Transcription factor jun-D - Homo sapiens (Human)

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P17535 (JUND_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcription factor jun-D

Gene names

Name:

JUND

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara cellular response to calcium ion Inferred from electronic annotation. Source: Compara circadian rhythm Inferred from electronic annotation. Source: Compara osteoblast development Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc response to light stimulus Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara
Cellular_component	chromatin Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	double-stranded DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ACTR3	P61158	2	EBI-2682803,EBI-351428
FOS	P01100	3	EBI-2682803,EBI-852851
MDM2	Q00987	3	EBI-2682803,EBI-389668

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 347

347

Transcription factor jun-D

PRO_0000076442

Regions

Domain

268 – 331

bZIP

Region

268 – 295

Basic motif By similarity

Region

296 – 324

Leucine-zipper By similarity

Compositional bias

158 – 166

Poly-Ala

Amino acid modifications

Modified residue

251

Phosphoserine Ref.7

Modified residue

255

Phosphoserine Ref.7 Ref.8 Ref.9

Modified residue

259

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10

Natural variations

Natural variant

G → V. Ref.2
Corresponds to variant rs41478151 [ dbSNP | Ensembl ].

VAR_055247

Experimental info

Sequence conflict

S → T in CAA40010. Ref.1

Sequence conflict

157

A → R in CAA40010. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P17535 [UniParc].

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

347

35,174

        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' referencesShow '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. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00289547.

PIR

A43815.
TVHUJD. S10184.

RefSeq

NP_005345.3. NM_005354.4.

UniGene

Hs.2780.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3U86	X-ray	2.84	B	27-39	[»]

ProteinModelPortal

P17535.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1053N.

IntAct

P17535. 6 interactions.

MINT

MINT-260192.

STRING

9606.ENSP00000252818.

PTM databases

PhosphoSite

P17535.

Polymorphism databases

DMDM

229462969.

Proteomic databases

PaxDb

P17535.

PRIDE

P17535.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000252818; ENSP00000252818; ENSG00000130522.

GeneID

3727.

KEGG

hsa:3727.

UCSC

uc002nip.2. human.

Organism-specific databases

CTD

3727.

GeneCards

GC19M018391.

H-InvDB

HIX0040163.

HGNC

HGNC:6206. JUND.

HPA

CAB005268.

MIM

165162. gene.

neXtProt

NX_P17535.

PharmGKB

PA30008.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG283376.

HOGENOM

HOG000006648.

HOVERGEN

HBG001722.

InParanoid

P17535.

K04449.

OMA

QFLYPKV.

OrthoDB

EOG4RFKV3.

PhylomeDB

P17535.

Gene expression databases

Bgee

P17535.

CleanEx

HS_JUND.

Genevestigator

P17535.

GermOnline

ENSG00000130522. Homo sapiens.

Family and domain databases

Gene3D

1.10.880.10. 1 hit.

InterPro

IPR004827. bZIP.
IPR008917. Euk_TF_DNA-bd.
IPR005643. JNK.
IPR002112. Leuzip_Jun.
[Graphical view]

Pfam

PF00170. bZIP_1. 1 hit.
PF03957. Jun. 1 hit.
[Graphical view]

PRINTS

PR00043. LEUZIPPRJUN.

SMART

SM00338. BRLZ. 1 hit.
[Graphical view]

SUPFAM

SSF47454. Euk_transcr_DNA. 1 hit.

PROSITE

PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

JUND. human.

GenomeRNAi

3727.

NextBio

14591.

SOURCE

Search...

Entry information

Entry name

JUND_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents