wanglab/gogpt-training-data huggingface dataset:
Protein: Protein max (Myc-associated factor X) (P52164)
Organism: Rattus norvegicus (Rat)
Function: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17304222}. Cell projection, dendrite {ECO:0000269|PubMed:17304222}.
Interaction partners:
- Myc proto-oncogene protein
- MAX gene-associated protein
- Protein B-Myc
- Max dimerization protein 1
- Max-interacting protein 1
- N-myc proto-oncogene protein
- Mitogen-activated protein kinase 14
- E2F transcription factor 6
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 13
Sequence:
MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGGTISAFDGGSDSSSESEPEEPQNRKKLRMEAS
Protein: Large ribosomal subunit protein eL15 (60S ribosomal protein L15) (P61314)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P61313}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL5
Sequence:
MGAYKYIQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSVAEERAGRHCGALRVLNSYWVGEDSTYKFFEVILIDPFHKAIRRNPDTQWITKPVHKHREMRGLTSAGRKSRGLGKGHKFHHTIGGSRRAAWRRRNTLQLHRYR
Protein: Transcription factor kayak, isoforms D/sro (AP-1) (Fos-related antigen) (Dfos) (dFra) (A8MPH9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with Jra.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:2116361}.
Interaction partners:
Sequence:
MIALKATEMQHNNNALQQQQQLQHQLLQQHQQQHQQQLQQQLNSPDNNYIWATTHNANISRNNAMLQLQQQQLRAPWITDCNKQHHINNNNSMNVNYNQQLTQQPQQQQQQTQYMQHNYNNYTQQQQQQHLVPATTSQSNSHFYQCNQQQQQQQFLAPTTTTAAVVVAAAHQQHQTQQQHQSQQQQQHQRQDYASLQMGRQLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAIDVLGMGIPTGVSSLPLQQTFDLSLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSYQAGHIMAGSVNGGGVNNFSNVLAAVSSSRGSASVGSSNANTSNTPARRGGGRRPNRSTNMTPEEEQKRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRGESMRKEIEVLTNSKNQLEYLLATHRATCQKIRSDMLSVVTCNGLIAPAGLLSAGSSGSGASSHHNHNSNDSSNGTITGMDATLNSTGRSNSPLDLKPAANIDSLLMHIKDEPLDGAIDSGSSLDQDGPPPSKRITLPPMSTMPHVHLSTILTPTGASSGSLQTPITSTAPGGFGSAFPVTSNGSSINNINSIGNNMNSPTLNAHNKVPKERPNTLAFQRPLGQMHLTMANNKAGGPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLVPNSSSTNKHPLELPTPTAEPSKLVSL
Protein: LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 1.3 (EC 2.7.11.1) (Probable receptor-like serine/threonine-protein kinase LRK10L-1.3) (Q8VYG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:25510357}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MFSPVLFRFSKPNSFLVLLFFLSYIHFLPCAQSQREPCDTLFRCGDLTAGFPFWGVARPQPCGHPSLGLHCQKQTNSTSLIISSLMYRVLEVNTTTSTLKLVRQDFSGPFCSASFSGATLTPELFELLPDYKTLSAYYLCNPSLHYPAKFICPNKGVGSIHQDDLYHNHCGGIFNITVPIGYAPEEGALNVTNLESVLKKGFEVKLSIDERPCQECKTNGGICAYHVATPVCCKTNSSSEVNCTPMMPSGSSAHAGLSKKGKIGIGFASGFLGATLIGGCLLCIFIRRRKKLATQYTNKGLSTTTPYSSNYTMSNTPTSTTISGSNHSLVPSISNLGNGSVYSGIQVFSYEELEEATENFSKELGDGGFGTVYYGTLKDGRAVAVKRLFERSLKRVEQFKNEIDILKSLKHPNLVILYGCTTRHSRELLLVYEYISNGTLAEHLHGNQAQSRPICWPARLQIAIETASALSYLHASGIIHRDVKTTNILLDSNYQVKVADFGLSRLFPMDQTHISTAPQGTPGYVDPEYYQCYRLNEKSDVYSFGVVLSELISSKEAVDITRHRHDINLANMAISKIQNDAVHELADLSLGFARDPSVKKMMSSVAELAFRCLQQERDVRPSMDEIVEVLRVIQKDGISDSKDVVVEIDVNGGDDVGLLKHGVPPPLSPETDKTTASSSNTTASSF
