Reviewed, UniProtKB/Swiss-Prot P10809 (CH60_HUMAN)

Names and origin

Protein names

Recommended name:
    60 kDa heat shock protein, mitochondrial
Alternative name(s):
    Heat shock protein 60
      Short name=HSP-60
      Short name=Hsp60
    60 kDa chaperonin
    Chaperonin 60
      Short name=CPN60
    Mitochondrial matrix protein P1
    P60 lymphocyte protein
    HuCHA60

Gene names

Name:	HSPD1
Synonyms:	HSP60

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	573 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	Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix.
Subunit structure	Interacts with HBV protein X and HTLV-1 protein p40tax. Ref.9 Ref.19
Subcellular location	Mitochondrion matrix.
Involvement in disease	Defects in HSPD1 are a cause of spastic paraplegia autosomal dominant type 13 (SPG13) [MIM:605280]. Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Ref.24 Defects in HSPD1 are the cause of leukodystrophy hypomyelinating type 4 (HLD4) [MIM:612233]; also called mitochondrial HSP60 chaperonopathy or MitCHAP-60 disease. HLD4 is a severe autosomal recessive hypomyelinating leukodystrophy. Clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurrs within the first 2 decades of life.
Sequence similarities	Belongs to the chaperonin (HSP60) family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Mitochondrion
Disease	Disease mutation Hereditary spastic paraplegia Leukodystrophy Neurodegeneration
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	'de novo' protein folding Inferred from sequence or structural similarity. Source: UniProtKB B cell cytokine production Inferred from direct assay. Source: UniProtKB B cell proliferation Inferred from direct assay. Source: UniProtKB MyD88-dependent toll-like receptor signaling pathway Inferred from direct assay. Source: UniProtKB T cell activation Inferred from direct assay. Source: MGI activation of caspase activity Inferred from direct assay. Source: UniProtKB chaperone-mediated protein complex assembly Inferred from sequence or structural similarity. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW isotype switching to IgG isotypes Inferred from direct assay. Source: UniProtKB negative regulation of apoptosis Inferred from mutant phenotype. Source: UniProtKB positive regulation of T cell activation Inferred from direct assay. Source: UniProtKB positive regulation of T cell mediated immune response to tumor cell Inferred from direct assay. Source: UniProtKB positive regulation of apoptosis Inferred from mutant phenotype. Source: UniProtKB positive regulation of interferon-alpha production Inferred from direct assay. Source: UniProtKB positive regulation of interferon-gamma production Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-10 production Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-12 production Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-6 production Inferred from direct assay. Source: UniProtKB positive regulation of macrophage activation Inferred from direct assay. Source: UniProtKB protein maturation Inferred from sequence or structural similarity. Source: UniProtKB protein refolding Inferred from direct assay. Source: UniProtKB protein stabilization Inferred from mutant phenotype. Source: UniProtKB response to unfolded protein Inferred from direct assay. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB coated pit Inferred from direct assay. Source: UniProtKB coated vesicle Inferred from direct assay. Source: UniProtKB cytosol Inferred from direct assay. Source: UniProtKB early endosome Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB lipopolysaccharide receptor complex Inferred from direct assay. Source: UniProtKB mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Traceable author statement. Source: UniProtKB secretory granule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB DNA replication origin binding Inferred from sequence or structural similarity. Source: UniProtKB cell surface binding Inferred from direct assay. Source: UniProtKB chaperone binding Inferred from physical interaction. Source: UniProtKB lipopolysaccharide binding Inferred from direct assay. Source: UniProtKB p53 binding Inferred from physical interaction. Source: UniProtKB single-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB unfolded protein binding Inferred by curator. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FHIT	P49789	2	EBI-352528,EBI-741760

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Ref.9 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
	Chain	27 – 573	547	60 kDa heat shock protein, mitochondrial		PRO_0000005026
Amino acid modifications
	Modified residue	70	1	Phosphoserine Ref.21 Ref.22
	Modified residue	223	1	Phosphotyrosine By similarity
	Modified residue	227	1	Phosphotyrosine Ref.20
Natural variations
	Natural variant	29	1	D → G in HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature. Ref.25		VAR_054785
	Natural variant	98	1	V → I in SPG13. Ref.24		VAR_026748
Experimental info
	Sequence conflict	67	1	S → G in AAA36022. Ref.2
	Sequence conflict	111	1	D → N in BAG35173. Ref.5
	Sequence conflict	177	1	N → S in BAG35173. Ref.5
	Sequence conflict	202	1	K → KAS in ABB01006. Ref.4
	Sequence conflict	260	1	A → T in BAG35173. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P10809-1 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: E51E1BAD9615899C	FASTA	573	61,055
	10 20 30 40 50 60 MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR 70 80 90 100 110 120 TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA 130 140 150 160 170 180 RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK 190 200 210 220 230 240 EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ 250 260 270 280 290 300 DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV 310 320 330 340 350 360 KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG 370 380 390 400 410 420 KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR 430 440 450 460 470 480 VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA 490 500 510 520 530 540 KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT 550 560 570 TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen." Jindal S., Dudani A.K., Singh B., Harley C.B., Gupta R.S. Mol. Cell. Biol. 9:2279-2283(1989) [PubMed: 2568584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families." Venner T.J., Singh B., Gupta R.S. DNA Cell Biol. 9:545-552(1990) [PubMed: 1980192] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter." Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H., Boerglum A.D., Mogensen J., Kristiansen K., Bolund L., Gregersen N. Hum. Genet. 112:71-77(2003) [PubMed: 12483302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Genetic variation in immune response genes." Tan J., Ong R., Hibberd M.L., Seielstad M. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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: Adrenal gland.
[6]	"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: Lung, Skin and Uterus.
[7]	"Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein)." Waldinger D., Eckerskorn C., Lottspeich F., Cleve H. Biol. Chem. Hoppe-Seyler 369:1185-1189(1988) [PubMed: 2907406] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-573.
[8]	"Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis." Ward L.D., Hong J., Whitehead R.H., Simpson R.J. Electrophoresis 11:883-891(1990) [PubMed: 2079031] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-55. Tissue: Colon carcinoma.
[9]	"Complex formation of human T-cell leukemia virus type I p40tax transactivator with cellular polypeptides." Nagata K., Ide Y., Takagi T., Ohtani K., Aoshima M., Tozawa H., Nakamura M., Sugamura K. J. Virol. 66:1040-1049(1992) [PubMed: 1731090] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-55, INTERACTION WITH HTLV-1 P40TAX.
[10]	"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 27-50. Tissue: Mammary carcinoma.
[11]	"The human myocardial two-dimensional gel protein database: update 1994." Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J. Electrophoresis 15:1459-1465(1994) [PubMed: 7895732] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-46. Tissue: Heart.
[12]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-37. Tissue: Platelet.
[13]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-35. Tissue: Liver.
[14]	Bienvenut W.V. Submitted (OCT-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 61-72, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[15]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 61-72; 206-218; 237-249; 251-290; 430-446 AND 463-469, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 97-121; 251-268 AND 430-446. Tissue: Adipocyte.
[17]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Colon carcinoma.
[18]	"Mitochondrial import of the human chaperonin (HSP60) protein." Singh B., Patel H.V., Ridley R.G., Freeman K.B., Gupta R.S. Biochem. Biophys. Res. Commun. 169:391-396(1990) [PubMed: 1972619] [Abstract] Cited for: MITOCHONDRIAL IMPORT.
[19]	"Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis." Tanaka Y., Kanai F., Kawakami T., Tateishi K., Ijichi H., Kawabe T., Arakawa Y., Kawakami T., Nishimura T., Shirakata Y., Koike K., Omata M. Biochem. Biophys. Res. Commun. 318:461-469(2004) [PubMed: 15120623] [Abstract] Cited for: INTERACTION WITH HBV PROTEIN X.
[20]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227, MASS SPECTROMETRY.
[21]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, MASS SPECTROMETRY. Tissue: Epithelium.
[22]	"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-70, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60." Hansen J.J., Durr A., Cournu-Rebeix I., Georgopoulos C., Ang D., Nielsen M.N., Davoine C.-S., Brice A., Fontaine B., Gregersen N., Bross P. Am. J. Hum. Genet. 70:1328-1332(2002) [PubMed: 11898127] [Abstract] Cited for: VARIANT SPG13 ILE-98.
[25]	"Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy." Magen D., Georgopoulos C., Bross P., Ang D., Segev Y., Goldsher D., Nemirovski A., Shahar E., Ravid S., Luder A., Heno B., Gershoni-Baruch R., Skorecki K., Mandel H. Am. J. Hum. Genet. 83:30-42(2008) [PubMed: 18571143] [Abstract] Cited for: VARIANT HLD4 GLY-29, CHARACTERIZATION OF VARIANT HLD4 GLY-29.
+	Additional computationally mapped references.

Web resources

GeneReviews

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	M22382 mRNA. Translation: AAA60127.1. M34664 mRNA. Translation: AAA36022.1. AJ250915 Genomic DNA. Translation: CAB75426.1. DQ217936 Genomic DNA. Translation: ABB01006.1. AK312240 mRNA. Translation: BAG35173.1. BC002676 mRNA. Translation: AAH02676.1. BC003030 mRNA. Translation: AAH03030.1. BC067082 mRNA. Translation: AAH67082.1. BC073746 mRNA. Translation: AAH73746.1.
IPI	IPI00784154.
PIR	A32800.
RefSeq	NP_002147.2. NP_955472.1.
UniGene	Hs.595053 Hs.632539
3D structure databases
HSSP	HSSP built from PDB template 1GR5 based on UniProtKB P06139.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:58N.
IntAct	P10809. 18 interactions.
PTM databases
PhosphoSite	P10809.
2-D gel databases
SWISS-2DPAGE	P10809.
DOSAC-COBS-2DPAGE	P10809.
HSC-2DPAGE	P10809.
OGP	P10809.
PHCI-2DPAGE	P10809.
PMMA-2DPAGE	P10809.
REPRODUCTION-2DPAGE	IPI00784154. P10809.
Siena-2DPAGE	P10809.
Proteomic databases
PRIDE	P10809.
Genome annotation databases
Ensembl	ENSG00000144381. Homo sapiens. [Contig view]
GeneID	3329.
KEGG	hsa:3329.
Organism-specific databases
GeneCards	GC02M198059.
H-InvDB	HIX0002709. HIX0032624.
HGNC	HGNC:5261. HSPD1.
HPA	CAB002775. HPA001523.
MIM	118190. gene. 605280. phenotype. 612233. phenotype.
Orphanet	100994. Autosomal dominant spastic paraplegia, type 13. 685. Familial spastic paraplegia. 702. Pelizaeus-Merzbacher disease.
PharmGKB	PA29527.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P10809.
OMA	P10809. AKGQKCE.
Gene expression databases
ArrayExpress	P10809.
Bgee	P10809.
CleanEx	HS_HSPD1.
GermOnline	ENSG00000144381. Homo sapiens.
Family and domain databases
InterPro	IPR018370. Chaperonin_Cpn60_CS. IPR001844. Chaprnin_Cpn60. IPR002423. Cpn60/TCP-1. [Graphical view]
PANTHER	PTHR11353. Cpn60/TCP-1. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. [Graphical view]
PRINTS	PR00298. CHAPERONIN60.
TIGRFAMs	TIGR02348. GroEL. 1 hit.
PROSITE	PS00296. CHAPERONINS_CPN60. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	13188.
SOURCE	Search...

Entry information

Entry name

CH60_HUMAN

Accession

Primary (citable) accession number: P10809
Secondary accession number(s): B2R5M6, Q38L19, Q9UCR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)