wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)] (P37295)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Function: Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and from lycopene to beta-carotene via the intermediate gamma-carotene and from 3,4-didehydrolycopene to torulene (lycopene cyclase). Torulene is further processed to the acidic carotenoid neurosporaxanthin. The cyclase preferentially catalyzes single cyclizations at only one end of the substrate to produce monocyclic carotenoids. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme al-2 first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase al-1 then introduces 5 desaturations to lead to 3,4-didehydrolycopene via the intermediates phytofluene, zeta-carotene, neurosporene and lycopene. Al-2 cyclase activity then converts 3,4-didehydrolycopene into torulene. Al-2 can also convet lycopene into gamma-carotene which in turn is converted to beta-carotene by an additional al-2 cyclization reaction. Torulene is the substrate of the dioxidase cao-2 that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase ylo-1 mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phytoene desaturase
- Geranylgeranyl pyrophosphate synthase
- Carotenoid dioxygenase
- Farnesyl pyrophosphate synthase
- Probable hexaprenyl pyrophosphate synthase, mitochondrial
- 3-keto-steroid reductase
- Squalene monooxygenase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Hydroxymethylglutaryl-CoA synthase
- ditrans,polycis-polyprenyl diphosphate synthase [
Sequence:
MYDYAFVHLKFTVPAAVLLTAIAYPILNRIHLIQTGFLVVVAFTAALPWDAYLIKHKVWSYPPEAIVGPRLLGIPFEELFFFVIQTYITALVYILFNKPVLHALHLNNQQNPPAWMRVVKVTGQVVLVALSVWGWNAAQVHQETSYLGLILVWACPFLLAIWTLAGRFILSLPWYATVLPMFLPTFYLWAVDEFALHRGTWSIGSGTKLDFCLFGKLDIEEATFFLVTNMLIVGGMAAFDQYLAVIYAFPTLFPKVNRYPTTHMLLQSRLINTSRYDLERIEGLREAVERLRLKSRSFYLANSLFSGRLRIDLILLYSFCRLADDLVDDAKSRREVLSWTAKLNHFLDLHYKDADATEDPKKKAERIDAYIKTAFPPCAYQALHLLPTHILPPKPLYDLIKGFEMDSQFTFHGTSDSTDLQYPIADDKDLENYAIYVAGTVGELCIALIIYHCLPDMSDTQKRELETAACRMGIALQYVNIARDIVVDARIGRVYLPTTWLKKEGLTHKMVLENPEGPEVIERMRRRLLENAFELYGGARPEMQRIPSEARGPMIGAVENYMAIGRVLRERKEGTVFVRMEGRATVPKRRRLSTLLRALYEQ
Protein: Guanine nucleotide binding protein gamma 12 (Q45QK0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
Sequence:
LEASIERIKVSKASADLMSYCEEHARSDPLLMG
Protein: adenosine deaminase (EC 3.5.4.4) (Q8IHF6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGDVEFQNVQEIRGTPQNAMRMIRLELDEEENRRQMSSSKYGGVCFHVAIAVMLCVMVLVLICSAPLGENMSNLTSEERHARLRQIYIEKERRQRLGSRMGLSPLEEEANDRLMAIRQVDEEFYNLWRNYHSQPPPFLKHLNIIDTNLYAALKSMPKGGFLHVHDSGMLRMEILIDLIYRDNLWVCVNLEQDFEDFRFSRYFPHIPPAEDYQCNWMLMSNFFQLESRLEFENRLRKILTVRPEGYKSSSELARHLRRHQRIIHGLITFRPIWSEFIFTMLSDFYADGVHYVELRSSLPNMYDLDGNNFTILETAEALVSVSNIFKNSFKDFIGIKLIYAPSRNLNDSRMDEYLENARLLKLHFPNFFAGFDLNTFGDECNLPLLENVTQLLRIGKNIDFYFHAGESRCPDSSRPDANLLEALLLQSKRIGNAVNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSAPLTDDFYVAFVGVISGWGDLRLLKQFALNSFLFSSLSETEKNMAVSKWQCSWNRWVRNLVNSSGY
Protein: Prohibitin-2 (B-cell receptor-associated protein BAP37) (D-prohibitin) (Repressor of estrogen receptor activity) (Q99623)
Organism: Homo sapiens (Human)
Function: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:28017329}. Cytoplasm {ECO:0000269|PubMed:17565718, ECO:0000269|PubMed:19496786, ECO:0000269|PubMed:32276428}. Nucleus {ECO:0000269|PubMed:17565718, ECO:0000269|PubMed:19496786, ECO:0000269|PubMed:20959514}. Cell membrane {ECO:0000269|PubMed:22997079, ECO:0000269|PubMed:24003225}. Note=Localizes within both nucleus and cytoplasm in proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. {ECO:0000269|PubMed:17565718}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane {ECO:0000305|PubMed:31522117}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane {ECO:0000305|PubMed:31522117}.
