wanglab/gogpt-training-data huggingface dataset:
Protein: Myogenin (C4P6Q3)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELFETNPYFFPEQRFYDGENFLGSRLQGYEAAAFPERPEVTLCPESRGALEEKDSTLPEHCPGQCLPWACKICKRKTVSIDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQSLLSSLNQQEREQRELRYRPAAPQPAAPSECGSGSSSCSPEWSTQLEFGTNPADHLLSDDQAEDRNLHSLSSIVESIAVEDVAVTFPEERVQN
Protein: Histone H1.4 (Histone H1b) (Histone H1s-4) (P10412)
Organism: Homo sapiens (Human)
Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
Subcellular location: Nucleus. Chromosome. Note=Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
Interaction partners:
- Chromobox protein homolog 3
- Histone H4
- Lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
- Histone H1.3
- Histone H3.1
- Histone H2B type 1-K
- Histone H3.2
- Histone H2A type 1-B/E
- Testis-specific H1 histone
- Histone H1.5
Sequence:
MSETAPAAPAAPAPAEKTPVKKKARKSAGAAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKSAKKTPKKAKKPAAAAGAKKAKSPKKAKAAKPKKAPKSPAKAKAVKPKAAKPKTAKPKAAKPKKAAAKKK
Protein: Sema domain, seven thrombospondin repeats (type 1 and type 1-like), transmembrane domain (TM) and short cytoplasmic domain, (semaphorin) 5Ba (Semaphorin-5B isoform X1) (F1QPQ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- Plexin A3
Sequence:
MTVLPRDVASLAVPGLILCFITLPFPTILSQNPPVPTETSPSPAPHHTRPECTRLEHPVVSIQALSPLISSFSHPGVRDYSQLTLDLTRNELIVGARNYLFRLNLSNISLIQATEWGPDEDTRRSCQSKGKTELECQNYIRVLLVNKTEVVTCGTNAFQPLCITREAGNMSRVLERVNGVARCPYDPRHNSTAVVTESGELYAATVIDFSGRDPVIYRSLGGMPPLRTAQYNSKWLNEPHFISAYDVGLFTFFFLRENAVEHDCGKTVYSRVARVCKNDIGGRFLLEDTWTTFTKARLNCSRSGEIPFYYNELQSTFYLPEQDLIYGIFTTNVNSIAASAVCAYNLSAITQAFNGPFRSQENPRSTWLPTPNPIPNFQCGTIDEEGPNERLTERSLQDAQRLFLMNDVVQPVSVDPLVWQDDVRFSKLVVDIVQGQDSLHHVMYIGTEYGTILKALATTNKSLQGCYLEEMQLFPPGLQQPILSLQILHGDRTLFVGLNDKVLKIPLARCSSYKTELMCLDARDPYCGWDRKQRRCTTIEDSSNMSQWFQNITACPLRNQTTDGAYGPWAPWQPCSHDDGEGTSTCLCRSRVCNSPPPRCGGKNCQGPTIEVSNCSRNGGWTPWSSWGQCSTSCEIGFEVRQRSCNNPSPRHGGRVCVGQSREQRFCNEKVSCPQPIFWSSWSPWSKCSADCGGGVHSRSRNCENGNSCPGCALEYQACNLESCPEVRRNTPWTPWMPVNITQGGARQEQRVRYICRAQLADPHELQLGKRKVETRFCPNDGMVTCETDSLVEELLRMPGVRLSGTGWSSWEMWSACTQECAKGYRTRKRSCTNTDGKNIPTACRGSPVEYQDCNPQPCPVKGAWSCWSSWSQCSVPCGGGHYQRTRTCTSPAPANGGDICIGLHTEEALCNTHTCDGGWMAWSVWSECDDSGLQLRSRVCGAQSMPCAGNSSQHRDCNEIPAILPASSYEKDQQCGGFTLLHLIATGVSCFLGAGLLSFLVYVYCQRFHKPSQESAIIHPTTPNHLNYKGNTTPKNEKYTPMEFKTLNKNNLLPDERTNYFPSPLQQTNVYTTTYYPTGLGKYDYRPDSSPSPCRTYNHS
Protein: Apoptosis-inducing factor homolog A (EC 1.-.-.-) (Q54NS9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Putative FAD-dependent oxidoreductase.
Interaction partners:
- Seipin
- Apoptosis-inducing factor 1, mitochondrial
Sequence:
MNYLYNISESLKKIFNYFSSITRDCEKKRVLIIGCGFGGSQVAKLLDSNFEVTVVERKQTFFNSIASIRAIVEPELAKKIYIPYDKLLKNGKFIYGTVIEISPTLVKLEDGKELTFDYLVIATGSNSLAPFKAPLEKISGTEIFNYYKDISEQIKQAKSILIVGGGSVGCEVVGEIINKYPIKNKELAKKITIVHSGNKLVSSKTNNKFNNLINESMKKRNVSVILNDRIEIPDDIKQCFINQTSPNFQVSLKTYKTKNGLSIESDFVIWTIGIKLNSESYKTNFSNEINEIGQIKVNQSCQVQGYDNIFAIGDITDFDELKTTYNALSHGNIVAKVIKDLSNGKNKNQLAKHKLLPPIISLSLGPKDGLTQINSNLNFGSFISRILKSNNLLINRFQTHFNNPEPLK
Protein: Uncharacterized protein (Q57VI6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cilia- and flagella-associated protein 45
- WW domain-containing protein
- WW domain-containing protein
Sequence:
MSGTSSSLGRQSRQSQDSPGRSTPQPPLCPVPVPTVSQASNQLPSPIETQEPTPSVSAPTGRRVEEGFSNAAASIANNVRQTVEYRAAWDLELWRAIQASKLRQQLETQKKKALTELSRLVKTREQQAVAGLEMREQEVSRREQRLAEEEKQMERRKWRLVEMEKDVRLLRQQLVDARRRAGTDAKVEVRRAKEDADHAIELQEQRVQAAEAQAKRADERLQQAQRDYLALSEEFHRFRTRELTSPPEKLSTVEARMRSEFVMEQQNLQDRLERRHQERLQQVEDRCSRLQEENSRLTELSIRRKEQLRRSADEIDRLKQLNRELEERLRKVGQKSLSIDSAADVKERKRCQRGVASPSLEAQTDPDIAALVREVERLRSERRIIVETSAGALDEDSDVVRSLDKRINDILDQLRAHGTVSCSIAV
Protein: D-gluconate/D-galactonate dehydratase (GAD) (GNAD) (EC 4.2.1.140) (EC 4.2.1.39) (EC 4.2.1.6) (Q6L1T2)
Organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)
Function: Involved in the degradation of glucose and galactose via the nonphosphorylative variant of Entner-Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-keto-3-deoxygluconate (KDG). It is also able to catalyze the dehydration of galactonate to produce 2-keto-3-deoxygalactonate (KDGal).
Interaction partners:
- 2-keto-3-deoxy gluconate aldolase
- 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase
- mannonate dehydratase
- Altronate hydrolase
- Altronate hydrolase
- Ribulose-phosphate 3-epimerase
Sequence:
METIKSVDIYELGSPGEKSSPWSSTILIVKLTSSNGNIGYGEAPTTFMTLPVKESMREVERVFKDQNYFNIEKNMREFYKHSFYLSRSMEATSALSAFEIASWDLIGKDLGTPVYNLLGGEYNSELRAYANGWYSDCLEPDDFVSRAKEYIKKGYTAFKFDPFRNNFDRIGNDGIKKAVDIVSAMRSELGENIDLLIECHGRFSTKYAIKVGQALDEFNPLFIEEPIHPEMELGLFDFKRYVNTPVALGERLLNKEDFARYISQGMVDIVQADLTNSKGILEAKKISAIVESFGGLMAFHNAFGPVQTAATLNVDYTLTNFLIQESFEDSWPDWKRNLFSGYRIENGHFKLSGKPGLGITADEKLMEKLIYDGMEEFNKNEPSWVVSGTYK
