wanglab/gogpt-training-data huggingface dataset:
Protein: Epsin-3 (EPS-15-interacting protein 3) (Q91W69)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Note=Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Epidermal growth factor receptor substrate 15
- Epidermal growth factor receptor substrate 15-like 1
- Clathrin heavy chain 1
- Epsin-1
- Clathrin coat assembly protein AP180
- Intersectin-1
- Synaptojanin-1
- Huntingtin-interacting protein 1-related protein
- Intersectin-2
- AP-2 complex subunit beta
Sequence:
MTTSALRRQVKNIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHALKTKERMALEGMGIGSGQLGYSRRSRGSPSSYTSASSSPRYASDLEQARPQTSGEEELQLQLALAMSREEAERPVPPASHRDEDLQLQLALSLSRQEHEKGVRSWKGDDSPVANGAEPAGQRRQRDREPEREERKEEEKLKTSQSSILDLADIFAPAPALPSTHCSADPWDIPGLRPNTEPSGSSWGPSADPWSPVPSGNALSRSQPWDLLPTLSSSEPWGRTPVLPSGPPIADPWAPSSPTRKLPSTGADPWGASMETSDTSALGGASPFDPFAKPLESTEPKESRDSAQALPTGKSPSTVELDPFGDSSPSCKQNGMKEPEALDLGVLGEALPQQPGKEARPCRTPESFLGPSASSLVNLDSLVKAPLAARTRNPFLTGLGVPSPTNPFGAGDQGRPTLNQMRTGSPALGLPPGGPVGAPVGSMTYSASLPLPLSSVPVGATLPASVSVFPQAGAFAPPPASLPQPLLPTSGPMGPLPPQAGTNPFL
Protein: All-trans-retinol 13,14-reductase (EC 1.3.99.23) (All-trans-13,14-dihydroretinol saturase) (RetSat) (PPAR-alpha-regulated and starvation-induced gene protein) (Q6NUM9)
Organism: Homo sapiens (Human)
Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol. Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers. May play a role in the metabolism of vitamin A. Independently of retinol conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP. May play a role in adipocyte differentiation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q64FW2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64FW2}.
Interaction partners:
- Lecithin retinol acyltransferase
- Dehydrogenase/reductase SDR family member 4
- Short-chain dehydrogenase/reductase 3
- Retinol dehydrogenase 8
- Retinol dehydrogenase 12
- Cytochrome P450 26A1
- Retinol dehydrogenase 10
- Cytochrome P450 27C1
- Retinol dehydrogenase 11
- Epidermal retinol dehydrogenase 2
Sequence:
MWLPLVLLLAVLLLAVLCKVYLGLFSGSSPNPFSEDVKRPPAPLVTDKEARKKVLKQAFSANQVPEKLDVVVIGSGFGGLAAAAILAKAGKRVLVLEQHTKAGGCCHTFGKNGLEFDTGIHYIGRMEEGSIGRFILDQITEGQLDWAPLSSPFDIMVLEGPNGRKEYPMYSGEKAYIQGLKEKFPQEEAIIDKYIKLVKVVSSGAPHAILLKFLPLPVVQLLDRCGLLTRFSPFLQASTQSLAEVLQQLGASSELQAVLSYIFPTYGVTPNHSAFSMHALLVNHYMKGGFYPRGGSSEIAFHTIPVIQRAGGAVLTKATVQSVLLDSAGKACGVSVKKGHELVNIYCPIVVSNAGLFNTYEHLLPGNARCLPGVKQQLGTVRPGLGMTSVFICLRGTKEDLHLPSTNYYVYYDTDMDQAMERYVSMPREEAAEHIPLLFFAFPSAKDPTWEDRFPGRSTMIMLIPTAYEWFEEWQAELKGKRGSDYETFKNSFVEASMSVVLKLFPQLEGKVESVTAGSPLTNQFYLAAPRGACYGADHDLGRLHPCVMASLRAQSPIPNLYLTGQDIFTCGLVGALQGALLCSSAILKRNLYSDLKNLDSRIRAQKKKN
Protein: Adhesion G protein-coupled receptor L4 (EGF,latrophilin and seven transmembrane domain-containing protein 1) (EGF-TM7-latrophilin-related protein) (ETL protein) (Q9ESC1)
Organism: Rattus norvegicus (Rat)
Function: Endothelial orphan receptor that acts as a key regulator of angiogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11050079}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Endomucin
Sequence:
MRLLLLLVGLSTLLNHSYTQNCKTPCLPNAKCEVLDEVAACFCSTGYTGNGITICEDVDECNETSVCGDHAVCENTNGGFSCFCVEGYQTSTGKTQFTPNDGSYCQDVDECNETSVCGDHAVCENTNGGFSCFCVEGYQTSTGKTQFTPNDGSYCQEIVNSNCHLEHDCIAANINKTLKRIGPITEQLTLLHEIYKNSEAELSLVDIVTYIEILTESSSLQGYIKNTTSPKDAYFGSALTEFGKTVNNFVEKNTHEMWDQLPTNRRRLHLTKLMHAAEHVTLQISQNIQKNTQFDMNSTDLALKVFVFDSVHMKHTHPHMNVDGGYVKISPRRKSAYDPNGNVIVAFLCYRSIGPLLSSSDDFLLGAQSDNSKGKEKVISSVISASISSNPPTLYELEKITFTLSHVKLSDKHQTQCAFWNYSVDDMNNGSWSSEGCELTYSNDTHTSCRCSHLTHFAILMSPSTSIEVKDYNILTRITQLGIIISLICLAICIFTFWFFSEIQSTRTTIHKNLCCSLFLAQLVFLVGININTNKLVCSIIAGLLHYFFLAAFAWMCIEGIYLYLIVVGLIYNKGFLHKNFYIFGYLSPAVVVGFSASLGYRYYGTTKVCWLSTENNFIWSFIGPACLIILVNLLAFGVIIYKVFRHTAGLKPEVSCYENIRSCARGALALLFLLGTTWTFGVLHVVHASVVTAYLFTVSNAFQGMFIFLFLCVLSRKIQEEYYRLFKNVPCCFECLR
Protein: Aladin WD repeat nucleoporin (F8VZ44)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKLQTQKKRLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASSTIVPSLKHRLQRNVASLAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPSGGRLLSASPVDAAIRVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKILATTPSAVFRVWEAQMWTCERWPTLSGRCQTGCWSPDGSRLLFTVLGEPLIYSLSFPERCGEGKGCVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGKPRVQDGKPVILLFRTRNSPVFELLPCGIIQGEPGAQPQLITFHPSFNKGALLSVGWSTGRIAHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHDLPLFTETSPTSAPWDPLPGPPPVLPHSPHSHL
Protein: Inosine monophosphate dehydrogenase 1 (C9K0R9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEPESDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVL
Protein: Protein fantom (Nephrocystin-8) (RPGR-interacting protein 1-like protein) (RPGRIP1-like protein) (Q68CZ1)
Organism: Homo sapiens (Human)
Function: Negatively regulates signaling through the G-protein coupled thromboxane A2 receptor (TBXA2R). May be involved in mechanisms like programmed cell death, craniofacial development, patterning of the limbs, and formation of the left-right axis (By similarity). Involved in the organization of apical junctions; the function is proposed to implicate a NPHP1-4-8 module. Does not seem to be strictly required for ciliogenesis. Involved in establishment of planar cell polarity such as in cochlear sensory epithelium and is proposed to implicate stabilization of disheveled proteins (By similarity). Involved in regulation of proteasomal activity at the primary cilium probably implicating association with PSDM2 (By similarity).