Interaction partners:
- Prohibitin 1
- Estrogen receptor
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Brefeldin A-inhibited guanine nucleotide-exchange protein 3
- Histone deacetylase 1
- Elongation factor Tu, mitochondrial
- Mitofusin-1
- Dynamin-like GTPase OPA1, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK
Protein: Fibromodulin (Keratan sulfate proteoglycan fibromodulin) (Q543D2)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MQWASVLLLAGLCSLSQGQYDEDSHWWIQYLRNQQSTYYDPYDPYPYEPSEPYPYGVEEGPAYAYGAPPPPEPRDCPQECDCPPNFPTAMYCDNRNLKYLPFVPSRMKYVYFQNNQISAIQEGVFDNATGLLWVALHGNQITSDKVGRKVFSKLRHLERLYLDHNNLTRMPGPLPRSLRELHLDHNQISRVPNNALEGLENLTALYLHHNEIQEVGSSMRGLRSLILLDLSYNHLRRVPDGLPSALEQLYLEHNNVYTVPDSYFRGSPKLLYVRLSHNSLTNNGLATNTFNSSSLLELDLSYNQLQKIPPVNTNLENLYLQGNRINEFSISSFCTVVDVMNFSKLQVLRLDGNEIKRSAMPVDAPLCLRLANLIEI
Protein: Right handed beta helix domain-containing protein (Q57ZK8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
METTTHVVNPGEEGAYSSITEAINAAVDGDTVLLKPGLYEELPKVFKDITVTAERDASLTESETIVTNGIVIGSNATLKGLQVRGRVDVRKGHAVIEECDIHHGCDGIRVGEAAKLTVRRSRIHHCESGGDGIYFSTGSMGEVEDCDIYECRVNGVHANNARVVIARNRVRDVLFGFYFRGQSSGSVERNSVEHVSKFGIYVTEGSDPVVQGNMVRECGMHCAFVSQGGKGIWVDNSFDGSMHVHSGCDAKLGSNHVVGRLDVDPPT
Protein: Unconventional myosin-IXa-like (F0IWT2)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ras-like GTP-binding protein rhoA
- Cell division control protein 42 homolog
- CHp/Wrch Rho-like protein homolog
- Rho-GAP domain-containing protein
- Ras-related protein ced-10
Sequence:
MSFDSISAGATGCFPRRAHTINATDDAHTHTVAVYMHSFNPDCENDTVHLEVHKRCTTEELIEKVLAGRAELEGQSVQDFDLFEMMGTPDGQTYKERRLDPGEYPVAVQAIWSRLPVVVDSATPKNRFVFRHRGYRAATGGTRFGSAEVASSIDAFLTKFLVQPQDREYADLCNLPELTEQTLLDNLRERFANGHIYTYIGPILVAVNPFCFFPIYNPKYARLYFQSKRLGSLPPHIFAIADVCYHNMLRIKENQCVVISGESGSGKTESTNHLMSHLISLSQKGSTGCSTEQTLLSAGPVLEAFGNAVTLTNNNSSRFGKFIKINYRENGMVSGANVEIYLLEKSRIIFQTKGERNYHVFYYLLEGADEEERKKYFLLKPHDYKYLNQNEPFALEGVNERNEFDRLRHAMSSVGFCAKTQQTIFGIISAVLLLGNITYIKRHGYHSDESGYIENEEVVDLVANLLHIKTDTLMQALTMKRHVMKTETVVLRYSVSEATNTRDAMAKCIYNSLFHYIVLRINQALLKKDFSAGKGYYIGILDIFGFEDVGSQCNSFEQLCINYANEKLQSYFNQHIFQFEQEEYLKEGISWTNIEYTDNTECVQLFQSKPYGILRLVDEESNINNGTDDSMLAKLNQFLKNNEYYETPQKKEPAFIVAHYAGKVKYQITGFREKNKDLMRQDVLNALKSSTSSVMKTLLGIDPVAVHRWNVLRSVFRAMNAFKQSTRKLQKSESAGHLRVMDSIVTSPRRGSDSALSAFLRGELRCEVPDFCDTSMFNTIRNQARRTPAGKSDDKMSLLKSLQILKEAIGGRRLAKKPSSVSKQFEYSLTRLMSTLANATPYFIRCIKSNNDKIANHFDDNIILRQLRYTGMLETVRIRRAGYSVRIEYPSFVQQYRILLRNGRDSTVDDVKEYIHSHASIDNDNIQYGTNKIFMRDAEKLILDDHLHRTIMQSIDTLQRWFRTMLARKRYLRMKEGIIKIQALIRGSFARAEVRKKALAAQTIQCNWKKYKQRQKYLSIRESVIALQSAYRGASVRKRVGEIPKGNGALNVKKSPFRVRKVHAVNLTKFDLSDPSSLAAFALSDDDSDSDKSTQDGLDDDISEESDAFQDDDAVDVDATFILEDTKLKLIEGADLSHHRRQSLAPTASTTKLKMLRRANSTESNNFSMSRCDDSFTLSPTHSKKKGGAGKLGFQKAKKNLKALFGRNEDEDEPSPGPSFASELTPDVFVAKDHQFKMSRLHRQEICALCNRHLTNFISQAHKCQRCKMCLHKECFVFASSIPCNPTSPVRSPTRLHSPKRPWDLMPHKQRQSSSPIPSTGTFSLTKTKQQIDPGNMLVESTDDLRQFSIFIFNKTRHLNESNAKRDTVVDAVFKKSLRAFHMELLGYEAVLSVEQSVLKYRDVITMFEGLLTKVCLEESVSFPTTLGVNAFRGFLNEYVHVQSKKKRGKEKSSMIKKVGKKRVKSDVAAVHAGHRFRAEAVHVPTYCEVCNQLIWHHEKLYTCVACRISCHKKCQPKVTHPCQMTGKAIDPKTNGGRFFGASLVSIVDDDHTVPTLLDRLFFAIETRALFVEGVYRKSGSLPQVRSIRKVIESTADADSVNLEDIGVHVLTTLVKAFFRELAEPIIIFDLYENFLNVSEVEDMGERVRCLSVMIELLPKPNRAVLDRLMYHLARVADQEAVNKMGCNNLALIFGPCVLRRQDSAHAQEQLNDVARQTGCVQTLIEEKLKQYKATIHNIVELEDASQKVSANLRKIEEHRRNSEPSKFSPNIGTAKQLFEEQLEFLGKQKERLLQELPPLAPVASSEDLSSSDENAIHASSSLSVEEYALDLDAPPVFCLLRYPTKLRPPGPAHRRRPDLDLRRKAFANSRGIVSFYSPV
Protein: Transcription factor Maf (Proto-oncogene c-Maf) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog) (O75444)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator or repressor. 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 (By similarity). 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.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Protein c-Fos
- Nuclear factor erythroid 2-related factor 2
- Transcription factor Jun
- Transcription regulator protein BACH2
- Transcription factor NF-E2 45 kDa subunit
- Endoplasmic reticulum membrane sensor NFE2L1
- Endonuclease 8-like 1 lyase Neil1)
- Nuclear factor erythroid 2-related factor 3
- Paired box protein Pax-6
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MASELAMSNSDLPTSPLAMEYVNDFDLMKFEVKKEPVETDRIISQCGRLIAGGSLSSTPMSTPCSSVPPSPSFSAPSPGSGSEQKAHLEDYYWMTGYPQQLNPEALGFSPEDAVEALISNSHQLQGGFDGYARGAQQLAAAAGAGAGASLGGSGEEMGPAAAVVSAVIAAAAAQSGAGPHYHHHHHHAAGHHHHPTAGAPGAAGSAAASAGGAGGAGGGGPASAGGGGGGGGGGGGGGAAGAGGALHPHHAAGGLHFDDRFSDEQLVTMSVRELNRQLRGVSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHVLESEKNQLLQQVDHLKQEISRLVRERDAYKEKYEKLVSSGFRENGSSSDNPSSPEFFM
Protein: Cch1p (Q5A936)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Mid1p
- Ecm7p
- Calmodulin
- Calcium-transporting ATPase
- Calcium channel YVC1 channel YVC1)
- Transcriptional regulator CRZ1
- Calcineurin subunit B
- Mlc1p
- Mlc2p
- Calcium-transporting ATPase
Sequence:
MDNSNTHSSRGRPGIIINPPTESNLNVHHIPEEEQASYDEDYDPNKTYISDSQYWQRQSSSHHEDDLASIEIPELHQIQDRAPDSLSAHSDKRSSRSGRDILNVLHLSRPSSPRSPHSSTSTPSLGHAIEDEDLDELKEGLNYALGTKENEANWFPVNKLAKSSTHSREENSGDENSSFVNYTTDIPLNDLSPYISNTNTNTNKNKSDTSLKYLVNSPFETRPNSSLHVDPGFLETGSLMSPYPKDGGGASPRIANAISRISDRIAGAGGNSRRNEESTDRLSAVESQTSLPLPTPMSEHFTFFDEYNKSSNKSDKTSIANTSIRNDRDAYSDSNIDGLGLYLQQTNKSQISGTTQHEYSREVPVTDYLRLPKKSHQNNKTNYQEFDTMYLFGKSLGIFTPESKVRQFCYHVCENKFINTFLLIILILQVALLTYRQWNPLVLNGYFVKGYNWADYLLMVINVIYTAEVIGKIIAYGFYDDHIMFDELGLPYPKNEITKEYFSKNYISKILKSLGFFKSRVEKKRQEKFISEDNDKRSSSEDSEIREIDLNDSRQDLLGEANRSFSLKDKYQMDSHHRNYIPLRSQANDPDNLDETTPAPKQMLEAKNTFFKPAPHTFEKLNLKRAFFRSSWQRIDFISMVCFWISLFLSINHYDADHHIMLFRALSCLRILRLCNLTTGTTTILTACKIAIPQLIDVSIFIACFWLFFGIIGVQTFKSSLTRHCVWTNPDDPSDTYVNSGSYCGSYIGLNGEPAAYLMRDGSSSNVIKGYRCPMYSQCISGDNPYNGTLNFDNILQSLEIVFVIMSANTFTDIMYYTMDTDNMAACLFFIGCIFVMTVWLINVFIAIIVASFNITRMEVAEEKKKKREGRRIFKIFGYADQDVQMHEERLEFLKNQNVFLKWYYNLEFFFVICVIIDLFVQCFRRADMSDRRAHLLYRFEASFTGVFMVEIILRFAFYFPNWRLFFRVKRNCFDLFLAVITTIIIIGPIKAALGHAYYWLTVFQVMRAYRVVLWTSITRNLWLKIMGNFKAIFDLALFYFILLFLVSIILARYFEGVVTEDEAGDLDFPMTTLPGVFIALYVITSTENWTEILYGMQQYATTTSSRSFGSIFLIGWFMLSNMIILNIFIAVIAKTLEVSEEAKRKQQLLQFIDTMTNKLQDIEQDSGLLSKIKKKLFRRKQVKDELEEAVVNLLLSGTAVNDFLENDARNEVDDEEEAIRTLPASTWKRWLGVNYWRTLNLFRNNPFYGNKAKGRKVSLENFNPANFARTIVKERKNIVSKQNEFLEANPRYNYVFYVIGPHHPLRRLCQKMVKPSYGERIDGVAPYKPVAEAMVVLMFIATVTLVVIACYMTPIFRMDHAGEAWVFWAEFVFVMVFTVEFAIKVIADGFIFTPNAYTRSSWNLIDFVVLLSLWIETIAYMKNDGKLSRIVRGLKALRALRLLTVSDTAKANFHNTMIAGFWKIINAAVISLCLLLPFSIWGLNIFNGRLGYCVDGSSDMSSCYNEYQNTVFNWQVVSPNVYTNPQLEFNRFASSFATLFEIVSLEGWVDLLNNVMASTGVGTPKETNATPFNGFFVVLFNFISIVFILTLFVSVIISNYSRSTGRAYMTTDQISWYRVKKILVQVKPSKRKNIENLHFIRRFCYRMTVERNPVWTRTLNCVLVLHVIALLLECFPSYDSLNQFRTSIYMIASSMFFVNSIMLFTGQGFSTFMQYKWNIFNLVVSLGAFGTTTGSYFLDPNSPLININKLFLVAILVFVIPRSNRLSQLLRFASASLPSLISLVFTWIIVFLVFAIAMNQIFGMTRLGPNTTGNINLRSVPKALILLFRCSFGEGWNYIMEDFALTQPFCTSKNNLDNSDCGNKQYAYILFIAWNIISMYIFLNMFISLILDSFDYIGHKESYNQLIQREEVRKFKRTWQKFDPQGTGYIKPIELPKLLHSLEGALSFHFYTGSLTIPELCKKWIIRNNPNDPYDVTINYGAIEHTMEQMDIPKIRERRKAYEMFIEEALLCMELNNDPGISFTRILLQLPLYTSFDTSNCFNLIDYLDRRLLIQKVMKRLHTKRVYETIATYVCRWKFKKDNRLGIKDTNLAFDKKLARNSYLRNDQLLINKNPPTIFVTDEGGKRNSSDINVRDSSSLSTERNSVIYGEHSMSSGVYYPSTPVAKLNHSQHVKHSHPKLFIEIPSQKPQREFVTTEDEVKVSPFMDPEEVNEYESKNSGSLVDVGSIEEILESSSWKNAFDELKSDEKRKK
Protein: B- and T-lymphocyte attenuator (B- and T-lymphocyte-associated protein) (CD antigen CD272) (Q7Z6A9)
Organism: Homo sapiens (Human)
Function: Inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2. May interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14. In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12796776}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 14
- Tyrosine-protein phosphatase non-receptor type 11
- V-set domain-containing T-cell activation inhibitor 1
- CD160 antigen
- Programmed cell death 1 ligand 1
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death protein 1
- Lymphocyte activation gene 3 protein
- Tumor necrosis factor ligand superfamily member 14
- Inducible T-cell costimulator
Sequence:
MKTLPAMLGTGKLFWVFFLIPYLDIWNIHGKESCDVQLYIKRQSEHSILAGDPFELECPVKYCANRPHVTWCKLNGTTCVKLEDRQTSWKEEKNISFFILHFEPVLPNDNGSYRCSANFQSNLIESHSTTLYVTDVKSASERPSKDEMASRPWLLYRLLPLGGLPLLITTCFCLFCCLRRHQGKQNELSDTAGREINLVDAHLKSEQTEASTRQNSQVLLSETGIYDNDPDLCFRMQEGSEVYSNPCLEENKPGIVYASLNHSVIGPNSRLARNVKEAPTEYASICVRS
Protein: Transcription factor LATE FLOWERING (OsLF) (Basic helix-loop-helix protein 119) (OsbHLH119) (A0A0P0WQ90)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor involved in the negative regulation of flowering. May be involved in the repression of the flowering factor GI and HD1 by interacting with PIL13 and PIL15 and competing with PRR1. Possesses transactivation activity in yeast.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21549224}.
Interaction partners:
Sequence:
MYMDAFGWSAPAAPCQPSCGPGGDDDDDVLLAAVLGASFELHSLVDGGGNGAAGAVRSDDAYGLDVDLPSHQMSLLRCQDGLSALHGDASPTAAAAAFLDSVDVLPVPAIAGATHDDGGLLDRFAFPNVAETTTVQAAASNTAFSGYSSNTTGGGNISSGESNTYTEVASTPCAVSTTTTTTALPPSKRKLPEKYPVVGTSPTTKTTTTSETAAERRSTKRGAGGSSSITFGGGCHGAGAAAALLGYGRGYEPDTEAIAQVKEMIYRAAAMRPVTLGGPASASDPSSRPPPPPQRPRRKNVRISSDPQTVAARLRRERVSERLRVLQRLVPGGSKMDTATMLDEAASYLKFLKSQLEALETLGNGNGNGNLLHHGYYTGSRNATATAATGSSNSTVLAFGRDGLAGFVKSNRNLQL
Protein: Chaperone protein ClpB3, chloroplastic (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 3) (Casein lytic proteinase B3) (Protein ALBINO OR PALE GREEN 6) (Q9LF37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone essential for chloroplast development and seedling viability. Mediates internal thylakoid membrane formation and confers thermotolerance to chloroplasts during heat stress.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16995899, ECO:0000269|PubMed:17144892}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 4, chloroplastic
- Heat shock 70 kDa protein 4
- ATP-dependent Clp protease proteolytic subunit-related protein 2, chloroplastic
- Heat shock protein 90-5, chloroplastic
- Heat shock 70 kDa protein 6, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 6, chloroplastic
- Chaperonin CPN60, mitochondrial
- Heat shock 70 kDa protein 5
Sequence:
MATATTTATAAFSGVVSVGTETRRIYSFSHLQPSAAFPAKPSSFKSLKLKQSARLTRRLDHRPFVVRCEASSSNGRLTQQEFTEMAWQSIVSSPDVAKENKQQIVETEHLMKALLEQKNGLARRIFSKIGVDNTKVLEATEKFIQRQPKVYGDAAGSMLGRDLEALFQRARQFKKDLKDSYVSVEHLVLAFADDKRFGKQLFKDFQISERSLKSAIESIRGKQSVIDQDPEGKYEALEKYGKDLTAMAREGKLDPVIGRDDEIRRCIQILSRRTKNNPVLIGEPGVGKTAISEGLAQRIVQGDVPQALMNRKLISLDMGALIAGAKYRGEFEDRLKAVLKEVTDSEGQIILFIDEIHTVVGAGATNGAMDAGNLLKPMLGRGELRCIGATTLDEYRKYIEKDPALERRFQQVYVDQPTVEDTISILRGLRERYELHHGVRISDSALVEAAILSDRYISGRFLPDKAIDLVDEAAAKLKMEITSKPTALDELDRSVIKLEMERLSLTNDTDKASRERLNRIETELVLLKEKQAELTEQWEHERSVMSRLQSIKEEIDRVNLEIQQAEREYDLNRAAELKYGSLNSLQRQLNEAEKELNEYLSSGKSMFREEVLGSDIAEIVSKWTGIPVSKLQQSERDKLLHLEEELHKRVVGQNPAVTAVAEAIQRSRAGLSDPGRPIASFMFMGPTGVGKTELAKALASYMFNTEEALVRIDMSEYMEKHAVSRLIGAPPGYVGYEEGGQLTETVRRRPYSVILFDEIEKAHGDVFNVFLQILDDGRVTDSQGRTVSFTNTVIIMTSNVGSQFILNNTDDDANELSYETIKERVMNAARSIFRPEFMNRVDEYIVFKPLDREQINRIVRLQLARVQKRIADRKMKINITDAAVDLLGSLGYDPNYGARPVKRVIQQNIENELAKGILRGDFKEEDGILIDTEVTAFSNGQLPQQKLTFKKIESETADAEQEEAAFSK
Protein: Transmembrane 4 L6 family member 20 (Q53R12)
Organism: Homo sapiens (Human)
Function: Polytopic transmembrane protein that inhibits regulated intramembrane proteolysis (RIP) of CREB3L1, inhibiting its activation and the induction of collagen synthesis. In response to ceramide, which alters TM4SF20 membrane topology, stimulates RIP activation of CREB3L1. Ceramide reverses the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20, this mechanism is called 'regulated alternative translocation' (RAT) and regulates the function of the transmembrane protein.