Protein: Inner kinetochore subunit CTF3 (CENP-I homolog) (Chromosome loss protein 3) (Chromosome transmission fidelity protein 3) (Constitutive centromere-associated network protein CTF3) (Q12748)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the central kinetochore, which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle-microtubule attachments and proper chromosome segregation.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Interaction partners:
- Inner kinetochore subunit MCM16
- Inner kinetochore subunit CTF19
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit IML3
- Inner kinetochore subunit MCM21
- Inner kinetochore subunit NKP1
- Inner kinetochore subunit CNN1
- Inner kinetochore subunit AME1
Sequence:
MSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSIIDTVTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHVYFLFPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMHPGYRDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRILSRAHPANFPADTVQNTIDMYLSEIHQLGADSIYPLRLQSLPEYVPSDSTVSLWDVTSLEQLAQNWPQLHIPNDVDYMMKPSLNSNVLLPRKVMSRDSLKHLYSSIILIKNSRDESSSPYEWCIWQLKRCFAHQIETPQEVIPIIISVSSMDNKLSSRIIQTFCNLKYLKLDELTLKKVCGGILPLWKPELISGTREFFVKFMASIFMWSTRDGHDNNCTFSETCFYVLQMITNWVLDDKLIALGLTLLHDMQSLLTLDKIFNNATSNRFSTMAFISSLDILTQLSKQTKSDYAIQYLIVGPDIMNKVFSSDDPLLLSAACRYLVATKNKLMQYPSTNKFVRMQNQYIMDLTNYLYRNKVLSSKSLFGVSPDFFKQILENLYIPTADFKNAKFFTITGIPALSYICIIILRRLETAENTKIKFTSGIINEETFNNFFRVHHDEIGQHGWIKGVNNIHDLRVKILMHLSNTANPYRDIAAFLFTYLKSLSKYSVQNS
Protein: Cell polarity protein mor2 (Morphological round protein 2) (Q9HDV6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the maintenance of cell polarity. Has a role in localizing F-actin at the cell tips.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12234926}. Membrane {ECO:0000269|PubMed:12234926}; Peripheral membrane protein {ECO:0000269|PubMed:12234926}. Note=Found at the cell tips and at the site of septum formation.
Interaction partners:
- Serine/threonine-protein kinase orb6
- Mo25-like protein
- Serine/threonine-protein kinase nak1
- Leucine-rich repeat-containing protein sog2
- Maintenance of ploidy protein mob2
- Serine/threonine-protein kinase sid2
Sequence:
MSLNEIAHDQPVENGPLYSEKQDHTAVDYALHILFTQFVRLSEQKISFLSRYHANEGKNAEPVRFNVGEQEAILLLKKGEDNEFDRCIQALVALASSKPVAVIESLLCWRKVRVDITSSSGTPRVVNERRSSISIYILCRVLTEIAETIPSNALEESTVSCLLECVFHQLLSAKNLPVSSSYFSLANWESFAFLVGSMSRFNFVMVSDRFIEEIEHLEKSGCDSRQKETVLVHLLRAMRYLRLQLYPTTLLEESIAFLQSLTSFFMKANTALKIEYAYLMEQLLRPLISRATFEVNIPAWSRTIETIYPVVLKMCTKTKYWNVFFPFCCTLLCLSPKQFFLKHWISSLDAAFFRVKDRRLRNTGLPHLSRVVWTYSNQYKEEPSIMNSNISNILKSGFSIGKKFSVVPFATLEELDGYAQIVRVVGAHFPELVIKEILTPLSTDAFTENIGPEKLMIVVRSVYYILHDMKYKKSDSTIFEYIEFEFVDLHEVAVGTPLQQFVHNLSQKLLFLVFQLSTNTNCYLDSKNATSLLALYINALKVFPCLMGKLEQRVIDAYVKCLNCSNKIIHTVCHNSLIYFSSGLKMSKSVISCLSRKLVKGSEYLLRTYHEVIRIWISQQEAVIEKRNSVLSNKSCASSESNTPASVKQDYDDIQSWTIIEEIQSLGVLHLSSPSVGIRKFAVALLNDVKQLNTEYLMLSSDKVEVGDIYSEPTIVDVLKDCDSSILSVESHLPTAAERSRLRKFINDGTKDMLLKLATSNSGVDISIWYNVFPRFIKVCFERFPTTMALLRNTVCEKLPSITMQLLSRIESSELNFNLKSAVKNDNFPEFLLVQWKLYLIVACCTITYTSNVDYSHTDLRRTLTAVQSGNHLRGLQETIKITSAESLFSMVLPLIFTEFSPIREAVVFAIGCINVNAFPQLVRSLKPYISVLKQDHQEFIFAGLNFPSVKRRNKPDLLLRSEIAHIFAMTSHLLLHELLNEDREALSVISEFLKDLKGFLSTPNVQADEKYLKLRCYFSQLLEKVLLVQNLHPSSEVLPFSGRASCWKLLDEWTGFGPARAITKNREELMRAHIRGNNKDIRERDKLLASFEAGKQNLEYLAIKAMIALCTAKLQQELTEGVFLFDIEILLNWFTAVFGSPSKAIVGLARKGLTALLLENSSNEVLLQKVINRCFSKEISQTISNYYFLSLSEMLIQINPNNLSKPKLLPLCLVNLSTNNLSVRLKAFELLGNFHLNNFTMTALMEFKTFLESSNPALYLKPQYLFSVQLASDFTEDSFTLTSECLRYFNYGHQHRRGLVTVLLPWLQNLELKMDVENKTFDSFTAVILIDLIEVTAKFTNDLPNEIEALWTSLALSRHKSNWTVILFFLMQQCYQRKTFSFVDCTRQITIYLAKTELLSDLYSTLLSFVCPANVSNENQEVYKFSLEDLSSTYVANLEDLFPSEKNHISYSPCQLSLLLLMDILPNPSIITVTDDVATILHAAFIQFDHYSRIVQEQCQQIFQYVVRKVLAMEGRLDYDDAYFDFNVESSLITGLRGKTKKEDDLVKYHNMILKTIELLSSSYPELKQIWGEVALSWATTCPSRRLACNSFQLFRSLLPDFDARMLLEIISRLVGTISDETSYLRDYSVEILRTFNSYVLVMNSDDLLSYSQILWTAIACLTTIHEDEFIESVKIAYAYFLRVEETDSATQQIMETFPQNWVGDYQGLQILILKGFRSTNSFEITMNFFLLLMDFKDNDLVGVGYLRILSCLLVSLPAMVYTYEHSDPITFDLSVFCHKLATLASQFNDDALIELLDTYLKRKFRSIKDFLKHTVSYLYSYYFEDYELEIVSTLTMFLSNNLTWFRKSTLDVLKELFPLIDFQKPIYSEHGLGIVSPLLRLLPTGYAMEALSLLTDSVLHVSAPTDMQTLKLLMVDPKLKNSDDRLAGFFEIPDEDGWYEPNSEYAAAITKSNVHAVFYSCSTTEASVSTPEVRFHADEVSNYPRHVPTDSHGSLDENSLGELVTTLHSLDVFFAEDRDEELIQPDVAVDPKLDITSEDYDDRIATILSGSLRRQKQGLMAYETESFRDYSPNEEIDASAKLPMDMPPVRVRKSSFISKLKPHYFMDAESYYPSLKALGNSAEHRLSLDEIRGAAELKQNKNWNSMLDQSVSMINEDSVEDHETHENYYHLRTMFQGSESNESFTDTTRSRGWH
Protein: Basic phospholipase A2 Bmaj-9 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (B3A0N3)
Organism: Bothrops marajoensis (Marajo lancehead)
Function: Snake venom phospholipase A2 (PLA2) that causes irreversible neuromuscular blockade in chick biventer cervicis muscle preparations. The neuromuscular blockade is mediated by inhibitory action at the presynaptic motor nerve endings. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|Ref.1}.
Interaction partners:
Sequence:
DLWQWGQMILKETGKLPFSYYTAYGCYCGWGGRGGKPKADTDRCCFVHDC
Protein: Paired-like homeobox 2a (Q6NYV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MDYSYLNTYDSCMAAMEASAYADFNSCSQSNGFQYNPIRSGFSSGPACAPLATASCTLGALREHQPAPYSTVPYKFFSDASGLNEKRKQRRIRTTFTSSQLKELERVFAETHYPDIYTREELALKIDLTEARVQVWFQNRRAKFRKQERAANSKASSSSGGKKPSDARSSSEDDESKESTCSPTPDSTANMSSPGARSSLSPSPAPGPASTFSPASISPALKSSPWPSLGSGTPGPTHTHTQELLKAWQPADSMSGPFAGVLSSFHRKNNTIKSNLF
Protein: Ppp1r9a protein (Q7TSA7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPSENAAIIAKTRGKGRPSSPQRRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSVHESGQNHRYSPKKEKGGGTEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSEPPGALTSGKAESADYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSKPPSNKQDTDTEDAQKSDAVPVPEVAQKGTSLASLPSEEIQLSTEAEDVTTAQPEALDSTDKDSPEEPSAENQAMPKSHILSPRNEPLEDAEANVVGSERAQHQKKDLTGGDLTSPDASASSCGREVPEDSNSFESSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEEEDSDENNYYQPDMEYSEIVGLPEEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTDGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDETGEYATDEEEDEGGPILPSGDVAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEVERKKREEVEKAHLLEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKVSTLNGWQTLAECRCPPVYLLNVIAVLLICALLGRKSPKFVFNCYMVVI
Protein: Aquaporin-1 (Aquaporin-CHIP) (A0A494C115)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
XGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK
Protein: Protocadherin alpha-5 (PCDH-alpha-5) (Q9Y5H7)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MVYSRRGSLGSRLLLLWLLLAYWKAGSGQLHYSIPEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKGRGDLLEVNLQNGILFVNSRIDREELCRRRAECSIHLEVIVDRPLQVFHVEVAVKDINDNPPRFSRQEQRLFILESRMPDSRFPLEGASDLDIGANAQLRYRLNPNEYFDLDVKTNEEETNFLELVLRKSLDREETQEHRLLVIATDGGKPELTGTVQLLINVLDANDNAPEFDKSIYNVRLLENAPSGTLVIKLNASDADEGINKEIVYFFSNLVLDDVKSKFIINSNTGEIKVNGELDYEDYNSYEINIDAMDKSTFPLSGHCKVVVKLLDVNDNTPEMAITTLFLPVKEDAPLSTVIALISVSDRDSGANGQVTCSLMPHVPFKLVSTFKNYYSLVLDSALDRESVSVYELVVTARDGGSPSLWATASVSVEVADVNDNAPAFAQPQYTVFVKENNPPGCHIFTVSARDADAQENALVSYSLVERRVGERPLSSYVSVHAESGKVYALQPLDHEEVELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLVPRVGGTGGAVSELVPRSVGAGHVVAKVRAVDPDSGYNAWLSYELQPAPGSARIPFRVGLYTGEISTTRSLDETEAPRHRLLVLVKDHGEPPLTATATVLVSLVESGQAPKASSRASAGAVGPEAALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSAQPTEAVCTRGKPTLLCSSAVGSWSYSQQRRQRVCSGEAPPKTDLMAFSPSLPQGPTSTDNPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: GAIP c-terminus interacting protein 1 (GIPC PDZ domain-containing family, member 1) (PDZ domain-containing protein GIPC1) (Regulator of G-protein signaling 19-interacting protein 1) (Q6B337)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Neuropilin 1b.
- Neuropilin-1a
- HESX homeobox 1.
- Syndecan 4.
- Myosin VIa
- Protein tyrosine phosphatase non-receptor type 1.
- Early endosome antigen 1
- Myosin VIb
Sequence:
MPLGLGRRKKASPLVENEEAEPIRAGLNVSGLDGLDGGRVGLGEGAAHEGLPPPPTSLRPRLIFHTQLAHGSPTGRIEGFSNVRELYAKIGEAFGIPPTEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKGEDALGLTITDNGAGYAFIKRIREGSIIHQIQVINVGDMIESINGQILIGCRHYEVAKMLKELPKGKTFFLKMVEPLKAFDMISQRSGSRSGSAQLGTGRGTLRLRSKGPATVEELPSAFEEKAIEKVDDLLESYMGIRDSELAATMVELGKDKKNPDEFAEALDETLGDFAFPDEFVFDVWGAIGDAKVGRV
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) (O59816)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P12695}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Probable citrate synthase, mitochondrial
- Probable ATP-citrate synthase subunit 2
- Succinate--CoA ligase subunit alpha, mitochondrial
- Probable ATP-citrate synthase subunit 1
- [Pyruvate dehydrogenase
- Probable acetyl-coenzyme A synthetase
Sequence:
MLSANMLRRMHHGVAVTRMLLVSNGKVQVKKSALYPVMAKLARTYATKNYPAHTVINMPALSPTMTTGNIGAFQKKIGDKIEPGDVLCEIETDKAQIDFEQQDEGYLAKILIETGTKDVPVGKPLAVTVENEGDVAAMADFTIEDSSAKEPSAKSGEEKSAPSSEKQSKETSSPSNVSGEERGDRVFASPLARKLAEEKDLDLSQIRGSGPNGRIIKVDIENFKPVVAPKPSNEAAAKATTPAASAADAAAPGDYEDLPLSNMRKIIASRLAESKNMNPHYYVTVSVNMEKIIRLRAALNAMADGRYKLSVNDLVIKATTAALRQVPEVNAAWMGDFIRQYKNVDISMAVATPSGLITPVIRNTHALGLAEISTLAKDYGQRARNNKLKPEEYQGGTFTISNLGMFPVDQFTAIINPPQACILAVGTTVDTVVPDSTSEKGFKVAPIMKCTLSSDHRVVDGAMAARFTTALKKILENPLEIML
Protein: Coiled-coil domain-containing protein 89 (Bc8 orange-interacting protein) (Q9DA73)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7ZW57}. Nucleus {ECO:0000250|UniProtKB:Q7ZW57}. Note=Uniformly distributed within the cell, but becomes recruited to the nucleus upon binding to HEY1. {ECO:0000250|UniProtKB:Q7ZW57}.
Interaction partners:
Sequence:
MPQEEKTLRMDTPPPDEILGKQNENLQNQDEELGFKEMDGLREALANLRGLSEEEKGEKAMLRSRIQEQSQLICILKRRSDEALERCQILELLNSELEEKRLQEMEKLKAQSEHIQKLENHFMILASNHEQMIRFKDAHKSENVKLKEENARLRQENNSLFSQALKDQEAKVLELTTLNKALVEELEVLKQRCAHEASQAQAREEELLGLQNQQACDHAKETEELRSQLQSIKQQHQQATEQMGKEQEANLNLNQELQARLQTVLREKEELLQLSMERGKVLQNKQAEIRQLEEKLETAAMAKKHALERFEQEAVAVDSNLRVRELQRRVDGIQKAYDELRLQSEAFKKHSLDLLSKERELNAKLRHLFP
Protein: CCAAT/enhancer-binding protein zeta (CCAAT-box-binding transcription factor) (CBF) (CCAAT-binding factor) (Q03701)
Organism: Homo sapiens (Human)
Function: Stimulates transcription from the HSP70 promoter.
Subcellular location: Nucleus.
Interaction partners:
- Nucleolar complex protein 2 homolog
- Protein RRP5 homolog
- RNA-binding protein 28
- GTP-binding protein 4
- Probable ATP-dependent RNA helicase DDX56
- U3 small nucleolar ribonucleoprotein protein MPP10
- Ribosome production factor 2 homolog
- RRP12-like protein
- Pumilio homolog 3
- Small subunit processome component 20 homolog
Sequence:
MAAVKEPLEFHAKRPWRPEEAVEDPDEEDEDNTSEAENGFSLEEVLRLGGTKQDYLMLATLDENEEVIDGGKKGAIDDLQQGELEAFIQNLNLAKYTKASLVEEDEPAEKENSSKKEVKIPKINNKNTAESQRTSVNKVKNKNRPEPHSDENGSTTPKVKKDKQNIFEFFERQTLLLRPGGKWYDLEYSNEYSLKPQPQDVVSKYKTLAQKLYQHEINLFKSKTNSQKGASSTWMKAIVSSGTLGDRMAAMILLIQDDAVHTLQFVETLVNLVKKKGSKQQCLMALDTFKELLITDLLPDNRKLRIFSQRPFDKLEQLSSGNKDSRDRRLILWYFEHQLKHLVAEFVQVLETLSHDTLVTTKTRALTVAHELLCNKPEEEKALLVQVVNKLGDPQNRIATKASHLLETLLCKHPNMKGVVSGEVERLLFRSNISSKAQYYAICFLNQMALSHEESELANKLITVYFCFFRTCVKKKDVESKMLSALLTGVNRAYPYSQTGDDKVREQIDTLFKVLHIVNFNTSVQALMLLFQVMNSQQTISDRYYTALYRKMLDPGLMTCSKQAMFLNLVYKSLKADIVLRRVKAFVKRLLQVTCQQMPPFICGALYLVSEILKAKPGLRSQLDDHPESDDEENFIDANDDEDMEKFTDADKETEIVKKLETEETVPETDVETKKPEVASWVHFDNLKGGKQLNKYDPFSRNPLFCGAENTSLWELKKLSVHFHPSVALFAKTILQGNYIQYSGDPLQDFTLMRFLDRFVYRNPKPHKGKENTDSVVMQPKRKHFIKDIRHLPVNSKEFLAKEESQIPVDEVFFHRYYKKVAVKEKQKRDADEESIEDVDDEEFEELIDTFEDDNCFSSGKDDMDFAGNVKKRTKGAKDNTLDEDSEGSDDELGNLDDDEVSLGSMDDEEFAEVDEDGGTFMDVLDDESESVPELEVHSKVSTKKSKRKGTDDFDFAGSFQGPRKKKRNLNDSSLFVSAEEFGHLLDENMGSKFDNIGMNAMANKDNASLKQLRWEAERDDWLHNRDAKSIIKKKKHFKKKRIKTTQKTKKQRK
Protein: Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Lipoyltransferase 2) (Q9D009)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes, which catalyze essential redox reactions (By similarity). Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:A6NK58}.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Lipoyl synthase, mitochondrial
- Glycine cleavage system H protein, mitochondrial
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Acyl carrier protein, mitochondrial
- Fatty acid synthase
- S-acyl fatty acid synthase thioesterase, medium chain
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
Sequence:
MSLPVVRLVWLGRVHYSELLALQEHWLRRLQADPRPGTLSGTKAGVLLVCEPAGPVYTGGLRGGLTPEETTRLRALGAEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARARPPPYTGVWLGERKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAFKETFKCTLISEDSPS
Protein: Short-chain dehydrogenase/reductase aba4 (EC 1.1.1.-) (Abscisic acid biosynthesis cluster protein 4) (A0A384JQF5)
Organism: Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Interaction partners:
Sequence:
MSSQPFTNKVIALTGSASGIGLETAKLLASRGARLSLADIQEDKLKELQAQLESEYYVDVITTKVDVRKFGEVEAWINKTIDNFGKLDGSANLAGVAPESIGLKGIVEQDLDEWEFVLGVNLTGTMNSLKAQLKVMANNGSIVNASSIRGLTGAAKNASYSSAKHGIIGLTRTAAKEVGGKGIRVNAICPGRISTPMLKTAENSIGLHLQPGSANYPPIALGRDGEAKEVAQLVAFLLSDESTYISGADISIDGGWRC
Protein: Prostatic acid phosphatase (EC 3.1.3.2) (5'-nucleotidase) (5'-NT) (EC 3.1.3.5) (Acid phosphatase 3) (Ecto-5'-nucleotidase) (Fluoride-resistant acid phosphatase) (FRAP) (Protein tyrosine phosphatase ACP3) (EC 3.1.3.48) (Thiamine monophosphatase) (TMPase) (Q8CE08)
Organism: Mus musculus (Mouse)
Function: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (By similarity).
Subcellular location: [Isoform 1]: Secreted {ECO:0000305|PubMed:17638863}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17638863}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863}; Single-pass type I membrane protein {ECO:0000255}. Note=Appears to shuttle between the cell membrane and intracellular vesicles. Colocalizes with FLOT1 at cell membrane and in intracellular vesicles (PubMed:17638863). Colocalizes with LAMP2 on the lysosome membrane (By similarity). {ECO:0000250|UniProtKB:P15309, ECO:0000269|PubMed:17638863}.
Interaction partners:
- Solute carrier family 45 member 3
- Plasma kallikrein
- Beta-microseminoprotein
Sequence:
MRAVPLPLSRTASLSLGFLLLLSLCLDPGQAKELKFVTLVFRHGDRGPIETFPTDPITESSWPQGFGQLTQWGMEQHYELGSYIRKRYGRFLNDTYKHDQIYIRSTDVDRTLMSAMTNLAALFPPEGISIWNPRLLWQPIPVHTVSLSEDRLLYLPFRDCPRFEELKSETLESEEFLKRLHPYKSFLDTLSSLSGFDDQDLFGIWSKVYDPLFCESVHNFTLPSWATEDAMIKLKELSELSLLSLYGIHKQKEKSRLQGGVLVNEILKNMKLATQPQKYKKLVMYSAHDTTVSGLQMALDVYNGVLPPYASCHMMELYHDKGGHFVEMYYRNETQNEPYPLTLPGCTHSCPLEKFAELLDPVISQDWATECMATSSHQGRN