wanglab/gogpt-training-data huggingface dataset:
Protein: Ribonuclease Z (RNase Z) (EC 3.1.26.11) (tRNA 3 endonuclease) (tRNase Z) (P54548)
Organism: Bacillus subtilis (strain 168)
Function: Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Interaction partners:
- Ribonuclease R
- Ribonuclease J1
- Ribonuclease PH
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease J2
- Ribonuclease 3
- Ribonuclease M5
- 3'-5' exoribonuclease YhaM
- Ribonuclease Y
- Endoribonuclease YbeY
Sequence:
MELLFLGTGAGIPAKARNVTSVALKLLEERRSVWLFDCGEATQHQILHTTIKPRKIEKIFITHMHGDHVYGLPGLLGSRSFQGGEDELTVYGPKGIKAFIETSLAVTKTHLTYPLAIQEIEEGIVFEDDQFIVTAVSVIHGVEAFGYRVQEKDVPGSLKADVLKEMNIPPGPVYQKIKKGETVTLEDGRIINGNDFLEPPKKGRSVVFSGDTRVSDKLKELARDCDVLVHEATFAKEDRKLAYDYYHSTTEQAAVTAKEARAKQLILTHISARYQGDASLELQKEAVDVFPNSVAAYDFLEVNVPRG
Protein: Cilia- and flagella-associated protein 95 (Q5VTT2)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9CQC3}. Cell membrane {ECO:0000269|PubMed:28345668}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:28345668}.
Interaction partners:
- Tektin-1
- Cilia- and flagella-associated protein 52
- Cilia- and flagella-associated protein 276
- Tektin-3
- Protein Flattop
- EF-hand domain-containing family member B
- Cilia- and flagella-associated protein 53
- Cilia- and flagella- associated protein 210
- Tektin-4
- RIB43A-like with coiled-coils protein 2
Sequence:
MDSLDRSCQDWCDRKQHWLEIGPPDLVERKGSLTLRSHHKKYSKPVLVYSWHRDREAFPKGYDIEGPEKVKKLCNSTYRRLGTDESPIWTSETHEKLSQMCLNTEWVEMKSKALLNEETVSSGIIERVTGLPATGFGAVFPRHPPDWSKMCALTTYSEDYVPPYDYQPHAYPCQDDYSIVHRKCRSQFTDLNGSKRFGINTWHDESGIYANSDVKQKLYPLTSGPIVPI
Protein: tRNA/rRNA methyltransferase SpoU type domain-containing protein (Q381U1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFFNQLLLRLRVTPRRFPQASAPPRKVCTDDPLTRWSQMLRLGWPKHCHLPHLSVGLEGCTSAFNAMNSIRTCMFYGTAVPPSFLSLSKAEDIKNIRDRQCGTDDAGSNPETTSLVLNRVAQFGKEAFFRGQWAENFPLVALENFTHRSQSLFTCRISSVARLLIGHENRGVSSKYIECDNATISDESDGQCADCVVYVPQYGTISSLNVVTSMGIALFYAFLDQNFPHSRSLMTETTKRAFCPNTDDELEALLSYQRCFRERIPTTHGYGVPSRIDPRPIHPLYFGKNVENIIDTHNHLRKLLLRACSDQRRPGKGRCFGLSVLCQNEIDLRNLGGIVRSANAFLVDNIFYFGRRKINVVGTVGTQHYTPPTYLGDLFEGCGSSIEDMEPQLNLMKKRLDEANVPCRWWFLDCGHKFLYSASRSRVSDLQDLQGSGGSQAALEAVKWYETRYSDPNCMLSLCESEETLREAIREGVLLVVPQEGILPPLHILQRCEKILTVLPHDFTDTVSAGLPVAVAAGIALQRLSAVMHPNITTL
Protein: Zinc finger protein 335 (NRC-interacting factor 1) (NIF-1) (Q9H4Z2)
Organism: Homo sapiens (Human)
Function: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters. Enhances ligand-dependent transcriptional activation by nuclear hormone receptors. Plays an important role in neural progenitor cell proliferation and self-renewal through the regulation of specific genes involved brain development, including REST. Also controls the expression of genes involved in somatic development and regulates, for instance, lymphoblast proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12215545}.