Subcellular location: Membrane {ECO:0000269|PubMed:23810381}; Multi-pass membrane protein {ECO:0000269|PubMed:23810381}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25310401}; Multi-pass membrane protein {ECO:0000269|PubMed:25310401}. Note=Ceramide alters the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20. {ECO:0000269|PubMed:27499293}.
Interaction partners:
Sequence:
MTCCEGWTSCNGFSLLVLLLLGVVLNAIPLIVSLVEEDQFSQNPISCFEWWFPGIIGAGLMAIPATTMSLTARKRACCNNRTGMFLSSLFSVITVIGALYCMLISIQALLKGPLMCNSPSNSNANCEFSLKNISDIHPESFNLQWFFNDSCAPPTGFNKPTSNDTMASGWRASSFHFDSEENKHRLIHFSVFLGLLLVGILEVLFGLSQIVIGFLGCLCGVSKRRSQIV
Protein: PPPDE domain-containing protein (Q382J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGGCCRPSSKSLKDSKSTRLKQQCPPAESKRGQLSSEQSSPETSEDEGRCRSVGMGVPVFLNIYNLQNKVDKTTYNLNARIGLGIYHTGMEIFSTEWAFSGSTRPIPGVCGITCGRPREMLPKYLFEKSKLLGYLPRGTSIRQILAIVGKLRPEWEASKYHMLRRNCNHFTKAFRDSLEAEFPEAGLKKIPAYINRAARFARVLVPRAFVPSVRQPIHSISPAAERANPENVSFLRLAENKRGSDSSRRVPREEEGVIADAKVLRTREELEAMTVRNLRTLMWLNWLSLERCRDKRDMVEALLRHQMAQQQQQQRRQHQHPHGEHRQRQQRSE
Protein: Glutamate receptor interacting protein 2 (E0CXS4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLAVSLKWRLGVVRRRPKDDGPYSKGGKDTAGADGALVCRRQSIPEEFRGITMVELIKREGSTLGLTISGGTDKDGKPRVSNLRPGGLAARSDLLNVGDYIRSVNGIHLTRLRHDEIITLLKNVGERVVLEVEYELPPPAPENNPRIISKTVDVSLYKEGNSFGFVLRGGAHEDLHKSRPLVLTYVRPGGPADREGSLKVGDRLLSIDGIPLHGASHATAIATLQQCSHEALFQVEYDVATPDTVANASGPLVVEIAKTPGSALGISLTTGSHRNKPAITIDRIKPASVVDRSGALHAGDHILAIDGTSTEHCSLVEATKLLASVTEKVRLEILPSPQSRRPLKPPEAAVSSTPFSSPTMNPAFPCANASTLPRGPMSPRTTAGRRRQRRKEHRSSLSLASSTVGPGGQIVHTETTEVVLCGDPLSGFGLQLQGGIFATETLSSPPLVRFIEPDSPAERCGLLQVGDRVLAINGIATEDGTMEEANQLLRDAALARKVVLEIEFDVAESVIPSSGTFHVKLPKRRGVELGITISSASRKRGEPLIISDIKKGSVAHRTGTLEPGDKLLAIDNIRLDHCPMEDAVQILRQCEDLVKLKIRKDEDNSDEQESSGAVSYTVELKRYGGPLGITISGTEEPFDPIIISGLTKRGLAERTGAIHVGDRILAINSVSLKGRPLSEAIHLLQVAGETVTLKIKKQLDRPLLPRQSGSLSEASDVDEDPPEALKGGLLATRFSPAVPSVDSAVESWGSSATDGGFGGTGSYTPQVAVRSVTPQEWRPSRLKSSPPPLEPRRTSYTPGPSDESFPEEEGDWEPPMSPAPGPAREEGFWRVLGEALEDLESCGQSELLRELEASIMTGTVHSVAVDGRPGSRPWRRSREVRTSPEDLQELLLPTPLEMHRVTLHKDPVRNDFGFSVSDGLLEKGVYVHTVRIDGPAQLGGLQPFDRLLQVNHVRTRDFDCCLAVPLLAEAGDILELVVSRNPLAQSRRTPGAPGPSSPQML
Protein: SAM pointed domain-containing Ets transcription factor (Prostate epithelium-specific Ets transcription factor) (Prostate-specific Ets) (Prostate-derived Ets factor) (Q9WTP3)
Organism: Mus musculus (Mouse)
Function: May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Anterior gradient protein 2 homolog
- Homeobox protein Nkx-2.1
- Mucin-2
Sequence:
MGSASPGLSNVSPGCLLLFPDVAPRTGTEKAASGAMGPEKQEWSPSPPATPEQGLSAFYLSYFNMYPDDSSWVAKVPEARAGEDHPEEPEQCPVIDSQASGSTLDEHSLEQVQSMVVGEVLKDIETACKLLNITADPGDWSPGNVQKWLLWTEHQYRLPPAGKAFQELGGKELCAMSEEQFRQRAPLGGDVLHAHLDIWKSAAWMKERTSPGTLHYCASTSEEGWTDGEVDSSCSGQPIHLWQFLKELLLKPHSYGRFIRWLNKEKGIFKIEDSAQVARLWGVRKNRPAMNYDKLSRSIRQYYKKGIIRKPDISQRLVYQFVHPV
Protein: Probable G-protein coupled receptor 162 (Gene-rich cluster gene A protein) (Q16538)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MARGGAGAEEASLRSNALSWLACGLLALLANAWIILSISAKQQKHKPLELLLCFLAGTHILMAAVPLTTFAVVQLRRQASSDYDWNESICKVFVSTYYTLALATCFTVASLSYHRMWMVRWPVNYRLSNAKKQALHAVMGIWMVSFILSTLPSIGWHNNGERYYARGCQFIVSKIGLGFGVCFSLLLLGGIVMGLVCVAITFYQTLWARPRRARQARRVGGGGGTKAGGPGALGTRPAFEVPAIVVEDARGKRRSSLDGSESAKTSLQVTNLVSAIVFLYDSLTGVPILVVSFFSLKSDSAPPWMVLAVLWCSMAQTLLLPSFIWSCERYRADVRTVWEQCVAIMSEEDGDDDGGCDDYAEGRVCKVRFDANGATGPGSRDPAQVKLLPGRHMLFPPLERVHYLQVPLSRRLSHDETNIFSTPREPGSFLHKWSSSDDIRVLPAQSRALGGPPEYLGQRHRLEDEEDEEEAEGGGLASLRQFLESGVLGSGGGPPRGPGFFREEITTFIDETPLPSPTASPGHSPRRPRPLGLSPRRLSLGSPESRAVGLPLGLSAGRRCSLTGGEESARAWGGSWGPGNPIFPQLTL