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P17535 (JUND_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor jun-D
Gene names
Name:JUND
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor binding AP-1 sites. Ref.6

Subunit structure

Binds DNA as a dimer By similarity. Interacts with MEN1; this interaction represses transcriptional activation. Ref.6

Subcellular location

Nucleus.

Sequence similarities

Belongs to the bZIP family. Jun subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Sequence caution

The sequence CAA40010.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

osteoblast development

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromatin

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondouble-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Transcription factor jun-D
PRO_0000076442

Regions

Domain268 – 33164bZIP
Region268 – 29528Basic motif By similarity
Region296 – 32429Leucine-zipper By similarity
Compositional bias158 – 1669Poly-Ala

Amino acid modifications

Modified residue2511Phosphoserine Ref.7
Modified residue2551Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue2591Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Natural variations

Natural variant201G → V. Ref.2
Corresponds to variant rs41478151 [ dbSNP | Ensembl ].
VAR_055247

Experimental info

Sequence conflict241S → T in CAA40010. Ref.1
Sequence conflict1571A → R in CAA40010. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17535 [UniParc].

Last modified May 5, 2009. Version 3.
Checksum: FE85A1AA2B5B9597

FASTA34735,174
        10         20         30         40         50         60 
METPFYGDEA LSGLGGGASG SGGSFASPGR LFPGAPPTAA AGSMMKKDAL TLSLSEQVAA 

        70         80         90        100        110        120 
ALKPAAAPPP TPLRADGAPS AAPPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS 

       130        140        150        160        170        180 
SQFLYPKVAA SEEQEFAEGF VKALEDLHKQ NQLGAGAAAA AAAAAAGGPS GTATGSAPPG 

       190        200        210        220        230        240 
ELAPAAAAPE APVYANLSSY AGGAGGAGGA ATVAFAAEPV PFPPPPPPGA LGPPRLAALK 

       250        260        270        280        290        300 
DEPQTVPDVP SFGESPPLSP IDMDTQERIK AERKRLRNRI AASKCRKRKL ERISRLEEKV 

       310        320        330        340 
KTLKSQNTEL ASTASLLREQ VAQLKQKVLS HVNSGCQLLP QHQVPAY 

« Hide

References

« Hide 'large scale' references
[1]"Structure and function of human jun-D."
Berger I., Shaul Y.
Oncogene 6:561-566(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIEHS SNPs program
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-20.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Isolation of human cDNA clones of jun-related genes, jun-B and jun-D."
Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.
Nucleic Acids Res. 18:3047-3048(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-347.
[6]"Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription."
Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M., Park S.Y., Saggar S., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L.
Cell 96:143-152(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEN1.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56681 mRNA. Translation: CAA40010.1. Frameshift.
EF044249 Genomic DNA. Translation: ABJ53425.1.
AK223630 mRNA. Translation: BAD97350.1.
CH471106 Genomic DNA. Translation: EAW84684.1.
X51346 mRNA. Translation: CAA35739.1.
PIRA43815.
TVHUJD. S10184.
RefSeqNP_001273897.1. NM_001286968.1.
NP_005345.3. NM_005354.5.
UniGeneHs.2780.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3U86X-ray2.84B27-39[»]
ProteinModelPortalP17535.
SMRP17535. Positions 243-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109930. 27 interactions.
DIPDIP-1053N.
IntActP17535. 8 interactions.
MINTMINT-260192.
STRING9606.ENSP00000252818.

PTM databases

PhosphoSiteP17535.

Polymorphism databases

DMDM229462969.

Proteomic databases

PaxDbP17535.
PRIDEP17535.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252818; ENSP00000252818; ENSG00000130522.
GeneID3727.
KEGGhsa:3727.
UCSCuc002nip.2. human.

Organism-specific databases

CTD3727.
GeneCardsGC19M018391.
H-InvDBHIX0040163.
HGNCHGNC:6206. JUND.
HPACAB005268.
HPA042102.
MIM165162. gene.
neXtProtNX_P17535.
PharmGKBPA30008.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283376.
HOGENOMHOG000006648.
HOVERGENHBG001722.
InParanoidP17535.
KOK04449.
OMAQFLYPKV.
OrthoDBEOG75MVXV.
PhylomeDBP17535.
TreeFamTF323952.

Enzyme and pathway databases

SignaLinkP17535.

Gene expression databases

BgeeP17535.
CleanExHS_JUND.
GenevestigatorP17535.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
IPR008917. TF_DNA-bd.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]
PRINTSPR00043. LEUZIPPRJUN.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSJUND. human.
GeneWikiJunD.
GenomeRNAi3727.
NextBio14591.
PROP17535.
SOURCESearch...

Entry information

Entry nameJUND_HUMAN
AccessionPrimary (citable) accession number: P17535
Secondary accession number(s): Q53EK9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 136 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM