wanglab/gogpt-training-data huggingface dataset:
Protein: D-amino-acid N-acetyltransferase HPA3 (DNT) (EC 2.3.1.36) (P39979)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: N-acetyltransferase that acetylates histone H4 at 'Lys-8'. Also acetylates polyamines like putrescine, spermidine and spermine. Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated. D-amino acids are toxic for the cell and their N-acetylation, preceding removal from cells, plays an important role in detoxification of D-amino acids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Histone acetyltransferase HPA2
- Uncharacterized protein YIR042C
Sequence:
MSNEEPEKMVNDRIVVKAIEPKDEEAWNKLWKEYQGFQKTVMPPEVATTTFARFIDPTVKLWGALAFDTETGDAIGFAHYLNHLTSWHVEEVVYMNDLYVTERARVKGVGRKLIEFVYSRADELGTPAVYWVTDHYNHRAQLLYTKVAYKTDKVLYKRNGY
Protein: Mannosyltransferase KTR6 (EC 2.4.1.-) (Mannosylphosphate transferase MNN6) (P54070)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glycosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for addition of mannosylphosphate in yeast mannan. Recognizes any oligosaccharides with at least one alpha-1,2-linked mannobiose unit.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Alpha-1,3-mannosyltransferase MNN1
- Alpha-1,2-mannosyltransferase MNN5
- Mannosyltransferase regulator 4
- Probable alpha-1,3-mannosyltransferase MNT4
- Alpha-1,2-mannosyltransferase MNN2
- Mannan polymerase complexes subunit MNN9
- Initiation-specific alpha-1,6-mannosyltransferase
- Glycolipid 2-alpha-mannosyltransferase
- Probable alpha-1,6-mannosyltransferase MNN10
- Putative glycosyltransferase HOC1
Sequence:
MHVLLSKKIARFLLISFVFVLALMVTINHPKTKQMSEQYVTPYLPKSLQPIAKISAEEQRRIQSEQEEAELKQSLEGEAIRNATVNAIKEKIKSYGGNETTLGFMVPSYINHRGSPPKACFVSLITERDSMTQILQSIDEVQVKFNKNFAYPWVFISQGELDGMKQEMIRQAITDSMNGDPELINIKFAEIPADEWVYPEWIDENKAAESLISLANVPDGDSRAVRYQARYFAGFFWRHPVLDEFDWYWRVDPGIKLYCDIDHDLFRWMQDEGKVFGFTLSMSEAKEANEKIWDVTKKFAKDFPKFISENNFKSFITKKDSEDFNNCEFTSNFEIGNLNFYRSPAYRKFFNYIDEEGGIFYWKWSDSIIHTIGLSMLLPKDKIHFFENIGFHYDKYNNCPLNDDIWNQYNCNCDQGNDFTFRSGSCGGHYFDIMKKDKPEGWDRLP
Protein: Plasmacytoid dendritic cell-specific receptor (Triggering receptor expressed in myeloid cells 4) (Triggering receptor expressed on myeloid cells 4) (Q8BNV8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Plexin-A1
- TYRO protein tyrosine kinase-binding protein
- Triggering receptor expressed on myeloid cells 3
Sequence:
MAWEPTYLLSPVLLLLLASGSWTQNPELLRTQEGETVSVTCWYDSLYHSSEKIWCKQIDNLCYPFVSKSAEKPRFLIQQSSRFNFFTVTMTKLKMSDSGIYHCGIVANNTSVYLRNIHLVVSKGSSVVSTPDIIPATRLTKLPTLITTKHSPSDTTTTRSLPQPTTVVSSPDPRVIIINGTDADRGFVSSVTIPVVCGLLSKTLVFTVLFIVTQKSFGRQAMKAHNSNS
Protein: Protein SHI RELATED SEQUENCE 6 (Q9M2U4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influences vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM) (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Electron carrier/iron ion-binding protein
Sequence:
MLGLRNIILLSPPPTQITRPSLPPVNFAAVEDNNTVGEKVCRDCGNRAKKECLFERCRTCCKSRGYNCVTHVKSTWIPSSATRSSSSPSERKKKLKIDKQSSPNVSLLPTTTSRQERGFREGLPGKIEAPAVFKRTRVTAISNNEQAEIGYQATVTISGHIFKGFLHYYGVDHNKAFPCLSQK
Protein: Transcription factor STP1 (Q00947)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes, including the amino-acid permeases AGP1, BAP2, BAP3 and GNP1. Binding to promoters is facilitated by DAL81. Involved in the repression of genes subject to nitrogen catabolite repression and genes involved in stress response. Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and ASI3, which prevent unprocessed precursor forms that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes. May be involved in pre-tRNA splicing.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Localizes to the cytoplasm in its unprocessed form and is targeted to the nucleus after proteolytic processing upon induction by amino acids. The SCF(MET30) ubiquitin ligase complex negatively regulates nuclear accumulation of the processed form in the absence of high extracellular methionine levels.