Protein: Protein LEAFY (Q00958)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that promotes early floral meristem identity in synergy with APETALA1. Is required subsequently for the transition of an inflorescence meristem into a floral meristem, by an immediate upstream regulation of the ABC classes of floral homeotic genes. Activates directly APETALA1, CAULIFLOWER and AGAMOUS, and indirectly APETALA3 and PISTILLATA with the cooperation of UFO.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- MADS-box protein SOC1
- Floral homeotic protein APETALA 3
- Transcription factor CAULIFLOWER
- Protein TERMINAL FLOWER 1
- Floral homeotic protein APETALA 1
- MADS-box protein AGL24
- Agamous-like MADS-box protein AGL8
- Developmental protein SEPALLATA 3
- MADS-box protein SVP
- Inactive protein FRIGIDA
Sequence:
MDPEGFTSGLFRWNPTRALVQAPPPVPPPLQQQPVTPQTAAFGMRLGGLEGLFGPYGIRFYTAAKIAELGFTASTLVGMKDEELEEMMNSLSHIFRWELLVGERYGIKAAVRAERRRLQEEEEEESSRRRHLLLSAAGDSGTHHALDALSQEGLSEEPVQQQDQTDAAGNNGGGGSGYWDAGQGKMKKQQQQRRRKKPMLTSVETDEDVNEGEDDDGMDNGNGGSGLGTERQREHPFIVTEPGEVARGKKNGLDYLFHLYEQCREFLLQVQTIAKDRGEKCPTKVTNQVFRYAKKSGASYINKPKMRHYVHCYALHCLDEEASNALRRAFKERGENVGSWRQACYKPLVNIACRHGWDIDAVFNAHPRLSIWYVPTKLRQLCHLERNNAVAAAAALVGGISCTGSSTSGRGGCGGDDLRF
Protein: Desmin (P02542)
Organism: Gallus gallus (Chicken)
Function: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P17661}. Cytoplasm {ECO:0000250|UniProtKB:P17661}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P17661}.
Interaction partners:
- Vimentin
- Alpha-actinin-2
Sequence:
MSQSYSSSQRVSSYRRTFGGGTSPVFPRASFGSRGSGSSVTSRVYQVSRTSAVPTLSTFRTTRVTPLRTYQSAYQGAGELLDFSLADAMNQEFLQTRTNEKVELQELNDRFANYIEKVRFLEQQNALMVAEVNRLRGKEPTRVAEMYEEELRELRRQVDALTGQRARVEVERDNLLDDLQKLKQRLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLQEEIAFLKKVHEEEIRELQAQLQEQHIQVEMDISKPDLTAALRDIRAQYESIAAKNIAEAEEWYKSKVSDLTQAANKNNDALRQAKQEMLEYRHQIQSYTCEIDALKGTNDSLMRQMREMEERFAGEAGGYQDTIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEENRISIPMHQTFASALNFRETSPDQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
Protein: (thale cress) hypothetical protein (A0A384KCR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAKACLLQSTLLPAYSPLHKLRNQNITLSFSPLPLSRCRPGIHCSVSAGETTIQSMEEAPKISWGCEIDSLENATSLQNWLSDSGLPPQKMAIDRVDIGERGLVASQNLRKGEKLLFVPPSLVISADSEWTNAEAGEVMKRYDVPDWPLLATYLISEASLQKSSRWFNYISALPRQPYSLLYWTRTELDMYLEASQIRERAIERITNVVGTYEDLRSRIFSKHPQLFPKEVFNDETFKWSFGILFSRLVRLPSMDGRFALVPWADMLNHNCEVETFLDYDKSSKGVVFTTDRPYQPGEQVFISYGNKSNGELLLSYGFVPREGTNPSDSVELALSLRKNDKCYEEKLDALKKHGLSTPQCFPVRITGWPMELMAYAYLVVSPPDMRNNFEEMAKAASNKTSTKNDLKYPEIEEDALQFILDSCETSISKYSRFLKESGSMDLDITSPKQLNRKAFLKQLAVDLSTSERRILYRAQYILRRRLRDIRSGELKALRLFSGLRNFFK
Protein: Neutral ceramidase (N-CDase) (NCDase) (EC 3.5.1.23) (Neutral N-acylsphingosine amidohydrolase) (Neutral acylsphingosine deacylase) (Slug-a-bed protein) (Q9VA70)
Organism: Drosophila melanogaster (Fruit fly)
Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-7.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Regulates synaptic vesicle exocytosis and trafficking by controlling presynaptic terminal sphingolipid composition.