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8CG73, ECO:0000269|PubMed:21685204}. Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8CG73}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8CG73}. Note=In cultured renal cells, it localizes diffusely in the cytoplasm but, as cells approach confluence, it accumulates to basolateral tight junctions. Localizes to the ciliary transition zone. {ECO:0000250|UniProtKB:Q8CG73}.
Interaction partners:
- Nephrocystin-4
- Nephrocystin-1
- X-linked retinitis pigmentosa GTPase regulator
- Centrosomal protein of 290 kDa
- Meckelin
- Coiled-coil and C2 domain-containing protein 2A
- Transmembrane protein 216
- Jouberin
- Nephrocystin-3
- 26S proteasome non-ATPase regulatory subunit 2
Sequence:
MSGPTDETAGDLPVKDTGLNLFGMGGLQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKNTITLEVHQAYSTEYETIAACQLKFHEILEKSGRIFCTASLIGTKGDIPNFGTVEYWFRLRVPMDQAIRLYRERAKALGYITSNFKGPEHMQSLSQQAPKTAQLSSTDSTDGNLNELHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDLDRYLKSESLSFYVFDDSDTQENIYIGKVNVPLISLAHDRCISGIFELTDHQKHPAGTIHVILKWKFAYLPPSGSITTEDLGNFIRSEEPEVVQRLPPASSVSTLVLAPRPKPRQRLTPVDKKVSFVDIMPHQSDETSPPPEDRKEISPEVEHIPEIEINMLTVPHVPKVSQEGSVDEVKENTEKMQQGKDDVSLLSEGQLAEQSLASSEDETEITEDLEPEVEEDMSASDSDDCIIPGPISKNIKQSLALSPGLGCSSAISAHCNFRLPGSSDFPASASQVDGITGACHHTQPSEKIRIEIIALSLNDSQVTMDDTIQRLFVECRFYSLPAEETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDILKAILQKQEMPNRSLRFTVVSDPPEDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHALQSVYKQYRDDLEA
Protein: Tyrosyl-DNA phosphodiesterase 1 (Tyr-DNA phosphodiesterase 1) (EC 3.1.4.-) (Protein expressed in male leptotene and zygotene spermatocytes 501) (MLZ-501) (Q8BJ37)
Organism: Mus musculus (Mouse)
Function: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20339383}. Cytoplasm {ECO:0000269|PubMed:17948061}.
Interaction partners:
- DNA topoisomerase 1
- DNA repair protein XRCC1
- Aprataxin
- Bifunctional polynucleotide phosphatase/kinase
- DNA ligase 3
- Tyrosyl-DNA phosphodiesterase 2
- DNA polymerase beta
- DNA topoisomerase I, mitochondrial
- X-ray repair cross-complementing protein 6
- Structure-specific endonuclease subunit MUS81
Sequence:
MSQESSYGKWTISSSDESEDEKPKPDKPSASSHPQAGQGVSKELIYTCSEARKVAHKRQISPVKFNDADSVLPHKKQKSDSPEGLGWCLSSSDDDQQPDVTQQEQPKRVLPQEKKHVSSPDVTTAQKVVDRSPPASLRPQRADDEYETSGEGQDIWDMLDKGNPFQFYLTRVSGIKAKYNSKALHIKDILSPLFGTLVSSAQFNYCFDVDWLIKQYPPEFRKNPILLVHGDKREAKADLHAQAKPYANISLCQAKLDIAFGTHHTKMMLLLYEEGLRVVIHTSNLIREDWHQKTQGIWLSPLYPRIDQGSHTAGESSTRFKADLTSYLTAYNAPPLQEWIDIIQEHDLSETNVYLIGSTPGRFQGSHRDNWGHFRLRKLLQAHAPSTPKGECWPIVGQFSSIGSLGPDESKWLCSEFKDSLLALREEGRPPGKSAVPLHLIYPSVENVRTSLEGYPAGGSLPYSIQTAEKQRWLHSYFHKWSAETSGRSNAMPHIKTYMRPSPDFSKLAWFLVTSANLSKAAWGALEKNGTQLMIRSYELGVLFLPSAFGLDTFKVKQKFFSSSCEPTASFPVPYDLPPELYRSKDRPWIWNIPYVKAPDTHGNMWVPS
Protein: Equilibrative nucleoside transporter 3 (F5GU99)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDVTTFLQFNVFAFIGSIVAGRKQWPAPNKLWIPVYLRLLYIPFFIFCNYLPETRSLPVFFESTWLFVIIAASMSFGSGYFSGLAMMYTSKTVDPSKAQVAGMMAGFFLISGIVSGLIFTMVIKMVVTA
Protein: Anthranilate synthase component 1 (AS) (ASI) (EC 4.1.3.27) (P00897)
Organism: Serratia marcescens
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable).
Interaction partners:
- Fused indole-3-glycerolphosphatesynthetase/N-
- Anthranilate phosphoribosyltransferase
- Aminodeoxychorismate synthase component 2
- Anthranilate synthase component 2
- Tryptophan synthase, beta subunit
- Tryptophan synthase alpha chain
- Chorismate synthase
- Fused chorismate mutase P/prephenate dehydratase.
- Fused chorismate mutase T/prephenate dehydrogenase.
- Putative glycosyl transferase.
Sequence:
MNTKPQLTLLKVQASYRGDPTTLFHQLCGARPATLLLESAEINDKQNLQSLLVIDSALPITALGHTVSVQALTANGPALLPVLDEALPPEVRNQARPNGRELTFPAIDAVQDEDARLRSLSVFDALRTLLTLVDSPADEREAVMLGGLFAYDLVAGFENLPAVRQDQRCPDFCFYLAETLLVLDHQRGSARLQASVFSEQASEAQRLQHRLEQLQAELQQPPQPIPHQKLENMQLSCNQSDEEYGAVVSELQEAIRQGEIFQVVPSRRFSLPCPAPLGPYQTLKDNNPSPYMFFMQDDDFTLFGASPESALKYDAGNRQIEIYPIAGTRPRGRRADGSLDLDLDSRIELEMRTDHKELAEHLMLVDLARNDLARICQAGSRYVADLTKVDRYSFVMHLVSRVVGTLRADLDVLHAYQACMNMGTLSGAPKVRAMQLIAALRSTRRGSYGGRVGYFTAHRHLDTCIVIRSAYVEDGHRTVQAGAGVVQDSIRRREADETRNKARAVLRAIATAHHAKEVF
Protein: Translin-associated factor X-interacting protein 1 (Trax-interacting protein 1) (Q99P25)
Organism: Mus musculus (Mouse)
Function: Possible role in spermatogenesis.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12036294}.
Interaction partners:
- Leucine-rich repeat-containing protein 23
- Radial spoke head 14 homolog
- Cilia- and flagella-associated protein 161
Sequence:
MANLQERKSFSKPRISIQASGGTPEAKGIEKRKLSQKRRTLPLQLSLGGHLSPWPTYTSGQTVLHNRKPCSDDSRNRANSCQQQSMSISKPKYLEQLENYLRKELLLLDLSTDSAQELRLQPYREIFEFFIEDFKTYKPLLSSIKNAYEVMLAHQKERIRSLEPLKAKIVTMNEDCSERVLAMRAEERYEISVLKKEKMNLLKLIDKKNEEKISLQSEVAKLRRSLAEEYLRYLTERDARKILIGDLNELRYQQEDMSLAQTPGVWGEDPVKLTLALKMTRQDLTRTQMELNTMKANSGDVVPRRDLEMQEKTNMELQEQLESLKADYEEVQKEHELLLQLHMSTLKERDQFYNELQEIQRTSTPRPDWTKCESIIAGGPERWLVLAEGKNSDQLVDVLLEEIGMGLLREKDFFPGLGFGDAIPPFLRFDGPVKNKKPSKKEVVNLLKDAWKERIAEEQKEPFPDFFFNFLERRFGVNDAMAWAYTIFENIKLFRSSEIMNQFYAVLMGKNLESVYINQKKTLSHLLKELLSVDTQNEGSITMEQFSTILKTTFPLKKEEQIQELMEAVGWGPDSSNTDMLNYRSLFNEDEEGQSEPFVQRLWEQYESDKEAYLEELKQELDLDPLEDVTLLKMRGTLMNIDPTMDKQTLSAYLSQAYQIPAIDVPLEDEEKQGIISIKVETALDRLRMADTKRVGPREPDPAS
Protein: Cilia- and flagella-associated protein 410 (C21orf-HUMF09G8.5) (Leucine-rich repeat-containing protein 76) (YF5/A2) (O43822)
Organism: Homo sapiens (Human)
Function: Plays a role in cilia formation and/or maintenance (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Involved in DNA damage repair.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9325172}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26294103}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:27548899}. Cytoplasm {ECO:0000269|PubMed:26290490}. Note=Colocalizes with NEK1 and SPATA7 at the basal body. {ECO:0000269|PubMed:26167768}.
Interaction partners:
Sequence:
MKLTRKMVLTRAKASELHSVRKLNCWGSRLTDISICQEMPSLEVITLSVNSISTLEPVSRCQRLSELYLRRNRIPSLAELFYLKGLPRLRVLWLAENPCCGTSPHRYRMTVLRTLPRLQKLDNQAVTEEELSRALSEGEEITAAPEREGTGHGGPKLCCTLSSLSSAAETGRDPLDSEEEATSGAQDERGLKPPSRGQFPSLSARDASSSHRGRNVLTAILLLLRELDAEGLEAVQQTVGSRLQALRGEEVQEHAE
Protein: Cuticle collagen dpy-7 (Protein dumpy-7) (P34688)
Organism: Caenorhabditis elegans
Function: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Mutations in dpy-7 affects the body shape.
Interaction partners:
- LiPocalin-Related protein
- Cuticle collagen dpy-2
- Fungal lipase-like domain-containing protein
- WaRThog
- SSD domain-containing protein
- YitH/HolE acetyltransferase
- Apple domain-containing protein
- LiPocalin-Related protein
- Apple domain-containing protein
- Uncharacterized protein
Sequence:
MEKPSSGANHVAKATVSLSIASVLILGAVLTMLSIQLDEAHERLQNRMGSFKFVARNIWHDIVLVKSNGRIKRQYGGYGSDSAQSDNQQCTSCVQLRCPPGPIGPPGVSGEPGMDGANGRPGKPGLDGLDVPLDPEPAFPCVICPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPPGDDSIGGTGIKGPPGPPGPRGPKGPPGSNGLPSQNSGPPGPIGEMGPPGPPGPRGEPGPPGPFGPPGDSGEPGGHCPSSCGVQEIVAPSVSELDTNDEPEKPARGGYSGGGYGKK
Protein: Uncharacterized protein (O07764)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAEAFDATQAVARILAEHGPLSEDDIARRLLDSGVADPDAVLRALRLETEWPARQLVDDRWVWLPTLLAGRVFTHRLGADEAVHDMLGVTPDLDPITTLCEHEEYGRLADGSAARIVLAGYDEELLERRGIPDEAIDPGGALLLEPGTLATLGAAAGDLVGVRLTAAGLVLERIGTAGADTSVGARLAELVDPDEPAFFPAAVWTACVDDPAAFTEPVAPLREILDQHGLTHEDDWLAPGGFNFDAWRFENRCELLAFRHDLDPNDAVALYTLIKLHETMSLLLEATDPDELPRDVLATAAETATETGSDSLVDLLGDIGAALADPLLAELLVAETVGTDSGGAAALGLLTEMLEPKVPRAARVAVRWLRAVALDRIGDVEAAERELLAAESMDTEWPLPLLDLARIASDRGDAERGLALLRRAGTEPDHPLVRLLERHRAQPRRDLGRNEACWCGSGRKYKKCHLGREALPLAERVDWLYAKASQHALSGDWTGLLAEVSYERFRYADSDDEDALAAALADPLVLDAVLFEGGAFAEFLEVRGSLLPDDERLLAEQWLLVERSVFEVEHVQPGEGVIVRDVRTGDTHEVHERAASRQLRAGQLICARPVPAGDTMVFFGGIEPVALHERAVLIELLDDEPDPVTLVAQLSRRFAPPTLVNTEGDSLAICEASVRVDDPAGIQGALDGVYDRVDGEEPPRWIEHVTNDGMLRVRATLVLDGDTLRVETNSEPRMDRVLATLTRLDPAMTVLDDDRRPLRNTREAAALAEQMPVTGAGAPDPDSPELAAALEEFIRDYETSWLDQPIPALDGHTPRQAADDPTRRADLIKLLDTFPAGAGARGGMDADRLRTALGL
Protein: MYB transcription factor (MYB40-putative transcription factor) (Q9LY95)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKPCCDKIGLKRGPWTIEEDHRLMNFILNNGIHCWRIVPKLAGLLRCGKSCRLRWINYLRPDLKRGGFTDAEEDRIMELHSQLGNRWSKIASHFSGRTDNEIKNHWNTKIKKKMKHLGLDPATHKPMNDITHQTDPNQDKKPNMCSTINEGEEIKDQTPKDDVITETTKTLMLSDNDEELVAKNCKILCAEEVDLESLFETQCNEISSSSFSSLCSNISRSESSSYLAEDSISLEQWDLDMTDPFVPWDLFANLDDNLFLL
Protein: QRFP-like peptide (C3Z6E6)
Organism: Branchiostoma floridae (Florida lancelet) (Amphioxus)
Function: Ligand for the G-protein coupled receptor QRFPR.
Subcellular location: Secreted {ECO:0000305|PubMed:25449662}.
Interaction partners:
Sequence:
MGVRVMRSRICVIGLLVLMLTQSEAYSFREKSWRTSPYYRQYGGYFRRRDGGDQAPSFTSTGNGEDVSNGLDDDAGIYLSDQAGDDGISPADKRSAMLQQLAQQLKNRPREKGGFTFRFGKRESRRSFGSD
Protein: Major outer membrane protein P.IB (PIB) (Protein IB) (Porin) (P18195)
Organism: Neisseria gonorrhoeae
Function: Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity.
Subcellular location: Cell outer membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MKKSLIALTLAALPVAATADVTLYGAIKAGVQTYRSVEHTDGKVSKVETGSEIADFGSKIGFKGQEDLGNGLKAVWQLEQGASVAGTNTGWGNKQSFVGLKGGFGTIRAGSLNSPLKNTDANVNAWESGKFTGNVLEISGMAKREHRYLSVRYDSPEFAGFSGSVQYAPKDNSGSNGESYHVGLNYQNSGFFAQYAGLFQRYGEGTKKIEYEHQVYSIPSLFVEKLQVHRLVGGYDNNALYVSVAAQQQDAKLYGARRANSHNSQTEVAATAAYRFGNVTPRVSYAHGFKGTVDSADHDNTYDQVVVGAEYDFSKRTSALVSAGWLQEGKGADKIVSTASAVVLRHKF
Protein: Integrator complex subunit 13 (H0YH12)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
GDSHLGGGSREGSFKETITLKWCTPRTNNIELHYCTGAYRISPVDVNSRPSSCLTNFLLNGRSVLLEQPRKSGSKVISHMLSSHGGEIFLHVLSSSRSILEDPPSISEGCGGRVTDYRITVVPLASVIVKESLTEEDVLNCQKTIYNLVDMERKNDPLPISTVGTRGKGPKRDEQYRIMWNELETLVRAHINNSEKHQRVLECLMACRSKPPEEEERKKRGRKREDKEDKSEKAVKDYEQEKSWQDSERLKGILERGKEELAEAEIIKDSPDSPEPPNKKPLVEMDETPQVEKSKGPVSLLSLWSNRINTANSRKHQEFAGRLNSVNNRAELYQHLKEENGMETTENGKASRQ
Protein: Cyclic AMP-responsive element-binding protein 3-like protein 4 (cAMP-responsive element-binding protein 3-like protein 4) (Androgen-induced basic leucine zipper protein) (AIbZIP) (Attaching to CRE-like 1) (ATCE1) (Cyclic AMP-responsive element-binding protein 4) (CREB-4) (cAMP-responsive element-binding protein 4) (Transcript induced in spermiogenesis protein 40) (Tisp40) (hJAL) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 4] (Q8TEY5)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that may play a role in the unfolded protein response. Binds to the UPR element (UPRE) but not to CRE element. Preferentially binds DNA with to the consensus sequence 5'-T[GT]ACGT[GA][GT]-3' and has transcriptional activation activity from UPRE. Binds to NF-kappa-B site and has transcriptional activation activity from NF-kappa-B-containing regulatory elements (By similarity).
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=May also be located in Golgi apparatus.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 4]: Nucleus. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. {ECO:0000250}.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 3
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-responsive element-binding protein 5
- cAMP-responsive element modulator
- CREB-regulated transcription coactivator 2
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- Cyclic AMP-dependent transcription factor ATF-6 beta
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Cyclic AMP-responsive element-binding protein 3-like protein 2
Sequence:
MDLGIPDLLDAWLEPPEDIFSTGSVLELGLHCPPPEVPVTRLQEQGLQGWKSGGDRGCGLQESEPEDFLKLFIDPNEVYCSEASPGSDSGISEDPCHPDSPPAPRATSSPMLYEVVYEAGALERMQGETGPNVGLISIQLDQWSPAFMVPDSCMVSELPFDAHAHILPRAGTVAPVPCTTLLPCQTLFLTDEEKRLLGQEGVSLPSHLPLTKAEERVLKKVRRKIRNKQSAQDSRRRKKEYIDGLESRVAACSAQNQELQKKVQELERHNISLVAQLRQLQTLIAQTSNKAAQTSTCVLILLFSLALIILPSFSPFQSRPEAGSEDYQPHGVTSRNILTHKDVTENLETQVVESRLREPPGAKDANGSTRTLLEKMGGKPRPSGRIRSVLHADEM
Protein: Nuclear receptor coactivator 4 (NCoA-4) (Androgen receptor coactivator 70 kDa protein) (70 kDa AR-activator) (70 kDa androgen receptor coactivator) (Androgen receptor-associated protein of 70 kDa) (Ferritin cargo receptor NCOA4) (Ret-activating protein ELE1) (Q13772)
Organism: Homo sapiens (Human)
Function: Enhances the androgen receptor transcriptional activity in prostate cancer cells. Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:25327288}. Autolysosome {ECO:0000269|PubMed:25327288}. Nucleus {ECO:0000269|PubMed:24910095}. Chromosome {ECO:0000269|PubMed:24910095}.
Interaction partners:
- Ferritin heavy chain
- Androgen receptor
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Ferritin light chain
- Coiled-coil domain-containing protein 6
- Protein patched homolog 1
- Protein patched homolog 2
- E3 ubiquitin-protein ligase RNF14
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GABA type A receptor associated protein like 1
Sequence:
MNTFQDQSGSSSNREPLLRCSDARRDLELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLYEQVDLIYQLKEETLQQQAQQLYSLLGQFNCLTHQLECTQNKDLANQVSVCLERLGSLTLKPEDSTVLLFEADTITLRQTITTFGSLKTIQIPEHLMAHASSANIGPFLEKRGCISMPEQKSASGIVAVPFSEWLLGSKPASGYQAPYIPSTDPQDWLTQKQTLENSQTSSRACNFFNNVGGNLKGLENWLLKSEKSSYQKCNSHSTTSSFSIEMEKVGDQELPDQDEMDLSDWLVTPQESHKLRKPENGSRETSEKFKLLFQSYNVNDWLVKTDSCTNCQGNQPKGVEIENLGNLKCLNDHLEAKKPLSTPSMVTEDWLVQNHQDPCKVEEVCRANEPCTSFAECVCDENCEKEALYKWLLKKEGKDKNGMPVEPKPEPEKHKDSLNMWLCPRKEVIEQTKAPKAMTPSRIADSFQVIKNSPLSEWLIRPPYKEGSPKEVPGTEDRAGKQKFKSPMNTSWCSFNTADWVLPGKKMGNLSQLSSGEDKWLLRKKAQEVLLNSPLQEEHNFPPDHYGLPAVCDLFACMQLKVDKEKWLYRTPLQM
Protein: Uncharacterized bolA-like protein C8C9.11 (O14280)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Monothiol glutaredoxin-4
- UV-induced protein uvi31
- Monothiol glutaredoxin-3
- Monothiol glutaredoxin-5
- Iron-sensing transcriptional repressor
- Uncharacterized peptidase C22G7.01c
- CCAAT-binding factor complex subunit php4
- Fe-S cluster assembly protein dre2
- Transcriptional activator hap2
Sequence:
MVNAQQLELLIQNTLEPTHIEIQDMSGGCGQNFEVIIVSPLFEGKSTLARHRLVNHKLQEVIKDIHAFTQKCYSPAQWEALQAK
Protein: Uncharacterized protein (Q38E16)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleotide exchange factor Fes1 domain-containing protein
- Heat shock protein, putative
- Glucose-regulated protein 78, putative
- Heat shock 70 kDa protein, putative
- Lipophosphoglycan biosynthetic protein, putative
- Heat shock protein, mitochondrial, putative
- Heat shock protein 83
- Heat shock protein 70
- Heat shock protein 70, putative
- Heat shock 70 kDa protein, putative
Sequence:
MRVLANEIRRMLVAFLLTAAFGYDVTSANVIGVDFGSDYIEVAGPINGVNVDIILNEQSHRKTDNYIGFRNGERSIGAQAKSLAARFPTNMIAMINHLVGITYNSSDFANFKKLQCEFDPHPEERGTVGFRFEDNNDTYTAEEIYAMMLNYCRSISEKAGVPNPQNVVITLPFHSSLGRRQTILEAARLVHINTLGLLHSTTATALYYGVRRRGFGNRTVHLLVYDIGSTHTEVGVYKFSPPVQEQGKRTKNVESFGTLTTMGIVSDATLGGRALDSCIAKGIEAEAISKMKISPVLGGSTVSQRKAQFSLFRAAKRAREVLSVNSKTPVTVEGIAPDRDFSTEVSRKEFETNCSELLKRFPRVAQEAVTKSSLTLKDIDAFEMMGGASRTPKIISDLSTFWGKEVNRTLNSDEAAAMGAAYYALRLSPHYRPHSFRIIERVPYTFLFAVSPEVKNSSNSKRMLANNPIIGSRWSITVNRTDDFSIQLFDSDARIGNVNITGVKGALERLGFFQPKLNHTNNSHIIRIQVRFNESGLLEVEEAGVFYRYAVNVSSSTKTTGVQADSNSSNESGYVVEMKRKSARLSARVTFTNPEPLSYELLNNSRVKIFQLLEKERKKHEAATAKNNLETYLFWAKTEGILENTTALEPYTPEEVNSLKNALAEAQEWLEDGDGSNESCSKEEYENKLATLKELVKNSGKNKNTTNTTSGSDDAVKGDL