Interaction partners:
- SPS-sensor serine protease component SSY5
- SPS-sensor component PTR3
- SPS-sensor component SSY1
- Transcription factor STP2
- Transcriptional activator protein DAL81
- Probable ERAD-associated E3 ubiquitin-protein ligase ASI1
- ERAD-associated E3 ubiquitin-protein ligase ASI1
- Protein ASI2
- General amino acid permease AGP1
Sequence:
MPSTTLLFPQKHIRAIPGKIYAFFRELVSGVIISKPDLSHHYSCENATKEEGKDAADEEKTTTSLFPESNNIDRSLNGGCSVIPCSMDVSDLNTPISITLSPENRIKSEVNAKSLLGSRPEQDTGAPIKMSTGVTSSPLSPSGSTPEHSTKVLNNGEEEFICHYCDATFRIRGYLTRHIKKHAIEKAYHCPFFNSATPPDLRCHNSGGFSRRDTYKTHLKARHVLYPKGVKPQDRNKSSGHCAQCGEYFSTIENFVENHIESGDCKALPQGYTKKNEKRSGKLRKIKTSNGHSRFISTSQSVVEPKVLFNKDAVEAMTIVANNSSGNDIISKYGNNKLMLNSENFKVDIPKRKRKYIKKKQQQVSGSTVTTPEVATQNNQEVAPDEISSATIFSPFDTHLLEPVPSSSSESSAEVMFHGKQMKNFLIDINSFTNQQQQAQDNPSFLPLDIEQSSYDLSEDAMSYPIISTQSNRDCTQYDNTKISQILQSQLNPEYLSENHMRETQQYLNFYNDNFGSQF
Protein: Transcription factor GATA-4 (GATA-binding factor 4) (Q08369)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator that binds to the consensus sequence 5'-AGATAG-3' and plays a key role in cardiac development. In cooperation with TBX5, it binds to cardiac super-enhancers and promotes cardiomyocyte gene expression, while it down-regulates endocardial and endothelial gene expression (By similarity). Involved in bone morphogenetic protein (BMP)-mediated induction of cardiac-specific gene expression (By similarity). Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). Acts as a transcriptional activator of ANF in cooperation with NKX2-5. Promotes cardiac myocyte enlargement (By similarity). Required during testicular development (By similarity). May play a role in sphingolipid signaling by regulating the expression of sphingosine-1-phosphate degrading enzyme, sphingosine-1-phosphate lyase (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P43694}.
Interaction partners:
- Zinc finger protein ZFPM2
- Homeobox protein Nkx-2.5
- T-box transcription factor TBX5
- Nuclear factor of activated T-cells, cytoplasmic 4
- Serum response factor
- Heart- and neural crest derivatives-expressed protein 2
- Myocyte-specific enhancer factor 2C
- Transcription factor SOX-9
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3
- Sequestosome-1
Sequence:
MYQSLAMAANHGPPPGAYEAGGPGAFMHSAGAASSPVYVPTPRVPSSVLGLSYLQGGGSAAAAGTTSGGSSGAGPSGAGPGTQQGSPGWSQAGAEGAAYTPPPVSPRFSFPGTTGSLAAAAAAAAAREAAAYGSGGGAAGAGLAGREQYGRPGFAGSYSSPYPAYMADVGASWAAAAAASAGPFDSPVLHSLPGRANPGRHPNLDMFDDFSEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLIKPQRRLSASRRVGLSCANCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQTRKRKPKNLNKSKTPAGPAGETLPPSSGASSGNSSNATSSSSSSEEMRPIKTEPGLSSHYGHSSSMSQTFSTVSGHGPSIHPVLSALKLSPQGYASPVTQTSQASSKQDSWNSLVLADSHGDIITA
Protein: MLLT10 histone lysine methyltransferase DOT1L cofactor (F8W451)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- MLLT1 super elongation complex subunit a.
Sequence:
MVSSELYLAEEDDDSPSNMKEMIGGCCVCSDERGWAENPLVYCDGHGCNVAVHQACYGIVQVPTGPWFCRKCESQERAARVIKGWRGRKPSWQTPEGGGQSTTCNKEEEDSRLSRSLKTLNIVRCELCPQKDGALKRTDNGGWAHVVCALYIPEVEFANVSTMEPIVLQSVPHERYNKTCYICEEQGRESKAATGACMTCNKHGCRQAFHVTCAQLAGLLCEEQGSDADNVKYCGYCKYHYNKLRRSKGRGSRAQSLSDSSTHSLDKHHDKEKKKHKERDRHKPKHKKPLELSPSLVPALMVTPEKSYNNSSSGGSVSSISSTQKRLDDSGARFTNANFQEVPPHSSSSSKDGGSSDGKSSDSKSKKSSHSTSSSSGSRGRKSVAGKPHGPVVTTATSSTAPSSTSPFQQGHLLGSNSSSKSATSGSVVQPTSDFLSFSDPSLRAGDSYTPPSFGRCHMKGGAESGASESMVALNTFSMIPLSQSSSSSSSKHYENCHTTGELGSLASASYKRPQPSSSSSSATSSSSTGEDGVKKKKRGNWRNRYGPCFTTQDSKTTDAGEHISTMPSSTSPSPSSMSNMVCRGSTVSSTASVGAVGAGTSSLGIQKSPSLLRNGSLQGMTVSSPPAVPGSYPSSSDVACPLPSAVLGGSMSASNSELPAHQSVVVTSMPTLTSLPSAAPFTSTPSTHANSLPGSFNLAPSHMFGNRLNPNSAMAALIAQSEGSPADQELGDGALGFSRRGNSPKTNLSPRSPLSGLHIRYDAGPMVPGLGSGSDTLPPAATSIDQLLERQWNEGQQFLLQQGSQGDVLAMLKSLHQLQVENRRLEEQIRTLTMKKERLQLLSAQLSVPFTPASTTATTASSPMYPSNTHTDMLHSKSIQLGSVLTESSQPLPTQDPQSGGHSSGSSTSSLSTPPSAAHSPPQQQVNGVGMAGVPVQPGNANSSLPAIAGVTGLMGALQGNHLAMSGIVGALNGVIQTSQSSLTQNSSPLPQSATASSASLSMSSSLTNSSMSTTKTRLFTEQHRQILLHQHQLQQLFGSQQPTPEQQQVLLYQLMQQQQQQQQQQQQNDIQFQQLPINSLLPGNQPTTSTNPFLAHHNDNNTPKAGVNTAAIKQTKRLGEKAVPVTGQEKT
Protein: POU domain, class 5, transcription factor 1 (NF-A3) (Octamer-binding protein 3) (Oct-3) (Octamer-binding protein 4) (Oct-4) (Octamer-binding transcription factor 3) (OTF-3) (P20263)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q01860}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163, ECO:0000269|PubMed:29153991}. Note=Expressed in a diffuse and slightly punctuate pattern (By similarity). Colocalizes with MAPK8 and MAPK9 in the nucleus (PubMed:29153991). {ECO:0000250|UniProtKB:Q01860, ECO:0000269|PubMed:29153991}.
Interaction partners:
- Homeobox protein NANOG
- Transcription factor SOX-2
- Catenin beta-1
- WD repeat-containing protein 5
- Sal-like protein 4
- Transcription factor SOX-17
- Pyruvate kinase PKM
- Krueppel-like factor 4
- Steroid hormone receptor ERR2
- Histone deacetylase 1
Sequence:
MAGHLASDFAFSPPPGGGDGSAGLEPGWVDPRTWLSFQGPPGGPGIGPGSEVLGISPCPPAYEFCGGMAYCGPQVGLGLVPQVGVETLQPEGQAGARVESNSEGTSSEPCADRPNAVKLEKVEPTPEESQDMKALQKELEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSLKNMCKLRPLLEKWVEEADNNENLQEICKSETLVQARKRKRTSIENRVRWSLETMFLKCPKPSLQQITHIANQLGLEKDVVRVWFCNRRQKGKRSSIEYSQREEYEATGTPFPGGAVSFPLPPGPHFGTPGYGSPHFTTLYSVPFPEGEAFPSVPVTALGSPMHSN
Protein: Capsid protein (CP) (Coat protein) (P03615)
Organism: Escherichia virus Qbeta (Bacteriophage Q-beta)
Function: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation. The capsid contains also 1 copy of the A2 maturation protein.
Subcellular location: Virion {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}. Note=The shell is composed of 89 dimers of the capsid protein, one of them being sequestered inside the virion, and 1 copy of the maturation protein. {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}.
Interaction partners:
Sequence:
MAKLETVTLGNIGKDGKQTLVLNPRGVNPTNGVASLSQAGAVPALEKRVTVSVSQPSRNRKNYKVQVKIQNPTACTANGSCDPSVTRQAYADVTFSFTQYSTDEERAFVRTELAALLASPLLIDAIDQLNPAY
Protein: Type VI collagen alpha 3 subunit N7 domain (O88494)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VHVNKRDIIFLLDGSDNVGKNNFPYVRDFVTNLVNSLDVGSDNIRVGLVQFSDTPVTEFSLDTYQTKSELLAHLRRLQLKGGSGLNAGSALSYIHANHFTEAGGSRTRAHVPQLLLLLMAGPSEDAYLQAADAMVRSGVLTLCVGTTRADKAESEHIAFNPSLVYVMDDFRSLPYLPQQPIQPLTTYVSGGVQEVPLSQP
Protein: Late expression factor 11 (P21288)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Plays an essential role in viral genome replication. Involved also in late/very late gene activation.
Subcellular location: Host nucleus {ECO:0000269|PubMed:11514741}.
Interaction partners:
Sequence:
MPPKNCTHLGGCDSDCLTRSEIQALFREAINTLKHTMNTENVCAHMLDIVSFERIKEYIRANLGHFTVITDKCSKRKVCLHHKRIARLLGIKKIYHQEYKRVVSKVYKKQTW
Protein: Translation initiation factor eIF2B subunit alpha (eIF2B GDP-GTP exchange factor subunit alpha) (Q14232)
Organism: Homo sapiens (Human)
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9USP0}.
Interaction partners:
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit 3
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2 subunit 1
- eIF-2-alpha kinase GCN2
- Thymidine phosphorylase
- Aprataxin
Sequence:
MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVDSSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIKDGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLDAAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFPLNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDELIKLYL
Protein: Clusterin associated protein 1 (I3L121)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
Sequence:
MRTEAIARPLEINETEKVMRIAIKEILTQVQKTKDLLNNVASDEANLEAKIEKRKLELERNRKRLETLQSVRPCFMDEYEKTEEELQKQYDTYLEKFQNLTYLEQQLEDHHRMEQERFEEAKNTLCLIQNKLKEEEKRLLKSGSNDDSDID
Protein: Guanylate-binding protein 7 (EC 3.6.1.-) (EC 3.6.5.-) (GTP-binding protein 7) (GBP-7) (Guanine nucleotide-binding protein 7) (Guanylate-binding protein 4-like) (Q8N8V2)
Organism: Homo sapiens (Human)
Function: Hydrolyzes GTP to GMP in two consecutive cleavage reactions and predominantly uses GTP and not GDP or GMP as the substrate (By similarity). Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii (By similarity). Promotes IFN-gamma-mediated host defense against bacterial infections by regulating oxidative responses and bacteriolytic peptide generation (By similarity). May help to assemble NADPH oxidase on phagosomal membranes by acting as a bridging protein between NADPH oxidase cytosolic subunits NCF2-NCF4 and the membrane subunits CYBA-CYBB (By similarity). Participates along with GBP1 in trafficking monoubiquinated protein cargo to autolysosomes for generating ubiquitin-derived antimicrobial peptides (By similarity). Required for disruption of the parasitophorous vacuole formed following T.gondii infection and subsequent killing of the parasite (By similarity). Facilitates influenza A virus replication by inhibiting the activation of NF-kappaB and JAK-STAT signaling pathways and the expression of type I, type III interferons and pro-inflammatory cytokines.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q91Z40}.
Interaction partners:
- Cysteine protease ATG4B
Sequence:
MASEIHMPGPVCLTENTKGHLVVNSEALEILSAITQPVVVVAIVGLYRTGKSYLMNKLAGKNKGFPLGCTVKSETKGIWMWCVPHPSKPNHTLILLDTEGLGDMEKSDPKSDSWIFALAVLLSSSFVYNSMGTINHQALEQLHYVTELTELIRAKSCPRPDEVEDSSEFVSFFPDFIWTVRDFTLELKLDGHPITEDEYLENALKLISGKNPQIQNSNKPREWIRHFFPKQKCFVFDRPINDKKLLLHVEEVREDQLDSNFQMQSENFCSYIFTHAKTKTLREGILVTGNRLGMLVETYLDAINSGATPCLENAMAVLAQCENSAAVQRAANHYSQQMAQQVRFPTDTLQELLDVHAVCEREAIAVFMEYSFKDKSQEFQKKLVDTMEKKKEDFVLQNEEASAKYCQAELKRLSELLTESISRGTFFVPGGHNIYLEAKKKIEQDYTLVPRKGVKADEVLQSFLQSQVVIEESILQSDKALTAGEKAIAAKQAKKEAAEKEQELLRQKQKEQQQMMEAQERSFQENIAQLKKKMERERENYMRELRKMLSHKMKVLEELLTEGFKEIFESLNEEINRLKEQIEAAENEEPSVFSQILDVAGSIFIAALPGAAKLVDLGMKILSSLCNRLRNPGKKIIS
Protein: Antigen peptide transporter 2 (APT2) (EC 7.4.2.14) (ATP-binding cassette sub-family B member 3) (P36372)
Organism: Rattus norvegicus (Rat)
Function: ABC transporter associated with antigen processing. In complex with TAP1 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (By similarity). Uses the chemical energy of ATP to export peptides against the concentration gradient (By similarity). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (By similarity). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q03519}; Multi-pass membrane protein {ECO:0000255}. Note=The transmembrane segments seem to form a pore in the membrane. {ECO:0000250|UniProtKB:Q03519}.
Interaction partners:
- Antigen peptide transporter 1
- TAP binding protein
- Calreticulin
- Calreticulin
- Protein disulfide-isomerase A3
- ABC-type oligopeptide transporter ABCB9
- Beta-2-microglobulin
- RT1 class I histocompatibility antigen, AA alpha chain
Sequence:
MALSHPRPWASLLLVDLALLGLLQSSLGTLLPPGLPGLWLEGTLRLGVLWGLLKVGGLLRLVGTFLPLLCLTNPLFFSLRALVGSTMSTSVVRVASASWGWLLADYGAVALSLAVWAVLSPAGAQEKEPGQENNRALMIRLLRLSKPDLPFLIVAFIFLAMAVWWEMFIPHYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSLSAGCRGGSFLFAESRINLRIREQLFSSLLRQDLAFFQETKTGELNSRLSSDTSLMSQWLSLNANILLRSLVKVVGLYYFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVRRYKEALERCRQLWWRRDLEKSLYLVIQRVMALGMQVLILNVGVQQILAGEVTRGGLLSFLLYQEEVGHHVQNLVYMYGDMLSNVGAAEKVFSYLDRRPNLPNPGTLAPPRLEGRVEFQDVSFSYPSRPEKPVLQGLTFTLHPGKVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDAECEQALQTWRSQEDRTMLVIAHRLHTVQNADQVLVLKQGQLVEHDQLRDEQDVYAHLVQQRLEA
Protein: Cyclic AMP-responsive element-binding protein 3 (CREB-3) (cAMP-responsive element-binding protein 3) (Transcription factor LZIP) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3] (Q61817)
Organism: Mus musculus (Mouse)
Function: Endoplasmic reticulum (ER)-bound sequence-specific transcription factor that directly binds DNA and activates transcription. Plays a role in the unfolded protein response (UPR), promoting cell survival versus ER stress-induced apoptotic cell death. Also involved in cell proliferation, migration and differentiation, tumor suppression and inflammatory gene expression. Acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Associates with chromatin to the HERPUD1 promoter. Also induces transcriptional activation of chemokine receptors. Functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Also decreases the acetylation level of histone H4. Does not promote the chemotactic activity of leukocyte cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43889}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O43889, ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:O43889}. Nucleus {ECO:0000250|UniProtKB:O43889}. Cytoplasm {ECO:0000250|UniProtKB:O43889}. Note=Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia. Colocalizes with DCSTAMP in the ER membrane of immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane. {ECO:0000250|UniProtKB:O43889}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3]: Nucleus {ECO:0000250|UniProtKB:O43889}. Note=Upon RIP activation the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form translocates into the nucleus. Detected in the nucleus upon dendritic cell maturation and RIP activation. Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF in promyelocytic leukemia protein nuclear bodies (PML-NB). {ECO:0000250|UniProtKB:O43889}.
Interaction partners:
- CREB3 regulatory factor
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 5
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Host cell factor 1
- Cyclic AMP-responsive element-binding protein 3-like protein 4
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-dependent transcription factor ATF-6 beta
Sequence:
MDPGGQDLLALDPGDQDLLGFLLEESGDLWAATEPDVKASLDLELSPSENSVQELSDWEVEDLLSSLLSPSVSRDVLGSSSSSILHDHNYSLPQEHVSIDLGECEMISCRGRRELTGLAGSTFPFADTESFEKEGFHVTPLPGEERAAEQEMSRLILTEEEKKLLEKEGLTLPSTLPLTKVEEQVLKRVRRKIRNKRAAQESRKKKKVYVVGLESRVLKYTAQNRELQNKVQRLEEQNLSLLDQLRKLQAMVIEIANKTSSGSTCVLVLVFSFCLLLVPAMYSSDARGSVPAEYVVLHRKLRALPSEDDHQPKPSALSSELPMDSTHQSLDSSEHMFLVSSNFSCVLYHAPQAEQPLHWPLWDLSSEMLFSDSNLLLQANLSESEGWQPNHSPSLVIFQGRYSG