ID DNJC2_HUMAN Reviewed; 621 AA. AC Q99543; A4VCI0; Q9BVX1; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 4. DT 27-MAR-2024, entry version 202. DE RecName: Full=DnaJ homolog subfamily C member 2; DE AltName: Full=M-phase phosphoprotein 11; DE AltName: Full=Zuotin-related factor 1; DE Contains: DE RecName: Full=DnaJ homolog subfamily C member 2, N-terminally processed; GN Name=DNAJC2; Synonyms=MPHOSPH11, MPP11, ZRF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PHOSPHORYLATION. RC TISSUE=Blood; RX PubMed=8885239; DOI=10.1091/mbc.7.9.1455; RA Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.; RT "Identification of novel M phase phosphoproteins by expression cloning."; RL Mol. Biol. Cell 7:1455-1469(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] RP PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Osteosarcoma; RA Bienvenut W.V., Glen H., Frame M.C.; RL Submitted (MAR-2008) to UniProtKB. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-621 (ISOFORM 1). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP TISSUE SPECIFICITY. RX PubMed=11034098; RA Resto V.A., Caballero O.L., Buta M.R., Westra W.H., Wu L., Westendorf J.M., RA Jen J., Hieter P., Sidransky D.; RT "A putative oncogenic role for MPP11 in head and neck squamous cell RT cancer."; RL Cancer Res. 60:5529-5535(2000). RN [6] RP INDUCTION IN LEUKEMIA. RX PubMed=12800198; DOI=10.1002/ijc.11200; RA Greiner J., Ringhoffer M., Taniguchi M., Hauser T., Schmitt A., Dohner H., RA Schmitt M.; RT "Characterization of several leukemia-associated antigens inducing humoral RT immune responses in acute and chronic myeloid leukemia."; RL Int. J. Cancer 106:224-231(2003). RN [7] RP INDUCTION IN LEUKEMIA. RX PubMed=14696097; DOI=10.1002/ijc.11623; RA Greiner J., Ringhoffer M., Taniguchi M., Li L., Schmitt A., Shiku H., RA Dohner H., Schmitt M.; RT "mRNA expression of leukemia-associated antigens in patients with acute RT myeloid leukemia for the development of specific immunotherapies."; RL Int. J. Cancer 108:704-711(2004). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, AND RP INTERACTION WITH HSPA14. RX PubMed=16002468; DOI=10.1073/pnas.0504400102; RA Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P., Rucknagel P., RA Stahl J., Rospert S.; RT "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated RT complex."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005). RN [9] RP FUNCTION, AND MUTAGENESIS OF 512-HIS-GLN-513. RX PubMed=15802566; DOI=10.1126/science.1109247; RA Hundley H.A., Walter W., Bairstow S., Craig E.A.; RT "Human Mpp11 J protein: ribosome-tethered molecular chaperones are RT ubiquitous."; RL Science 308:1032-1034(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-60 AND RP SER-63, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP INDUCTION. RX PubMed=17242690; DOI=10.1038/sj.cr.7310121; RA Wang C., Chen X., Wang Y., Gong J., Hu G.; RT "C/EBPalphap30 plays transcriptional regulatory roles distinct from RT C/EBPalphap42."; RL Cell Res. 17:374-383(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP EPITOPE REGION. RX PubMed=20231810; DOI=10.1016/s1658-3876(10)50053-0; RA Al Qudaihi G., Lehe C., Dickinson A., Eltayeb K., Rasheed W., Chaudhri N., RA Aljurf M., Dermime S.; RT "Identification of a novel peptide derived from the M-phase phosphoprotein RT 11 (MPP11) leukemic antigen recognized by human CD8+ cytotoxic T RT lymphocytes."; RL Hematol. Oncol. Stem Cell Ther. 3:24-33(2010). RN [15] RP FUNCTION AS CHROMATIN REGULATOR, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, RP AND DOMAIN ZRF1-UBD. RX PubMed=21179169; DOI=10.1038/nature09574; RA Richly H., Rocha-Viegas L., Ribeiro J.D., Demajo S., Gundem G., RA Lopez-Bigas N., Nakagawa T., Rospert S., Ito T., Di Croce L.; RT "Transcriptional activation of polycomb-repressed genes by ZRF1."; RL Nature 468:1124-1128(2010). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Acts both as a chaperone in the cytosol and as a chromatin CC regulator in the nucleus. When cytosolic, acts as a molecular CC chaperone: component of the ribosome-associated complex (RAC), a CC complex involved in folding or maintaining nascent polypeptides in a CC folding-competent state. In the RAC complex, stimulates the ATPase CC activity of the ribosome-associated pool of Hsp70-type chaperones CC HSPA14 that bind to the nascent polypeptide chain. When nuclear, CC mediates the switching from polycomb-repressed genes to an active CC state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' CC (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex CC from chromatin, thereby facilitating transcription activation. CC {ECO:0000269|PubMed:15802566, ECO:0000269|PubMed:16002468, CC ECO:0000269|PubMed:21179169}. CC -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type CC chaperone DNAJC2 (PubMed:16002468). Interacts (via ZRF1-UBD region) CC with ID1 (By similarity). {ECO:0000250|UniProtKB:P54103, CC ECO:0000269|PubMed:16002468}. CC -!- INTERACTION: CC Q99543; P0C0S8: H2AC17; NbExp=2; IntAct=EBI-11017224, EBI-1390628; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179169}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:16002468, ECO:0000269|PubMed:21179169}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99543-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99543-2; Sequence=VSP_023562; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11034098}. CC -!- INDUCTION: Expression is repressed by CEBPA. Strongly overexpressed in CC leukemic cells. {ECO:0000269|PubMed:12800198, CC ECO:0000269|PubMed:14696097, ECO:0000269|PubMed:17242690}. CC -!- DOMAIN: The ZRF1-UBD region specifically recognizes and binds CC H2AK119ub. The ZRF1-UBD region is also involved in protein-protein CC interactions with other proteins, suggesting that it may be masked by CC some regulator, thereby preventing its association with H2AK119ub. CC {ECO:0000269|PubMed:21179169}. CC -!- PTM: Phosphorylated in M (mitotic) phase. {ECO:0000269|PubMed:8885239}. CC -!- MISCELLANEOUS: Constitutes a myeloid leukemia-associated antigen and CC might be a target for leukemia T-cell therapy. CC -!- SEQUENCE CAUTION: CC Sequence=AAI39752.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA66913.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X98260; CAA66913.1; ALT_INIT; mRNA. DR EMBL; AC004668; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000859; AAH00859.1; -; mRNA. DR EMBL; BC139751; AAI39752.1; ALT_INIT; mRNA. DR CCDS; CCDS43628.1; -. [Q99543-1] DR CCDS; CCDS47679.1; -. [Q99543-2] DR RefSeq; NP_001123359.1; NM_001129887.1. [Q99543-2] DR RefSeq; NP_055192.1; NM_014377.1. [Q99543-1] DR PDB; 2M2E; NMR; -; A=551-621. DR PDB; 6CGH; NMR; -; A=346-432. DR PDBsum; 2M2E; -. DR PDBsum; 6CGH; -. DR AlphaFoldDB; Q99543; -. DR BMRB; Q99543; -. DR SMR; Q99543; -. DR BioGRID; 117946; 248. DR ComplexPortal; CPX-2642; Ribosome-associated complex. DR DIP; DIP-60462N; -. DR IntAct; Q99543; 13. DR MINT; Q99543; -. DR STRING; 9606.ENSP00000368565; -. DR GlyGen; Q99543; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99543; -. DR MetOSite; Q99543; -. DR PhosphoSitePlus; Q99543; -. DR SwissPalm; Q99543; -. DR BioMuta; DNAJC2; -. DR DMDM; 296439472; -. DR EPD; Q99543; -. DR jPOST; Q99543; -. DR MassIVE; Q99543; -. DR MaxQB; Q99543; -. DR PaxDb; 9606-ENSP00000368565; -. DR PeptideAtlas; Q99543; -. DR ProteomicsDB; 78318; -. [Q99543-1] DR ProteomicsDB; 78319; -. [Q99543-2] DR Pumba; Q99543; -. DR Antibodypedia; 9291; 221 antibodies from 30 providers. DR DNASU; 27000; -. DR Ensembl; ENST00000249270.11; ENSP00000249270.7; ENSG00000105821.15. [Q99543-2] DR Ensembl; ENST00000379263.8; ENSP00000368565.3; ENSG00000105821.15. [Q99543-1] DR GeneID; 27000; -. DR KEGG; hsa:27000; -. DR MANE-Select; ENST00000379263.8; ENSP00000368565.3; NM_014377.3; NP_055192.1. DR UCSC; uc003vbo.4; human. [Q99543-1] DR AGR; HGNC:13192; -. DR CTD; 27000; -. DR DisGeNET; 27000; -. DR GeneCards; DNAJC2; -. DR HGNC; HGNC:13192; DNAJC2. DR HPA; ENSG00000105821; Low tissue specificity. DR MIM; 605502; gene. DR neXtProt; NX_Q99543; -. DR OpenTargets; ENSG00000105821; -. DR PharmGKB; PA162383835; -. DR VEuPathDB; HostDB:ENSG00000105821; -. DR eggNOG; KOG0724; Eukaryota. DR GeneTree; ENSGT00940000155441; -. DR HOGENOM; CLU_019916_0_0_1; -. DR InParanoid; Q99543; -. DR OMA; SFWYDFD; -. DR OrthoDB; 168809at2759; -. DR PhylomeDB; Q99543; -. DR TreeFam; TF105834; -. DR PathwayCommons; Q99543; -. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR SignaLink; Q99543; -. DR BioGRID-ORCS; 27000; 95 hits in 1185 CRISPR screens. DR ChiTaRS; DNAJC2; human. DR GeneWiki; ZRF1; -. DR GenomeRNAi; 27000; -. DR Pharos; Q99543; Tbio. DR PRO; PR:Q99543; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q99543; Protein. DR Bgee; ENSG00000105821; Expressed in sural nerve and 209 other cell types or tissues. DR ExpressionAtlas; Q99543; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:CACAO. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0001671; F:ATPase activator activity; TAS:Reactome. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0042393; F:histone binding; IDA:UniProtKB. DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; IDA:UniProtKB. DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:Ensembl. DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR CDD; cd06257; DnaJ; 1. DR CDD; cd00167; SANT; 2. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 2. DR Gene3D; 1.10.8.840; Ribosome-associated complex head domain; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR018253; DnaJ_domain_CS. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR017930; Myb_dom. DR InterPro; IPR032003; RAC_head. DR InterPro; IPR042569; RAC_head_sf. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR017884; SANT_dom. DR InterPro; IPR044634; Zuotin/DnaJC2. DR PANTHER; PTHR43999; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1. DR PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF00249; Myb_DNA-binding; 1. DR Pfam; PF16717; RAC_head; 1. DR SMART; SM00271; DnaJ; 1. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS00636; DNAJ_1; 1. DR PROSITE; PS50076; DNAJ_2; 1. DR PROSITE; PS51293; SANT; 2. DR Genevisible; Q99543; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Chaperone; KW Chromatin regulator; Cytoplasm; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation. FT CHAIN 1..621 FT /note="DnaJ homolog subfamily C member 2" FT /id="PRO_0000425752" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.3" FT CHAIN 2..621 FT /note="DnaJ homolog subfamily C member 2, N-terminally FT processed" FT /id="PRO_0000071123" FT DOMAIN 88..161 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT DOMAIN 449..511 FT /note="SANT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT DOMAIN 549..604 FT /note="SANT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT REGION 23..31 FT /note="Epitope (recognized by CD8(+) cytotoxic T- FT lymphocytes)" FT REGION 160..250 FT /note="ZRF1-UBD" FT REGION 294..315 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 426..453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..453 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT VAR_SEQ 362..414 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8885239" FT /id="VSP_023562" FT MUTAGEN 512..513 FT /note="HQ->AA: Loss of function." FT /evidence="ECO:0000269|PubMed:15802566" FT CONFLICT 252 FT /note="R -> G (in Ref. 1; CAA66913)" FT /evidence="ECO:0000305" FT CONFLICT 472 FT /note="G -> R (in Ref. 1; CAA66913)" FT /evidence="ECO:0000305" FT CONFLICT 578 FT /note="E -> K (in Ref. 4; AAI39752)" FT /evidence="ECO:0000305" FT HELIX 348..362 FT /evidence="ECO:0007829|PDB:6CGH" FT TURN 363..365 FT /evidence="ECO:0007829|PDB:6CGH" FT HELIX 370..386 FT /evidence="ECO:0007829|PDB:6CGH" FT HELIX 389..399 FT /evidence="ECO:0007829|PDB:6CGH" FT HELIX 404..431 FT /evidence="ECO:0007829|PDB:6CGH" FT HELIX 556..568 FT /evidence="ECO:0007829|PDB:2M2E" FT HELIX 576..583 FT /evidence="ECO:0007829|PDB:2M2E" FT HELIX 589..618 FT /evidence="ECO:0007829|PDB:2M2E" SQ SEQUENCE 621 AA; 71996 MW; E4DAEE7A73D0F64C CRC64; MLLLPSAADG RGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF QELEDKKELS EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKAMVLKHHP DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE VFTPVFERNS RWSNKKNVPK LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC RDERRWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT SCTKEVGKAA LEKQIEEINE QIRKEKEEAE ARMRQASKNT EKSTGGGGNG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP SERFEGPYTD FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV EMVKAKKAAQ EQVLNASRAK K //