Full text data of DNAJC2
DNAJC2
(MPHOSPH11, MPP11, ZRF1)
[Confidence: low (only semi-automatic identification from reviews)]
DnaJ homolog subfamily C member 2 (M-phase phosphoprotein 11; Zuotin-related factor 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DnaJ homolog subfamily C member 2 (M-phase phosphoprotein 11; Zuotin-related factor 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99543
ID DNJC2_HUMAN Reviewed; 621 AA.
AC Q99543; A4VCI0; Q9BVX1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 4.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=DnaJ homolog subfamily C member 2;
DE AltName: Full=M-phase phosphoprotein 11;
DE AltName: Full=Zuotin-related factor 1;
GN Name=DNAJC2; Synonyms=MPHOSPH11, MPP11, ZRF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression
RT 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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 MASS
RP 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
RT project: 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.,
RA Westendorf J.M., 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.,
RA Dohner H., Schmitt M.;
RT "Characterization of several leukemia-associated antigens inducing
RT humoral 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
RT acute myeloid leukemia for the development of specific
RT 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.,
RA Rucknagel P., Stahl J., Rospert S.;
RT "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-
RT associated 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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 SER-49, AND MASS
RP SPECTROMETRY.
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;
RA Al Qudaihi G., Lehe C., Dickinson A., Eltayeb K., Rasheed W.,
RA Chaudhri N., Aljurf M., Dermime S.;
RT "Identification of a novel peptide derived from the M-phase
RT phosphoprotein 11 (MPP11) leukemic antigen recognized by human CD8+
RT cytotoxic T lymphocytes.";
RL Hematol. Oncol. Stem Cell Ther. 3:24-33(2010).
RN [15]
RP FUNCTION AS CHROMATIN REGULATOR, SUBCELLULAR LOCATION,
RP UBIQUITIN-BINDING, 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts both as a chaperone in the cytosol and as a
CC chromatin regulator in the nucleus. When cytosolic, acts as a
CC molecular chaperone: component of the ribosome-associated complex
CC (RAC), a complex involved in folding or maintaining nascent
CC polypeptides in a folding-competent state. In the RAC complex,
CC stimulates the ATPase activity of the ribosome-associated pool of
CC Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide
CC chain. When nuclear, mediates the switching from polycomb-
CC repressed genes to an active state: specifically recruited at
CC histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes
CC the displacement of the polycomb PRC1 complex from chromatin,
CC thereby facilitating transcription activation. Specifically binds
CC DNA sequence 5'-GTCAAGC-3'.
CC -!- SUBUNIT: Interacts (via ZRF1-UBD region) with ID1 (By similarity).
CC Component of ribosome-associated complex (RAC), a heterodimer
CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC chaperone DNAJC2.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol.
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.
CC -!- INDUCTION: Expression is repressed by CEBPA. Strongly
CC overexpressed in leukemic cells.
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
CC by some regulator, thereby preventing its association with
CC H2AK119ub.
CC -!- PTM: Phosphorylated in M (mitotic) phase.
CC -!- MISCELLANEOUS: Constitutes a myeloid leukemia-associated antigen
CC and might be a target for leukemia T-cell therapy.
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- SIMILARITY: Contains 2 SANT domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI39752.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAA66913.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_001123359.1; NM_001129887.1.
DR RefSeq; NP_055192.1; NM_014377.1.
DR UniGene; Hs.558476; -.
DR PDB; 2M2E; NMR; -; A=551-621.
DR PDBsum; 2M2E; -.
DR ProteinModelPortal; Q99543; -.
DR SMR; Q99543; 85-162, 551-620.
DR DIP; DIP-60462N; -.
DR STRING; 9606.ENSP00000368565; -.
DR PhosphoSite; Q99543; -.
DR DMDM; 296439472; -.
DR PaxDb; Q99543; -.
DR PRIDE; Q99543; -.
DR DNASU; 27000; -.
DR Ensembl; ENST00000249270; ENSP00000249270; ENSG00000105821.
DR Ensembl; ENST00000379263; ENSP00000368565; ENSG00000105821.
DR GeneID; 27000; -.
DR KEGG; hsa:27000; -.
DR UCSC; uc003vbo.3; human.
DR CTD; 27000; -.
DR GeneCards; GC07M102952; -.
DR HGNC; HGNC:13192; DNAJC2.
DR HPA; HPA020454; -.
DR MIM; 605502; gene.
DR neXtProt; NX_Q99543; -.
DR PharmGKB; PA162383835; -.
DR eggNOG; COG5269; -.
DR HOGENOM; HOG000006900; -.
DR HOVERGEN; HBG008782; -.
DR InParanoid; Q99543; -.
DR KO; K09522; -.
DR OMA; YMNLHST; -.
DR OrthoDB; EOG73V6KR; -.
DR GeneWiki; ZRF1; -.
DR GenomeRNAi; 27000; -.
DR NextBio; 49486; -.
DR PRO; PR:Q99543; -.
DR ArrayExpress; Q99543; -.
DR Bgee; Q99543; -.
DR CleanEx; HS_DNAJC2; -.
DR Genevestigator; Q99543; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; 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-dependent; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.60; -; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeodomain-like.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 2.
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; Activator; Alternative splicing; Chaperone;
KW Chromatin regulator; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 621 DnaJ homolog subfamily C member 2.
FT /FTId=PRO_0000071123.
FT DOMAIN 88 161 J.
FT DOMAIN 449 511 SANT 1.
FT DOMAIN 549 604 SANT 2.
FT REGION 23 31 Epitope (recognized by CD8(+) cytotoxic
FT T-lymphocytes).
FT REGION 160 250 ZRF1-UBD.
FT MOD_RES 47 47 Phosphoserine.
FT MOD_RES 49 49 Phosphoserine.
FT MOD_RES 60 60 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT VAR_SEQ 362 414 Missing (in isoform 2).
FT /FTId=VSP_023562.
FT MUTAGEN 512 513 HQ->AA: Loss of function.
FT CONFLICT 252 252 R -> G (in Ref. 1; CAA66913).
FT CONFLICT 472 472 G -> R (in Ref. 1; CAA66913).
FT CONFLICT 578 578 E -> K (in Ref. 4; AAI39752).
FT HELIX 556 568
FT HELIX 576 583
FT HELIX 589 618
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
//
ID DNJC2_HUMAN Reviewed; 621 AA.
AC Q99543; A4VCI0; Q9BVX1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 4.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=DnaJ homolog subfamily C member 2;
DE AltName: Full=M-phase phosphoprotein 11;
DE AltName: Full=Zuotin-related factor 1;
GN Name=DNAJC2; Synonyms=MPHOSPH11, MPP11, ZRF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Westendorf J.M.;
RT "Identification of novel M phase phosphoproteins by expression
RT 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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 MASS
RP 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
RT project: 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.,
RA Westendorf J.M., 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.,
RA Dohner H., Schmitt M.;
RT "Characterization of several leukemia-associated antigens inducing
RT humoral 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
RT acute myeloid leukemia for the development of specific
RT 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.,
RA Rucknagel P., Stahl J., Rospert S.;
RT "The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-
RT associated 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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 SER-49, AND MASS
RP SPECTROMETRY.
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;
RA Al Qudaihi G., Lehe C., Dickinson A., Eltayeb K., Rasheed W.,
RA Chaudhri N., Aljurf M., Dermime S.;
RT "Identification of a novel peptide derived from the M-phase
RT phosphoprotein 11 (MPP11) leukemic antigen recognized by human CD8+
RT cytotoxic T lymphocytes.";
RL Hematol. Oncol. Stem Cell Ther. 3:24-33(2010).
RN [15]
RP FUNCTION AS CHROMATIN REGULATOR, SUBCELLULAR LOCATION,
RP UBIQUITIN-BINDING, 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts both as a chaperone in the cytosol and as a
CC chromatin regulator in the nucleus. When cytosolic, acts as a
CC molecular chaperone: component of the ribosome-associated complex
CC (RAC), a complex involved in folding or maintaining nascent
CC polypeptides in a folding-competent state. In the RAC complex,
CC stimulates the ATPase activity of the ribosome-associated pool of
CC Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide
CC chain. When nuclear, mediates the switching from polycomb-
CC repressed genes to an active state: specifically recruited at
CC histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes
CC the displacement of the polycomb PRC1 complex from chromatin,
CC thereby facilitating transcription activation. Specifically binds
CC DNA sequence 5'-GTCAAGC-3'.
CC -!- SUBUNIT: Interacts (via ZRF1-UBD region) with ID1 (By similarity).
CC Component of ribosome-associated complex (RAC), a heterodimer
CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC chaperone DNAJC2.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol.
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.
CC -!- INDUCTION: Expression is repressed by CEBPA. Strongly
CC overexpressed in leukemic cells.
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
CC by some regulator, thereby preventing its association with
CC H2AK119ub.
CC -!- PTM: Phosphorylated in M (mitotic) phase.
CC -!- MISCELLANEOUS: Constitutes a myeloid leukemia-associated antigen
CC and might be a target for leukemia T-cell therapy.
CC -!- SIMILARITY: Contains 1 J domain.
CC -!- SIMILARITY: Contains 2 SANT domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI39752.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAA66913.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_001123359.1; NM_001129887.1.
DR RefSeq; NP_055192.1; NM_014377.1.
DR UniGene; Hs.558476; -.
DR PDB; 2M2E; NMR; -; A=551-621.
DR PDBsum; 2M2E; -.
DR ProteinModelPortal; Q99543; -.
DR SMR; Q99543; 85-162, 551-620.
DR DIP; DIP-60462N; -.
DR STRING; 9606.ENSP00000368565; -.
DR PhosphoSite; Q99543; -.
DR DMDM; 296439472; -.
DR PaxDb; Q99543; -.
DR PRIDE; Q99543; -.
DR DNASU; 27000; -.
DR Ensembl; ENST00000249270; ENSP00000249270; ENSG00000105821.
DR Ensembl; ENST00000379263; ENSP00000368565; ENSG00000105821.
DR GeneID; 27000; -.
DR KEGG; hsa:27000; -.
DR UCSC; uc003vbo.3; human.
DR CTD; 27000; -.
DR GeneCards; GC07M102952; -.
DR HGNC; HGNC:13192; DNAJC2.
DR HPA; HPA020454; -.
DR MIM; 605502; gene.
DR neXtProt; NX_Q99543; -.
DR PharmGKB; PA162383835; -.
DR eggNOG; COG5269; -.
DR HOGENOM; HOG000006900; -.
DR HOVERGEN; HBG008782; -.
DR InParanoid; Q99543; -.
DR KO; K09522; -.
DR OMA; YMNLHST; -.
DR OrthoDB; EOG73V6KR; -.
DR GeneWiki; ZRF1; -.
DR GenomeRNAi; 27000; -.
DR NextBio; 49486; -.
DR PRO; PR:Q99543; -.
DR ArrayExpress; Q99543; -.
DR Bgee; Q99543; -.
DR CleanEx; HS_DNAJC2; -.
DR Genevestigator; Q99543; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; TAS:UniProtKB.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:Ensembl.
DR GO; GO:0030308; P:negative regulation of cell growth; 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-dependent; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.60; -; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeodomain-like.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 2.
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; Activator; Alternative splicing; Chaperone;
KW Chromatin regulator; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 621 DnaJ homolog subfamily C member 2.
FT /FTId=PRO_0000071123.
FT DOMAIN 88 161 J.
FT DOMAIN 449 511 SANT 1.
FT DOMAIN 549 604 SANT 2.
FT REGION 23 31 Epitope (recognized by CD8(+) cytotoxic
FT T-lymphocytes).
