDIQATKRLDREEKPVYILRAQAINRRTGRPVEPESEFIIKIHDINDNEPIFTKEVYTATVPEMSDVGTFVVQVTATDADDPTYGNSAKVVYSILQGQPYFSVESETGIIKTALLNMDRENREQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQSTYQFKTPESSPPGTPIGRIKASDADVGENAEIEYSITDGEGLDMFDVITDQETQEGIITVKKLLDFEKKKVYTLKVEASNPYVEPRFLYLGPFKDSATVRIVVEDVDEPPVFSKLAYILQIREDAQINTTIGSVTAQDPDAARNPVKYSVDRHTDMDRIFNIDSGNGSIFTSKLLDRETLLWHNITVIATEINNPKQSSRVPLYIKVLDVNDNAPEFAEFYETFVCEKAKADQLIQTLHAVDKDDPYSGHQFSFSLAPEAASGSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCACDHHGNMQSCHAEALIHPTGLSTGALVAILLCIVILLVTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPEAIEDNKLRRDIVPEALFLPRRTPTARDNTDVRDFINQRLKENDTDPTAPPYDSLATYAYEGTGSVADSLSSLESVTTDADQDYDYLSDWGPRFKKLADMYGGVDSDKDS
Protein: Arachidonate 5-lipoxygenase-activating protein (FLAP) (MK-886-binding protein) (P20292)
Organism: Homo sapiens (Human)
Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes.
Subcellular location: Nucleus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Polyunsaturated fatty acid 5-lipoxygenase
- Leukotriene A-4 hydrolase
- Microsomal glutathione S-transferase 1
- Glutathione S-transferase 3, mitochondrial
- Prostaglandin E synthase
- Coactosin-like protein
- Cysteinyl leukotriene receptor 1
- Leukotriene C4 synthase
- Cysteinyl leukotriene receptor 2
- Cytosolic phospholipase A2
Sequence:
MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLIP
Protein: Putative inactive L-type lectin-domain containing receptor kinase III.2 (LecRK-III.2) (Q9ZW11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9LSR8}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Protein NRT1/ PTR FAMILY 6.1
- Delta-9 acyl-lipid desaturase 2
- Protein NRT1/ PTR FAMILY 1.1
- Cyclic nucleotide-gated ion channel 17
Sequence:
MANTYKSIAVSIIFLLYFSCVSSQQQTKFLNHGFLEANLLKSGSSKIHPSGHLELTNTSMRQIGQAFHGFPIPFLNPNSSNLVSFPTSFVFAITPGPGAPGHGLAFVISPSLDFSGALPSNYLGLFNTSNNGNSLNCILAVEFDTVQAVELNDIDDNHVGIDLNGVISIESTSAEYFDDREAKNISLRLASGKPIRVWIEYNATETMLNVTLAPLDRPKPKLPLLSRKLNLSGIISEENYVGFSAATGTVTSSHFVLGWSFSIEGKASDFDITKLPSLPDPLPPLSPSPSPPVSVMKNSSNTMLIIIIAASAIFGILILSFLAVCFFRRTENFTGGARKFSHQTISSATGGFDNSKLLGEGNSGSFYKGQLAPTEIIAVKRITCNTRQEKTALIAEIDAISKVKQRNLVDLHGYCSKGNEIYLVYEYVINRSLDRFLFSNDLPVLKWVHRFCIIKGIASALQHLHAEVQKPLIHGNVKASNVLLDGELNARLGDYGHGSRHSTTGHVAPELVNTGKATCATDVFEFGVLIMEIVCGRRAIEPTKEPVEISLVNWVLRGVKSGNLLRRCDKRIKKKNLVSEEVLLVLKTGLLCVRRSPEDRPMMKKVLEYLNGTEHLPHDDYVV
Protein: RAD51-associated protein 1 (RAB22) (Q8C551)
Organism: Mus musculus (Mouse)
Function: Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination.
Subcellular location: Chromosome {ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:9192668}. Nucleus {ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:9192668}. Chromosome, telomere {ECO:0000250|UniProtKB:Q96B01}. Note=Colocalizes with RAD51 to multiple nuclear foci (PubMed:21307306, PubMed:9192668). Colocalizes with DMC1 on meiotic chromatin (PubMed:21307306). {ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:9192668}.
Interaction partners:
- DNA repair protein RAD51 homolog 1
- WD repeat-containing protein 48
- Partner and localizer of BRCA2
- Exonuclease 1
- Breast cancer type 1 susceptibility protein homolog
- DNA repair and recombination protein RAD54-like
- Centromere protein H
- Ubiquitin carboxyl-terminal hydrolase 1
- Breast cancer type 2 susceptibility protein homolog
- Chromosome-associated kinesin KIF4
Sequence:
MVRPTRNRKPINYSQFEDSGNDSDDDFISSSTPVNKSKTVPKVLKQDKPKPNLKNLQKEEVLPTEPPKKRVALDDKVFQRGLEVALALSVKELPTLTNQVKKSKEKSTDKQGKEKTENTGKPPRVSNCSVASDDVEDLDKITEEGDASSVEGERKSPSQAKAPRRRAPSEGSDGSSANDTESESATGEGSESDPDFDESKESDEDFGVRRSKESKKKTVQKKPAGEKKERKSKPKCEASVTSVDPAPAAIKSGSPSLPQAVGLPSEATRKPAIMCSPSAESKRPKWVPPAASGSRNSSSNALAGTPAKSPSQSLRLGLSRLAPVKRLHPSATSSQVR
Protein: DNA repair protein RAD4 (Q8W489)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May have a role in the nucleotide excision repair (NER) pathway.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:29283431}.
Interaction partners:
- Ubiquitin receptor RAD23b
- Ubiquitin receptor RAD23d
- Probable ubiquitin receptor RAD23a
- Ubiquitin receptor RAD23c
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH helicase subunit XPD
- Calcium-binding protein CML19
- General transcription and DNA repair factor IIH subunit TFB1-3
- General transcription and DNA repair factor IIH subunit TFB1-1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB1
Sequence:
MKSRSESKNCRLAQASRVAVNKVLDKSSARGSRGKKKQDDNCDSAKRDKGVNGKGKQALDARLIDNVLEDRGCGNVDDDEMNDSDWEDCPIPSLDSTVDDNNVDDTRELTIEFDDDVPDAKKQKNAYRATAEDKVRAELVHKVHLLCLLARGRIVDSACNDPLIQAALLSLLPSYLTKVSNLEKVTVKDIAPLLRWVRENFSVSCSPSSEKSFRTSLAFALESRKGTAEELAALAVALLRALKLTTRFVSILDVASLKPGADRNESSGQNRAKMKHGIFRTSTLMVPKQQAISSYPKKSSSHVKNKSPFEKPQLGNPLGSDQVQDNAVNSSCEAGMSIKSDGTRRKGDVEFERQIAMALSATADNQQSSQVNNTKKVREITKISNSSSVSDQVISTAFGSKKVDSPLCWLEVYCNGENMDGKWVHVDAVNGMIDAEQNIEAAAAACKTVLRYVVAFAAGGAKDVTRRYCTKWHTISSKRVSSVWWDMVLAPLVHLESGATHDEDIALRNFNGLNPVSSRASSSSSSFGIRSALEDMELATRALTESLPTNQQAYKSHEIYAIEKWLHKNQILHPKGPVLGFCSGHPVYPRTCVQTLKTKERWLRDGLQLKANEVPSKILKRNSKFKKVKDFEDGDNNIKGGSSCMELYGKWQMEPLCLPPAVNGIVPKNERGQVDVWSEKCLPPGTVHLRFPRIFAVAKRFGIDYAPAMVGFEYRSGGATPIFEGIVVCTEFKDTILEAYAEEQEKKEEEERRRNEAQAASRWYQLLSSILTRERLKNRYANNSNDVEAKSLEVNSETVVKAKNVKAPEKQRVAKRGEKSRVRKSRNEDESHEHVFLDEEETFDEETSVKTKRCKCGFSVEVEQM
Protein: Agrocybin (P84797)
Organism: Agrocybe cylindracea (Toadstool) (Pholiota aegerita)
Function: Has antifungal activity against M.arachidicola with an IC(50) of 125 uM, but not against F.oxysporum. Inhibits human immunodeficiency virus-1 (HIV-1) reverse transcriptase with an IC(50) of 60 uM. Has mitogenic activity towards murine splenocytes. Lacks antiproliferative activity towards HepG2 hepatoma cells. Has antibacterial activity against the Gram-negative bacterium P.fluorescens. No antibacterial activity against the Gram-positive bacteria B.subtilis, B.cereus, B.megaterium, M.phei and S.aureus, or against the Gram-negative bacteria E.aerogenes, E.coli, P.aeruginosa, P.fluorescens and P.vulgaris.
Interaction partners:
Sequence:
ANDPQCLYGNVAAKF
Protein: B-type flagellar hook-associated protein 2 (HAP2) (Filament cap protein) (Flagellar cap protein) (Q9K3C5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. Essential for motility. Responsible for adhesion to mucin, which is the initial event in colonization by this organism of the airways of cystic fibrosis patients.
Subcellular location: Secreted. Bacterial flagellum.
Interaction partners:
- Flagellar hook-associated protein 1
- B-type flagellin
- Flagellar secretion chaperone FliSB
- Flagellar hook-associated protein type 3 FlgL
- Flagellar hook protein FlgE
- Flagellar motor switch protein FliG
- Flagellar M-ring protein
- Flagellar hook-basal body complex protein FliE
- Flagellar basal-body rod protein FlgC
- Flagellar basal body rod protein FlgB
Sequence:
MAGISIGVGSTDYTDLVNKMVNLEGAAKTNQLATLEKTTTTRLTALGQFKSAISAFQTALTALNSNAVFMARTAKSSNEDILKASATQSAVAGTYQIQVNSLATSSKIALQAIADPANAKFNSGTLNISVGDTKLPAITVDSSNNTLAGMRDAINQAGKEAGVSATIITDNSGSRLVLSSTKTGDGKDIKVEVSDDGSGGNTSLSQLAFDPATAPKLSDGAAAGYVTKAANGEITVDGLKRSIASNSVSDVIDGVSFDVKAVTEAGKPITLTVSRDDAGVKDNVKKFVEAYNTLTKFINEQTVVTKVGEDKNPVTGALLGDASVRALVNTMRSELIASNENGSVRNLAALGITTTKDGTLEIDEKKLDKAISADFEGVASYFTGDTGLAKRLGDKMKPYTDAQGILDQRTTTLQKTLSNVDTQKADLAKRLAALQEKLTTQFNLLSAMQDEMTKRQKSITDNLASLPYGSGKKT
Protein: PPR repeat protein (S7UEN8)
Organism: Toxoplasma gondii (strain ATCC 50853 / GT1)
Interaction partners:
Sequence:
MRRPSLFSFLSCSLFLLACSSAVSALPLAAPLRSAPLCPFASSASSSSLHRRPAGLRCTPHFAFASFEKAKGSEKCEPAKTPRPTVETADGEPLRRDPADPSSGSARVCGVHTSGAPLATVPKANNESCEGKRHFRFRTNDEEGNHGNELEGRFEEPEEPEEPDRAAEGQEKRRRENSGKTPGRATGKRKSLNGYHASWLASAFNRHQASHIHSLRVSSFRSPLSSFLSSSHSSSLALCSSSFSPFASSLLSPSPLFLNPASSASGRRVSLSNFLSSPSSSSPSVSASSSCSSSSSLLRALVACHSSPQTASVSLSPPRGSSFSSLSPSVLLRRSETRTQAPTLQAPLLSVRGSWPPDAGDDRETEKRLSPLRIDYRQAFELLENADPTGIKALTAAYNAALHACERQRDRPGALRIYAAMREKEIPIDVVTLHSLFTLLEAFADDTALLQILAQVDSADPESSMAFLSRSPSSSLSPSPRSDSQASPTVSVTPSLLSLGISTCCRAGNATAAVQLMERLKVLLRRNADKFLLNFTSVLPPDTADATAAVAHPPTGVYVQLVVALTQEGRYEEALAYYEELKSLQRRFVEKQQLLEREVARRAELVERELKNAPEQERKKLLGDIERQVVEEQELLLEDYQPPIGAVNAALEACLYTGRLKQALLIYKEDVEFPEKQRLRAGEALDQDLAPSKAAPTLRTFELLLRACSQQRQAFALAQIWRDFEELQATVAETQNASPFRLPSAAPCVASAIQGFAACGLWTYALRLLLLLHKETGDARQRHCELLSDLLRDAREAAERSGAARETQSKMRSENEGERSSEQKDGDARAAASESGDWERCLEGRFVDLGVEPYLAVLRACRDVGAWKPALGILRLLQQRHTQAKLLHALGAARERREAERREQFQQRVRALRRRLSEAKRKTNGADCVGEAAEQQRPTSASPTGDSDPLLSRDMERFLGSLHNSVAVGRTPLLPEFPYEAYALTLGTMAAARAWDRVLAVSSEFFSRRDSGACGSASLGADGPAGEANEERKPARRAVGFGGERDEGGQPERGAEGERRDAPLEIRKSVHAYRLMALMHLGRHEEVEAERRSLIRLTEMERRTRERRDARQREREGGEEKREEGEGSEEAFLPKWREETEHEEGEGGEDEGSHGIATLVLEEAETWLMRGVTRERRTQGKDNIYPTPSIHETTPHTYEATHHSFPSPSKSSSASSSASSSASSSASSSASSSSFSSASSSSFSSSPLQPSFIAGSGGGRSMSLRDVRHLEGVSAMSEGLKEGRGEETSVARRAEFLIGGGTKRKVCVQEEDRGDAVAEGEANHKSVCRDETGEEHSGRSLDRFFAGLEPVSEREARAVAEAVERRRTEEHWRQEKMQSGVKRATGDREGMQPKRSADPEGDKNDPGCQTAGNDPGGETGLRRREGERDGVNEEAGGREKGASGQIEREREGEHDTEEARERLEEKEEEREKENSEREGRAIRAVSGERGLSVSAFLSSVLGPRRAVLESMREEPVLEDTVTEEPESLELHADAEAQLEAKQREGESRDRSGENTEASTERRNSPDREEEKQDPVTTATQETDANTGGTLSQAGGRKSEAASRSESVETSLDLLLRLKHKTPAETQQLEDGPPRWLARRSGTGEPGAEAVAGSRRGVHPPDGRAGVGIPGGGAGSQRQRQETRGQSAFLFAGDHGWGWPPHWEEKLDKARARLQRTNDESGETEENAKTETPWGMRPT
Protein: Protein transport protein SEC31 (Protein WEB1) (P38968)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Protein transport protein SEC13
- Protein transport protein SEC23
- Protein transport protein SEC24
- Small COPII coat GTPase SAR1
- SED5-binding protein 3
- COPII coat assembly protein SEC16
- SED5-binding protein 2
- Peflin
- Guanine nucleotide-exchange factor SEC12
- GTPase-activating protein NEL1
Sequence:
MVKLAEFSRTATFAWSHDKIPLLVSGTVSGTVDANFSTDSSLELWSLLAADSEKPIASLQVDSKFNDLDWSHNNKIIAGALDNGSLELYSTNEANNAINSMARFSNHSSSVKTVKFNAKQDNVLASGGNNGEIFIWDMNKCTESPSNYTPLTPGQSMSSVDEVISLAWNQSLAHVFASAGSSNFASIWDLKAKKEVIHLSYTSPNSGIKQQLSVVEWHPKNSTRVATATGSDNDPSILIWDLRNANTPLQTLNQGHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEAPDLFACASFDNKIEVQTLQNLTNTLDEQETETKQQESETDFWNNVSREESKEKPTVFHLQAPTWYGEPSPAAHWAFGGKLVQITPDGKGVSITNPKISGLESNTTLSEALKTKDFKPLINQRLVKVIDDVNEEDWNLLEKLSMDGTEEFLKEALAFDNDESDAQDDANNEKEDDGEEFFQQIETNFQPEGDFSLSGNIEQTISKNLVSGNIKSAVKNSLENDLLMEAMVIALDSNNERLKESVKNAYFAKYGSKSSLSRILYSISKREVDDLVENLDVSQWKFISKAIQNLYPNDIAQRNEMLIKLGDRLKENGHRQDSLTLYLAAGSLDKVASIWLSEFPDLEDKLKKDNKTIYEAHSECLTEFIERFTVFSNFINGSSTINNEQLIAKFLEFINLTTSTGNFELATEFLNSLPSDNEEVKTEKARVLIASGKSLPAQNPATATTSKAKYTNAKTNKNVPVLPTPGMPSTTSIPSMQAPFYGMTPGASANALPPKPYVPATTTSAPVHTEGKYAPPSQPSMASPFVNKTNSSTRLNSFAPPPNPYATATVPATNVSTTSIPQNTFAPIQPGMPIMGDYNAQSSSIPSQPPINAVSGQTPHLNRKANDGWNDLPLKVKEKPSRAKAVSVAPPNILSTPTPLNGIPANAASTMPPPPLSRAPSSVSMVSPPPLHKNSRVPSLVATSESPRASISNPYAPPQSSQQFPIGTISTANQTSNTAQVASSNPYAPPPQQRVATPLSGGVPPAPLPKASNPYAPTATTQPNGSSYPPTGPYTNNHTMTSPPPVFNKPPTGPPPISMKKRSNKLASIEQNPSQGATYPPTLSSSASPLQPSQPPTLASQVNTSAENVSHEIPADQQPIVDFLKEELARVTPLTPKEYSKQLKDCDKRLKILFYHLEKQDLLTQPTIDCLHDLVALMKEKKYKEAMVIHANIATNHAQEGGNWLTGVKRLIGIAEATLN
Protein: Cytochrome P450, family 2, subfamily R, polypeptide 1 (Vitamin D 25-hydroxylase (EC 1.14.15.15)) (F6P2A1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cytochrome P450, family 27, subfamily B, polypeptide 1
- Cytochrome P450, family 24, subfamily A, polypeptide 1
- Vitamin D3 receptor A.
- Vitamin D-binding protein
- 7-dehydrocholesterol reductase
Sequence:
MISIKRLTSPLSLSWEQTLICLLGLFTTLLILLVIRQLVKQRRPRGFPPGPTPLPIIGNMLSLATEPHVYMKRQSDIHGQIFSLDLGGIPTVILNGYDAIKECLYHQSEVFADRPSLPLFQKMTKMGGLLNCKYGRGWIEHHKLAVNCFRYFGTGQRMFERISEECLYFLDAIDQHQGKPFNPKHLVTNAVSNITNLIIFGQRFTYDDGDFQHMIEIFSENVELAASSWAFLYNAFPWMEYLPFGKHQRLFRNANEVYKFLLQIIRRFSQGRVPQSPQHYIDAYLDEMEQSTPDKATSFSQDNLIFSVGELIIAGTETTTNCLRWAMLYMALYPRIQEKVQMEIDSVLNGRQPAFEDRQRMPYVEAVLHEVLRLCNIVPLGIFRATSQDAVVRGYTIPKGTMVITNLYSVHFDEKYWSDPSIFCPERFLDCNGKFIRHEAFLPFSIGKRHCLGEQLARLEMFLFFTTLLQRFHLQFSEGFIPSLSAKLGMTLQPQPYSICAIRRQQ
Protein: Transcription factor Maf (Proto-oncogene c-Maf) (Transcription factor Maf-2) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog) (P54844)
Organism: Rattus norvegicus (Rat)
Function: Acts as a transcriptional activator or repressor. When overexpressed, represses anti-oxidant response element (ARE)-mediated transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Binds to the ARE sites of detoxifying enzyme gene promoters. Involved in embryonic lens fiber cell development. Recruits the transcriptional coactivators CREBBP and/or EP300 to crystallin promoters leading to up-regulation of crystallin gene during lens fiber cell differentiation. Activates the expression of IL4 in T-helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis by interacting with MYB and decreasing BCL2 expression. Together with PAX6, transactivates strongly the glucagon gene promoter through the G1 element. Activates transcription of the CD13 proximal promoter in endothelial cells. Represses transcription of the CD13 promoter in early stages of myelopoiesis by affecting the ETS1 and MYB cooperative interaction. Involved in the initial chondrocyte terminal differentiation and the disappearance of hypertrophic chondrocytes during endochondral bone development. Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf response element) sites of lens-specific alpha- and beta-crystallin gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-rich region adjacent to the TGC motif (atypical Maf response element) in the CD13 proximal promoter in endothelial cells. It may interact with additional basic-zipper proteins that determine a subtype of Maf-responsive element binding (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:9038383}.
Interaction partners:
- Protein c-Fos
- Nuclear factor erythroid 2-related factor 2
- Transcription factor Jun
- BTB domain and CNC homolog 2
- Paired box protein Pax-6
- Transcription factor NF-E2 45 kDa subunit
- Fos-related antigen 2.
- Cyclic AMP-responsive element-binding protein 1
- Nei endonuclease VIII-like 1
- Basic leucine zipper transcriptional factor ATF-like
Sequence:
MASELAMNNSDLPTSPLAMEYVNDFDLMKFEVKKEPVETDRIISQCGRLIAGGSLSSTPMSTPCSSVPPSPSFSAPSPASGSEQKAHLEDYYWMTGYPQQLNPEALGFSPEDAVEALISNSHQLQGGFDGYARGAQQLAAAAGAGAGASLGGSGEEMGPAAAVVSAVIAAAAAQSGGAPHYHHHHHHATGHHHHPTAGAPGAAGSASASASGAGGAGGGGPASAGGGGGGGGGGTAGAGGALHPHHAAGGLHFDDRFSDEQLVTMSVRELNRQLRGVSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHVLESEKNQLLQQVDHLKQEISRLVRERDAYKEKYEKLVSSGFRENCSSSDNPSSPEFFM
Protein: Immunoglobulin-like domain-containing receptor 1 (Angulin-2) (Q86SU0)
Organism: Homo sapiens (Human)
Function: Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (tTJs). Crucial for normal hearing by maintaining the structural and functional integrity of tTJs, which are critical for the survival of auditory neurosensory HCs. Mediates fatty acids and lipoproteins-stimulated CCK/cholecystokinin secretion in the small intestine. In the inner ear, may regulate alternative pre-mRNA splicing via binding to TRA2A, TRA2B and SRSF1 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15381095}; Single-pass type I membrane protein {ECO:0000269|PubMed:15381095}. Cell junction, tight junction {ECO:0000269|PubMed:23239027}. Cytoplasm {ECO:0000269|PubMed:35595813}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytosol {ECO:0000269|PubMed:15381095}.
Interaction partners:
- MARVEL domain-containing protein 2
Sequence:
MAWPKLPAPWLLLCTWLPAGCLSLLVTVQHTERYVTLFASIILKCDYTTSAQLQDVVVTWRFKSFCKDPIFDYYSASYQAALSLGQDPSNDCNDNQREVRIVAQRRGQNEPVLGVDYRQRKITIQNRADLVINEVMWWDHGVYYCTIEAPGDTSGDPDKEVKLIVLHWLTVIFIILGALLLLLLIGVCWCQCCPQYCCCYIRCPCCPAHCCCPEEALARHRYMKQAQALGPQMMGKPLYWGADRSSQVSSYPMHPLLQRDLSLPSSLPQMPMTQTTNQPPIANGVLEYLEKELRNLNLAQPLPPDLKGRFGHPCSMLSSLGSEVVERRIIHLPPLIRDLSSSRRTSDSLHQQWLTPIPSRPWDLREGRSHHHYPDFHQELQDRGPKSWALERRELDPSWSGRHRSSRLNGSPIHWSDRDSLSDVPSSSEARWRPSHPPFRSRCQERPRRPSPRESTQRHGRRRRHRSYSPPLPSGLSSWSSEEDKERQPQSWRAHRRGSHSPHWPEEKPPSYRSLDITPGKNSRKKGSVERRSEKDSSHSGRSVVI
Protein: Prefoldin subunit alpha (GimC subunit alpha) (O58263)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Prefoldin subunit beta
- Thermosome subunit
- Large ribosomal subunit protein eL20
- Translation initiation factor 6
- DNA-binding protein PH1060
- Peroxiredoxin
Sequence:
MAQNNKELEKLAYEYQVLQAQAQILAQNLELLNLAKAEVQTVRETLENLKKIEEEKPEILVPIGAGSFLKGVIVDKNNAIVSVGSGYAVERSIDEAISFLEKRLKEYDEAIKKTQGALAELEKRIGEVARKAQEVQQKQSMTSFKVKK
Protein: Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16 (EC 3.6.4.13) (Q9P774)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable ATP-binding RNA helicase involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 17
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor cwf2
- Pre-mRNA-splicing factor slu7
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor cwf3
- Pre-mRNA-splicing ATP-dependent RNA helicase prp28
- Splicing factor YJU2
Sequence:
MLSHNQNDLLFTKLIDKLTDYMSSKDAATSLASRVLTIAKGSSSSTEFSNALHTFGRFSDNDSVLIYDLCKSIIGLETNLGISKDKLPGNDGSQVAGLVLSNRSGLKGREPKKSQLGLDVLAVQKKKEKSQVEGRSELSQVENDSLESIGNYDRVEFKRPKNPHEKHFRPLRQRSSVDDHQEFESEDDKYRRNSYSSWSGSNFESSNGSNRRRYRTQMEEPLSSKRRNRFGNGSRRDVDSSKYSHDSDYSYGAHSSWDARDVEYPEEDPESKADRQRWEEEQAHLDRDWYMNSESQNLLGDEVHNPFSDFETVEDRAHEAEFIEKQKKHLSIEASDRFKENSMWEKNRMITSGVSKAPGLESDYSLMEERRVHLLVDELRPHFLDGAEFSSKKVGDITSVRDPQSDLAINARLGSRLVRERREFRERQKAASAATSLAGTSLGNVMGLKDSNDEDAKAGTTPVKVAGRSEQSNKKDTEFARTKSYREQREFLPAFAVREQLLSVIRDNQVLIVVGETGSGKTTQLAQFLYEDGYHRNGMIGCTQPRRVAAMSVAKRVSEEMGVRLGSTVGYSIRFEDVTGPDTVIKYMTDGVLLRESLMQNNLEKYSVIIMDEAHERSLNTDILMGLLKKVLSRRRDIKLLVTSATMNSQKFSDFFGGAPQFTIPGRTYPVDIMFAKAPCSDYVEAAVRQVLQIHLSQPAGDILVFMTGQEDIEATCEIIADRLNQLHDAPRLSILPIYSQMPADLQAKIFDSAEPGVRKVVVATNIAETSLTVHGISYVVDTGYCKLKMYNSKLGIDTLQVTPISQANANQRAGRAGRTGPGIAYRLYTEMAYIREMFETTLPEIQRTNLSNTVLILKSLGVEEISDFDFMDRPPNDTLMASLYELWTLGALDNFGKLTTLGKKMSLFPMDPSLSKLIIIAEDYKCTEEIITIVSMLSVPSVFYRPKERAEESDAAREKFNVPESDHLMLLNIYQHWQRNGYSNSWCSKHFLHSKTLKRARDIRQQLVEIMSKQKISLESVSDWDIVRRVLCSAYFHQAACAKGIGEYVHLRSGMPCHLHVTSSLYGLGYLPDYVIYHELVLTSKEYMNIVTSVDPYWLAEFGGVYYSVKERFRNETESYDRVFSSKPQLDAQIAADRELDAKQKLAKNQEPVKSKRKSVIRAKPPRRVRGF
Protein: Zinc finger-containing ubiquitin peptidase 1 (EC 3.4.19.12) (Lys-63-specific deubiquitinase ZUFSP) (DUB) (Zinc finger with UFM1-specific peptidase domain protein) (Q96AP4)
Organism: Homo sapiens (Human)
Function: Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29476094}. Nucleus {ECO:0000269|PubMed:29476094, ECO:0000269|PubMed:29576527, ECO:0000269|PubMed:29576528}. Note=Mostly present in the nuclear fraction. Localizes to DNA lesions. {ECO:0000269|PubMed:29576527, ECO:0000269|PubMed:29576528}.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 12
- OTU domain-containing protein 1
- Ubiquitin carboxyl-terminal hydrolase 30
- Deubiquitinase OTUD6B
- AMSH-like protease
- OTU domain-containing protein 6A
Sequence:
MLSCNICGETVTSEPDMKAHLIVHMESEIICPFCKLSGVNYDEMCFHIETAHFEQNTLERNFERINTVQYGTSDNKKDNTLQCGMEVNSSILSGCASNHPKNSAQNLTKDSTLKHEGFYSENLTESRKFLKSREKQSSLTEIKGSVYETTYSPPECPFCGKIEEHSEDMETHVKTKHANLLDIPLEDCDQPLYDCPMCGLICTNYHILQEHVDLHLEENSFQQGMDRVQCSGDLQLAHQLQQEEDRKRRSEESRQEIEEFQKLQRQYGLDNSGGYKQQQLRNMEIEVNRGRMPPSEFHRRKADMMESLALGFDDGKTKTSGIIEALHRYYQNAATDVRRVWLSSVVDHFHSSLGDKGWGCGYRNFQMLLSSLLQNDAYNDCLKGMLIPCIPKIQSMIEDAWKEGFDPQGASQLNNRLQGTKAWIGACEVYILLTSLRVKCHIVDFHKSTGPLGTHPRLFEWILNYYSSEGEGSPKVVCTSKPPIYLQHQGHSRTVIGIEEKKNRTLCLLILDPGCPSREMQKLLKQDIEASSLKQLRKSMGNLKHKQYQILAVEGALSLEEKLARRQASQVFTAEKIP
Protein: Muscleblind-like splicing regulator 1 (A0A8I5ZVU8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM