P62807 (H2B1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B type 1-C/E/F/G/I

Alternative name(s):
Histone H2B.1 A
Histone H2B.a
Short name=H2B/a
Histone H2B.g
Short name=H2B/g
Histone H2B.h
Short name=H2B/h
Histone H2B.k
Short name=H2B/k
Histone H2B.l
Short name=H2B/l

Gene names

Name:	HIST1H2BC
Synonyms:	H2BFL
AND
Name:	HIST1H2BE
Synonyms:	H2BFH
AND
Name:	HIST1H2BF
Synonyms:	H2BFG
AND
Name:	HIST1H2BG
Synonyms:	H2BFA
AND
Name:	HIST1H2BI
Synonyms:	H2BFK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	126 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	Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Ref.7 Ref.9 Ref.10 Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. Ref.7 Ref.9 Ref.10
Subunit structure	The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Subcellular location	Nucleus. Chromosome.
Post-translational modification	Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription By similarity. Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Ref.12 GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes. Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. Ref.19
Sequence similarities	Belongs to the histone H2B family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Antibiotic Antimicrobial
PTM	Acetylation Glycoprotein Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Non-traceable author statement Ref.6Ref.2. Source: UniProtKB
Cellular_component	nucleosome Non-traceable author statement Ref.6Ref.2. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Non-traceable author statement Ref.6Ref.2. 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 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
	Chain	2 – 126	125	Histone H2B type 1-C/E/F/G/I		PRO_0000071826
Amino acid modifications
	Modified residue	2	1	N-acetylproline By similarity
	Modified residue	6	1	N6-acetyllysine; alternate Ref.11 Ref.14
	Modified residue	6	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	12	1	N6-acetyllysine; alternate Ref.11
	Modified residue	12	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	13	1	N6-acetyllysine; alternate Ref.11 Ref.14
	Modified residue	13	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	15	1	Phosphoserine; by STK4/MST1 Ref.12
	Modified residue	16	1	N6-acetyllysine; alternate Ref.11 Ref.14
	Modified residue	16	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	17	1	N6-acetyllysine; alternate Ref.11
	Modified residue	17	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	21	1	N6-acetyllysine; alternate Ref.11 Ref.14
	Modified residue	21	1	N6-crotonyl-L-lysine; alternate
	Modified residue	24	1	N6-acetyllysine; alternate By similarity
	Modified residue	24	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	35	1	N6-acetyllysine; alternate By similarity
	Modified residue	35	1	N6-crotonyl-L-lysine; alternate Ref.19
	Modified residue	37	1	Phosphoserine; by AMPK By similarity
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	47	1	N6-acetyllysine; alternate By similarity
	Modified residue	47	1	N6-methyllysine; alternate Ref.11
	Modified residue	58	1	N6,N6-dimethyllysine Ref.11
	Modified residue	79	1	Phosphoserine By similarity
	Modified residue	86	1	N6-acetyllysine By similarity
	Modified residue	109	1	N6-acetyllysine; alternate By similarity
	Modified residue	109	1	N6-methyllysine; alternate Ref.11
	Modified residue	113	1	Phosphoserine; alternate By similarity
	Modified residue	117	1	N6-acetyllysine By similarity
	Modified residue	121	1	N6-acetyllysine; alternate By similarity
	Glycosylation	113	1	O-linked (GlcNAc...); alternate Ref.18
	Cross-link	35		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.17
	Cross-link	121		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.11 Ref.13 Ref.15 Ref.18
Natural variations
	Natural variant	27	1	G → S. Ref.2 Corresponds to variant rs7766641 [ dbSNP | Ensembl ].		VAR_055887
Experimental info
	Sequence conflict	5	1	A → S in CAB02545. Ref.2
	Sequence conflict	33	1	S → T in CAB02545. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P62807 [UniParc]. Last modified March 2, 2010. Version 4. Checksum: FAE1479F44BE703D	FASTA	126	13,906
	10 20 30 40 50 60 MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM 70 80 90 100 110 120 GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two human H1 histone genes within clusters of core histone genes." Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D. Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BG).
[2]	"Human histone gene organization: nonregular arrangement within a large cluster." Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D. Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF AND HIST1H2BI), VARIANT SER-27.
[3]	"The human and mouse replication-dependent histone genes." Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J. Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG AND HIST1H2BI).
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG AND HIST1H2BI).
[5]	"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]. Tissue: Lung and Ovary.
[6]	"Human spleen histone H2B. Isolation and amino acid sequence." Ohe Y., Hayashi H., Iwai K. J. Biochem. 85:615-624(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-126. Tissue: Spleen.
[7]	"Endotoxin-neutralizing antimicrobial proteins of the human placenta." Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C. J. Immunol. 168:2356-2364(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION.
[8]	"Biochemical and antibacterial analysis of human wound and blister fluid." Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A., Liden S., Joernvall H., Boman H.G. Eur. J. Biochem. 237:86-92(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13.
[9]	"Antimicrobial peptides in the first line defence of human colon mucosa." Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H., Agerberth B. Peptides 24:523-530(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
[10]	"Antimicrobial polypeptides of the human colonic epithelium." Howell S.J., Wilk D., Yadav S.P., Bevins C.L. Peptides 24:1763-1770(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
[11]	"Quantitative proteomic analysis of post-translational modifications of human histones." Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N. Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109, UBIQUITINATION AT LYS-121, MASS SPECTROMETRY.
[12]	"Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase." Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D. Cell 113:507-517(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15.
[13]	"Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation." Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-121.
[14]	"Inhibition of core histones acetylation by carcinogenic nickel(II)." Golebiowski F., Kasprzak K.S. Mol. Cell. Biochem. 279:133-139(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
[15]	"Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II." Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-121.
[16]	"Gene-specific characterization of human histone H2B by electron capture dissociation." Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J. J. Proteome Res. 5:233-239(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[17]	"The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation." Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y. Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-35.
[18]	"GlcNAcylation of histone H2B facilitates its monoubiquitination." Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S., Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F., Kitagawa H., Roeder R.G., Brown M., Kato S. Nature 480:557-560(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-113, UBIQUITINATION AT LYS-121.
[19]	"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification." Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y. Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-24 AND LYS-35.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60750 Genomic DNA. Translation: AAA63189.1. Z80782 Genomic DNA. Translation: CAB02544.1. Z80779 Genomic DNA. Translation: CAB02541.1. Z80780 Genomic DNA. Translation: CAB02542.1. Z80783 Genomic DNA. Translation: CAB02545.1. AF531286 Genomic DNA. Translation: AAN06686.1. AF531288 Genomic DNA. Translation: AAN06688.1. AF531289 Genomic DNA. Translation: AAN06689.1. AF531290 Genomic DNA. Translation: AAN06690.1. AF531292 Genomic DNA. Translation: AAN06692.1. AL031777 Genomic DNA. Translation: CAC03411.1. AL031777 Genomic DNA. Translation: CAC03417.1. AL031777 Genomic DNA. Translation: CAC03420.1. AL353759 Genomic DNA. Translation: CAC04130.1. BC001131 mRNA. No translation available. BC009612 mRNA. No translation available. BC096120 mRNA. Translation: AAH96120.1. BC096122 mRNA. Translation: AAH96122.1. BC096123 mRNA. Translation: AAH96123.1. BC101653 mRNA. Translation: AAI01654.1. BC101655 mRNA. Translation: AAI01656.1. BC101748 mRNA. Translation: AAI01749.1. BC101750 mRNA. Translation: AAI01751.1. BC106899 mRNA. Translation: AAI06900.1.
IPI	IPI00020101.
PIR	HSHUB2. E40335. S65409.
RefSeq	NP_003509.1. NM_003518.3. NP_003513.1. NM_003522.3. NP_003514.2. NM_003523.2. NP_003516.1. NM_003525.2. NP_003517.2. NM_003526.2. NP_066407.1. NM_021063.3.
UniGene	Hs.182137. Hs.534369. Hs.553506. Hs.591797. Hs.591809. Hs.658713. Hs.726509.
3D structure databases
ProteinModelPortal	P62807.
SMR	P62807. Positions 5-126.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62807. 13 interactions.
MINT	MINT-276222.
STRING	9606.ENSP00000321744.
PTM databases
PhosphoSite	P62807.
Proteomic databases
PaxDb	P62807.
PRIDE	P62807.
Protocols and materials databases
DNASU	8339. 8344. 8347.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000244601; ENSP00000244601; ENSG00000187990. ENST00000314332; ENSP00000321744; ENSG00000180596. ENST00000356530; ENSP00000348924; ENSG00000197697. ENST00000359985; ENSP00000353074; ENSG00000197846. ENST00000377733; ENSP00000366962; ENSG00000168242. ENST00000396984; ENSP00000380180; ENSG00000180596.
GeneID	3017. 8339. 8343. 8344. 8346. 8347.
KEGG	hsa:3017. hsa:8339. hsa:8343. hsa:8344. hsa:8346. hsa:8347.
UCSC	uc003ngk.4. human.
Organism-specific databases
CTD	3017. 8339. 8343. 8344. 8346. 8347.
GeneCards	GC06M026115. GC06M026216. GC06P026183. GC06P026199. GC06P026273.
HGNC	HGNC:4757. HIST1H2BC. HGNC:4753. HIST1H2BE. HGNC:4752. HIST1H2BF. HGNC:4746. HIST1H2BG. HGNC:4756. HIST1H2BI.
MIM	602798. gene. 602804. gene. 602805. gene. 602807. gene. 602847. gene.
neXtProt	NX_P62807.
PharmGKB	PA29132.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG289161.
HOGENOM	HOG000231213.
HOVERGEN	HBG007774.
InParanoid	P62807.
KO	K11252.
OMA	NITAQYQ.
OrthoDB	EOG4HHP3Z.
PhylomeDB	P62807.
Enzyme and pathway databases
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_116125. Disease.
Gene expression databases
ArrayExpress	P62807.
Bgee	P62807.
CleanEx	HS_HIST1H2BC. HS_HIST1H2BE. HS_HIST1H2BF. HS_HIST1H2BG. HS_HIST1H2BI.
Genevestigator	P62807.
GermOnline	ENSG00000168242. Homo sapiens. ENSG00000180596. Homo sapiens. ENSG00000187990. Homo sapiens. ENSG00000197697. Homo sapiens. ENSG00000197846. Homo sapiens. ENSG00000197903. Homo sapiens.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view]
PANTHER	PTHR23428. PTHR23428. 1 hit.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00621. HISTONEH2B.
SMART	SM00427. H2B. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00357. HISTONE_H2B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HIST1H2BC. human.
NextBio	11956.
SOURCE	Search...

Entry information

Entry name

H2B1C_HUMAN

Accession

Primary (citable) accession number: P62807
Secondary accession number(s): P02278 , Q3B872, Q4VB69, Q93078, Q93080

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 2, 2010
Last modified:	April 3, 2013
This is version 106 of the entry and version 4 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.