FT REGION 160 250 ZRF1-UBD.
FT MOD_RES 47 47 Phosphoserine.
FT MOD_RES 49 49 Phosphoserine.
FT MOD_RES 60 60 Phosphoserine.
FT MOD_RES 63 63 Phosphoserine.
FT VAR_SEQ 362 414 Missing (in isoform 2).
FT /FTId=VSP_023562.
FT MUTAGEN 512 513 HQ->AA: Loss of function.
FT CONFLICT 252 252 R -> G (in Ref. 1; CAA66913).
FT CONFLICT 472 472 G -> R (in Ref. 1; CAA66913).
FT CONFLICT 578 578 E -> K (in Ref. 4; AAI39752).
FT HELIX 556 568
FT HELIX 576 583
FT HELIX 589 618
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
//
MIM
605502
*RECORD*
*FIELD* NO
605502
*FIELD* TI
*605502 DNAJ/HSP40 HOMOLOG, SUBFAMILY C, MEMBER 2; DNAJC2
;;ZUOTIN-RELATED FACTOR 1; ZRF1;;
read moreM-PHASE PHOSPHOPROTEIN 11; MPHOSPH11; MPP11
*FIELD* TX
CLONING
Progression of cells from interphase to mitosis involves alterations in
cell structures and activities. The transition from G2 to M phase is
induced by M phase-promoting factor, or MPF (see CCNB1; 123836). In M
phase, many proteins are phosphorylated directly by MPF or indirectly by
kinases activated by MPF. These M-phase phosphoproteins (MPPs, or
MPHOSPHs) permit disassembly of interphase structures and generation of
M-phase enzymatic activities and structures. By treating bacterial
expression libraries with M-phase cytosol containing the relevant
kinases in the presence of a phosphatase inhibitor, followed by
immunoscreening with MPM2 antibody, Matsumoto-Taniura et al. (1996)
isolated cDNAs for a number of MPHOSPHs, including MPHOSPH11, or ZRF1
(zuotin-related factor-1), which they called MPP11. Zuotin is a nucleic
acid-binding protein and ribosomal chaperone identified in yeast (Yan et
al., 1998). By immunoblot analysis, Matsumoto-Taniura et al. (1996)
showed that when phosphorylated, ZRF1 is expressed as a 130-kD protein
in M-phase cells. Immunofluorescence microscopy localized ZRF1 in
punctate foci throughout the cell, including the nucleus, in both
interphase and mitotic cells.
Otto et al. (2005) cloned human MPP11. The deduced 568-amino acid
protein contains an N-terminal domain, followed by a J domain, a central
charged region, and 2 C-terminal MYB (189990)-like domains.
GENE FUNCTION
Hundley et al. (2005) reported that ribosome-associated molecular
chaperones have been maintained throughout eukaryotic evolution, as
illustrated by MPP11, the human ortholog of the yeast
ribosome-associated J protein Zuo. When expressed in yeast, MPP11
partially substituted for Zuo by partnering with the multipurpose Hsp70
Ssa, the homolog of mammalian Hsc70 (600816). Hundley et al. (2005)
proposed that in metazoans, ribosome-associated MPP11 recruits the
multifunctional soluble Hsc70 to nascent polypeptide chains as they exit
the ribosome.
Otto et al. (2005) found that MPP11 and HSP70L1 (HSPA14; 610369) formed
a complex in HeLa cells, rat liver, and rabbit reticulate lysate. The 2
proteins coeluted on cation and anion exchange columns, and sucrose
density gradients showed that they comigrated with polysomes and
ribosomes. The 200-kD dimeric ribosome-associated complex (RAC) formed
by MPP11 and HSP70L1 was sensitive to salt treatment and could rescue
growth defects in yeast strains lacking functional RAC.
Richly et al. (2010) showed in human cell lines that ZRF1 is
specifically recruited to histone H2A (see 613499) when it is
ubiquitinated at lys119 by means of a novel ubiquitin-interacting domain
that is located in the evolutionarily conserved zuotin domain. At the
onset of differentiation, ZRF1 specifically displaces
polycomb-repressive complex-1 (PRC1; see 603079) from chromatin and
facilitates transcriptional activation. A genomewide mapping of ZRF1,
RING1B (608985), and H2A-ubiquitin targets revealed its involvement in
the regulation of a large set of polycomb target genes, emphasizing the
key role ZRF1 has in cell fate decisions. Richly et al. (2010) provided
a model of the molecular mechanism of switching polycomb-repressed genes
to an active state.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ZRF1
gene to chromosome 7 (TMAP WI-14926).
*FIELD* RF
1. Hundley, H. A.; Walter, W.; Bairstow, S.; Craig, E. A.: Human
Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science 308:
1032-1034, 2005.
2. Matsumoto-Taniura, N.; Pirollet, F.; Monroe, R.; Gerace, L.; Westendorf,
J. M.: Identification of novel M phase phosphoproteins by expression
cloning. Molec. Biol. Cell 7: 1455-1469, 1996.
3. Otto, H.; Conz, C.; Maier, P.; Wolfle, T.; Suzuki, C. K.; Jeno,
P.; Rucknagel, P.; Stahl, J.; Rospert, S.: The chaperones MPP11 and
Hsp70L1 form the mammalian ribosome-associated complex. Proc. Nat.
Acad. Sci. 102: 10064-10069, 2005.
4. Richly, H.; Rocha-Viegas, L.; Ribeiro, J. D.; Demajo, S.; Gundem,
G.; Lopez-Bigas, N.; Nakagawa, T.; Rospert, S.; Ito, T.; Di Croce,
L.: Transcriptional activation of polycomb-repressed genes by ZRF1. Nature 468:
1124-1128, 2010.
5. Yan, W.; Schilke, B.; Pfund, C.; Walter, W.; Kim, S.; Craig, E.
A.: Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO
J. 17: 4809-4817, 1998.
*FIELD* CN
Ada Hamosh - updated: 3/29/2011
Ada Hamosh - updated: 6/2/2005
*FIELD* CD
Paul J. Converse: 12/27/2000
*FIELD* ED
mgross: 01/11/2013
alopez: 3/31/2011
terry: 3/29/2011
mgross: 10/1/2009
mgross: 9/1/2006
alopez: 6/3/2005
terry: 6/2/2005
mgross: 12/27/2000
*RECORD*
*FIELD* NO
605502
*FIELD* TI
*605502 DNAJ/HSP40 HOMOLOG, SUBFAMILY C, MEMBER 2; DNAJC2
;;ZUOTIN-RELATED FACTOR 1; ZRF1;;
read moreM-PHASE PHOSPHOPROTEIN 11; MPHOSPH11; MPP11
*FIELD* TX
CLONING
Progression of cells from interphase to mitosis involves alterations in
cell structures and activities. The transition from G2 to M phase is
induced by M phase-promoting factor, or MPF (see CCNB1; 123836). In M
phase, many proteins are phosphorylated directly by MPF or indirectly by
kinases activated by MPF. These M-phase phosphoproteins (MPPs, or
MPHOSPHs) permit disassembly of interphase structures and generation of
M-phase enzymatic activities and structures. By treating bacterial
expression libraries with M-phase cytosol containing the relevant
kinases in the presence of a phosphatase inhibitor, followed by
immunoscreening with MPM2 antibody, Matsumoto-Taniura et al. (1996)
isolated cDNAs for a number of MPHOSPHs, including MPHOSPH11, or ZRF1
(zuotin-related factor-1), which they called MPP11. Zuotin is a nucleic
acid-binding protein and ribosomal chaperone identified in yeast (Yan et
al., 1998). By immunoblot analysis, Matsumoto-Taniura et al. (1996)
showed that when phosphorylated, ZRF1 is expressed as a 130-kD protein
in M-phase cells. Immunofluorescence microscopy localized ZRF1 in
punctate foci throughout the cell, including the nucleus, in both
interphase and mitotic cells.
Otto et al. (2005) cloned human MPP11. The deduced 568-amino acid
protein contains an N-terminal domain, followed by a J domain, a central
charged region, and 2 C-terminal MYB (189990)-like domains.
GENE FUNCTION
Hundley et al. (2005) reported that ribosome-associated molecular
chaperones have been maintained throughout eukaryotic evolution, as
illustrated by MPP11, the human ortholog of the yeast
ribosome-associated J protein Zuo. When expressed in yeast, MPP11
partially substituted for Zuo by partnering with the multipurpose Hsp70
Ssa, the homolog of mammalian Hsc70 (600816). Hundley et al. (2005)
proposed that in metazoans, ribosome-associated MPP11 recruits the
multifunctional soluble Hsc70 to nascent polypeptide chains as they exit
the ribosome.
Otto et al. (2005) found that MPP11 and HSP70L1 (HSPA14; 610369) formed
a complex in HeLa cells, rat liver, and rabbit reticulate lysate. The 2
proteins coeluted on cation and anion exchange columns, and sucrose
density gradients showed that they comigrated with polysomes and
ribosomes. The 200-kD dimeric ribosome-associated complex (RAC) formed
by MPP11 and HSP70L1 was sensitive to salt treatment and could rescue
growth defects in yeast strains lacking functional RAC.
Richly et al. (2010) showed in human cell lines that ZRF1 is
specifically recruited to histone H2A (see 613499) when it is
ubiquitinated at lys119 by means of a novel ubiquitin-interacting domain
that is located in the evolutionarily conserved zuotin domain. At the
onset of differentiation, ZRF1 specifically displaces
polycomb-repressive complex-1 (PRC1; see 603079) from chromatin and
facilitates transcriptional activation. A genomewide mapping of ZRF1,
RING1B (608985), and H2A-ubiquitin targets revealed its involvement in
the regulation of a large set of polycomb target genes, emphasizing the
key role ZRF1 has in cell fate decisions. Richly et al. (2010) provided
a model of the molecular mechanism of switching polycomb-repressed genes
to an active state.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ZRF1
gene to chromosome 7 (TMAP WI-14926).
*FIELD* RF
1. Hundley, H. A.; Walter, W.; Bairstow, S.; Craig, E. A.: Human
Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science 308:
1032-1034, 2005.
2. Matsumoto-Taniura, N.; Pirollet, F.; Monroe, R.; Gerace, L.; Westendorf,
J. M.: Identification of novel M phase phosphoproteins by expression
cloning. Molec. Biol. Cell 7: 1455-1469, 1996.
3. Otto, H.; Conz, C.; Maier, P.; Wolfle, T.; Suzuki, C. K.; Jeno,
P.; Rucknagel, P.; Stahl, J.; Rospert, S.: The chaperones MPP11 and
Hsp70L1 form the mammalian ribosome-associated complex. Proc. Nat.
Acad. Sci. 102: 10064-10069, 2005.
4. Richly, H.; Rocha-Viegas, L.; Ribeiro, J. D.; Demajo, S.; Gundem,
G.; Lopez-Bigas, N.; Nakagawa, T.; Rospert, S.; Ito, T.; Di Croce,
L.: Transcriptional activation of polycomb-repressed genes by ZRF1. Nature 468:
1124-1128, 2010.
5. Yan, W.; Schilke, B.; Pfund, C.; Walter, W.; Kim, S.; Craig, E.
A.: Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO
J. 17: 4809-4817, 1998.
*FIELD* CN
Ada Hamosh - updated: 3/29/2011
Ada Hamosh - updated: 6/2/2005
*FIELD* CD
Paul J. Converse: 12/27/2000
*FIELD* ED
mgross: 01/11/2013
alopez: 3/31/2011
terry: 3/29/2011
mgross: 10/1/2009
mgross: 9/1/2006
alopez: 6/3/2005
terry: 6/2/2005
mgross: 12/27/2000