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Q99543

- DNJC2_HUMAN

UniProt

Q99543 - DNJC2_HUMAN

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Protein

DnaJ homolog subfamily C member 2

Gene

DNAJC2

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (2)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

  1. chromatin binding Source: UniProtKB
  2. DNA binding Source: InterPro
  3. histone binding Source: UniProtKB
  4. Hsp70 protein binding Source: UniProtKB
  5. poly(A) RNA binding Source: UniProtKB
  6. ubiquitin binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' cotranslational protein folding Source: UniProtKB
  2. chromatin modification Source: UniProtKB-KW
  3. DNA replication Source: Ensembl
  4. negative regulation of cell growth Source: Ensembl
  5. negative regulation of DNA biosynthetic process Source: Ensembl
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

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:
DnaJ homolog subfamily C member 2, N-terminally processed
Gene namesi
Name:DNAJC2
Synonyms:MPHOSPH11, MPP11, ZRF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:13192. DNAJC2.

Subcellular locationi

Nucleus. Cytoplasm › cytosol

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. nuclear membrane Source: HPA
  4. 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.

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.5 Publications

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.
GenevestigatoriQ99543.

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. Align

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. [Q99543-1]
GeneIDi27000.
KEGGihsa:27000.
UCSCiuc003vbo.3. human. [Q99543-1]
uc010lix.3. human. [Q99543-2]

Polymorphism databases

DMDMi296439472.

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.
CCDSi CCDS43628.1. [Q99543-1 ]
CCDS47679.1. [Q99543-2 ]
RefSeqi NP_001123359.1. NM_001129887.1. [Q99543-2 ]
NP_055192.1. NM_014377.1. [Q99543-1 ]
UniGenei Hs.558476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M2E NMR - A 551-621 [» ]
ProteinModelPortali Q99543.
SMRi Q99543. Positions 87-163, 551-620.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117946. 3 interactions.
DIPi DIP-60462N.
STRINGi 9606.ENSP00000368565.

PTM databases

PhosphoSitei Q99543.

Polymorphism databases

DMDMi 296439472.

Proteomic databases

MaxQBi Q99543.
PaxDbi Q99543.
PRIDEi Q99543.

Protocols and materials databases

DNASUi 27000.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249270 ; ENSP00000249270 ; ENSG00000105821 . [Q99543-2 ]
ENST00000379263 ; ENSP00000368565 ; ENSG00000105821 . [Q99543-1 ]
GeneIDi 27000.
KEGGi hsa:27000.
UCSCi uc003vbo.3. human. [Q99543-1 ]
uc010lix.3. human. [Q99543-2 ]

Organism-specific databases

CTDi 27000.
GeneCardsi GC07M102952.
HGNCi HGNC:13192. DNAJC2.
HPAi HPA020454.
HPA049603.
MIMi 605502. gene.
neXtProti NX_Q99543.
PharmGKBi PA162383835.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5269.
GeneTreei ENSGT00530000063419.
HOGENOMi HOG000006900.
HOVERGENi HBG008782.
InParanoidi Q99543.
KOi K09522.
OMAi LTSCTKE.
OrthoDBi EOG73V6KR.
PhylomeDBi Q99543.
TreeFami TF105834.

Miscellaneous databases

GeneWikii ZRF1.
GenomeRNAii 27000.
NextBioi 49486.
PROi Q99543.
SOURCEi Search...

Gene expression databases

Bgeei Q99543.
CleanExi HS_DNAJC2.
ExpressionAtlasi Q99543. baseline and differential.
Genevestigatori Q99543.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
1.10.287.110. 1 hit.
InterProi IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view ]
Pfami PF00226. DnaJ. 1 hit.
PF00249. Myb_DNA-binding. 2 hits.
[Graphical view ]
SMARTi SM00271. DnaJ. 1 hit.
SM00717. SANT. 2 hits.
[Graphical view ]
SUPFAMi SSF46565. SSF46565. 1 hit.
SSF46689. SSF46689. 2 hits.
PROSITEi PS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view ]
ProtoNeti Search...

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].
+Additional computationally mapped references.

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: January 7, 2015
This is version 135 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.
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