wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-binding cassette sub-family A member 1 (K9J4V5)
Organism: Sus scrofa (Pig)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAYWTQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVSRLFSDARRLLLYSQRDTSMKDIHKVLRTLYQMERSRSAGLKLRDFLADNETFSEFLHHNLSLPRPTVDKMLGADVRLRKVFLQGYQLHLTNLCNGSKLEEVIQLGDQEVSRLCSLPREKLDAAEQVLRSNMDILKPILTQLNSTSPFPSKELAEATKALLDSLGNLAQELFSMKSWSDMRQEVMFLTNANSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEDDAGTFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDMEGMWQELSPKIWTFMESSSEMDLVRTLLNSRGSDHFWEKRLEGLDWTAKDIVAFLAKHPEDVQSTNGSTYTWREAFNETNQAVQTISRFMECVNLNKIEPVATEARLINKSMELLDERKFWAGIVFPGITPGSVELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFTYLQDVVEQAIIRVLTGMEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNGILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFSLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPMEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSSQKGPSEICMEEEPTHLKLGVSIQNLMKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYPKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVAEARLVEDIGHELTYVLPYEAAREGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRVFGDKQSCLRPFTEDDAADPNDSDVDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIILPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDVGTQELLNALTRKPGFGTRCMEGNPIPDKPCLVGEKEWITAPVPQTIRDLFQNGNWTMANPSPACQCSSDKIKKMLPVCPLGAGGLPPPQRKQNTADILQNLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGASNYQSLPPSEEVNDAIKQMKKHLKVAKDSSADRFLSNLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSQYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTNNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVKAKLPPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTGGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIVKEGRSVLLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLQPVQEFFGHAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSVLSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
Protein: Glutathione transferase (O45451)
Organism: Caenorhabditis elegans
Interaction partners:
- Epoxide hydrolase
- Glutathione S-transferase omega
- Glutathione S-transferase P 10
- Probable glutathione S-transferase 6
- Glutathione peroxidase 1
- Glutathione S-transferase P
- Glutathione S-transferase
- Putative cytochrome P450 CYP13A4
- Glutathione S-transferase 4
- Gamma-glutamyltranspeptidase 1
Sequence:
MVSYKLTYFDGRGAGELCRQIFAAAEQKYEDNRLTDEEWEKFKAAGKTPYNQLPMLEVDGKPLAQSHAMARYLAREFGFNGKSRWEEAQVNSLADQYKDYYAEARPYLAVKLGYTEGDAEALYTSVYLPVFKKHYGFFVNALKASGSGFLVGNSLTFIDLLVAQHSADLLGREKSDLFNDVPEMKAHSEKVQSIPQIKKWIETRPASDW
Protein: Krueppel-like factor 9 (Kruppel-like factor 9) (Si:dkey-201c13.3) (A2BGS7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Paired amphipathic helix protein Sin3a
Sequence:
MTDVDIAARSLGTVSNVERSDKLTGEEGSEESQESRTLLMVAMILLDLNQCIPSGISAKRIVDSDAENRENREKCKQTAGRVKRTRKRDRLHASAEKRHCCPYAGCGKIYGKSSHLKAHFRVHTGERPFQCTWPGCAKKFSRSDELTRHFRTHTGEKRFMCPLCDKCFMRSDHLTKHARRHAGFHPSMLQGHAGRRRHSSTSTSSSGSSDHMSAGV
Protein: TM6SF1 protein (Transmembrane 6 superfamily member 1) (Q6P4D7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSASAATGVFVLSLSAIPVTYVFNHLAAQHDSWTIVGVAALILFLVALLARVLVKRKPPRDPLFYVYAVFGFTSVVNLIIGLEQDGIIDGFMTHYLREGEPYLNTAYGHMICYWDGSAHYLMYLVMVAAIAWEETYRTIGLYWVGSIIMSVVVFVPGNIVDAGIYVLFCSLLCDCTVWLSGSWMFLDA
Protein: Helicase ARIP4 (EC 3.6.4.12) (Androgen receptor-interacting protein 4) (RAD54-like protein 2) (Steroid receptor-interacting SNF2 domain-containing protein-like) (Q99NG0)
Organism: Mus musculus (Mouse)
Function: DNA helicase that modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. Not able to remodel mononucleosomes in vitro. Acts as an AR-coregulator in Sertoli cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:12058073, ECO:0000269|PubMed:15199138}. Note=Localizes in speckle-like nuclear compartments.
