DNJC2_HUMAN
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 03-AUG-2022, entry version 193.
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};
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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; 177.
DR DIP; DIP-60462N; -.
DR IntAct; Q99543; 12.
DR MINT; Q99543; -.
DR STRING; 9606.ENSP00000368565; -.
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; Q99543; -.
DR PeptideAtlas; Q99543; -.
DR PRIDE; Q99543; -.
DR ProteomicsDB; 78318; -. [Q99543-1]
DR ProteomicsDB; 78319; -. [Q99543-2]
DR Antibodypedia; 9291; 188 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 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; QNGVDHK; -.
DR OrthoDB; 1392575at2759; -.
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; 91 hits in 1114 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 207 other tissues.
DR ExpressionAtlas; Q99543; baseline and differential.
DR Genevisible; Q99543; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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 transcription, DNA-templated; 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; -; 1.
DR Gene3D; 1.10.8.840; -; 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; PTHR43999; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR Pfam; PF16717; RAC_head; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51293; SANT; 2.
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