Subcellular location: Secreted {ECO:0000269|PubMed:12153720}.
Interaction partners:
- Alkaline ceramidase
- Ceramide kinase, isoform A
- LD18904p
- sphingosine kinase
- Putative neutral sphingomyelinase
- sphingosine kinase
- ceramide glucosyltransferase
- 3-dehydrosphinganine reductase
- Non-lysosomal glucosylceramidase
- Sphingolipid delta
Sequence:
MANSKMAFLAFLAVSFLCGLVSATYKVGVGRADITGPPVEINFMGYANIKQVGRGIHTRVFARAFVVEDEKGNRVAFVSADAGMMGYGLKREVIKRLQARYGNIYHNDNVAISGTHTHGAPGGFLMHLLYDISILGFVPQTFEVMAQGLYLCIKRATDNLVDGRILLSKTTVLNVNINRSPSSYLRNPAEERAQYEHDTDKTLTQLRFVDLENNLLGAFNWYAVHATSMNNTNRLVTSDNVGYAALLLEKEYNPNKMPGKGKFVGAFCSSNLGDVSPNIMGPKCSISGNECDLLTSRCPTGEGDCFASGPGKDMFESTQILGQRLADAALGLLNEQSQESTAREVTGDVRFIHQFVDMPNYNGSTYNPLSRKVDKIRGCQPAMGYSFAAGTTDGPGAFSFEQGTTTDNPMWNFVRDFIAAPTQEDIKCHEPKPILLATGRATFPYEWQPKIVSDQLLKIGDVIIAAVPCEFTTMAGRRLRNQIRAAASAVGGIDTEVIIAGLTNIYTSYTVTPEEYQAQRYEAASTIFGPHTHSIYMDVFERLTKAMMRNETVDAGPSPPYMNDVMLSLNTGVLFDGHPINTDFGYVKSQPNKEYGINETVKVTYISGNPRNNLFTEKTYFTIERKINEDRWKVAYTDASWETKMVWHRTNTILGFSEMDIYWDISPQTLPGEYRIRHSGEYKYILGGKYPYEGLTHSFTVKED
Protein: Calcineurin subunit B type 1 (Protein phosphatase 2B regulatory subunit 1) (Protein phosphatase 3 regulatory subunit B alpha isoform 1) (Q63810)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20639889}. Cell membrane {ECO:0000269|PubMed:20639889}. Cell membrane, sarcolemma {ECO:0000269|PubMed:20639889}. Cell membrane {ECO:0000250|UniProtKB:P63098}; Lipid-anchor {ECO:0000250|UniProtKB:P63098}. Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy. {ECO:0000269|PubMed:20639889}.
