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Q99543 (DNJC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 2
Alternative name(s):
M-phase phosphoprotein 11
Zuotin-related factor 1
Gene names
Name:DNAJC2
Synonyms:MPHOSPH11, MPP11, ZRF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus. When cytosolic, acts as a molecular chaperone: component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide chain. When nuclear, mediates the switching from polycomb-repressed genes to an active state: specifically recruited at histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex from chromatin, thereby facilitating transcription activation. Specifically binds DNA sequence 5'-GTCAAGC-3'. Ref.8 Ref.9 Ref.15

Subunit structure

Interacts (via ZRF1-UBD region) with ID1 By similarity. Component of ribosome-associated complex (RAC), a heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type chaperone DNAJC2. Ref.8

Subcellular location

Nucleus. Cytoplasmcytosol Ref.8 Ref.15.

Tissue specificity

Widely expressed. Ref.5

Induction

Expression is repressed by CEBPA. Strongly overexpressed in leukemic cells. Ref.6 Ref.7 Ref.11

Domain

The ZRF1-UBD region specifically recognizes and binds H2AK119ub. The ZRF1-UBD region is also involved in protein-protein interactions with other proteins, suggesting that it may be masked by some regulator, thereby preventing its association with H2AK119ub. Ref.15

Post-translational modification

Phosphorylated in M (mitotic) phase. Ref.1

Miscellaneous

Constitutes a myeloid leukemia-associated antigen and might be a target for leukemia T-cell therapy.

Sequence similarities

Contains 1 J domain.

Contains 2 SANT domains.

Sequence caution

The sequence AAI39752.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA66913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionActivator
Chaperone
Chromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' cotranslational protein folding

Traceable author statement Ref.8. Source: UniProtKB

DNA replication

Inferred from electronic annotation. Source: Ensembl

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.15. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.8Ref.15. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

Hsp70 protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.15. Source: UniProtKB

histone binding

Inferred from direct assay Ref.15. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99543-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99543-2)

The sequence of this isoform differs from the canonical sequence as follows:
     362-414: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621DnaJ homolog subfamily C member 2
PRO_0000425752
Initiator methionine11Removed; alternate Ref.3
Chain2 – 621620DnaJ homolog subfamily C member 2, N-terminally processed
PRO_0000071123

Regions

Domain88 – 16174J
Domain449 – 51163SANT 1
Domain549 – 60456SANT 2
Region23 – 319Epitope (recognized by CD8(+) cytotoxic T-lymphocytes)
Region160 – 25091ZRF1-UBD

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue471Phosphoserine Ref.10 Ref.13 Ref.16 Ref.18
Modified residue491Phosphoserine Ref.10 Ref.13 Ref.16 Ref.18
Modified residue601Phosphoserine Ref.10
Modified residue631Phosphoserine Ref.10

Natural variations

Alternative sequence362 – 41453Missing in isoform 2.
VSP_023562

Experimental info

Mutagenesis512 – 5132HQ → AA: Loss of function. Ref.9
Sequence conflict2521R → G in CAA66913. Ref.1
Sequence conflict4721G → R in CAA66913. Ref.1
Sequence conflict5781E → K in AAI39752. Ref.4

Secondary structure

....... 621
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: E4DAEE7A73D0F64C

FASTA62171,996
        10         20         30         40         50         60 
MLLLPSAADG RGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF QELEDKKELS 

        70         80         90        100        110        120 
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKAMVLKHHP 

       130        140        150        160        170        180 
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE 

       190        200        210        220        230        240 
VFTPVFERNS RWSNKKNVPK LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC 

       250        260        270        280        290        300 
RDERRWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE 

       310        320        330        340        350        360 
AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC 

       370        380        390        400        410        420 
KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT SCTKEVGKAA LEKQIEEINE 

       430        440        450        460        470        480 
QIRKEKEEAE ARMRQASKNT EKSTGGGGNG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI 

       490        500        510        520        530        540 
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP 

       550        560        570        580        590        600 
SERFEGPYTD FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV 

       610        620 
EMVKAKKAAQ EQVLNASRAK K 

« Hide

Isoform 2 [UniParc].

Checksum: 390BA8AC8C0DFCAD
Show »

FASTA56865,913

References

« Hide 'large scale' references
[1]"Identification of novel M phase phosphoproteins by expression cloning."
Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION.
Tissue: Blood.
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Bienvenut W.V., Glen H., Frame M.C.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-621 (ISOFORM 1).
Tissue: Cervix.
[5]"A putative oncogenic role for MPP11 in head and neck squamous cell cancer."
Resto V.A., Caballero O.L., Buta M.R., Westra W.H., Wu L., Westendorf J.M., Jen J., Hieter P., Sidransky D.
Cancer Res. 60:5529-5535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Characterization of several leukemia-associated antigens inducing humoral immune responses in acute and chronic myeloid leukemia."
Greiner J., Ringhoffer M., Taniguchi M., Hauser T., Schmitt A., Dohner H., Schmitt M.
Int. J. Cancer 106:224-231(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION IN LEUKEMIA.
[7]"mRNA expression of leukemia-associated antigens in patients with acute myeloid leukemia for the development of specific immunotherapies."
Greiner J., Ringhoffer M., Taniguchi M., Li L., Schmitt A., Shiku H., Dohner H., Schmitt M.
Int. J. Cancer 108:704-711(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION IN LEUKEMIA.
[8]"The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex."
Otto H., Conz C., Maier P., Wolfle T., Suzuki C.K., Jeno P., Rucknagel P., Stahl J., Rospert S.
Proc. Natl. Acad. Sci. U.S.A. 102:10064-10069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE RAC COMPLEX, INTERACTION WITH HSPA14.
[9]"Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous."
Hundley H.A., Walter W., Bairstow S., Craig E.A.
Science 308:1032-1034(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 512-HIS-GLN-513.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-60 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"C/EBPalphap30 plays transcriptional regulatory roles distinct from C/EBPalphap42."
Wang C., Chen X., Wang Y., Gong J., Hu G.
Cell Res. 17:374-383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Identification of a novel peptide derived from the M-phase phosphoprotein 11 (MPP11) leukemic antigen recognized by human CD8+ cytotoxic T lymphocytes."
Al Qudaihi G., Lehe C., Dickinson A., Eltayeb K., Rasheed W., Chaudhri N., Aljurf M., Dermime S.
Hematol. Oncol. Stem Cell Ther. 3:24-33(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: EPITOPE REGION.
[15]"Transcriptional activation of polycomb-repressed genes by ZRF1."
Richly H., Rocha-Viegas L., Ribeiro J.D., Demajo S., Gundem G., Lopez-Bigas N., Nakagawa T., Rospert S., Ito T., Di Croce L.
Nature 468:1124-1128(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CHROMATIN REGULATOR, SUBCELLULAR LOCATION, UBIQUITIN-BINDING, DOMAIN ZRF1-UBD.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98260 mRNA. Translation: CAA66913.1. Different initiation.
AC004668 Genomic DNA. No translation available.
BC000859 mRNA. Translation: AAH00859.1.
BC139751 mRNA. Translation: AAI39752.1. Different initiation.
RefSeqNP_001123359.1. NM_001129887.1.
NP_055192.1. NM_014377.1.
UniGeneHs.558476.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M2ENMR-A551-621[»]
ProteinModelPortalQ99543.
SMRQ99543. Positions 86-186, 449-620.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117946. 3 interactions.
DIPDIP-60462N.
STRING9606.ENSP00000368565.

PTM databases

PhosphoSiteQ99543.

Polymorphism databases

DMDM296439472.

Proteomic databases

PaxDbQ99543.
PRIDEQ99543.

Protocols and materials databases

DNASU27000.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249270; ENSP00000249270; ENSG00000105821. [Q99543-2]
ENST00000379263; ENSP00000368565; ENSG00000105821. [Q99543-1]
GeneID27000.
KEGGhsa:27000.
UCSCuc003vbo.3. human. [Q99543-1]
uc010lix.3. human. [Q99543-2]

Organism-specific databases

CTD27000.
GeneCardsGC07M102952.
HGNCHGNC:13192. DNAJC2.
HPAHPA020454.
HPA049603.
MIM605502. gene.
neXtProtNX_Q99543.
PharmGKBPA162383835.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5269.
HOGENOMHOG000006900.
HOVERGENHBG008782.
InParanoidQ99543.
KOK09522.
OMAYMNLHST.
OrthoDBEOG73V6KR.
PhylomeDBQ99543.
TreeFamTF105834.

Gene expression databases

ArrayExpressQ99543.
BgeeQ99543.
CleanExHS_DNAJC2.
GenevestigatorQ99543.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.10.287.110. 1 hit.
InterProIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00249. Myb_DNA-binding. 2 hits.
[Graphical view]
SMARTSM00271. DnaJ. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF46689. SSF46689. 2 hits.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiZRF1.
GenomeRNAi27000.
NextBio49486.
PROQ99543.
SOURCESearch...

Entry information

Entry nameDNJC2_HUMAN
AccessionPrimary (citable) accession number: Q99543
Secondary accession number(s): A4VCI0, Q9BVX1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM