wanglab/gogpt-training-data huggingface dataset:
Protein: Non-structural protein V (Q997F2)
Organism: Nipah virus
Function: Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Blocks the type I interferon signaling pathway by interacting with host STAT1 and STAT2 and thereby inhibiting their phosphorylation and subsequent nuclear translocation. Efficiently blocks the type II interferon signaling pathway. Suppresses interferon induction by interacting with and stabilizing host UBXN1, a negative regulator of both RIG-I-like receptors (RLR) and NF-kappa-B pathways.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:19141449, ECO:0000269|PubMed:29769705}.
Interaction partners:
Sequence:
MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVEGGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHGGECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENKLSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTSDDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKDNKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDAQPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKKGHRREISICWDGKRAWVEEWCNPACSRITPLPRRQECQCGECPTECFHCG
Protein: Annexin A3 (35-alpha calcimedin) (Annexin III) (Annexin-3) (Lipocortin III) (Placental anticoagulant protein III) (PAP-III) (O35639)
Organism: Mus musculus (Mouse)
Function: Inhibitor of phospholipase A2, also possesses anti-coagulant properties.
Interaction partners:
Sequence:
MASIWVGPRGTIKDYPGFSPSVDAEAIRKAIRGLGTDEKTLINILTERSNAQRQLIVKQYQAAYEQELKDDLKGDLSGHFEHVMVALVTAPALFDAKQLKKSMKGTGTDEDALIEILTTRSSRQMKEISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKKDAQILYNAGENKWGTDEDKFTEVLCLRSFPQLKLTFDEYRNISQKDIEDSIKGELSGHFEDLLLAIVHCARNTPAFLAERLHQALKGAGTDEFTLNRIMVSRSEIDLLDIRHEFKKHYGYSLYSAIQSDTSGDYRTVLLKICGEDD
Protein: Rifin (Q8I3D9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKFNYNNILLFSLSLNIFLLSSQVYNQRNHYITRTPKTNTRTLCECELYAPSNYDNDPEMKAVMQDFDRQTSQRFEEYNERMMKNRQKCKEQCDKEIQKIILKDKLEKELMDKFATLHTDIQSDAIPTCVCEKSLADKVEKTCLKCGGVLGGGVTPAWGLISGIVYTGWKAAALAAAKKLAAEAGAAKGLAAGAEVGKDAVILGLNSEFGLSTQAVQKIGLVINGTNYTNVSMITEAIFTKYKGSCMLSVPGASPGSFRILVTDPKFCNLFLKKFVPIGSGLDRNAITNAIEKKVETMVLQAEGVAEATKTQVTSETTAELTAKQTTAINTIYMGKQTAIIASIVAIVVIVLVMVIIYLILRYRRKKKMKKKLQYIKLLDE
Protein: RIC3 acetylcholine receptor chaperone, isoform Q (E1JGP9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLGAATATAAAKKPAAKDTEKELYNASVSATEVASSLSASLKSHQQLKEAEQLMEIEKLRQKLESTERAMAQLVAEMNTDQYEAKKNDNEKTREQPLDKQNLSNGHASSTDQNPEQETVAKGARKRRDLSAEQELTSKLEDNLPEPQSIYLEGALAHESQILVADSQIKREEVYDSELNGSAEEPAIILSSRMTLSLINLDANQQNGNAGKSAVESPLADDIEIIGHDEQ
Protein: Transmembrane protein (Q382I6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNPSKVVQGTPNSVEWDPRNPPDTPFFTETTAVERSRIPTEYIRRMEEATRLYAMHREGRHALHTACQIASWTVATQCCWLCVGVWLTVRGYRHANPAHSFVSGMTSNKVFCRVFTPIPVLGLTMMGVTAAQLPRDVKVLITAREGRMEEENCMKSAFDQCMAALAEGRLAMGKEGILTA
Protein: Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG2 (EC 3.2.2.n1) (Protein LONELY GUY 2) (Q5BPS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19837870}. Nucleus {ECO:0000269|PubMed:19837870}.
Interaction partners:
Sequence:
MEETKSRFRRICVFCGSSSGNKTTYHDAALQLAHQLVERNIDLVYGGGSVGLMGLISQAVHDGGRHVLGIIPKSLAPREITGESIGEVITVSTMHQRKAEMGRQADAFIALPGGYGTFEELLEVITWSQLGIHTKPVGLLNVDGFYDSLLTFIDKAVDEGFVSSTARRIIVSAPNAPQLLQLLEEYVPKHDDFVSKMVWDNTTDAFTLEGDSF
Protein: Early growth response protein 3 (EGR-3) (Zinc finger protein pilot) (Q06889)
Organism: Homo sapiens (Human)
Function: Probable transcription factor involved in muscle spindle development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- E3 SUMO-protein ligase EGR2
- NGFI-A-binding protein 2
- Protein FosB
- NGFI-A-binding protein 1
- Protein c-Fos
- CREB-binding protein
- Histone acetyltransferase p300
- Early growth response protein 1
- Nuclear receptor subfamily 4immunitygroup A member 1
- Transcription factor JunB
Sequence:
MTGKLAEKLPVTMSSLLNQLPDNLYPEEIPSALNLFSGSSDSVVHYNQMATENVMDIGLTNEKPNPELSYSGSFQPAPGNKTVTYLGKFAFDSPSNWCQDNIISLMSAGILGVPPASGALSTQTSTASMVQPPQGDVEAMYPALPPYSNCGDLYSEPVSFHDPQGNPGLAYSPQDYQSAKPALDSNLFPMIPDYNLYHHPNDMGSIPEHKPFQGMDPIRVNPPPITPLETIKAFKDKQIHPGFGSLPQPPLTLKPIRPRKYPNRPSKTPLHERPHACPAEGCDRRFSRSDELTRHLRIHTGHKPFQCRICMRSFSRSDHLTTHIRTHTGEKPFACEFCGRKFARSDERKRHAKIHLKQKEKKAEKGGAPSASSAPPVSLAPVVTTCA
Protein: Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOD) (DHODase) (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase) (Q874I4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: In the de novo pyrimidine biosynthesis pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate with reduction of flavin and the transfer of electrons to ubiquinone, which is part of the repiratory chain. Does not use fumarate and NAD as electron acceptors.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- dihydroorotase
- orotate phosphoribosyltransferase
- Uncharacterized protein
- Allantoinase
- Orotidine 5'-phosphate decarboxylase
- Xut1p
- NADH-cytochrome b5 reductase
- Altered inheritance of mitochondria protein 32
- Oxidoreductase
- NADH-cytochrome b5 reductase 2
Sequence:
MFRPSIKFKQSTLSIIARRLKSSAQHQPLRSSFVPSPIVFVAGLAVAAVGGYYCLDSRSAIHEYVLCPLIRTFTDAESGHKLGIFFMKYGLSPRLLDDGKNDQSDVLGVQVFGHKLKNPIGLAAGLDKDGEAIESLFNCGFSYVEIGSITPEPQPGNPQPRFFRLPKDDAVINRYGFNSSGHFNVLATLKLRFNKLLNKFGTSHSSEQHPFSNAFQQGKLLGINLGKNKFGDEVNDYVKGVERLGPYADVLVINVSSPNTPGLRDLQSEAKLTNLLTTVVKERNVLGKNLLGNKPPVLVKVAPDLTEPEIESIANSAKEAKVDGIIISNTTIQRPVDRLLTTDKQLINQAGGLSGKPLKPLSLKALRTLRKYTKDSDLVLIGCGGISNGKDALEFGKAGATFIELYTAFAYKGPGLVGKIRDELAEELRKEGKTWEQIIGSDDK
Protein: Tyrosine-protein kinase SYK (EC 2.7.10.2) (F1N9Y5)
Organism: Gallus gallus (Chicken)
Function: Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors.
Subcellular location: Cell membrane {ECO:0000305}. Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Uncharacterized protein.
- Caspase recruitment domain family member 9.
- SH2 domain-containing protein.
- B-cell linker protein
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- E3 ubiquitin-protein ligase CBL
- Uncharacterized protein.
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein phosphatase non-receptor type 11
- B-cell antigen receptor complex-associated protein beta chain
Sequence:
MASNMANPANHLPYFFGNITREEAEEYLMQGGMSDGLYLLRQSRNYLGGFALSLAYGRKVHHYTIERELSGTYAIAGGKSHASPAELINYHSEEADGLICLLRKSFNRPPGVEPKTGPFEDLKENLIREYVKQTWNLQGHALEQAIISQKPQLEKLIATTAHEKMPWFHGRISREESEHRILIGSRNNGKFLIRERDSNGSYALCLLNDGKVLHYRIDRDKTGKLSIPDGKRFDTLWQLVEHYSYKPDGLLRVLSIPCPRHGSESDNVVFDTRPLPGTPSKLQTPIGAPSDDQTPFNPYVLQRARGLIGAEKGDQREALPMDTEVYESPYADPDEIKPKNVTLDRKLLTLEEGELGSGNFGTVKKGFYKMKKGAKPVAVKILKNESNDPAIKDELLREANVMQQLDNPYIVRMIGICEAEAWMLVMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEENNFVHRDLAARNVLLVTQHYAKISDFGLSKALSADENYYKAQSHGKWPVKWYAPECMNFYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGGEVAQMIERGERMECPEACPVEVYDLMKLCWTYNVDDRPGFVAVELRLRNYYYDISH
Protein: cAMP-regulated D2 protein (P18142)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasmic vesicle, esterosome membrane. Note=Membrane-enclosed crystals (esterosome).
Interaction partners:
Sequence:
MNKLLVFILLLLLLINISFARKRSYIKNTDASIVVTQFGAIKGIVEDTHRVFYGVPFAQPPVNQLRWENPIDLKPWENVRETLTQKSQCAQKCNLGPGVCSPIGTSEDCLYLDVFTPKDATPNSKYPVIVYIPGGAFSVGSGSVPLYDATKFAQSSVIVVNINYRLGVLGFMGTDLMHGNYGFLDQIKALEWVYNNIGSFGGNKEMITIWGESAGAFSVSAHLTSTYSRQYFNAAISSSSPLTVGLKDKTTARGNANRFATNVGCNIEDLTCLRGKSMDEILDAQEKVGLTFGDKILDAFTIWSPVIDGDIIPMQPLTAVKEGKTYDVPTIIGNVKHEAIPFIYSFFQDSVGIDYYRVLVAIVFPLNAMKILPLYPAAPRGQDSRPILSELITDYLFRCPDRYHTVTNAKKLSSPTYHYHYVHVKSTGHSLDACDDKVCHGTELSLFFNSYELMGERLDNDEKELAIDINNYIVNFATTHNPNTGLDVPVQWRQVTSTQNSTLILETTIETKDTFTNDPKCNALDLTYYRNQVRP
Protein: Negative regulator of flagellin synthesis (Anti-sigma-28 factor) (P26477)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA.
Subcellular location: Cytoplasm. Note=After completion of the hook-basal body structure, it is exported out of the cell through the completely assembled hook-basal body structures.
Interaction partners:
- RNA polymerase sigma factor FliA
- Flagella synthesis protein FlgN
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 1
- Flagella basal body P-ring formation protein FlgA
- Flagellar hook-associated protein 2
- Flagellar hook protein FlgE
- Flagellar basal body rod protein FlgB
- Flagellin
- Basal-body rod modification protein FlgD
Sequence:
MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK
Protein: Kinesin-like protein KIF3B (HH0048) (Microtubule plus end-directed kinesin motor 3B) [Cleaved into: Kinesin-like protein KIF3B, N-terminally processed] (O15066)
Organism: Homo sapiens (Human)
Function: Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation. Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors. Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q61771}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61771}.
Interaction partners:
- Kinesin-associated protein 3
- Kinesin-like protein KIF3A
- Intraflagellar transport protein 88 homolog
- Polycomb group protein ASXL1
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 46 homolog
- Kinesin light chain 2
- Tripartite motif-containing protein 60
- Kinesin-like protein KIF11
- Kinesin-like protein KIFC3
Sequence:
MSKLKSSESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPASYNVEETLTTLRYANRAKNIKNKPRVNEDPKDALLREFQEEIARLKAQLEKRSIGRRKRREKRREGGGSGGGGEEEEEEGEEGEEEGDDKDDYWREQQEKLEIEKRAIVEDHSLVAEEKMRLLKEKEKKMEDLRREKDAAEMLGAKIKAMESKLLVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYSSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLEEKSKIMNRAFFDEEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSMMIRPEARYRAENIVLLELDMPSRTTRDYEGPAIAPKVQAALDAALQDEDEIQVDASSFESTANKKSKARPKSGRKSGSSSSSSGTPASQLYPQSRGLVPK
Protein: Uncharacterized protein (Q585L0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDIREIIDLVNGYQSTGETSADESLLQAVQRLKSALVDIPQLGSNTQEALKALVRAAVVWPSEWNDILQLLHDALADAALSCAHRTLLLELLPGLLEGDSDVKAHGESVCDVLLQWLLATVRKQGESAGDSKHQEDWRAALKALLVLPKECYSKIVQFCASQLPQSLPLCKAILTNSSASDLLKRAFEEWLVLSGNASQHADCARDIERLLRENFSGFGSLLCEKACSTLLSSGSLSSMSSLRTLQGALQVVHAFSMLHREIVRTHVPNSFVVSTTVGLLDIVGAENKDDKQQDAKGPWPCIKMTQEESTLVVSILRSLVKLSGIVTAVPGCVSISEVRKLCAPLLAIRNEAAALDCHLPLVECVFNLTLRILSCVCAGADEMRELLQELVDVSNVMLPVLSDSHNQIESFGPFCEKKSRRDNHSGPGGKEKDYDFWNMSDEQQQTMLSALRVLRAVSAMCRVCRAQNRSKPEDKSDEEHWKAVASDIASAARTLAPSWKIEVVEQPRPTVTSNPRLTEGTTVGRSAPTSRHESRNPYSQSHSSPSNHQYYSSNHSSYSPTPRHHSPSHHPHHHPPSHTHHGVPRSSRYSDYEGAPHRLSKRPRR
Protein: Polynucleotide 5'-hydroxyl-kinase NOL9 (EC 2.7.1.78) (Nucleolar protein 9) (E7F654)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q3TZX8}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5SY16}. Note=Colocalizes with pre-60S rRNP particles. {ECO:0000250|UniProtKB:Q5SY16}.
Interaction partners:
- WD repeat-containing protein 18
- Testis-expressed protein 10 homolog
- Proline-, glutamic acid- and leucine-rich protein 1
- LAS1-like ribosome biogenesis factor
- X-box-binding protein 1
- SUMO-specific peptidase 3b.
- C2 calcium-dependent domain-containing 2
- Nucleolar MIF4G domain-containing protein 1
- Kelch-like protein 21
- 5'-3' exoribonuclease
Sequence:
MTMKVHKVHSRSQQRQRNASKQHGKNKWNKKVRSLDSTLLNTSSGTAKLEQEIAKKEKPAIKRLKKLYAKPVTLLSDNNCADEDKVKPTSVTFAHVHTNGGTELDDSSRSVDSQEWSEYANSVLQNGMETSTLPDSDQAEDGLQFHAHLDHTKNRAVLVMKQSQVLCFRGKCLLTCLYGHVEVLGFTIEEGQQPYPVFSPPTHCPLTITALGNNQSSSKNKKEGQLEAKAIVRKYFTTEPSKKLMNEVDSDSCVVLLESLDTPLTRFLSSFSELTELFGLNSKELKSQAAIYSPVLSAVGVTALRGPCAQGLVMSRSYKETISSLLSAWAGEFDRCPIILVCGGKSSGKSTFNRHLINSLLNHTASVEYLECDLGQTEFTPPGCLSLCTVTEPLLGPPFTHLRDPEHMVYYGQADCQSDIDRYLESLKSLWRNVSGESPVIINTMGWIRGHGFQILVDLVRLFSVTHVVQLSYGTAPQCQLLTSEFIRSAHGWQTHPPTTPALTEDSHSPSRSHVFLSVQSEFEGAGVSGEMRFQRSNELRDLALLSYISKLQSSDPGPIRPLHCFIPYQVPHSSVAIGVTHCEVAPNNILYAANASVVGLCCLSEKVVGRGGPVILSQTPICQCVGLGVLRGVDMGRGLYFLVTPVSPSVLKHVNCLLLGEISLPKILLTQQHGVEGDLPYITTDYSFEVQGAGKLHIFKGLTRPGFIKSDN
Protein: Mitochondrial DNA polymerase beta-PAK (EC 2.7.7.7) (Q57ZV5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein artemis
- DNA polymerase
- Polynucleotide kinase 3'-phosphatase, putative
- Flap endonuclease 1
- ATP-dependent DNA helicase-like PIF8
- ATP-dependent DNA helicase PIF5
- DNA primase
Sequence:
MLLFRPTLLLSAAKRTAASANARRPAKRAVVAAATTSPAATSVPPPVRPAKRPVVPSPTPAPPPPRPSKKPVAQAGAPAPVAPPSPRPVKRPVVAAAAPTPPTPRPVKKPPAAPAQTPAPPPPRPWKKPVAQAGAPAPVAPPSPRPVKRPVVAAAAPTPPTPRPVKKPPAAPAQTPAPPPPRPSKKPVAQAGAPAPVAPPSPRPVKRPVVAAAAPTPPTPRPVKKPPAAPAASAPPSPKPAKKQAAAAASAPVSPRPVKQPAGTRARSQPKKPATKAKSPPAPPPAALPAPAPAAVPVTPKIKPTDFVPDYRERVLQIFQQLAEINKALDERYKASSYVVAVERLKRNDYIYMNFPPNIMPPGVNDEERKRLVAKVKNTTAMGDKLREKIVEILTTGDLAELHLLQQTPLIRAVRELTQVHGVGPRTAVIFFKKHGLKTVEELRKRVEEQEANEGGKGSSGDKSALKLTEAQRLGLKYYSDITQRIPHAEVRLHEAFLKLRLRKYLGKSYELAICGSYRRRLATSGDIDVLITRKIVADEGATPQGASEETSREKDGSLKVEKQLEPQEVLAAFVSALKEERYIEATLAQGATKFMGVSRLKSYKYNAGTANPRMYPARRLDIRFVEPECFPAALLYFTGSKNFNVVMRAEAIKRNFILNEYGLFRNDATGNEPTSSSETGGRVAGDGADKGAIRGRWSAEAFQKLVRANYYSAKSPAFVGTIEDAVDDEKDGEAAVGKNAKGSSATSRKQKQQQAKELAALWREVEARRVKVKHEREIFAALGMAYVHPEKRDVGTKTEGNVVGADKKRRSK
Protein: Histone deacetylase 1 (HD1) (EC 3.5.1.98) (Protein deacetylase HDAC1) (EC 3.5.1.-) (Protein deacylase HDAC1) (EC 3.5.1.-) (Q13547)
Organism: Homo sapiens (Human)
Function: Histone deacetylase that catalyzes 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. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
Subcellular location: Nucleus {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}.
Interaction partners:
- Histone deacetylase complex subunit SAP30
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- Paired amphipathic helix protein Sin3a
- Methyl-CpG-binding domain protein 2
- Chromodomain-helicase-DNA-binding protein 4
- Chromodomain-helicase-DNA-binding protein 3
- Methyl-CpG-binding protein 2
- Histone-lysine N-methyltransferase EHMT2
- Metastasis-associated protein MTA2
Sequence:
MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
Protein: K+/Cl-Cotransporter (H2KZC3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Anion exchange protein
- Serine/threonine-protein kinase WNK
- Germinal center kinase 3
Sequence:
MSGGRFRVQSVADGGGGGAGSVGALDSVSDSNLAVNSATKKEITNKAHDFEPEPTSSTSTNTVTSRRSSGGSGSGLGPASKKPPNMHINIPTDEGAERIPLCEQHSPLALYEQDYDTQGQKIGTMLRKLSVYNATEATSVEADEKPKAAAAKMGTIMGVFLPCLQNIFGVLFFIRLAWIIGTAGVFQAFFVVLTCVSVTFLTSISLSAIATNGVVPSGGPYYMISRNLGPELGGAVGILFYLGTTIAASMYITGAIEILLLYIYPQAKLFDDIYHNFRVLGTVLLLILGLIVMAGVKFVNRCALPLVIVVILCILSAILGVFVRYDGSDSLKFCMVGDRPVDLSTYFEKTQVQPNCTADGLQDLFCSTNGTCDHYYDRMKNIKVWKSSGMPAIREERAIKGIASGVFFDNLWPKYLRAGEVLSKDRKDKGDLNRGGHPSYIYAESVTNFMILVGVFFPSATGIMAGSNRSGNLRDAAKSIPLGTLAAQNFSSFIYLLGVVLFGASVSEMFIRDKYGRSAMGKLIISEISWPFPQVILFGCFMSTAGAGMQSLTGAPRLLQAIAADDVLPFLKPFRKMDSRGEPIRAILLTLAICECGILIAVIENITALITQFFLMCYLGVNAACALQSLLKSPGWRPGFRYFHWSLSMIGAILCVAVMFISAWHFALFAIIIGAGVYKYIEYAGAEKEWGDGLRGLGLSAARFALLNLDDKPQHSRNWRPQLLVLAPDVESANTNGILSFVSQLKAGKGLTLVAHCMEGEYADNYLKAQAVQEKLKAVVKKNKIKGFCDVLVTSNVIEGISCLVQTSGLGGMRHNTVVLSWPNDWKAEQEWVVANKFVSAIRAISAAKCAIMVPKYAEKFPANGTKVSGFIDVWWVVHDGGLLMLLPFLLRQHKTWKNTTVRLFAIAQMEDNNVQMKTDLEKFLYHLRIDAAVNVIEMTDSDISDYTYERTMKMEERNQYLKNLNKSDRDKDIQNHLEIVTRERKLSRINEEAPAVVPEQRNLEVVDEEQEDGKSENGSAKIEHKGVRFSDDEDSKEVKVGNGTLERDREERQRKRRYNVHKMHTAVKLNELMRQKSSDAQLVFVNLPGPPDADSDSYYMDFIEALTEGLDRVLLVRGTGAEVVTIYS
Protein: Paired box protein Pax-6 (O42348)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQTHADAKVQVLDNQNVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGTWGTRPGWYPGTSVPGQPAQDGCPQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQYWPRLQ
Protein: Clathrin heavy chain (P22137)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi.
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles.
Interaction partners:
- Clathrin light chain
- AP-1 complex subunit beta-1
- Auxilin-like clathrin uncoating factor SWA2
- AP-2 complex subunit beta
- AP-1 complex subunit gamma-1
- Epsin-5
- Epsin-3
- Epsin-1
- AP-2 complex subunit alpha
- Protein SLA2
Sequence:
MSDLPIEFTELVDLMSLGISPQFLDFRSTTFESDHFVTVRETKDGTNSVAIVDLAKGNEVTRKNMGGDSAIMHPSQMVISVRANGTIVQIFNLETKSKLKSFTLDEPVIFWRWLSETTLGFVTARSILTSNVFDGNVNAKPQLLTLRHANLNNTQIINFVANKNLDWFAVVGILQENGRIAGRIQLFSKQRNISQAIDGHVAIFTNILLEGNGSTPVQVFVTGNRNATTGAGELRIIEIDHDASLPSQYQKETTDIFFPPDATNDFPIAVQVSEKYGIIYLLTKYGFIHLYELETGTNLFVNRITAESVFTAAPYNHENGIACINKKGQVLAVEISTSQIVPYILNKLSNVALALIVATRGGLPGADDLFQKQFESLLLQNDYQNAAKVAASSTSLRNQNTINRLKNIQAPPGAISPILLYFSTLLDKGKLNKEETIELARPVLQQDRKQLFEKWLKEDKLECSEELGDIVKPFDTTLALACYLRAGAHAKVISCLAELQQFEKIIPYCQKVGYQPNFLVLISSLIRSSPDRASEFAVSLLQNPETASQIDIEKIADLFFSQNHIQQGTSLLLDALKGDTPDQGHLQTRVLEVNLLHAPQVADAILGNNIFSHYDKPTIASLSEKAGLYQRALENYTDIKDIKRCVVHTNALPIDWLVGYFGKLNVEQSLACLKALMDNNIQANIQTVVQVATKFSDLIGPSTLIKLFEDYNATEGLYYYLASLVNLTEDKDVVYKYIEAAAKMKQYREIERIVKDNNVYDPERVKNFLKDANLEDQLPLVIVCDRFDFVHEMILYLYKSQNLKFIETYVQQVNPSKTAQVVGALLDMDCDEAFIQSLLQSVLGQVPINELTTEVEKRNRLKILLPFLEQSLSQGIQDQAVYNALAKIYIDSNNSPEKFLKENDQYDTLDVGHYCEKRDPYLAYIAYEKGQNDDDLIRITNENSMYKYQARYLLERSDLDLWNKVLNQENIHRRQLIDSVISVGIPELTDPEPVSLTVQAFMTNGLKLELIELLEKIILEPSPFNENVALQGLLLLSAIKYEPTKVSSYIEKLDNYDADEIAPLCIEHDLKEEAFEIYDKHEMYGKALKVLIEDIMSLDRAASYADKINTPELWSQIGTAQLDGLRIPDAIESYIKAEDPSNYENVIDIAEQAGKYEELIPFLLMARKTLKEPKIDGALILAYAELNKIHEIENLLAGSNVANLDHVGDKLFENKEYKAARLCYSAVSNYSKLASTLVYLGDYQAAVDTARKASNIKVWKLVNDACIEKKEFKLAQICGLNLIVHAEELDELVERYESNGYFEELISLFEAGLGLERAHMGMFTELAILYSKYEPDKTFEHLKLFWSRINIPKVIRAVEQAHLWSELVFLYAHYDEWDNAALTLIEKSTKDLDHAYFKEVVVKVSNLEIYYKAINFYVKFHPSLLVDLLTSLTPRLDIPRTVKIFSKSDNLPLIKPFLINVLPKNNSVVNQAYHDLMIEEEDYKALQDAVDSYDKFDQLGLASRLESHKLIFFKKIGALLYRRNKKWAKSLSILKEEKLWKDAIETAAISQDPKVVEALLTYFVETGNREGFVALLYAAYNLVRIEFVLEISWMNSLEDYIKPFEISIKKEQNDSIKKITEELAKKSGSNEEHKDGQPLMLMNSAMNVQPTGF