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Protein

DnaJ homolog subfamily C member 2

Gene

DNAJC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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'.3 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • DNA binding Source: InterPro
  • histone binding Source: UniProtKB
  • Hsp70 protein binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_264487. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily C member 2
Alternative name(s):
M-phase phosphoprotein 11
Zuotin-related factor 1
Cleaved into the following chain:
Gene namesi
Name:DNAJC2
Synonyms:MPHOSPH11, MPP11, ZRF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:13192. DNAJC2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • nuclear membrane Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi512 – 5132HQ → AA: Loss of function. 1 Publication

Organism-specific databases

PharmGKBiPA162383835.

Polymorphism and mutation databases

BioMutaiDNAJC2.
DMDMi296439472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621DnaJ homolog subfamily C member 2PRO_0000425752Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 621620DnaJ homolog subfamily C member 2, N-terminally processedPRO_0000071123Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei47 – 471Phosphoserine4 Publications
Modified residuei49 – 491Phosphoserine4 Publications
Modified residuei60 – 601Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated in M (mitotic) phase.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ99543.
PaxDbiQ99543.
PRIDEiQ99543.

PTM databases

PhosphoSiteiQ99543.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Expression is repressed by CEBPA. Strongly overexpressed in leukemic cells.3 Publications

Gene expression databases

BgeeiQ99543.
CleanExiHS_DNAJC2.
ExpressionAtlasiQ99543. baseline and differential.
GenevisibleiQ99543. HS.

Organism-specific databases

HPAiHPA020454.
HPA049603.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi117946. 3 interactions.
DIPiDIP-60462N.
STRINGi9606.ENSP00000368565.

Structurei

Secondary structure

1
621
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi556 – 56813Combined sources
Helixi576 – 5838Combined sources
Helixi589 – 61830Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M2ENMR-A551-621[»]
ProteinModelPortaliQ99543.
SMRiQ99543. Positions 87-163, 551-620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 16174JPROSITE-ProRule annotationAdd
BLAST
Domaini449 – 51163SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini549 – 60456SANT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 319Epitope (recognized by CD8(+) cytotoxic T-lymphocytes)
Regioni160 – 25091ZRF1-UBDAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation
Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5269.
GeneTreeiENSGT00530000063419.
HOGENOMiHOG000006900.
HOVERGENiHBG008782.
InParanoidiQ99543.
KOiK09522.
OMAiLTSCTKE.
OrthoDBiEOG73V6KR.
PhylomeDBiQ99543.
TreeFamiTF105834.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00249. Myb_DNA-binding. 2 hits.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF46689. SSF46689. 2 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99543-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLLLPSAADG RGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF
60 70 80 90 100
QELEDKKELS EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY
110 120 130 140 150
KATQRQIKAA HKAMVLKHHP DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD
160 170 180 190 200
PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE VFTPVFERNS RWSNKKNVPK
210 220 230 240 250
LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC RDERRWIEKQ
260 270 280 290 300
NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE
310 320 330 340 350
AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK
360 370 380 390 400
KERQKLRNSC KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT
410 420 430 440 450
SCTKEVGKAA LEKQIEEINE QIRKEKEEAE ARMRQASKNT EKSTGGGGNG
460 470 480 490 500
SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI ANYMNIHSSS GVKRTAKDVI
510 520 530 540 550
GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP SERFEGPYTD
560 570 580 590 600
FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV
610 620
EMVKAKKAAQ EQVLNASRAK K
Length:621
Mass (Da):71,996
Last modified:May 18, 2010 - v4
Checksum:iE4DAEE7A73D0F64C
GO
Isoform 2 (identifier: Q99543-2) [UniParc]FASTAAdd to basket

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

Show »
Length:568
Mass (Da):65,913
Checksum:i390BA8AC8C0DFCAD
GO

Sequence cautioni

The sequence AAI39752.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA66913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521R → G in CAA66913 (PubMed:8885239).Curated
Sequence conflicti472 – 4721G → R in CAA66913 (PubMed:8885239).Curated
Sequence conflicti578 – 5781E → K in AAI39752 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei362 – 41453Missing in isoform 2. 1 PublicationVSP_023562Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43628.1. [Q99543-1]
CCDS47679.1. [Q99543-2]
RefSeqiNP_001123359.1. NM_001129887.1. [Q99543-2]
NP_055192.1. NM_014377.1. [Q99543-1]
UniGeneiHs.558476.

Genome annotation databases

EnsembliENST00000249270; ENSP00000249270; ENSG00000105821. [Q99543-2]
ENST00000379263; ENSP00000368565; ENSG00000105821.
GeneIDi27000.
KEGGihsa:27000.
UCSCiuc003vbo.3. human. [Q99543-1]
uc010lix.3. human. [Q99543-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43628.1. [Q99543-1]
CCDS47679.1. [Q99543-2]
RefSeqiNP_001123359.1. NM_001129887.1. [Q99543-2]
NP_055192.1. NM_014377.1. [Q99543-1]
UniGeneiHs.558476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M2ENMR-A551-621[»]
ProteinModelPortaliQ99543.
SMRiQ99543. Positions 87-163, 551-620.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117946. 3 interactions.
DIPiDIP-60462N.
STRINGi9606.ENSP00000368565.

PTM databases

PhosphoSiteiQ99543.

Polymorphism and mutation databases

BioMutaiDNAJC2.
DMDMi296439472.

Proteomic databases

MaxQBiQ99543.
PaxDbiQ99543.
PRIDEiQ99543.

Protocols and materials databases

DNASUi27000.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249270; ENSP00000249270; ENSG00000105821. [Q99543-2]
ENST00000379263; ENSP00000368565; ENSG00000105821.
GeneIDi27000.
KEGGihsa:27000.
UCSCiuc003vbo.3. human. [Q99543-1]
uc010lix.3. human. [Q99543-2]

Organism-specific databases

CTDi27000.
GeneCardsiGC07M102952.
HGNCiHGNC:13192. DNAJC2.
HPAiHPA020454.
HPA049603.
MIMi605502. gene.
neXtProtiNX_Q99543.
PharmGKBiPA162383835.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5269.
GeneTreeiENSGT00530000063419.
HOGENOMiHOG000006900.
HOVERGENiHBG008782.
InParanoidiQ99543.
KOiK09522.
OMAiLTSCTKE.
OrthoDBiEOG73V6KR.
PhylomeDBiQ99543.
TreeFamiTF105834.

Enzyme and pathway databases

ReactomeiREACT_264487. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

GeneWikiiZRF1.
GenomeRNAii27000.
NextBioi49486.
PROiQ99543.
SOURCEiSearch...

Gene expression databases

BgeeiQ99543.
CleanExiHS_DNAJC2.
ExpressionAtlasiQ99543. baseline and differential.
GenevisibleiQ99543. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00249. Myb_DNA-binding. 2 hits.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF46689. SSF46689. 2 hits.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDNJC2_HUMAN
AccessioniPrimary (citable) accession number: Q99543
Secondary accession number(s): A4VCI0, Q9BVX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 18, 2010
Last modified: July 22, 2015
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.