Interaction partners:
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Nuclear factor of activated T-cells, cytoplasmic 1
- Calmodulin-like protein 4
- Nuclear factor of activated T-cells, cytoplasmic 3
- Nuclear factor of activated T-cells, cytoplasmic 4
- Nuclear factor of activated T-cells, cytoplasmic 2
- Calmodulin-1
- Dynein axonemal assembly factor 10
Sequence:
MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
Protein: Amphiphysin (LD19810p) (Q7KLE5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Dynamin
- Clathrin heavy chain
- RE12101p
- phosphoinositide 5-phosphatase
- AT02057p
- Dynamin associated protein 160, isoform D
- dynamin GTPase
- Vacuolar protein sorting-associated protein 29
- Cdc42-interacting protein 4, isoform B
- WHAMM and JMY related, isoform B
Sequence:
MTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSPTSTSSSLQEPRFDSVSSTPEPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLGNDTTVTATETVTVTQHSVTSTDTDNIVTISDTNTDTDTKTSTGTSQKGRPVPVVNRHSVNNLNKNPFEDDDERIYEVPADANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI
Protein: tRNA uridine(34) acetyltransferase (EC 2.3.1.311) (Elongator complex protein 3 homolog) (MinElp3) (D5VRB9)
Organism: Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)
Function: tRNA uridine(34) acetyltransferase, which mediates formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. The proposed mechanism is the following: (i) recruits S-adenosyl-L-methionine and cleaves it to generate a 5'-deoxyadenosine radical (5'-dA) in the radical S-adenosyl-L-methionine (rSAM) region, (ii) hydrolyzes acetyl-CoA in the N-acetyltransferase domain and (iii) an acetyl radical is formed by the products of the two domains and (iv) is transferred onto the C5 position of uridine(34) in the bound tRNA molecule. Does not show protein lysine acetyltransferase activity.
Interaction partners:
- L-seryl-tRNA
- NMD3 family protein
Sequence:
MKEKLMRCIIERILKEYKEGKTLDKKRIEQIKSECLRIYRIGIGHPSNSEILKYATEEEKKILIPILRKKPVRTISGVAVVAVMTSPAKCPHGKCIFCPGGLDSVFGDVPQSYTGREPATMRGLMFNFDPYLQTRARIEQLEKVGHPTDKIELIIMGGTFPAREIEYQDWFIKRCLDAMNERESKSLEEAQKINETAKHRCVALCIETRPDYCSEKEINQMLKLGATRVELGVQSIYNEILKLCKRGHSVEDTIKATQLLKDSGLKVSYHLMPGMPGSSIEMDKKMFKEIFTNPDFMPDMVKIYPCLVIEGTELYEMWKRGEFKPYREEEAIEVISYAKSIMPKWVRTSRIQRDIPATVIVDGVKKSNLGELVYKYMEKKGLRCRCIRCREVGHVYYKKGILPDPEHIKLVREDYEASGGTEIFLSFEDVKNDILIAFLRLRDPYKPFRKEIDDKTMLVRQLHVFGWEKALTRDIKEVSWQHMGYGRMLMKEAERIAKEEFGKKKILVTSGIGVREYYRKLGYKRVGAYMGKEL
Protein: Ankyrin repeat and sterile alpha motif domain containing 1A (A0A3B3ISP1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGKEQELLEAARTGHLPAVEKLLSGKRLSSGFGGGGGGGSGGGGGGSGGGGGGLGSSSHPLSSLLSMWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNALEIKELKKYGPFDPYINAKNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMGSALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALDTVRELPSQKSQQIAALIEDHMTGKRSTKEVDKTPPPQPPLISSMDSISQKSQGDVEKAVTELIIDFDANAEEEGPYEALYNAISCHSLDSMASGRSSDQDSTNKEAEAAGVKPAGVRPRERPPPPAKPPPDEEEEDHIDKKYFPLTASEVLSMRPRIHGSAAREEDEHPYELLLTAETKKVVLVDGKTKDHRRSSSSRSQDSAEGQDGQVPEQFSGLLHGSSPVCEVGQDPFQLLCTAGQSHPDGSPQQGACHKASMQLEETGVHAPGASQPSALDQSKRVGYLTGLPTTNSRSHPETLTHTASPHPGGAEEGDRSGARSRAPPTSKPKAELKLSRSLSKSDSDLLTCSPTEDATMGSRSESLSNCSIGKKRLEKSPSFASEWDEIEKIMSSIGEGIDFSQERQKISGLRTLEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSNVMEEQDLRDIGISDPQHRRKLLQAARSLPKVKALGYDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVQLLGHRKRIIASLADRPYEEPPQKPPRFSQLRCQDLLSQTSSPLSQNDSCTGRSADLLLPPGDTGRRRHDSLHDPAAPSRAERFRIQEEHREAKLTLRPPSLAAPYAPVQSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKSRATGASAAEMIETKSSKPVPKPRVGVRKSAVPLPPDSRCCYCHTCTTHRPSYLPLPSVSPGVKLEPPDMDQDAQSHASVSWVVDPKPDSKRSLSTKYETTIF
Protein: Histone deacetylase 4 (HD4) (EC 3.5.1.98) (Q99P99)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1.
Subcellular location: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-245, Ser-466 and Ser-630 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation (By similarity). Interaction with SIK3 leads to HDAC4 retention in the cytoplasm (By similarity). Interacts with ZNF638 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q6NZM9}.
Interaction partners:
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
- Runt-related transcription factor 2
- Histone deacetylase
- Ankyrin repeat family A member 2, 2)
- Calcium/calmodulin-dependent protein kinase type IV
- Nuclear pore complex protein Nup155
- Paired amphipathic helix protein Sin3a
- BCL6, transcription repressor
- 14-3-3 protein gamma
Sequence:
MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPAAVPMDLRLDHQFSLPLEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCMSSDPRYWYGKTQHSSLDQSSPPQSGVSASYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVATALKKRPLDVTDSACSSAPGSGPSSPNSSSGNVSTENGIAPTVPSTPAETSLAHRLVTREGSVAPLPLYTSPSLPNITLGLPATGPAAGAAGQQDAERLALPALQQRISLFPGTHLTPYLSTSPLERDGGAAHNPLLQHMVLLEQPPTQTPLVTGLGALPLHTQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLHLSKMISKPSEPPRQPESHPEETEEELREHQALLDEPYLDRLPGQKEPSLAGVQVKQEPIESEEEEVEATREAEPSQRPATEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGSHRPLSRAQSSPASATFPMSVQEPPTKPRFTTGLVYDTLMLKHQCTCGNTNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSSLTSVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYNDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIANEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELEPLPEKVLHQRPNANAVHSMEKVMGIHSEYWRCLQRLSPTVGHSLIEAQKCENEEAETVTAMASLSVGVKPAEKRSEEEPMEEEPPL
Protein: Zinc finger protein 425 (Q6IV72)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:21266108}. Cytoplasm {ECO:0000269|PubMed:21266108}. Note=Predominantly expressed in the nucleus.
Interaction partners:
Sequence:
MAEPASVTVTFDDVALYFSEQEWEILEKWQKQMYKQEMKTNYETLDSLGYAFSKPDLITWMEQGRMLLISEQGCLDKTRRTTSPPTDEQLNMKNTGKLLCFDDEGTPRTKEEDCRLNGPQKQDLCAALRGKERKILLAQTATFQSPSLRETEILNKKVSITAYDPDKKDLRHKPRETPGRLEIPTGPRCYSCYVCRKVFQVRRDLLKHKRSHSKSQLCRYPKYKNSSRGKSELRRTQRLLCQKKRFQCSECEKSYFLKGSLVTHQVVHTGQRPYPCPECDKTFRYRANLKKHLCLHRGERPFCCGECGRAFVQQCELTEHLRLHSGEKPFQCPQCDRCFRLKRGMKVHLTQHSGKRPFHCPECGRSFSRKAALKTHQRTHSEEKPFSCGECGRKFIYKIKLDEHIRVHTGEKPFSCPECNKSFRLKRSLKAHGLQHIGKRPFQCPECSRGFFWRNAMRAHQRLHSEQKPFPCAECGKRFTRPSKLACHTRVHDRQKEFPCGECKKTFSQQSRLTQHLKVHTTEKPFSCAECGRSFRRRAHLTEHTRLHSGEEPFQCPECDKSFSWKASMKFHQRMHRDEKPFACGECDKTYTHQSQLTEHLRLHSGEKPYQCPECEKTFRLKGNLKSHLLQHSGQKPFSCVMCGKSFTQQYRLTEHIRVHSGEKPFQCPECDKSYCIRGSLKVHLYKHSGERPFQCPECGKGFLQKRSLKAHLCLHSGERPFSCDECGRSFTYVGALKTHIAVHAKEKPSSL
Protein: Guanylyl cyclase (Q551V8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Patatin family protein
Sequence:
MENVSSPSLLSLSLNNNNNINNNNNNNNNNNNVPFINSFNVNQLDEFERKTIEYGRSIVYDIARIEELILASEFVSELEIVMFSRRMTSKCSELSTSISPNIAVLRQQIQILQSTPIINTNNNNNSNNNSSLSSSTSSSPNQSSPQTNRRSAGLLSSYSPSSSPNLKSHQMNNNNNNNNNNQLSQSLFLLDSKSIEKMVKEECFGIIDPEELSHEEKSKLIRSTVSSVNSIIMTVKEYNKQHQLGKDLLPLQNEYFLHRTNILQSWKFLTIFVSKTSWKIPKLPQPPTKSCSSSSIVTTPVIRQIRDIKTDDISNSNSNSNSNNSNNNSIPSSPILSGSPSSSISTPPILTSPILQPQKPLIPPILGSAASNKRLSMSFNSFFDGASNGTINNNSNNNQQQQQQQQQQQQQQQQQQLSSSPENSPIVSRAKGNNIITLTKTNVSSNVNNSNSNSPTQSSKKQHKSALNVNSSNVSVNSNSNSSSNNSTTSVIKPDLFDQIFQLSDTLMTLMYHLKNIQKIKLKKQQQQQQQQQQGGPITPRGVSTPRGNPSSVNKTTASPTNSGSTTPLTQSPPLSPISNNNNNQSSPTSPSSSSSTPKIGTLYIEQAKNVIIPSLLSKLLDICNHLKIKITDESLIDHLFNLSTINSNDLIEPLEIVLEMFQKFTFSQPTIVIENPTTSNPTSTTGLNINSLSNSKTTKSKPPHHPKSLESKNHDKTSSSPIKSIFKLNSKVKDKSDKLDSINNNNSNSSSSSKSRPTTPILSPISSPIISPVSSPVTSPSSSSHSKISPSTSLERISDLIPISSPNNNNNNNNNNNNNNNNNNTTTTTTTTTTTTTAITNTTDTVQNQNLIYDLLNTIDNNEEMDRYNNVNNNNNGNTSPMSVVVSNNDQQTVTYGFKVPELNISKLNDSTTTTSTSTNNNSGNLGTSINNSNNKKLNQILGASEDVLSKKQLLKPKDLSKQNKIGLSIFSKHLRSMKQNDEHQQRNSFNQFWLEGSTHRERQDQVPLDEKQRHQITSLGSYVSNLVIKGLLASATPIVPPHLEKYSSCVLFADISGFTSLTERLGNHGKEGVELLTKNLNSYFTILIKIVKGFGGDIVKFAGDAVLAHWPTNGELINRVRIACECSLALQKKLHNFPVPGGFLTLHIGIGCGDISGVYVGGCKEKVEFLICGEALIQATLCEKEAESGEIYVSPATQEKMKPYATFSQKKQKHNYKLESITTLLEKDLINDFDFLSTMVGSQINHKFLQELPLLMDMEDSLKRFVPNAVHNQFKNDYLAELRYITVLFMNLSYGTPNPDTDLDKLQNIVFESQAIVYKHEGTVRQFIVDDKGCVLIAAWGVPPYSHEDDPSRAVEAAMEIVVNVFKLAVISSVGITTGKCFCGDVGSDERREYAVVGDIVNLAARLMSHSQGGVLCDEETSKTAKMIEFVKLANPIKVKGKVAPINVYKPIKKLQSMKNSSPRHMIKNKGIIGRHTQLRQMANIIDQITSNSGPTHVAIIEAEAGLGKSRLISEIKYSFCMDLKMFKASGIQMSESISFYIWKQILLQFLKDESINGYQSFSDFNFTQIQLLNQVLDINIINNNNNNGNENNEKLPIVEQNQLQTSVIKLTSEELKENRRYSAQQRAESLQLTMMKILTKAIPTGSIIVIDDAQFMDSASWTLTLNAVKNLANCLIIISLRPSKDGIPYGFSQLPTELVTKIQLEPLNGKVETTLLVERMLDFPSDESGIPDEIIEEIYNRSQGNHFVIEEMVNGLISNGLIDEASSRFINPKEAIDHVRLSLPRTVTSLITSRVDRLSPIQQLELKIASVIGMPFTVDSLHRILPLDAISKQDLAKDLAVLERLDFIKSTTINTQQQLLQQLQQQQQLQKQLLNNQADHSSYKTNNVLLLASQPNINNNNNNNNNNNNNNNNNNANEQPSTPTSIINNNLLYSFHHTRTQEVIYDLMLFSQRRELHQKIAKVLEDTCTPQHSLFISLVHHYHSAQNNSKTIEYATKAGVLAQAENNNKEAIKFFQLALKCMEQEFIAEEEVKIHKKLHRRSSSQNLKDAVSISSNSNNPNNISFQDLMDSNNSNLVNSNSNNNNSNNNSNNNSNNNSLSNLGEDIKDKDKEKEKDKDKEKEKEKEKEKEKEKDKEKDKNNNNNNNNNNNNNTILNPPTLADLVSLGFKKVPIEIISITRKLGLALFNVGRFRQASYHLLNALKYLGLEPPTPKDYSSGASKPKLRTLAKAAVRQDSATKFFSCNLDMLEKREAILCLFVQSKISLHDCSKTLDSWCSYVSLQLSFDNSHSSIKNRLFNSLGNNNSNNNNNNNNNNNNNNNNNSSNNNELSSSSTTTTTTTVQTSLTDWNLQAEAYSIGIRVLGNNGDSSTPLKYYAEVLSKMDQTNGFVYGNSHQSWGIYMSGLGRWEEAESGYKKSIEASHKTGDKKLMEESNIFLSVCYLLLGSNGGKLSLIYQQTTKALESARNRGDNHNQILALTVEGCALFYERQFQRCHTILQDIERLVDLLSIKELSNSAHANYTILKAQIAINEKDWQLAYDCCRRVSIIISKCDANNFSMYEAYTGLPLVLIKILQNHQHISATAVTVPKSRLVTEINDSITILERFAETFPIGQPRLLLVKTLMFALGYRESDDQNNLSALKEAKEKCQKLGMSFDFVCIHNPNNNNNNSNNNNSGGSGSPSGNNSPINKRYSVGGIGNYQQANGGQDIKSPVLSPQHSISDFHYTAADTGTTQPSVQIGSSRSRPVSVHENVNSSQPLRTVSSQDLSSSSSGSNNSYNGSSDQQSPQSPQSPQSPQSPQSPQSPNSITSQQFSPPNQPSNNGAKKDILKKIGIKFWKE
Protein: Ras guanine nucleotide exchange factor L (RasGEF domain-containing protein L) (B0M0P8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Interaction partners:
Sequence:
MKSMSSGGINKLFEGSLSKDGKTSRIEHQKIKQSGCPLLIKLMKDNGHITNVIIKSCRLKVLPGEISSLGGHLKKLHIEDNKIQEIPNLEQLEQLEELILPNNDIAKFQVSISKLTTLRLLDLSGNQLGTIPVRLFSLVSMRELYLDENQFSNFPSHLCELQKLTTLGFSNNLLKSIPTQIGQMIGLKKLILSGNQMESIPMEISNLKSLTHLDCSSNILSSIPNELGNKLSQLSFLFLQHNKLRSIPDEIGQCQSLVSLRLNNNSITLLPQSIGELENLQELYLQENRLNTLPSELGNCCSLKKLYLEFNKLIALPDRFKRLHCLNVLSLHDNLLDDLPNFLSLEFSQHLIRFTIHNNPFLRENGIDVIDSLQFLNSHLLSIQNFINNHDQQNDNSNNNNNNNNTTTTTTTTTTTTTTSTTNNNNTLFTDSYLSSASSSSFLNKSPSGLSLVGSFNGTIKKSISNSSNMNGSGSNGVGHGSGLTPKLNFKSLITSRDFSSDSDSDTDSTSSFSTYSSSTINTKRASISPRTSLTLSNSASNDSVSAVANGNGNNNNNNNNNNNNNNNSNNNNSGLVNSISSFSLSSGQINYYNISRARRGTHGNDQPHQTISPSTSTEKLQQTVSTPRQQSFFISVLNRRKSSLNNSQNGNNSNNNSNNNNNNSNNNISSLSSSNFANSLYNPLMSSSPTSSPSSSYSNLHSSFNGTSTPPFSSPSQSSPLSNSINGIHCNYSNNNNNNNNSNNNNNNNNNNNINNNNNNSNNNNNINTNGNNNSFNGIIMGSPIYKSFQSLYETLLDDLDYSKKRREELLNLSVEEKWIFLQRIKPDCTNSLVSNGVYQLQHQISSNDLKTLISSPPKLNSSQQLLSSSSSSSSLSSSSTSATHSLQNKSLPSISVCPKSPRTHMKVLSASSLFTLEDITKLRQQLVSKPVSWVINFAESTGIVSILSMITTYSQNLINNVNKDQPQSQPQPQPQPQPRPQPQQPQPQQPQPQQLLPLLSQLQPQQQQQQQQQTQQPQPQLQAQTKSDDHFIINECLGCIKLLVELEMQSLLLNDTAEIIFPLILSSQVSTKRMTFEVLELICKIFSLGSTIVLESIKNYSKKINEPLTKVFSHITSPLDSEYPADLKVSCMSLINHLIGSNHLSLEARIETRSKFLSNDILLIIKNLRIDGEGIETSSWKQLELEMKQFESMMVQDDNQTSNAEANELVSNELSQSIDNNNNNNNNNNNNSSTNLVNNNNNNNINSNCNSIINGGNSSDSLINNSVGTGVGSIMGVGSFMGVNEIEYDSPRKEFDELKSSNNNNSNSNSVNNFINNITEPIMPLTPTEGKLVVIVSMQQTRQQAQLQQQLQQQLEEEDDDEVPLSSSVATTASTTANTTLIEPNHLPIQTREVIVSVQRKSQAGDVIRSLLASNSNLKELGEWGLFVNDSNSNNNNNNNNNNNNKLSTNVIGRFLKDDEYIFDQMTTSSTSGSLSSDDGATPRLMTRSIPRFKEYRLKMIPWKVRVSLEKVKEMGLVLNANNTANGQFNESKFIAEAPMDPTMTCTGLVYHLIKKYLPNVNDRYCLEADDFGLYLDTNAGGLMWGGGTGGGYWLEPLEKLHDYEIFKDPKSTVALKLRPKGVKLKFADGTYEIFRLDLMSPTEKIFQEISEKVIDSNNNINLSYYGIFVDRQQGGANGNGISDSPILVSQSSSTSLIEESKKQRKPEWLEKGLPLYHYKINSRCCLRFALRPSNITLLIDISLFKSFQQQQQQQQQQQQQSTSSSSSSSSSSSVSSNNNSTNNSNNLIGSLNNSINTISELDESIDDNGLSSSSSDKEDQISTPSTSNLLSKFQQVDESISNLKFQLPQPIQSKQIIVQLPLHLPLGEALETDENWIETGIEREKCSFHFDSFDGILMNQTQPLNTQNFTEKNRICVLMADELEINSEQTNHNKTNIWDEPFDSSTIICDPDNPGQIRAATLNKLLEQATNNIEKDRELMNILLMTYMSFATSDILLDKLVERYNVPEHEKEQKSVVQLHTIVFLKNWLEQQAPQAASGGGLEEKFLVRLSEFVDKQISLDGYTKIVPQLKKWIDSALKEKRAYAMPEAARPNQLTTKLPSLTSSLLDDELFVAQQLTLREYETFKRIQAVEFLGQAWGKPKLQYKAPNLLKMIERFNKISTGVSTAILSQPKIKTRVKLICRFIKIAQHCRDLNNYHLLTAFMAGIRNSNVVRLRLSWAKVPKKHLHILEDLEKIMSMEGSFKEFRTKMAETIPPCIPYLGVYLKDLTFIEEGNPDSINSLINWGKKKLIYNIISIIQRCQQVSYDFGNQNQSQVAQKSDLVLNYFDSLPIALDELLYKISLNLEPRSNFNN