Interaction partners:
- Androgen receptor
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- Nuclear receptor subfamily 5 group A member 2
Sequence:
MSDESASGSDPDLDPDVELEDEEEEEEEEEVAVEEHDRDDEEGLLDDTSLEGMCGTEHAQLGEDGQRPPRCTSTTSSQSEPSEQLRHQGKILASEDPKKKRAQKPSHMRRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKEYAAPIPTVPLEFLPEEIVLRASDGPQLPPRVLAQEVICLDSSSGSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEEDEEEEKGGTHVNDALNQHDALGRVLVNLNHPPEEENVFLAPQLARAVKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLPAPEALPADSKPEEVQPRFFKVHILNDEHKTVASRAKVTADWVSEGGVLLMGYEMYRLLTLKKSLATSRPKKTKKRSHPVIIDLDEEDRQQEFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSQIQRDLYTQFMDRFRDCGTSGWLGLNPLKAFCVCCKIWNHPDVLYEALQKENLANEQDLDVEELGSAGTSARCPPHGTKVKGEDSALPSSMGEATNSKFLQGVGFNPFQERGNNIVTYEWAKELLTNYQTGVLENSPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRDMPCLPGAEGQGTQKWVRNVSYFRLDGSTPAFERERLINQFNDPSNLTTWLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCHIYRLVADYTLEKKIYDRQISKQGMSDRVVDDLNPMLNFTRKEVENLLHFVEKEPAPQTSLDIKGIKESVLQLACLKYPHLITKEPFEHESLLLNRKDHKLTKAEKKAAKKSYEEDKRTSVPYTRPSYAQYYPASDQSLTSIPAFSQRNWQPTLKGDEKPVASVRPVQSTPIPMMPRHVPLSGGVSSASSTNTSMNFPINYLQRAGVLVQKVVTTTDIVIPGLNSSTDVQARINAGESIHIIRGTKGTYIRTSDGRIFAVRATGKPKAPEDGRMAASGSQGPSLASTSNGRHSASSPKAPDPEGLARPVSPDSPEIISELQQYADVAAARESRQSSPSISAALPGPPGQLMDNSTIPGTALGTEPCLGGHCLNSSLLVTGQPSGGRHPVLDLRGHKRKLATPSVTQESIRRRSRKGHLPAPVQPYEHGYPVSGGFAMPPVSLNHNLTTPFTSQAGENSLFMGSNPSYYQLSNLLADARLVFPVTTDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGMLPSYSLPFSQPLLSEPRMFAPFPSPGLPSNLSRGVSVYPGYMSPHAGYPAGGLLRSQVPPFDSHEVAEVGFSSNDDEDKDDDVIEVTGK
Protein: Dual specificity mitogen-activated protein kinase kinase 7 (MAP kinase kinase 7) (MAPKK 7) (EC 2.7.12.2) (JNK-activating kinase 2) (MAPK/ERK kinase 7) (MEK 7) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2) (Q4KSH7)
Organism: Rattus norvegicus (Rat)
Function: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by pro-inflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8CE90}. Cytoplasm {ECO:0000250|UniProtKB:Q8CE90}.
Interaction partners:
- C-Jun-amino-terminal kinase-interacting protein 1
- Mitogen-activated protein kinase 10
- C-Jun-amino-terminal kinase-interacting protein 3
- C-Jun-amino-terminal kinase-interacting protein 2
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase kinase kinase 11
- Mitogen-activated protein kinase kinase kinase 1
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Mitogen-activated protein kinase kinase kinase 7
Sequence:
MAASSLEQKLSRLEAKLKQENREARRRIDLNLDISPQRPRPTLQLPLANDGGSRSPSSESSPQHPTPPSRPRHMLGLPSTLFTPRSMESIEIDQKLQEIMKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHIIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKHYETLEVDVASWFKDVMAKTESPRTSGVLSQHHLPFFR
Protein: MIP15217p (Midline fasciclin, isoform Q) (D3DMM4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRLSSGYDTEFVPLEHQQQPQGRQETAATVPAQTPSGVEQKPFNVDTITTDVNSPNPAIFFQQSFPFFGNEFFNSFGGFGFGAAQEPWWKGPNVCTEKEEDETVASETEAEETVDTFGQERDGVTNVVRSPLFGQFQFSVNSCAEKPNKHVCTKIVNQNGKKKTLTLTRQCCYGYGRPRNADFTTPCEKIDIKDVEATASDMGAKQFLESARTAGELADMLGAGSGKKVTLFVPNDAAFMEYRGHHQQENNVEDAKAEASKPSIYKLHAVLGEVQLEDVPNEKLLQTELPDQKIRINSYQLPAALGLEPYRFAANCVPIEKHDKLSEQALVHTLGGVLKPLTKNLMDIIRERADMSIMRTVLEKTNLSAMLEDDKPVTIFVPTDAAFDKLEPHLRRALKEGRGCASNILKNHLLDLTFCSLATVPGAKTTAYNLLGEPLLLNRTHRAANQTGPTPIYINNLAKIIDADIMGTNGVLHVIDTILPTESALPMTSLMSQKNLTIFQRLLEASGYDDQFDDLDNVTIFAPTDKALQNTEWARMLKEQPELLNHNLDLLEFLNYHVVKPMIKTCDLSEKSLPTVAGSSVRLNLYSTHALFSDVMNRATVNCARLVHFDDESCGSVLHQVDRALAPPKNNMLKLLEANPNYSKFLELVRKANLTQLLSNDSRSLTLLVPKNDIFEELNESGEGSKPADPMALVKTHIVEDVVCCAGIIPTNWPFVRSIESISGQHLRITRDRRPKIENAGVTKCDVVATNGILHEINDIIVPRPQRQQQQRPQLIPPGAGYQPQGDFDVFF
Protein: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ (EC 4.2.1.59) ((3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase) ((3R)-hydroxymyristoyl-ACP dehydrase) (Beta-hydroxyacyl-ACP dehydratase) (Q9PIM2)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- Malonyl CoA-acyl carrier protein transacylase
- Acyl carrier protein
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase 3
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- 3-oxoacyl-[acyl-carrier-protein] reductase
Sequence:
MIDVMQIQEILPHRYPFLLVDKITELKVKEVVLGYKNISISDHVFMGHFPGHPIYPGVLILEGMAQTGGVLAFESMEDKVDPKSKVVYFTGIDGAKFRNPVRPGDRLDYEMSVVKNRGNMWIFKGQAFVDGNLVAEAELKAMIVDK
Protein: Chaperonin GroEL 1 (EC 5.6.1.7) (60 kDa chaperonin 1) (Chaperonin-60 1) (Cpn60 1) (Q05972)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
- Co-chaperonin GroES
- Chaperone protein DnaK2
- Protein GrpE
- Heat shock protein
- Chaperone protein dnaK1
- Chaperone protein dnaK3
- Chaperone protein DnaJ 1
- Chaperone protein DnaJ 2
- DnaJ protein
- Chaperone protein ClpB 1
Sequence:
MAKSIIYNDEARRALERGMDILAEAVAVTLGPKGRNVVLEKKFGSPQIINDGITIAKEIELEDHVENTGVSLIRQAASKTNDVAGDGTTTATVLAHAIVKEGLRNVAAGANPISLKRGIDKATDFLVARIKEHAQPVGDSKAIAQVGAISAGNDEEVGQMIANAMDKVGQEGVISLEEGKSMTTELEITEGMRFDKGYISPYFVTDAERMEAVLEDPRILITDKKINLVQDLVPILEQVARQGKPLLIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKQMLEDIATLTGGQVISEDAGLKLESATVDSLGSARRINITKDNTTIVAEGNEAAVKSRCEQIRRQIEETDSSYDKEKLQERLAKLAGGVAVIKVGAATETEMKDRKLRLEDAINATKAAVEEGIVPGGGTTLAHLAPQLEDWATGNLKDEELTGALIVARALPAPLKRIAENAGQNGAVISERVKEKEFNVGYNAASLEYVDMLAAGIVDPAKVTRSALQNAASIAGMVLTTECIVVDKPEKEKAPAGAPGGDFDY
Protein: PPi-type phosphoenolpyruvate carboxykinase 2 (EhPEPCK2) (PPi-PEPCK2) (EC 4.1.1.38) (Diphosphate-dependent phosphoenolpyruvate carboxykinase 2) (PEP carboxyphosphotransferase 2) (C4M1E4)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Inorganic pyrophosphate (PPi)-dependent phosphoenolpyruvate carboxykinase, which regulates the carbon flow of the central metabolism by fixing CO(2) to phosphoenolpyruvate to produce oxaloacetate. Can also produce pyruvate and diphosphate from phosphoenolpyruvate and phosphate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26269598}.
Interaction partners:
- PPi-type phosphoenolpyruvate carboxykinase 1
- PPi-type phosphoenolpyruvate carboxykinase 3
- Pyruvate kinase
- Malate dehydrogenase
- Malate dehydrogenase
- Malate dehydrogenase
- Pyruvate, phosphate dikinase
Sequence:
MFNQEQGTDYPVLNKKKLESLANLKLAMGGHEYPTDDLTQQGLKLAGPLLEEVEESEVNHTTAPIDARLQTFLNSYFAECGEEVPKIPDDTFILDREGLGRVLSFPPHKQEFFCETMKSYKIKQGVLHNPAKDKRTTVGVFHICQSDVPVPADKIECPKIAFLRMLKAAFYGAPDDHLIIPYTAECKEPTRSWVSLYMRPVVVPGVKGVKGFEHEKATEMHFFVPGNMVSCLDFVESVFGNAGNPRLSKNDAALDPLGWTGHSGMAILAPHLTRMTKKECGLPHISQATERQKRERMCWEKEDELYNDGKTFKMYCRDASGVICTIIADNYFGYCKKEVKTQISYSANLYGFAEEEHAGGAVTRPSYDLGEACKAVQYAEGYKFSEMVEKNKHSIIVKEEGYAVDKKYPEGIIYVPEDSVFTIEDASIKFNHNGKEESILLTPKVNYVLPNGYTIILHDTMTSRRWTLRGILPQYTLCHKPCTVSGGGKSEISKSIRDAVIEGSVFVNNKEEDFKAVQEIFDHDFSKRYANGEVKPIHILDPNVTLGTVVELLTPSHLFTKEHNDYISSISPLIVELVMTIKSLYREDWKGDWQSRITVDKINGNEGNELKYRGANLCSQYLRVGFERDETTWRVFQLRKDFFPAAKLQMEDDITASVIVPTKLLKTPINNMQKKACKIVKNCELRLFQRPDDAVFRGFDKQTEYDFSIPGHFISNYQPMTREEAKDFTKDVVRLYQYTEPMRKCLQDFVAGKDEAKYIVSSSYTRLVPEGDKLVGSKNPRYLQRRPDMLDPEYTYMTFKAIQLYRKISDEEPLYTPVDAVLSGRRNNPPQVAKNGMKLRPLSVFAPLHYFELPELLMECITSMTGASPSMFGAGSEGALTKGPFNSLPAVVDLNNYLLGMICCGYSGFVSSASYCGPHYKVAHDISLLIPEIWSKMRRYEQEPKYLIEHGYLEPCPDVTYNGKTYSGKRLGYRITTAFANHFLRTLFSMPNSVMPEDFLKPELQDLAIYADSYEYMSQTDKGIAMNYVKDGTVEGACPPLKALIYIMANGEYNGMTRESKEFREMFDPEVVLNSEWYKERLVTRQKLEVAKLNKDLAYLNKTIAEKPRLVETLNKQIAAVKEELQYVSSEEYLIDIDGSIGTDPYPYKCMKH
Protein: INO80 complex subunit B (B8ZZH7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKLWRRGSTSGAMEAPEPGFPSTGEALELSLAGAHGHGVHKKKHKKHKKKHKKKHHQEEDAGPTQPSPAKPQLKLKIKLGGQVLGTKSVPTFTVIPEGPRSPSPLMVVDNEEEPMEGVPLEQYRAWLDEDSNLSPSPLRDLSGGLGGQEEEEEQRWLDALEKGELDDNGDLKKEINERLLTARQRALLQKARSQPSPMLPLPVAEG
Protein: Translocator protein (Mitochondrial benzodiazepine receptor) (PKBS) (Peripheral-type benzodiazepine receptor) (PBR) (P16257)
Organism: Rattus norvegicus (Rat)
Function: Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis (By similarity). Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides.
Subcellular location: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:2555358}; Multi-pass membrane protein {ECO:0000269|PubMed:2555358}.
Interaction partners:
- Steroidogenic acute regulatory protein, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- ADP/ATP translocase 2
- Non-selective voltage-gated ion channel VDAC2
- Non-selective voltage-gated ion channel VDAC3
- Peripheral-type benzodiazepine receptor-associated protein 1
- Golgi resident protein GCP60
- ADP/ATP translocase 1
- ADP/ATP translocase
- Acyl-CoA-binding protein
Sequence:
MSQSWVPAVGLTLVPSLGGFMGAYFVRGEGLRWYASLQKPSWHPPRWTLAPIWGTLYSAMGYGSYIIWKELGGFTEEAMVPLGLYTGQLALNWAWPPIFFGARQMGWALVDLMLVSGVATATTLAWHRVSPPAARLLYPYLAWLAFATMLNYYVWRDNSGRRGGSRLTE
Protein: Myosin heavy chain (Q4WQC6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MPRRARLVTESESDYSESDVSMDIPRHRHFVRRRSISRHRYDPDFSSTTYLSPVVHEDVRIHRSASTGARRRRELQPPPPPPAVIVDINNVSRNKSTNRSANKNRKHRQEDTTIVDIESEDETVLRKHRRPRASTSVSREASPRHEASPRHQRDFELVIDQRMLEKNDVRQDLELMKQQMEIERLERELARRRGEHENNQTQLIREEETWYEDEISDRLRRLERFEKKQRMEEEQRQAEFRFKLRKFEEAERLAAEQEEVRAKLREEKLKELQRKIEEEEERERIKKELRDEQARQLLEQMEREKKEAAMKQAAIEEWKIAEERRRMAEREEKERKDREFRTRLKMEFGYTEAEIEDIINKKKNPPKEEEKKKDKEEKKEKEKEKEKEKEKEKEEKKEIDHHKTTWIKVHRKYILPETLIAYRLPWDFDELDGNYIIIKQWISEDLQEELFAHTRRLREGKLVTETSSTLTELKVNDRKKDRMYLVRKKSPNRRAWIFT
Protein: E3 ubiquitin-protein ligase SP1 (EC 2.3.2.27) (DIAP1-like protein 1) (Protein SUPPRESSOR OF PPI1 LOCUS 1) (RING-type E3 ubiquitin transferase SP1) (Q8L7N4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in the regulation of protein import in the chloroplast. Associates with TOC complexes and mediates ubiquitination of TOC components, promoting their degradation via the ubiquitin-proteasome system (UPS). Plays a role in the reorganization of the TOC machinery. Involved in a mechanism that regulates plastid biogenesis via UPS. Promotes stress tolerance by depleting the chloroplast protein import apparatus, which limits photosystem assembly and the potential for reactive oxygen species (ROS) formation. May act as negative regulator of programmed cell death (PCD) during biotic stress.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:23118188}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Trihelix transcription factor GT-1
- Protein HOTHEAD
- ABC transporter F family member 4
- Translocase of chloroplast 132, chloroplastic
- Translocase of chloroplast 159, chloroplastic
- Protein TOC75-3, chloroplastic
- Translocase of chloroplast 33, chloroplastic
- Translocase of chloroplast 34, chloroplastic
- U-box domain-containing protein 4
- Probable histone chaperone ASF1A
Sequence:
MIPWGGVTCCLSAAALYLLGRSSGRDAEVLETVTRVNQLKELAQLLELDSKILPFIVAVSGRVGSETPIKCEHSGIRGVIVEETAEQHFLKHNETGSWVQDSALMLSMSKEVPWFLDDGTSRVHVMGARGATGFALTVGSEVFEESGRSLVRGTLDYLQGLKMLGVKRIERVLPTGIPLTIVGEAVKDDIGEFRIQKPDRGPFYVSSKSLDQLISNLGKWSRLYKYASMGFTVLGVFLITKHVIDSVLERRRRRQLQKRVLDAAAKRAELESEGSNGTRESISDSTKKEDAVPDLCVICLEQEYNAVFVPCGHMCCCTACSSHLTSCPLCRRRIDLAVKTYRH
Protein: Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (PfeIF2alpha) (Q8IBH7)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (By similarity). May regulate protein translation in response to amino acid starvation (Probable). May regulate protein at various stages of parasite development (Probable).
Subcellular location: Cytoplasm, Stress granule {ECO:0000269|PubMed:22355110}. Note=When phosphorylated at Ser-59, localizes to stress granules in schizonts and male and female gametocytes (PubMed:22355110). When phosphorylated at Ser-59, localizes to stress granules in mosquito salivary glands (By similarity). {ECO:0000250|UniProtKB:A0A509AJP9, ECO:0000269|PubMed:22355110}.
Interaction partners:
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit beta
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit gamma
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 5, putative
- Eukaryotic translation initiation factor 4C
- 40S ribosomal protein S3
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
Sequence:
MTEMRVKADLGDCRFYKKKFPEVDDLIMVKVNRIEDMGAYVSILEYNDMEGMILMSELSKRRFRSVNKLIRVGRHEVVLVLRVDSQKGYIDLSKRRVSPKDIIKCEEKFSKSKKVHQTVRHVAKEHGITVEELNEKAIWPLYERYGHALDALKEATMNPENVFKGLDISEEIKNSLLKDIKLRLTPQALKLRGRIDVWCFGYEGIDAVKEALKKGKEISNDKVSINIKLIAPPQYVIVTSCHDKDLGMAKIQEAMKVISDKIKEYKGGDFKQQGEILVIGGDEEKRLEELLDKHDGISSDDDDYNTSDEDDENSSEEDENTSEDEEEED
Protein: ETS translocation variant 5a isoform 2 (ETS variant transcription factor 5a) (F1Q6X6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004019}.