Interaction partners:
- CCR4-NOT transcription complex subunit 6
- Protein YIPF6
- WD repeat-containing protein 62
- Ankyrin repeat and LEM domain-containing protein 2
Sequence:
MEENEVESSSDAAPGPGRPEEPSESGLGVGTSEAVSADSSDAAAAPGQAEADDSGVGQSSDRGSRSQEEVSESSSSADPLPNSYLPDSSSVSHGPVAGVTGGPPALVHSSALPDPNMLVSDCTASSSDLGSAIDKIIESTIGPDLIQNCITVTSAEDGGAETTRYLILQGPDDGAPMTSPMSSSTLAHSLAAIEALADGPTSTSTCLEAQGGPSSPVQLPPASGAEEPDLQSLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPVAAAAAAAGKKGRLRKWSTSTKSQEEEGPEEEDDDDIVDAGAIDDLEEDSDYNPAEDEPRGRQLRLQRPTPSTPRPRRRPGRPRKLPRLEISDLPDGVEGEPLVSSQSGQSPPEPQDPEAPSSSGPGHLVAMGKVSRTPVEAGVSQSDAENAAPSCPDEHDTLPRRRGRPSRRFLGKKYRKYYYKSPKPLLRPFLCRICGSRFLSHEDLRFHVNSHEAGDPQLFKCLQCSYRSRRWSSLKEHMFNHVGSKPYKCDECSYTSVYRKDVIRHAAVHSRDRKKRPDPTPKLSSFPCPVCGRVYPMQKRLTQHMKTHSTEKPHMCDKCGKSFKKRYTFKMHLLTHIQAVANRRFKCEFCEFVCEDKKALLNHQLSHVSDKPFKCSFCPYRTFREDFLLSHVAVKHTGAKPFACEYCHFSTRHKKNLRLHVRCRHASSFEEWGRRHPEEPPSRRRPFFSLQQIEELKQQHSAAPGPPPSSPGPPEIPPEATTFQSSEAPSLLCSDTLGGATIIYQQGAEESTAMATQTALDLLLNMSAQRELGGTALQVAVVKSEDVEAGLASPGGQPSPEGATPQVVTLHVAEPGGGAAAESQLGPPDLPQITLAPGPFGGTGYSVITAPPMEEGTSAPGTPYSEEPAGEAAQAVVVSDTLKEAGTHYIMATDGTQLHHIELTADGSISFPSPDALASGAKWPLLQCGGLPRDGPEPPSPAKTHCVGDSQSSASSPPATSKALGLAVPPSPPSAATAASKKFSCKICAEAFPGRAEMESHKRAHAGPGAFKCPDCPFSARQWPEVRAHMAQHSSLRPHQCSQCSFASKNKKDLRRHMLTHTKEKPFACHLCGQRFNRNGHLKFHIQRLHSPDGRKSGTPTARAPTQTPTQTIILNSDDETLATLHTALQSSHGVLGPERLQQALSQEHIIVAQEQTVTNQEEAAYIQEITTADGQTVQHLVTSDNQVQYIISQDGVQHLLPQEYVVVPEGHHIQVQEGQITHIQYEQGAPFLQESQIQYVPVSPGQQLVTQAQLEAAAHSAVTAVADAAMAQAQGLFGTDETVPEHIQQLQHQGIEYDVITLADD
Protein: Bowman-birk type proteinase inhibitor (TaTI) (P83284)
Organism: Amburana acreana (Cerejeira) (Torresea acreana)
Function: Inhibits trypsin, chymotrypsin, plasmin and factor XIIa. Does not inhibit factor Xa, thrombin and plasma kallikrein.
Interaction partners:
Sequence:
SSKWEACCDRCACTKSIPPQCHCADIRLNSCHSACESCACTRSIPAKCRCFDITDFCYKPCSG
Protein: Insulin-induced gene 2 protein (INSIG-2) (Q80UA9)
Organism: Rattus norvegicus (Rat)
Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5U4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y5U4}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- Sterol regulatory element-binding protein 2
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Insulin-induced gene 1 protein
- Sterol regulatory element-binding protein 1
- E3 ubiquitin-protein ligase AMFR
Sequence:
MAEGETESPRPKKRGPYISSVTSQSVNVVIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNFQFSLTLAALSVGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE
Protein: Cytochrome b-c1 complex subunit 2, mitochondrial (Complex III subunit 2) (Core protein II) (Ubiquinol-cytochrome-c reductase complex core protein 2) (P32551)
Organism: Rattus norvegicus (Rat)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties. May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated into complex III (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07257}; Matrix side {ECO:0000250|UniProtKB:P07257}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 7
- Ubiquinol-cytochrome c reductase, complex III subunit X.
Sequence:
MKLLSRAGSFSRFYSLKVAPKLKTSAPGGVPLQPQELEFTKLPNGLVIASLENYAPLSRIGLFIKAGSRYENYNYLGTSHLLRLASTLTTKGASSFKITRGIEAVGGKLSVTATRENMAYTVEGIRDDIEILMEFLLNVTTAPEFRRWEVAALRSQLKIDKAVAFQNPQTRIIENLHDVAYKNALANPLYCPDYRMGKITSEELHYFVQNHFTSARMALVGLGVSHSILKEVAEQFLNIRGGLGLAGAKAKYRGGEIREQNGDNLVHAAIVAESAAIGNAEANAFSVLQHLLGAGPHIKRGNNTTSLLSQSVAKGSQQPFDVSAFNASYSDSGLFGIYTVSQAAAAGDVINAAYNQVKAVAQGNLSSADVQAAKNKLKAGYLMSVETSEGFLSEIGSQALATGSYMPPPTVLQQIDAVADADVVKAAKKFVSGKKSMTASGNLGHTPFLDEL
Protein: PcfF (Plasmid mobilization relaxosome protein MobC) (Q5G3N6)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Interaction partners:
Sequence:
MENKQKLKRPIQRIVRLSEEENNLIKRKIEESFFPNFQNFALHLLIQGEIRHVDYSELNRLTTEIHKIGININQMARLANQFHEISSEDIKDLTDKVQSLNALVQSELNKLIKRKDQS
Protein: Telomerase Cajal body protein 1 homolog (WD repeat-containing protein 79) (Q6NL34)
Organism: Drosophila melanogaster (Fruit fly)
Function: RNA chaperone that plays a key role in Cajal body formation. Specifically recognizes and binds the Cajal body box (CAB box) present in both small Cajal body RNAs (scaRNAs). Probably acts by mediating localization of scaRNAs to Cajal bodies.
Subcellular location: Nucleus, Cajal body {ECO:0000269|PubMed:24149844}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit 4
- H/ACA ribonucleoprotein complex subunit 1
- H/ACA ribonucleoprotein complex subunit 3
- IP08469p
Sequence:
MIENSFKMEMHFKNRWQAASLFLRYPRTVTLCLSGKSGDMDESVNLSTSMGDVEASMLNHNVSFSSTMVTSNGDLSLPKLSVTLSAEEILKLRSGRPKNAVESPHAGVPMETSLAAEEEANGDEEEESVRVVDIEDTLELTSNGNEAKPEDQELAIAPVLQYFQGALVELGRRCWTSSTEAQHYTKGCYWSPDGTCLLVPVHLDGMHVIEMPSDLYSADTVQPARSLTKLQSEVHVPEGGTVYDCVWYPHMNSLQPETCLWLATRQHEPIHMWDAFDGSLRCSYSGYDAVDEVMAAISLAFSHDGEQIYAGYKRCIKIFDTSRPGRFCDDYPVKFAISCIAQTTAHPHTLTCGNWHGYIQHFDLRCSHKQGPLFTLGGHKGGITQLRYGEFGNGEWHLFSGARKCDKILQWDMRNYKQPLVELQRHVDTNQRIQFDLASDSNWLASGDTRGFVNVWDLKKYGDPSVLPLHSDCCNGVALNPAMPILATSSGQFHFTDQSAQGDNVTLNGTETTELPAPADVNQNQKEVLYENAVVMWWCGQTG
Protein: Inorganic phosphate transporter 1-1 (AtPht1;1) (H(+)/Pi cotransporter) (Q8VYM2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity transporter for external inorganic phosphate. Acts as a H(+):phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16284308, ECO:0000269|PubMed:24122828}; Multi-pass membrane protein {ECO:0000269|PubMed:16284308}. Note=Localizes at the plasma membrane, where it interacts with NLA. {ECO:0000269|PubMed:24122828}.
Interaction partners:
- SEC12-like protein 1
- Inorganic phosphate transporter 2-1, chloroplastic
- Phosphate transporter PHO1
- Probable ubiquitin-conjugating enzyme E2 24
- Protein PHOSPHATE STARVATION RESPONSE 1
- Phosphate transporter PHO1 homolog 1
- Protein PHR1-LIKE 1
- SPX domain-containing protein 1
- SPX domain-containing protein 3
- Inositol-3-phosphate synthase isozyme 1
Sequence:
MAEQQLGVLKALDVAKTQLYHFTAIVIAGMGFFTDAYDLFCVSLVTKLLGRIYYFNPESAKPGSLPPHVAAAVNGVALCGTLSGQLFFGWLGDKLGRKKVYGLTLVMMILCSVASGLSFGHEAKGVMTTLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFIAAVFAMQGVGILAGGFVALAVSSIFDKKFPAPTYAVNRALSTPPQVDYIWRIIVMFGALPAALTYYWRMKMPETARYTALVAKNIKQATADMSKVLQTDIELEERVEDDVKDPKQNYGLFSKEFLRRHGLHLLGTTSTWFLLDIAFYSQNLFQKDIFSAIGWIPKAATMNATHEVFRIARAQTLIALCSTVPGYWFTVAFIDTIGRFKIQLNGFFMMTVFMFAIAFPYNHWIKPENRIGFVVMYSLTFFFANFGPNATTFIVPAEIFPARLRSTCHGISAAAGKAGAIVGAFGFLYAAQSQDKAKVDAGYPPGIGVKNSLIMLGVLNFIGMLFTFLVPEPKGKSLEELSGEAEVSHDEK
Protein: Chromo domain-containing protein 1 (Q10103)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the kinetochore which plays a role in stabilizing microtubules and so allowing accurate chromosome segregation. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:9722643}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9722643}. Note=Associates with telomeric and mating-type region heterochromatin (PubMed:15607976).
Interaction partners:
- RNA-induced transcriptional silencing complex protein tas3
- Protein argonaute
- Histone H3.1/H3.2
- Argonaute-binding protein 1
- Argonaute-binding protein 2
- Chromatin modification-related protein rik1
- Protein Dicer
- Chromatin-associated protein swi6
- Histone H3.3
- RNA-dependent RNA polymerase 1
Sequence:
MVSVKPLPDIDSNEGETDADVYEVEDILADRVNKNGINEYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWKKRKKLIAKGLLEPFDAEDNEAKKMKREKEILRQQRQKRKSELTQLSQKVKEKFKKMRKKPARRIVTIANDEEEEDDQTMDEDAFERKSMQGELKERNLTDKTSTLSTSFGETSPDVNPFYLSEWPTVTDSILLSKSLSSDAIPLKNGEIKSTMLMPSDSDNSVPGIQNSNNLENTGAFVENANSPQSNTPLSTFRHSSPLSLSPVITSDNDVANSLFFSNSTPLPSSLKIKKEAPKLETHTILVSDNSGSLTKQDILSYFAFIKGNIEVFFLKSPKKDKVCNMAYIQFDSIEQAKLAYDKGHPSWHVTLVKGKISTDMEECKVSKSILKTTPSKKANARSVSFTQTTTDTLSESEKFASNVDLDENFDFNVNVTNEDAKQLKKSVIGSSWTTVNNDWNSVSKSDQTFENDGASKVVPAGNITLNSDNSLHHSISESEDLSSASTLSDYFRFVLRVGKSLYYAGELSFDISKLKAETEHQQLLRSLVSCKQVDVLRFVTSQYLEVFGTCLTKVLSGSLCIRSDVDMTHFKNILNRGNGAGIVLGSNYTLLLFTEDNNALMNLYDCQGQSNSPFWMVIFEPLESILVEWSAKNLRPKKPYHKSQSYLSYLLQLGHIDLHKIGAFQATQILIVSKQPSPEAEELEDTFREAAIPTFRGLEIPESLFLSQNVFVFLNVSLEDDFDQLQFLTLAKRKSCKFFLFGLSLPLKSPNDSHVGTDFKKNNEPLDKLTYSQYLRPMFPKGGVVSVTLSALIKTPRLLELISPFLEIKKDSWILILPPSIVDMVKSYFVTNNPDKSLLEIQNLLNTLQRYLTNPALKNVTLYQDWDIVIDDSADVSLASTLQLYQKKNYDKYRRFVLIHELKNELTPVNGLDIVDYDEFKETFMRAIGLK
Protein: At4g02075 (PIT1) (RING/FYVE/PHD zinc finger superfamily protein) (Q9XF50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- cyclin-dependent kinase
- cyclin-dependent kinase
- Serine/threonine-protein kinase MHK
Sequence:
MGDVILFIDDTKSKVRITRCRICHEEEEESFFEVPCACSGTVKFAHRNCIQRWCNEKGNTTCEICLQVYKDGYTAVLKQSKLIEQEVTIRVNGRRRRRSRRLVSIAESDISQCNSVADRGASFCRSLTFTLSVFLLMKHTFDVIYGTEEYPFSVFTVLTLKAIGILLPMFIIIRTISTIQKTLRRRHQYPESEEEDRLSSDDDDDLEEEDEEQQQHLA
Protein: Transcription factor MafB (Maf-B) (Transcription factor Maf-1) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog B) (P54842)
Organism: Rattus norvegicus (Rat)
Function: Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, osteoclast, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter. Involved either as an oncogene or as a tumor suppressor, depending on the cell context (By similarity). Required for the transcriptional activation of HOXB3 in the rhombomere r5 in the hindbrain (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:9038383}.
Interaction partners:
- Transcription factor Jun
- Protein c-Fos
- Homeobox protein Nkx-6.1
- Paired box protein Pax-4
- Interferon regulatory factor 8.
- Neurogenin 3
Sequence:
MAAELSMGPELPTSPLAMEYVNDFDLLKFDVKKEPLGRAERPGRPCTRLQPAGSVSSTPLSTPCSSVPSSPSFSPTEQKTHLEDLYWMASNYQQMNPEALNLTPEDAVEALIGSHPVPQPLQSFDGFRSAHHHHHHHHPHPHHGYPGAGVTHDELGPHAHPHHHHHHQASPPPSSAASPAQQLPTSHPGPGPHAAAAATAAGSNGSVEDRFSDDQLVSMSVRELNRHLRGFTKDEVIRLKQKRRTLKNRGYAQSCRYKRVQQKHHLENEKTQLIQQVEQLKQEVSRLARERDAYKVKCEKLANSGFREAGSTSDSPSSPEFFL
Protein: Serine/threonine-protein kinase 54 (EC 2.7.11.1) (Protein CONVERGENCE OF BLUE LIGHT AND CO2 1) (Q9SSA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29101334, ECO:0000269|PubMed:31904040}.
Interaction partners:
Sequence:
MKEKAESGGGVGYVRADQIDLKSLDEQLQRHLSKAWTMEKRKSLSDGEDNVNNTRHNQNNFGHRQLVFQRPLLGGGYSNNNNSSKNDIIRSTEVEKSRREWEIDPSKLIIKSVIARGTFGTVHRGIYDGQDVAVKLLDWGEEGHRSDAEIASLRAAFTQEVAVWHKLDHPNVTKFIGAAMGTSEMSIQTENGQMGMPSNVCCVVVEYCPGGALKSFLIKTRRRKLAFKVVIQLSLDLARGLSYLHSQKIVHRDVKTENMLLDKSRTLKIADFGVARLEASNPNDMTGETGTLGYMAPEVLNGSPYNRKCDVYSFGICLWEIYCCDMPYPDLSFSEVTSAVVRQNLRPEIPRCCPSSLANVMKRCWDANPEKRPEMEEVVAMLEAIDTSKGGGMIPPDQQQGCFCFRRHRGP
Protein: Major capsid protein P2 (Protein II) (P15794)
Organism: Pseudoalteromonas phage PM2 (Bacteriophage PM2)
Function: Major capsid protein.
Subcellular location: Virion {ECO:0000269|PubMed:12134022}.
Interaction partners:
Sequence:
MRSFLNLNSIPNVAAGNSCSIKLPIGQTYEVIDLRYSGVTPSQIKNVRVELDGRLLSTYKTLNDLILENTRHKRKIKAGVVSFHFVRPEMKGVNVTDLVQQRMFALGTVGLTTCEIKFDIDEAAAGPKLSAIAQKSVGTAPSWLTMRRNFFKQLNNGTTEIADLPRPVGYRIAAIHIKAAGVDAVEFQIDGTKWRDLLKKADNDYILEQYGKAVLDNTYTIDFMLEGDVYQSVLLDQMIQDLRLKIDSTMDEQAEIIVEYMGVWSRNGF
Protein: Conserved oligomeric Golgi complex subunit 3 (Component of oligomeric Golgi complex 3) (Q6AW08)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 5
- t-SNARE coiled-coil homology domain-containing protein
- Immediate early response 3-interacting protein 1
- Putative syntaxin-5
- BET1 homolog
Sequence:
MEIDHMRTVELLAAKAATWGLPEAVEDAESDTEEDVVGLISGALKDIKKREKDLAELQFPPEITAIRSNMKRFRDLQKQIDNSKATMNELREAYESVSSRTCSLHDACDRALAEQTSLSTGSQLIKTNLYYFKQADAIMKKLSVAKLMVTGHSFAAILVSIDECLTYLRAHPEYKESEAYISKFEQCLSRAMTWVRVAVLADLEACFNAVKDRQAQLELDYEKIGRAGQEEDTFALLYGVFASKAAVVKASINVVEQRFSAVPEFEEMLAECQYAYFAKRNLLLGPILESTLANLSGTHDDSTCRLTRDACTFMLRTCDDEYRLYRQFFVTRHTEERKLSTDGRISPAMSTITSVFTSAQSPQQVHPFETFSEQMCRTLYDMLRPRIVHNPHLETLAELCTMIKIEMIENRCSLQMVASILGDDASNDQNVSGLNPRAGFVSVMSELVGDIAERIVYRAGMYAQNDIAAYRPAAGDIAYPQMLQMIRKIENEQKEQQEKEPEEGSAPATAIDQHCLWYPTVRRTVMCLSKIFPCLDIGVFHSLARDMLFSCIDSLETASKAIMESPAPAKGWSKKLDAHLFVVKHLLILREQTAPYRQNVLSFRSDSLNTKDFSIDFSKFTNVLFDSKSKWFELSTDNALLELITTVPIEMREQEGDSRRVLDQQLRASTFRLAHEASLLMIRDLADWIEIAEDERMKEGFQLSGHPKLAAGVLKDVSAVAYRNVGTKFTEIRAAYTLYIGVPETEEILLSPVRKRVIDIFTRVISFASKTYDAESLAIAGLPNVQQLILLLNK
Protein: LIM domain 7 (A0A8I5ZWT3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEGMEDAEADCSVAFAEAQRWVEAVTEKNFETRDFRASLENGVLLCDLINKLKPGVVRKINRLSTPIAGLDNINVFLKACEQIGLKEAQLFHPGDLQDLSNRVTVKQEETDRRLKNVLITLYWLGRKAQNNPYYHGPYLNLKAFETLLGQALTKALEDSSCLKRSGRDSGYGDIWCPDRGDFPAPPGSHRREDSFESLDSLGSRSLTSCSSDLTLRGGREGCESDNDWEFTFKMQDYNKDDMSYRRISAIEPKSALPFNRFLPNKSKQPSYVPAPLRKKRPDKNEDNRRSWASPVYTETEGTFSRLFQKIYGENGSKSLSDVSAEDVQSLRQLRYEEMQKIKSQLKEQDQKWQDDLAKWKDRRKSYTSDLQKKKEEREEIEKQALEKSDRSSKTFREMLQDRESQSSTTTSRRRIYSSDDILDDGVLPPTVTLSETSYQSERLEDKARAHPAEMPKEDSTTFASREDGIAAEIPLASHIPEERRQAPWPSAETRQASSSSAESHQASLPSTESDQARLPSAEPHQASFSSAEPRQVPLVSAEPHQASSFSSTEPHQASLSSALQRPSSLSSSQQSWSTRGESTRISASLPRSYQRSDTARLTSVVTARPFGTSSRGISSLPRSYTMDDGWKYNGDVEVVKREQHDSGRAAGMKPDSSHFILGSSSEKEVATGEDVASLSSFVLPSSSSLSHDQAASSKATFSSTSGLDSVSDSGEGRSSSLREVSRSPDQFSDMRISINQTPGTKHDFGFTIKWDVSGISVASVEKGSPAEFSQLQVDDEILAINNTKFSYKDTKKWEEAMANAQETGNLVMDVRRYGKSGSPETKWIDTTSGIYSTEKSSSLSVTTDFSESLQSPYSESKEINGIHEESNAFDSKASESISLKNLKRRSQFFEQGSSDSVAPDLPVPTLSAPSRWAWDQEEERRRQERWQKEQDRLLQEKYQREQEKLREEWQRAQQEAERENSKYLDEELMVLNSNSISLTSRESVTASWEPSWSEGSKSLDREGTRAGDEDRGQLEDDAVYEDQSQKLQERLMLEHEKKRKEQEAQEEELRKQREAEAQARAEAEAQARAEAQARAEAQAQAEAEARKRAEAQKLQAERERETSVKIYQYRRPIDSYDLPKREEESSGLLPIDRSKSRSTTELNDPLIEKSGSSKYSDRIGTTSFSQRSSKKDQGPSEAELERQQILQEMRKKTSLHNDNSWIRQRSASVNKEPICLTGIMRRGESLDNLDSQRPGSWRQSSWHSQPAGVYASSSVQDFSRLPPQLLSTSNRAYMRNPSSAVPPLAGSVKTSPGSPSPRSHSPSMSQSGSQLRNRSVSGKRVCSYCNSILGKGAAMIIETLGLCYHLHCFKCVSCERDLGGSSSGAEVRIRNHQLYCNDCYLRFKSGRPTAM
Protein: Chaperone protein dnaJ GFA2, mitochondrial (Chaperone protein dnaJ A30) (AtDjA30) (Gametophytic factor 2) (Q8GWW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone that may play a role in mitochondrial protein folding. Involved in female gametophyte development. Required for cell death of the synergid cells during fertilization process, and fusion of the polar nuclei during megagametogenesis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12215516}.
Interaction partners:
- Heat shock 70 kDa protein 9, mitochondrial
- Small ribosomal subunit protein mS75
- Translation initiation factor eIF2 assembly protein
- Heat shock 70 kDa protein 7, chloroplastic
- Heat shock 70 kDa protein 6, chloroplastic
- Chaperone protein dnaJ C76, chloroplastic
- Heat shock 70 kDa protein 10, mitochondrial
- Heat shock 70 kDa protein BIP1
- 5'-adenylylsulfate reductase-like 5
- Chaperone protein ClpB4, mitochondrial
Sequence:
MVPSNGAKVLRLLSRRCLSSSLIQDLANQKLRGVCIGSYRRLNTSVGNHANVIGDYASKSGHDRKWINFGGFNTNFGSTRSFHGTGSSFMSAKDYYSVLGVSKNAQEGEIKKAYYGLAKKLHPDMNKDDPEAETKFQEVSKAYEILKDKEKRDLYDQVGHEAFEQNASGGFPNDQGFGGGGGGGFNPFDIFGSFNGDIFNMYRQDIGGQDVKVLLDLSFMEAVQGCSKTVTFQTEMACNTCGGQGVPPGTKREKCKACNGSGMTSLRRGMLSIQTTCQKCGGAGQTFSSICKSCRGARVVRGQKSVKVTIDPGVDNSDTLKVARVGGADPEGDQPGDLYVTLKVREDPVFRREGSDIHVDAVLSVTQAILGGTIQVPTLTGDVVVKVRPGTQPGHKVVLRNKGIRARKSTKFGDQYVHFNVSIPANITQRQRELLEEFSKAEQGEYEQRTATGSSQ