wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase 6 catalytic subunit (EC 3.1.3.16) (Protein phosphatase pph-6) (Q09496)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of protein phosphatase 6 (PP6) (By similarity). In complex with saps-1, promotes actomyosin contractility during cytokinesis by regulating the organization of cortical non-muscle myosin II nmy-2 and thus contributing to correct spindle positioning. Also required for the proper generation of pulling forces on spindle poles during anaphase by regulating the cortical localization of gpr-1, gpr-2 and lin-5.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20040490}. Cytoplasm, cell cortex {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20040490}. Note=In embryos, localizes mainly to the cytoplasm and to a lesser extent with microtubule asters. {ECO:0000269|PubMed:20040490}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit ppfr-4
- Serine/threonine-protein phosphatase 6 regulatory subunit
- Serine/threonine-protein phosphatase 2A regulatory subunit sur-6
- TIP41-like protein
- Probable serine/threonine-protein phosphatase PP2A regulatory subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 4
- Serine/threonine-protein phosphatase 2A activator
- Protein let-99
- Protein Phosphatase Four Regulatory subunit
- Casein kinase I gamma
Sequence:
MIDTNLLRVTVCDEGELEKSTTHFIGSRKIEPEQWITWASECKYLPESDAVALCATLIDRLSLEANVVPVSSPVTICGDIHGQFYDLLELFKTGGTVPNTKYVFMGDYVDRGHYSLETVTLLFCLLLKYPNQITLLRGNHESRRISNVYGFYDECQNKYGHGNVHKWFCKVFDVLPIGALIDESVLCVHGGLSPDIRTIDSLMLLDRAQEVPNKGPLCDIMWSDPDDDVEDWVISQRGAGFVFGAKVTEEFLMNNDLSLLCRSHQLVDEGFKYMFNEKLATVWSAPNYCYRCGNAAAVFEIDGNNRSTKYFNAVPDGSREKPDRVVAPYFL
Protein: Histone acetyltransferase KAT6B (EC 2.3.1.48) (Histone acetyltransferase MOZ2) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4) (MYST-4) (Monocytic leukemia zinc finger protein-related factor) (Q8WYB5)
Organism: Homo sapiens (Human)
Function: Histone acetyltransferase which may be involved in both positive and negative regulation of transcription. Required for RUNX2-dependent transcriptional activation. May be involved in cerebral cortex development. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Inhibitor of growth protein 5
- Peregrin
- Chromatin modification-related protein MEAF6
- Histone acetyltransferase KAT6A
- Bromodomain-containing protein 1
- Bromodomain and PHD finger-containing protein 3
- Histone H3.2
- Histone H3.1
- Histone H3.1t
- Histone H3.3
Sequence:
MVKLANPLYTEWILEAIQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKSAKGSRGSCNDLRNVDWNKLLRRAIEGLEEPNGSSLKNIEKYLRSQSDLTSTTNNPAFQQRLRLGAKRAVNNGRLLKDGPQYRVNYGSLDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTTNVKALRWQCIECKTCSACRVQGRNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMNAFTGRGSPGRGQKTKVCTTPSSGHAASGKDSSSRLAVTDPTRPGATTKITTTSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATGTTQKLKPPPSSLPPPTPISGQSPSSQKSSTATSSPSPQSSSSQCSVPSLSSLTTNSQLKALFDGLSHIYTTQGQSRKKGHPSYAPPKRMRRKTELSSTAKSKAHFFGKRDIRSRFISHSSSSSWGMARGSIFKAIAHFKRTTFLKKHRMLGRLKYKVTPQMGTPSPGKGSLTDGRIKPDQDDDTEIKINIKQESADVNVIGNKDVVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYHHHERHISIKAISRATGMCPHDIATTLQHLHMIDKRDGRFVIIRREKLILSHMEKLKTCSRANELDPDSLRWTPILISNAAVSEEEREAEKEAERLMEQASCWEKEEQEILSTRANSRQSPAKVQSKNKYLHSPESRPVTGERGQLLELSKESSEEEEEEEDEEEEEEEEEEEEDEEEEEEEEEEEEEENIQSSPPRLTKPQSVAIKRKRPFVLKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIEVEEDGRKPVLRKAFQHQPGKKRQTEEEEGKDNHCFKNADPCRNNMNDDSSNLKEGSKDNPEPLKCKQVWPKGTKRGLSKWRQNKERKTGFKLNLYTPPETPMEPDEQVTVEEQKETSEGKTSPSPIRIEEEVKETGEALLPQEENRREETCAPVSPNTSPGEKPEDDLIKPEEEEEEEEEEEEEEEEEEGEEEEGGGNVEKDPDGAKSQEKEEPEISTEKEDSARLDDHEEEEEEDEEPSHNEDHDADDEDDSHMESAEVEKEELPRESFKEVLENQETFLDLNVQPGHSNPEVLMDCGVDLTASCNSEPKELAGDPEAVPESDEEPPPGEQAQKQDQKNSKEVDTEFKEGNPATMEIDSETVQAVQSLTQESSEQDDTFQDCAETQEACRSLQNYTRADQSPQIATTLDDCQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQSAISVPSLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSNLTSSSLTQSSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLAEIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHISMRTKSASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGTQPYAQQPMQTPPHGNMMYTAPGHHGYMNTGMSKQSLNGSYMRR
Protein: Chaperedoxin (Heat shock protein CnoX) (Trxsc) (P77395)
Organism: Escherichia coli (strain K12)
Function: Chaperedoxin that combines a chaperone activity with a redox-protective function. Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation. Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes. After bleach stress, it transfers its substrates to the GroEL/GroES and DnaK/DnaJ/GrpE foldases. Lacks oxidoreductase activity.
Interaction partners:
- Protein GrpE
- ATP-dependent protease ATPase subunit HslU
- Glutathione reductase
- Uncharacterized oxidoreductase YbbO
- ATP-dependent protease subunit HslV
- Chaperone protein HtpG
- Thioesterase 1/protease 1/lysophospholipase L1
- Chaperone protein DnaK
- Chaperone protein DnaJ
- Chaperone protein ClpB
Sequence:
MSVENIVNINESNLQQVLEQSMTTPVLFYFWSERSQHCLQLTPILESLAAQYNGQFILAKLDCDAEQMIAAQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRALLDKVLPREEELKAQQAMQLMQESNYTDALPLLKDAWQLSNQNGEIGLLLAETLIALNRSEDAEAVLKTIPLQDQDTRYQGLVAQIELLKQAADTPEIQQLQQQVAENPEDAALATQLALQLHQVGRNEEALELLFGHLRKDLTAADGQTRKTFQEILAALGTGDALASKYRRQLYALLY
Protein: Regulating synaptic membrane exocytosis protein 3 (Nim3) (RIM3 gamma) (Rab-3-interacting molecule 3) (RIM 3) (Q9UJD0)
Organism: Homo sapiens (Human)
Function: Regulates synaptic membrane exocytosis.
Subcellular location: Synapse {ECO:0000250}.
Interaction partners:
Sequence:
MFNGEPGPASSGASRNVVRSSSISGEICGSQQAGGGAGTTTAKKRRSSLGAKMVAIVGLTQWSKSTLQLPQPEGATKKLRSNIRRSTETGIAVEMRSRVTRQGSRESTDGSTNSNSSDGTFIFPTTRLGAESQFSDFLDGLGPAQIVGRQTLATPPMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKVYLLENGACLAKKKTKMTKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQIMLDELDLSAAVTGWYKLFPTSSVADSTLGSLTRRLSQSSLESATSPSCS
Protein: PE family protein (O86338)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MRSMGFLHRACRAPSSLPAPLMARPGRSVLARPAATPPGPLCATTRPRPPQGNQPPASRISNFPPKRHKTRVLAAAEDEVSAAVAALISAHGRRHHSLNNQAAAFHGQFAQNLNVGAGSCASAETTADAPTQALLGPADRQRRQRRAVRQWLVRWAAHPGRATRGFHNHRQ
Protein: Response regulator ActA (Q93P59)
Organism: Myxococcus xanthus
Interaction partners:
Sequence:
MGFEAVNPGWASKSGGEKFTREGGTVGVRRKRVGKAGQPPTVLVVEPRAADLERTRLLLAEAGFRVVPVTRFDAAVPLFEVIRPAAVLLDAQAPDFAAVQVARRLRQLTHGAVPLLYLVDERDAEARRYCLERGQCVDLVPRSGSGSELATKLHAQLKLKDAVLRAAAGEEAGTAQALHDPVTGLYNRPFLLEFISLEARRAERYGGGFSVVAAEVGGWSAFRKEFGRGMAERLLVYSAVVLGQTVRDADAVARVGDCQFALMLPGTPAESVPEVVSRVAARFDTARFQVEGKVVRTSLELGTVSFPDSVGTPTQLLSAAQQDMRRAREFRRMVGSTSRLSV
Protein: Putative ATP-binding protein Rv3427c in insertion sequence (Q50701)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative transposase Rv3428c
- Replicative DNA helicase DnaB
- Ribonucleoside-diphosphate reductase subunit beta nrdF2
- Probable transposase for insertion sequence element IS1533
- Possible transposase
Sequence:
MSICDPALRNALRTLKLSGMLDTLDARLAQTRNGDLGHLEFLQALREDEIARRESAALTRRLRRAKFEAQATFEDFDFTANPKLPGAMLRDLAALRWLDAGESVILHGPVGVGKTHVAQALVHAVARRGGDVRFAKTSRMLSDLAGGHADRSWGQRIREYTKPLVLILDDFAMREHTAMHADDLYELISDRAITGKPLILTSNRAPNNWYGLFPNPVVAESLLDRLINTSHQILMDGPSYRPRKRPGRTTS
Protein: Protein SGT1 homolog B (AtSGT1b) (Protein ENHANCED DOWNY MILDEW 1) (Protein ENHANCER OF TIR1-1 AUXIN RESISTANCE 3) (Suppressor of G2 allele of SKP1 homolog B) (Q9SUT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plant innate immunity. Is essential for resistance conferred by multiple R genes recognizing different oomycete pathogen isolates like avirulent H.parasitica (downy mildew). Contributes additively with RAR1 to RPP5-dependent resistance. Not required for RPM1, RPS2, RPS4 and RPS5-mediated resistance. Functions as negative regulator of RPS5 accumulation by assisting its degradation. May be involved in heat shock response by associating with HSC70-1 chaperone. Required for the SCF(TIR1)-mediated degradation of Aux/IAA proteins, but maybe not for SCF(TIR1) assembly or binding to its Aux/IAA substrates. Probably required for SCF-mediated ubiquitination, by coupling HSP90 to SCF complex for ubiquitination of HSP90 client proteins. Required for the coronatine/jasmonic acid-mediated signal transduction pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18065690}. Nucleus {ECO:0000269|PubMed:18065690}.
Interaction partners:
- Endoplasmin homolog
- Heat shock protein 90-5, chloroplastic
- Heat shock protein 90-3
- Cysteine and histidine-rich domain-containing protein RAR1
- Heat shock protein 90-6, mitochondrial
- Heat shock protein 90-2
- Heat shock protein 90-1
- Heat shock protein 90-4
- SH3 domain-containing protein
- Heat shock 70 kDa protein 4
Sequence:
MAKELAEKAKEAFLDDDFDVAVDLYSKAIDLDPNCAAFFADRAQANIKIDNFTEAVVDANKAIELEPTLAKAYLRKGTACMKLEEYSTAKAALEKGASVAPNEPKFKKMIDECDLRIAEEEKDLVQPMPPSLPSSSTTPLATEADAPPVPIPAAPAKPMFRHEFYQKPEEAVVTIFAKKVPKENVTVEFGEQILSVVIDVAGEEAYHLQPRLFGKIIPEKCRFEVLSTKVEIRLAKAEIITWASLEYGKGQSVLPKPNVSSALSQRPVYPSSKPAKDWDKLEAEVKKQEKDEKLDGDAAMNKFFSDIYSSADEDMRRAMNKSFAESNGTVLSTNWKEVGTKKVESTPPDGMELKKWEY
Protein: Spermidine synthase (Q99MI5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Ornithine decarboxylase
- Antizyme inhibitor 2
- Guanidino acid hydrolase, mitochondrial
- S-methyl-5'-thioadenosine phosphorylase
- RCG27151, isoform CRA_a.
- Spermine synthase
- Diamine acetyltransferase 1
- Spermidine/spermine N1-acetyl transferase 2
- Amine oxidase
Sequence:
MEPGPDGPAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVSYAYCTIPTYPSGQIGFMLCSKNPSTNFREPVQQLTQAQVEQMQLKYYNSDMHRAAFVLPEFTRKALNDIS
Protein: Protein K7 (P68467)
Organism: Vaccinia virus (strain Copenhagen) (VACV)
Function: Virulence factor that affects the acute immune response to infection. Bcl-2-like protein which, through its interaction with the DEAD box RNA helicase DDX3X/DDX3, prevents TBK1/IKKepsilon-mediated IRF3 activation. Contributes to virulence by binding to the host TRAF6 and IRAK2 and preventing host NF-kappa-B activation.
Subcellular location: Host cytoplasm {ECO:0000250|UniProtKB:P68466}.
Interaction partners:
Sequence:
MATKLDYEDAVFYFVDDDKICSRDSIIDLIDEYITWRNHVIVFNKDITSCGRLYKELMKFDDVAIRYYGIDKINEIVEAMSEGDHYINFTKVHDQESLFATIGICAKITEHWGYKKISESRFQSLGNITDLMTDDNINILILFLEKKLN
Protein: Gap junction protein (F1RSW9)
Organism: Sus scrofa (Pig)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
Sequence:
MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHADPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAAFMYVFYLLYPGYAMVRLVKCEAYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIFRACARRAQRRSNPPSRKGSGGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (A1Z7L9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLSALRLIFLGALLGASVCASPIEFVMDTSLNGSRSDPATATHPGKWPPTTKAPALRAPAGTAGHAYQSPSSSLAADNRSHDNNNASAVSMLLPQDGDASGAVAPAVTPQLPIYIAQPSAKKPENKIKCHCDTCKESNNICETDGFCFTSVEKNSDGSIIFSYSCMVVKYNMQRSKPFECLTSNERFDTYRIDCCKSDFCNKNEIMKRIFETDYVPHRLTSWEFVAIILGATLFICFTGTSTWYYCQRRKRMASGRTFAKEDSAYDPILNGNTTIHDIIEMTTSGSGSAGLPLLVQRSIARQVQLCHVIGKGRFGEVWRGRWRGENVAVKIFSSREECSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVTDYHENGSLFDYLTTHPVDTNTMLNMSLSIATGLAHLHMDIVGTRGKPAIAHRDLKSKNILVKSNLSCAIGDLGLAVRHVEKNDSVDIPSTHRVGTKRYMAPEVLDESMNDQHFDSYKRADVYAFGLILWEIARRCNMGMIYDEYQLPYYDVVQPDPSIEEMKKVVCIEKCRPNIPNRWHASDVLHNMAKVMKECWYPNPVARLTALRIKKTLASISVEDKVKN
Protein: 17.4 kDa class I heat shock protein (17.4 kDa heat shock protein 1) (AtHsp17.4A) (P19036)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Chaperone protein ClpB1
- Heat shock protein 90-1
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 5
- Heat stress transcription factor A-2
- Heat shock 70 kDa protein 8
- Heat stress transcription factor A-9
- Heat stress transcription factor A-4a
- E3 UFM1-protein ligase 1 homolog
Sequence:
MSLVPSFFGGRRTNVFDPFSLDVWDPFEGFLTPGLTNAPAKDVAAFTNAKVDWRETPEAHVFKADVPGLKKEEVKVEVEDGNILQISGERSSENEEKSDTWHRVERSSGKFMRRFRLPENAKVEEVKASMENGVLSVTVPKVQESKPEVKSVDISG
Protein: Large ribosomal subunit protein bL34m (39S ribosomal protein L34, mitochondrial) (L34mt) (MRP-L34) (Q0E959)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BQ48}.
Interaction partners:
Sequence:
MLQGMLQRTCLAVVSTAQTLIVRDKHAFNRAVLKPKVRCHFPKPMEVKRINVHGWNARMSTPEGRRVLMNRILKGRHNLSH
Protein: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-) (Q97SE7)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Interaction partners:
Sequence:
MNFETVIGLEVHVELNTNSKIFSPTSAHFGNDQNANTNVIDWSFPGVLPVLNKGVVDAGIKAALALNMDIHKKMHFDRKNYFYPDNPKAYQISQFDEPIGYNGWIEVKLEDGTTKKIGIERAHLEEDAGKNTHGTDGYSYVDLNRQGVPLIEIVSEADMRSPEEAYAYLTALKEVIQYAGISDVKMEEGSMRVDANISLRPYGQEKFGTKTELKNLNSFSNVRKGLEYEVQRQAEILRSGGQIRQETRRYDEANKATILMRVKEGAADYRYFPEPDLPLFEISDEWIEEMRTELPEFPKERRARYVSDLGLSDYDASQLTANKVTSDFFEKAVALGGDAKQVSNWLQGEVAQFLNAEGKTLEQIELTPENLVEMIAIIEDGTISSKIAKKVFVHLAKNGGGAREYVEKAGMVQISDPAILIPIIHQVFADNEAAVADFKSGKRNADKAFTGFLMKATKGQANPQVALKLLAQELAKLKEN
Protein: pH-response transcription factor pacC/RIM101 (P0CS62)
Organism: Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Function: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including RIM101 itself) and represses transcription of acid-expressed genes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- pH-response regulator protein palA/RIM20
- Calpain-like protease palB/RIM13
- Mitogen-activated protein kinase HOG1
- Vacuolar-sorting protein SNF7
Sequence:
MAYPTLPPNLLSTPNTYSDSVSPTDPEPITPELVSREPEKPAQKAAKTAMNNTSTASKPSESKGETLPCKWTGCSHISDSPDELYDHLCTVHVGRKSTNNLCLTCGWENCGTKCVKRDHITSHLRVHTPLKPHPCAVCGKTFKRPQDLKKHERIHTAEHHQLHKLSKAPTTADPEFNSRVSLSSATRIDRPRSPLSTSLSPTSTSSHSLHSSSSPFDHLLATGFHTDKSVSPTPSALALLHKKQHEELAAYQQKEMLVLQQLAFNQQQSQAYAARLAAEPFGTGAGAKRGQADAFHDLLSDVKKRKVEPVYDQDMIHRLNALVPPSLPTSFPTLPSLGGYNQYQTFPSFNGYPSLPSLHTSIYPTTAPQAQYSNQSPLPIPEIKTEADLAMFNEFMISLGRDAAANKAGPHPMTQSASGSGASNGYSASNSGTPLSETSGGVEDLFNAEELASLGLAGMPGISIHSGGSHNSNDESTHSLSDASPPAVSFGGLYPSLDAMRNRTNSAPDVSALSGAARRPIAGLPRTSMGNAHNTSTNQSTKPSYLSGMFGHSSSQQYDGTTHNYLHGLSNEHHNDYSHSANNGATNAYASFDSLARNKQSFPAATLAPKMFHNKVYRDVAPLGTAVSKRARESAERTNVEDSDREELYADQESNHGYAVSNERAREERTPKIPVRSLIASIRTLSPSTAADGEDDLKLPAISPSHVEPGTDLPPLYSIQRGGHSSGQYRRASSLSSNSTSTSGSSSFNSSLAPSNVASGTTTPRGSTPPRGVPTKRHTEDEIVRGVKRLELGPAEPLRSTTPELPDSGTTEQALERDQKPDISALSLSSSPTPPSNNPPPSVSTANEEGKDMTIEEMRRRHAALIKSWLVAVNLQWRRKKMEEMQRQQREEMEELEEGGEAMNVDERERERVEVVA
Protein: UPF0250 protein YbeD (P0A8J4)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Octanoyltransferase
- UPF0716 protein FxsA
- PhoH-like protein
- Small heat shock protein IbpA
- Protein GrpE
Sequence:
MKTKLNELLEFPTPFTYKVMGQALPELVDQVVEVVQRHAPGDYTPTVKPSSKGNYHSVSITINATHIEQVETLYEELGKIDIVRMVL
Protein: 2-acylglycerol O-acyltransferase 2 isoform 2 (EC 2.3.1.22) (Monoacylglycerol O-acyltransferase 2) (F1QSW7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MRDYFPIRLIKTADLDTRKNYVMGFHPHGILVAGAFTNFCTEATGFSKLFPGIKSNLLMLPLWFRAPFFRDYIMSAGLVPSDKESAGYLLRRKGGGNAVVIAVGGAPEALDAHPGDYTVHLANKKGFIKLAIEHGADLVPIYSFGENEVFDQVQNPRGTWLRYIQERLQRIMGVSLPLFHARGVFQYTFGLMPYRKPINTVVGRPIPVEKNEKPTAEELDVYHQRYMDELARLFEDHKGNYGVPEDTHLVFQ
Protein: Corrinoid/iron-sulfur protein small subunit (C/Fe-SP small subunit) (CFeSP small subunit) (Q07341)
Organism: Moorella thermoacetica (Clostridium thermoaceticum)
Function: Acts as a methyl group carrier in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.
Interaction partners:
Sequence:
MAVQILRDRSRAAVQKVVLGATKDQGGTRSHTIVVGGDAALPFHHFEGEIVNRPVIGMEVQDIVPDWPDVLKDPFTDVINEPGRWAQKCVAEYGADLIYLKLDGADPEGANHSVDQCVATVKEVLQAVGVPLVVVGCGDVEKDHEVLEAVAEAAAGENLLLGNAEQENYKSLTAACMVHKHNIIARSPLDINICKQLNILINEMNLPLDHIVIDPSIGGLGYGIEYSFSIMERIRLGALQGDKMLSMPVICTVGYEAWRAKEASAPVSEYPGWGKETERGILWEAVTATALLQAGAHILLMRHPEAVARVKENIDQLMVSNAY
Protein: DNA replication licensing factor MCM5 (EC 3.6.4.12) (B1AHB0)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368063}.
Interaction partners:
Sequence:
MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK
Protein: Transcription termination factor 1 (TTF-1) (RNA polymerase I termination factor) (Transcription termination factor I) (TTF-I) (mTFF-I) (Q62187)
Organism: Mus musculus (Mouse)
Function: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:7720715}. Nucleus, nucleolus {ECO:0000269|PubMed:20513429, ECO:0000269|PubMed:7720715}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20513429}. Note=May be localized to the nucleolus in an NPM1/B23-dependent manner (PubMed:20513429). May be displaced from the nucleolus into the nucleoplasm in an CDKN2A/ARF-dependent manner (PubMed:20513429). May shuttle back and forth from nucleoplasm to nucleolus (PubMed:20513429). {ECO:0000269|PubMed:20513429}.
Interaction partners:
- Bromodomain adjacent to zinc finger domain protein 2A
- Thyroid transcription factor 1-associated protein 26
- Protein kinase C gamma type
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Protein kinase C beta type
- Protein kinase C alpha type
- Nucleolar transcription factor 1
- TATA box-binding protein-associated factor RNA polymerase I subunit D
- Caveolae-associated protein 1
Sequence:
MKGGTSKFKTHTETLYKKKKWSSVSEKRPQKCPSQCLESKQPQVSVLGKRRRASQTPAQETLESEWPQKAKRKKRRREPQTPAQETLESEWPQKAKKKKRRGEPQTPTQESLESEQPPVSLLGKRRRESQTPAQENSESEQPRKAKRRRKKRKGSQQPTSSLLKTPETFLKAKKTTSAHKKKKNSVLEVDMETGIILVDKENMENLLETSRKDVDIVYVDMSKGQRSAKVRETGELPAAKPQEHGCRELLGDVRSRKKQKHLQKVAPWDVVQGSQPESISLPPSEPLSSEDLEGKSTEAAVFCKKKSKKNVFRSQELEPIPDSLDDSETISERLDSTHHGGAVGAGEECESTKESHSIKKKSKKKKHKSVALATSSDSASVTDSKAKNALVDSSEGSGAVREEDVDHRPAEAEAQACSTEKHREAMQRLEPTHEEESNSESASNSAARHISEDRRESDDSDVDLGSAVRQLREFIPDIQERAATTIRRMYRDDLGRFKEFKAQGVAIRFGKFSAKENKQIEKNVQDFLSLTGIESADKLLYTDRYPEEKTLITNLKRKHAFRLHIGKGIARPWKLVYYRAKKIFDVNNYKGRYNEEDTKKLKAYHSLHGNDWKKIGAMVARSSLSVALKFSQIGGTRNQGAWSKAETQRLIKAVEDVILKKMSPQELRELDSKLQEDPEGRLSIVREKLYKGISWVEVEARVETRNWMQCKSKWTEILTKRMTHGGFVYRGVNALQAKITLIERLYELNVNDANEIDWEDLASAIGDVPPPFVQAKFYKLKAACVPFWQKKTFPEIIDYLYKNSLPLLKEKLDKKMKKKDGQIQTPAAPKQDFLFKDIFHCDDDSDEGSPEEPSASDVQ
Protein: Tyrosine-protein phosphatase non-receptor type 13 (EC 3.1.3.48) (A0A0G2K1K1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000933}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHVSLAEALEVRGGPLQEEEIWAVLNQSAESLQEVFRRVSIADPAALGFIISPWSLLLLPSGSVSFTDENVCSQDLRAFTAPEVLQSHSLTSLSDVEKVHIYSLGMTLYWGADHEVPQSQPIKLGDHLNSILLGMCEDVLYARVSVRTVLDACSAHIRNSNCAPSFSYVKQLVKLVLGNISGTDPLSHSSEEKPDRSQAIRDRLRGKGLPIGRSSTSDALDTHKAPLSQQTFLNKGLSKSMGFLSVRDTQEEEDYSKEIPSDNNSRHEDSEPFSSPYQFKTSSPHIDVLSKKKTWASSMDLLCAADRDLSGEIGRYQHCDPETGTGRTSITSRKKEGRYSDGSIALDVFGPQKAEPVIHSRELPASSAVSSALDRIRERQKKLQVLREAMNVEEPVRRYKTYHSDLFSTSSESPSIISSDSDFRQVRKSEASKRFESSSGLPGVDDTVQSRPSRQYETSLEGSLINQEMMLRRQEEEMMQLQARMALRQSRLSLYPGDTIKTSMLDISRDPLREMALETAMTQRKLRNFFGPEFVKTTVEPFASLDLPRSILLQTKKGKSEEQRKKVNIMLLSGQRLELTCDTKTVCRDVFDMVVAHIGLVEHHLFALATLKENEYFFVDPDLKLTKVAPEGWKEEPKRKGKAAVDFTLFFRIKFFMDDVSLIQHSLTCHQYYLQLRKDLLEERIHCDDEASLLLASLALQAEYGDYQPEVHGLSYFRLEHYLPARVMEKLDMSYIKEELPKLHNTYAGASEKETELEFLKVCQRLTEYGVHFHRVHPEKKSQTGILLGVCSKGVLVFEVHNGVRALVLRFPWRETKKISFSKKKITLQNTSDGIKHAFQTDSSKACQYLLQLCSSQHKFQLQMRARQSNQDAQDLERASFRSLNLQAESVRGFNVGRAISTGSLASSTFNKLAVRPLSVQAEILKRLSCSEWSLYQPLQNSSKEKNDKASWEEKPRGMSKSYHDLSQASLCPHRKQVINMESLPQAFAELVGKPLYPMARSDTESLAGLPQLNNSKSVASLNRSPERRSHESDSSVEDPGQAYVVGMSLPSSGKSSSQVPFKDNDSLHKRWSTVSSPEREITLVNLKKDLKHGLGFQIVGGGKMGRLDLGVFISAVTPGGPADLDGCLKPGDRLISVNSVSLEGVSHHAAVDILQNAPEDVTLVISQPKEKPTKVPSTPVHFANGMKNYTKKPSSMQDSAMDPSEDQPWPRGPLRHVPESPFGLSSGLREGSLSSQDSRTESASLSQSHVNGFFTSHLGDRGWQEPQHSSPSPPVTSKITEKTFSDSYRSPARRQGTCDVTELPGCADSDIDDPTYSSSQDRQAPKQEPSSPLKASDKMSFAAFPGPSPEPGDAFEVELAKTDGSLGISVTGGVNTSVRHGGIYVKAVIPNGAAETDGRIHKGDRVLAVNGVSLEGATHKQAVETLRNTGQVVHLLLEKGQSPTSRERDPASPRCPTPDQDAQSQAPEKMEKQTAHVKDYSFVTEDNTFEVKLFKNSSGLGFSFSREDNLTPELINGSIVRVKKLFPGQPAAESGKINVGDVILKVNGAPLKGLSQQDVISALRGTAPEVSLLLCRPAPGVLPEVNTALLTPLHSPAHAFLNSRKEHSQPSPLSVEQCASSDENGLSGQSKRQCKPPSRRESYSDHSDSGEEESVRAAAKMPNVIPLSAFAPEALRSQGEPASTMFYLPRKIPGKPESESSRLPHPLDVSPGQIRQPPAECAPSDSPGKHLTHLASQLHKEENMTALKNDLGNHLEDSELEVELLITLVKSEKGSLGFTVTKGSQSIGCYVHDVIQDPAKGDGRLRPGDRLVKVNDADVTNMTHTDAVNLLRAAPKTVRLVIGRILELPRMPVFPHLLPDITVTCHGEELGFSLSGGRGSPHGVVYISDINPRSAAAVDCSLQLLDIIHYVNGVSTHGMTLEEANRALDLSLPSVVLKVTRDGCPVVPCSTRSAISALRPLESSDLVVRCGRAFQVNGDGASGAMCPGGKGLSSPRKKSADLMEARESDSRDDDVYDDPQEAEVIQSLLDVVDEEAQNLLNQTKASRRACSPDPLRTNGEASEDGEDTDCDGSPLPEDVPESVNGGGGKACFASLIQASQEEKPVKEEATQESRESTTETTDREDSSKDPLFLTNEELAALPVVRVPPSGKYTGTQLQATIRTLQGLLDQGIPSKELENLQELKPLDQCLIGQTKENRRKNRYKNILPYDTTRVPLGDEGGYINASFIRIPVGTQEFVYIACQGPLPTTVGDFWQMVWEQNSTVIAMMTQEVEGEKIKCQRYWPSILGTTTMANERLRLALLRMQQLKGFVVRVMALEDIQTGEVRHISHLNFTAWPDHDTPSHPEDLLTFISYMRHIRRSGPVITHCSAGIGRSGTLICIDVVLGLISQDLEFDISDLVRCMRLQRHGMVQTEGQYVFCYQVVLYVLTHLQAEEQKAQPGLPQ