Interaction partners:
Sequence:
MDGFYDQQVPFMVPPNQKSLQVEEPYNRPVNDRKRKLVETELAQDTEELFQDLSQLQEIWIAEAQVPDDEQFVPDFQSESLMFHGPPLAKIKRELSPSKELSPCSQDRSPMPYGEKCLYSYSAYERKPSTGFKPLTPPSTPVSPCVPSNALATRPLHEQTPPPVSNTALGQRLLHGQPTMTKSTPNQTCVPHHSQSPPFVVPCPPLNRETHFSNEPRFQRQLSEPCLPFPPSDAQGRPSFMPQVACTSPRDGRPPYHRQMSEPLVPVPPQGFKQELLDPRYVEQGVPNMGPSQAAFHPMAIKQEPRDFCFDSEVPKCQSSFGRAASFYQNHENFSFDREQQLYFDDTCVVPERLEGKVKQEPSVYREGPPYQRRGSLQLWQFLVTLLDDPSNGHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPEALFSMAFPDNQRPNLKADPDGLPTVDDDTLPLAHYDDGSSYLVDGGEQCVSGMPFPDGYVY
Protein: Probable feruloyl esterase A (EC 3.1.1.73) (Ferulic acid esterase A) (A2QSY5)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLCNIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTVTGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVSSPETTQYFRVTHSNDGIPNLPPAEQGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW
Protein: DNA methyltransferase 1-associated protein 1 (Q568Y6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- YEATS domain containing 4
- Chromatin modification-related protein MEAF6
- Actin-like protein 6A
- RuvB-like helicase
- E1A-binding protein p400
- Vacuolar protein sorting-associated protein 72 homolog
- MRG domain binding protein
- DNA
- Inhibitor of growth protein 3
- Enhancer of polycomb homolog
Sequence:
MATGADVRDILELGGPEGDAASGTISKKDIINPDKKKSKKSSETLTFKRPEGMHREVYALLYSDKKDAPPLLPSDTGQGYRTVKAKLGSKKVRPWKWMPFTNPARKDGAMFFHWRRAAEEGKDYPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDHQQYKKRSVEDLKERYYHICAKLANVRAVPGTDLKIPVFDAGHERRRKEQLERLYNRTPEQVAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAEKPAVPETAGIKFPDFKSAGVTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEELVHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALARAGVLGGPATPAVGPTPASAEPTVSESGLGLDPSKDTIIDVVGAPLTPNSRKRRESASSSSSVKKAKKP
Protein: E3 ubiquitin-protein ligase pub2 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase pub2) (Q9UTG2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Has a role in the G2/M transition.
Subcellular location: Membrane {ECO:0000269|PubMed:11956316}; Peripheral membrane protein {ECO:0000269|PubMed:11956316}. Cytoplasm {ECO:0000269|PubMed:11956316}. Note=Predominantly found at the cell surface of the polar regions.
Interaction partners:
- E3 ubiquitin-protein ligase pub1
- E3 ubiquitin-protein ligase pub3
- Pheromone P-factor receptor
- Pheromone M-factor receptor
- Arrestin domain-containing protein C584.15c
- Polyubiquitin
Sequence:
MENIRFEVQLTILHVEGLWKNGLLRSLKPYLLISVDDDQFIKTNVASGTLRLSWGFTQKLTVSPQSIILLQLFDEKQKNETSDGFVGLGAAVVNSFLPFNNPKDDYKTRITLRSPSGSYRGSVVCLFKRSKFLPEELPADKSQICTDIIDDASGCAWETRIDEFGHVYYLKSPQLSVISAISHEKLENLTPKQLKEVFSQFLFNNQSKSSLKINLEYKVIKHLLEHYPLALSVRQQVAVEKGPLPAGWEMRLSEDYHVYFVDHSTKTTTWSDPRDNVVASDSVSENTDSIQQINDEYQRKIAYMYDRPEMAVNDAQLQLKVSRATTFEDAYDIISKLSVSDMKKKLLIRFRNEDGLDYGGVSREFFYILSHAIFNPGYSLFEYATDDNYGLQISPLSSVNPDFRSYFRFVGRVMGLAIYHRRYLDVQFVLPFYKRILQKPLCLEDVKDVDEVYYESLKWIKNNDVDESLCLNFSVEENRFGESVTVDLIPNGRNIAVNNQNKMNYLKALTEHKLVTSTEEQFNALKGGLNELIPDSVLQIFNENELDTLLNGKRDIDVQDWKRFTDYRSYTETDDIVIWFWELLSEWSPEKKAKLLQFATGTSRLPLSGFKDMHGSDGPRKFTIEKVGHISQLPKAHTCFNRLDIPPYNSKEELEQKLTIAIQETAGFGTE