P09429 (HMGB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
High mobility group protein B1

Alternative name(s):
High mobility group protein 1
Short name=HMG-1

Gene names

Name:	HMGB1
Synonyms:	HMG1

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	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells By similarity.
Subunit structure	Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 By similarity.
Subcellular location	Nucleus. Chromosome.
Sequence similarities	Belongs to the HMGB family. Contains 2 HMG box DNA-binding domains.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Traceable author statement. Source: Reactome DNA topological change Inferred from sequence or structural similarity. Source: UniProtKB V(D)J recombination Inferred from direct assay. Source: UniProtKB base-excision repair, DNA ligation Inferred from direct assay. Source: UniProtKB dendritic cell chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB inflammatory response to antigenic stimulus Inferred from expression pattern. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome myeloid dendritic cell activation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from direct assay. Source: UniProtKB neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of DNA binding Inferred from direct assay. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay. Source: UniProtKB positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB condensed chromosome Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA binding, bending Inferred from mutant phenotype. Source: UniProtKB RAGE receptor binding Inferred from sequence or structural similarity. Source: UniProtKB chemoattractant activity Inferred from sequence or structural similarity. Source: UniProtKB cytokine activity Inferred from sequence or structural similarity. Source: UniProtKB damaged DNA binding Inferred from sequence or structural similarity. Source: UniProtKB double-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB repressing transcription factor binding Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: UniProtKB single-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 215

214

High mobility group protein B1

PRO_0000048526

Regions

DNA binding

9 – 79

71

HMG box 1

DNA binding

95 – 163

69

HMG box 2

Compositional bias

186 – 215

30

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

12

1

N6-acetyllysine Ref.19

Modified residue

30

1

N6-acetyllysine Ref.15 Ref.19

Modified residue

35

1

Phosphoserine Ref.16 Ref.17

Modified residue

100

1

Phosphoserine Ref.17

Cross-link

112

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18

Natural variations

Natural variant

11

1

G → R in gastric-carcinoma cell line. Ref.3

VAR_046451

Natural variant

149

1

A → E in gastric-carcinoma cell line. Ref.3

VAR_046452

Natural variant

156

1

E → Q. Ref.10

VAR_046453

Natural variant

190

1

D → G in gastric-carcinoma cell line. Ref.3

VAR_046454

Experimental info

Sequence conflict

143

1

P → H in AAI41845. Ref.13

Sequence conflict

215

1

E → D in CAG33144. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

215

Helix Strand Turn

Details...

Helix

15 – 30

16

Helix

38 – 51

14

Turn

54 – 56

3

Helix

60 – 70

11

Helix

72 – 77

6

Beta strand

92 – 94

3

Helix

101 – 113

13

Helix

125 – 128

4

Helix

132 – 135

4

Helix

138 – 140

3

Helix

141 – 163

23

Sequences

	Sequence		Length	Mass (Da)
	P09429 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8A868CF277D417B5	FASTA	215	24,894
	10 20 30 40 50 60 MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF 70 80 90 100 110 120 EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL 130 140 150 160 170 180 SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK 190 200 210 SKKKKEEEED EEDEEDEEEE EDEEDEDEEE DDDDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1." Wen L., Huang J.K., Johnson B.H., Reeck G.R. Nucleic Acids Res. 17:1197-1214(1989) [PubMed: 2922262] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The active gene that encodes human high mobility group 1 protein (HMG1) contains introns and maps to chromosome 13." Ferrari S., Finelli P., Rocchi M., Bianchi M.E. Genomics 35:367-371(1996) [PubMed: 8661151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Expression of high-mobility group-1 mRNA in human gastrointestinal adenocarcinoma and corresponding non-cancerous mucosa." Xiang Y.-Y., Wang D.-Y., Tanaka M., Suzuki M., Kiyokawa E., Igarashi H., Niato Y., Shen Q., Sugimura H. Int. J. Cancer 74:1-6(1997) [PubMed: 9036861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-11; GLU-149 AND GLY-190.
[4]	"The genetic variation of the human HMGB1 gene." Kornblit B., Munthe-Fog L., Petersen S., Madsen H., Vindeloev L., Garred P. Tissue Antigens 70:151-156(2007) [PubMed: 17610420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	He F.T., Yang Z.H., Ji Q., Li R., Peng J., Jiang Y., Zhong X. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Small intestine.
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]	SeattleSNPs variation discovery resource Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-156.
[11]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	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].
[13]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Cervix and Testis.
[14]	"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2." Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S. Electrophoresis 18:588-598(1997) [PubMed: 9150946] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-65 AND 113-127. Tissue: Mammary carcinoma.
[15]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"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-35 AND SER-100, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells." Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X. Proteomics 8:2885-2896(2008) [PubMed: 18655026] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-112, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12 AND LYS-30, MASS SPECTROMETRY.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"Solution structure of the tandem HMG box domain from human high mobility group protein B1." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-166.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12597 mRNA. Translation: CAA31110.1.
U51677 Genomic DNA. Translation: AAB08987.1.
D63874 mRNA. Translation: BAA09924.1.
EF157968 Genomic DNA. Translation: ABM47301.1.
AY377859 mRNA. Translation: AAQ91389.1.
AK291494 mRNA. Translation: BAF84183.1.
AK122825 mRNA. Translation: BAG53745.1.
CR749614 mRNA. Translation: CAH18408.1.
CR456863 mRNA. Translation: CAG33144.1.
BT006940 mRNA. Translation: AAP35586.1.
BT020159 mRNA. Translation: AAV38961.1.
EU012027 Genomic DNA. Translation: ABS29271.1.
AL353648 Genomic DNA. Translation: CAI15600.1.
CH471075 Genomic DNA. Translation: EAX08457.1.
BC003378 mRNA. Translation: AAH03378.1.
BC030981 mRNA. Translation: AAH30981.1.
BC066889 mRNA. Translation: AAH66889.1.
BC067732 mRNA. Translation: AAH67732.1.
BC141844 mRNA. Translation: AAI41845.1.

IPI

IPI00419258.

PIR

S02826.

RefSeq

NP_002119.1. NM_002128.4.

UniGene

Hs.434102.
Hs.593339.
Hs.596078.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YRQ	NMR	-	A	1-166	[»]

ProteinModelPortal

P09429.

SMR

P09429. Positions 5-166.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24195N.

IntAct

P09429. 13 interactions.

MINT

MINT-153055.

STRING

P09429.

PTM databases

PhosphoSite

P09429.

Polymorphism databases

DMDM

123369.

2D gel databases

DOSAC-COBS-2DPAGE

P09429.

Proteomic databases

PeptideAtlas

P09429.

PRIDE

P09429.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339872; ENSP00000343040; ENSG00000189403.
ENST00000341423; ENSP00000345347; ENSG00000189403.
ENST00000399494; ENSP00000382417; ENSG00000189403.
ENST00000405805; ENSP00000384678; ENSG00000189403.

GeneID

3146.

KEGG

hsa:3146.

UCSC

uc001usw.1. human.

Organism-specific databases

CTD

3146.

GeneCards

GC13M031032.

H-InvDB

HIX0011209.
HIX0030745.

HGNC

HGNC:4983. HMGB1.

HPA

CAB005873.
HPA003506.

MIM

163905. gene.

neXtProt

NX_P09429.

PharmGKB

PA188.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09987.

HOVERGEN

HBG009000.

InParanoid

P09429.

OrthoDB

EOG4KWJV1.

PhylomeDB

P09429.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.

Reactome

REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P09429.

Bgee

P09429.

CleanEx

HS_HMGB1.

Genevestigator

P09429.

GermOnline

ENSG00000189403. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR017967. HMG_boxA_CS.
IPR000910. HMG_HMG1/HMG2.
IPR000135. HMG_HMG1/HMG2_subgr.
IPR009071. HMG_superfamily.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.
G3DSA:1.10.30.10. HMG-box. 2 hits.

KO

K10802.

Pfam

PF00505. HMG_box. 2 hits.
[Graphical view]

PRINTS

PR00886. HIGHMOBLTY12.

SMART

SM00398. HMG. 2 hits.
[Graphical view]

SUPFAM

SSF47095. HMG-box. 2 hits.

PROSITE

PS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

12470.

SOURCE

Search...

Entry information

Entry name

HMGB1_HUMAN

Accession

Primary (citable) accession number: P09429
Secondary accession number(s): A5D8W9 , Q14321, Q5T7C3, Q6IBE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 131 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.