P17535 (JUND_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor jun-D

Gene names

Name:

JUND

Organism

Homo sapiens (Human)

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 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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein dimerization activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
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	296 – 324	29	Leucine-zipper
	DNA binding	273 – 292	20	Basic motif
	Compositional bias	158 – 166	9	Poly-Ala
Amino acid modifications
	Modified residue	100	1	Phosphoserine Ref.10 Ref.11 Ref.12
	Modified residue	251	1	Phosphoserine Ref.9 Ref.11
	Modified residue	255	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11 Ref.12
	Modified residue	259	1	Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12
Natural variations
	Natural variant	20	1	G → V. Ref.2 Corresponds to variant rs41478151 [ dbSNP | Ensembl ].		VAR_055247
Experimental info
	Sequence conflict	24	1	S → T in CAA40010. Ref.1
	Sequence conflict	157	1	A → R in CAA40010. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17535 [UniParc]. Last modified May 5, 2009. Version 3. Checksum: FE85A1AA2B5B9597	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

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: 1903194] [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. , 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: 2112242] [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: 9989505] [Abstract] Cited for: FUNCTION, INTERACTION WITH MEN1.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-259, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-255 AND SER-259, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-251; SER-255 AND SER-259, MASS SPECTROMETRY.
[12]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-255 AND SER-259, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	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
ProteinModelPortal	P17535.
SMR	P17535. Positions 243-324.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1053N. DIP-24213N.
IntAct	P17535. 6 interactions.
MINT	MINT-260192.
STRING	P17535.
PTM databases
PhosphoSite	P17535.
Polymorphism databases
DMDM	229462969.
Proteomic databases
PRIDE	P17535.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252818; ENSP00000252818; ENSG00000130522.
GeneID	3727.
KEGG	hsa:3727.
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	maNOG18862.
GeneTree	ENSGT00390000009929.
HOGENOM	HBG446073.
HOVERGEN	HBG001722.
InParanoid	P17535.
OMA	QFLYPKV.
OrthoDB	EOG4RFKV3.
PhylomeDB	P17535.
Gene expression databases
ArrayExpress	P17535.
Bgee	P17535.
CleanEx	HS_JUND.
Genevestigator	P17535.
GermOnline	ENSG00000130522. Homo sapiens.
Family and domain databases
InterPro	IPR004827. bZIP. IPR011616. bZIP_1. IPR008917. Euk_TF_DNA-bd. IPR005643. JNK. IPR002112. Leuzip_Jun. [Graphical view]
Gene3D	G3DSA:1.10.880.10. G3DSA:1.10.880.10. 1 hit.
KO	K04449.
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
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:	January 25, 2012
This is version 118 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.