P60709 (ACTB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin, cytoplasmic 1

Alternative name(s):
Beta-actin

Cleaved into the following chain:

1. Actin, cytoplasmic 1, N-terminally processed

Gene names

Name:

ACTB

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	375 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	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subunit structure	Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2. Ref.11 Ref.12 Ref.21
Subcellular location	Cytoplasm › cytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.16
Post-translational modification	ISGylated. Ref.13
Involvement in disease	Defects in ACTB are a cause of dystonia juvenile-onset (DYTJ) [MIM:607371]. DYTJ is a form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYTJ patients manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss. Ref.22
Miscellaneous	In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation Dystonia
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome adherens junction organization Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cell junction assembly Traceable author statement. Source: Reactome cellular component movement Traceable author statement. Source: UniProtKB
Cellular component	MLL5-L complex Inferred from direct assay Ref.23. Source: UniProtKB NuA4 histone acetyltransferase complex Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from direct assay Ref.16. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW Tat protein binding Inferred from physical interaction. Source: BHF-UCL kinesin binding Inferred from physical interaction. Source: UniProtKB nitric-oxide synthase binding Inferred from physical interaction. Source: BHF-UCL structural constituent of cytoskeleton Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CFL2	Q9Y281	2	EBI-353944,EBI-351218
ERBB2	P04626	10	EBI-353944,EBI-641062
HSPA8	P11142	2	EBI-353944,EBI-351896
SMAD3	P84022	3	EBI-353944,EBI-347161

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Actin, cytoplasmic 1		PRO_0000367073
	Initiator methionine	1	1	Removed; alternate Ref.7 Ref.8
	Chain	2 – 375	374	Actin, cytoplasmic 1, N-terminally processed		PRO_0000000771
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in Actin, cytoplasmic 1; alternate By similarity
	Modified residue	2	1	N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed Ref.8
	Modified residue	53	1	Phosphotyrosine Ref.15 Ref.19
	Modified residue	73	1	Tele-methylhistidine By similarity
	Modified residue	91	1	Phosphotyrosine Ref.15 Ref.19
	Modified residue	166	1	Phosphotyrosine Ref.14
	Modified residue	169	1	Phosphotyrosine Ref.19 Ref.20
	Modified residue	198	1	Phosphotyrosine Ref.15 Ref.19 Ref.20
	Modified residue	218	1	Phosphotyrosine Ref.14 Ref.20
	Modified residue	294	1	Phosphotyrosine Ref.14 Ref.15 Ref.20
	Modified residue	318	1	Phosphothreonine Ref.18
Natural variations
	Natural variant	183	1	R → W in DYTJ; modifies cell response to latrunculin A. Ref.22		VAR_030026
	Natural variant	243	1	P → L. Corresponds to variant rs11546899 [ dbSNP | Ensembl ].		VAR_048185
Experimental info
	Sequence conflict	97	1	A → P in AAH16045. Ref.6
	Sequence conflict	116	1	R → L in AAH12854. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P60709 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 6AFD05CA94E360E2	FASTA	375	41,737
	10 20 30 40 50 60 MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 70 80 90 100 110 120 KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 130 140 150 160 170 180 QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 190 200 210 220 230 240 AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY 250 260 270 280 290 300 ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 310 320 330 340 350 360 GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 370 EYDESGPSIV HRKCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evolutionary conservation in the untranslated regions of actin mRNAs: DNA sequence of a human beta-actin cDNA." Ponte P., Ng S.Y., Engel J., Gunning P., Kedes L. Nucleic Acids Res. 12:1687-1696(1984) [PubMed: 6322116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular structure of the human cytoplasmic beta-actin gene: interspecies homology of sequences in the introns." Nakajima-Iijima S., Hamada H., Reddy P., Kakunaga T. Proc. Natl. Acad. Sci. U.S.A. 82:6133-6137(1985) [PubMed: 2994062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Direct proof that the primary site of action of cytochalasin on cell motility processes is actin." Ohmori H., Toyama S., Toyama S. J. Cell Biol. 116:933-941(1992) [PubMed: 1734024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	NIEHS SNPs program Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain, Eye, Kidney, Muscle, Pancreas, Placenta and Skin.
[7]	"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 2-28. Tissue: Platelet.
[8]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-95; 148-177; 184-191; 197-206; 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[9]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 19-62; 85-113; 184-191; 197-206; 216-254; 291-312; 316-326 AND 360-372, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]	"Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions." Hanukoglu I., Tanese N., Fuchs E. J. Mol. Biol. 163:673-678(1983) [PubMed: 6842590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 252-375.
[11]	"Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes." Stueven T., Hartmann E., Goerlich D. EMBO J. 22:5928-5940(2003) [PubMed: 14592989] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; XPO6 AND PFN1, INTERACTION WITH XPO6.
[12]	"Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane." Holaska J.M., Kowalski A.K., Wilson K.L. PLoS Biol. 2:1354-1362(2004) [PubMed: 15328537] [Abstract] Cited for: INTERACTION WITH EMD.
[13]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed: 16139798] [Abstract] Cited for: ISGYLATION.
[14]	"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-166; TYR-218 AND TYR-294, MASS SPECTROMETRY.
[15]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-198 AND TYR-294, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[16]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[17]	"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex." Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S. Genes Dev. 22:2370-2384(2008) [PubMed: 18765789] [Abstract] Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[18]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY. Tissue: Platelet.
[19]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-169 AND TYR-198, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[20]	"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 TYR-169; TYR-198; TYR-218 AND TYR-294, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes." Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., Hung M.C. Cancer Res. 71:4269-4279(2011) [PubMed: 21555369] [Abstract] Cited for: INTERACTION WITH ERBB2.
[22]	"A mutation of beta -actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia." Procaccio V., Salazar G., Ono S., Styers M.L., Gearing M., Davila A., Jimenez R., Juncos J., Gutekunst C.-A., Meroni G., Fontanella B., Sontag E., Sontag J.-M., Faundez V., Wainer B.H. Am. J. Hum. Genet. 78:947-960(2006) [PubMed: 16685646] [Abstract] Cited for: VARIANT DYTJ TRP-183, CHARACTERIZATION OF VARIANT DYTJ TRP-183.
[23]	"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis." Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S. Nature 459:455-459(2009) [PubMed: 19377461] [Abstract] Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00351 mRNA. Translation: CAA25099.1.
M10277 Genomic DNA. Translation: AAA51567.1.
X63432 mRNA. Translation: CAA45026.1.
AY582799 Genomic DNA. Translation: AAS79319.1.
AC006483 Genomic DNA. Translation: AAP22343.1.
BC001301 mRNA. Translation: AAH01301.1.
BC002409 mRNA. Translation: AAH02409.1.
BC004251 mRNA. Translation: AAH04251.1.
BC008633 mRNA. Translation: AAH08633.1.
BC012854 mRNA. Translation: AAH12854.1.
BC013380 mRNA. Translation: AAH13380.1.
BC014861 mRNA. Translation: AAH14861.1.
BC016045 mRNA. Translation: AAH16045.1.
V00478 mRNA. Translation: CAA23745.1.

IPI

IPI00021439.

PIR

ATHUB. A25168.

RefSeq

NP_001092.1. NM_001101.3.

UniGene

Hs.520640.
Hs.708120.
Hs.727576.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BYH	electron microscopy	12.00	A	2-375	[»]
3D2U	X-ray	2.21	C/G	170-178	[»]
3LUE	electron microscopy	-	A/B/C/D/E/F/G/H/I/J	2-375	[»]

ProteinModelPortal

P60709.

SMR

P60709. Positions 2-375.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29686N.

IntAct

P60709. 124 interactions.

MINT

MINT-220312.

STRING

P60709.

PTM databases

PhosphoSite

P60709.

Polymorphism databases

DMDM

46397333.

2D gel databases

SWISS-2DPAGE

P60709.

Aarhus/Ghent-2DPAGE

7316. IEF.

DOSAC-COBS-2DPAGE

P60709.
P60709_OR_P63261.

REPRODUCTION-2DPAGE

P60709.

Siena-2DPAGE

P60709.

UCD-2DPAGE

P60709.

Proteomic databases

PeptideAtlas

P60709.

PRIDE

P60709.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331789; ENSP00000349960; ENSG00000075624.

GeneID

60.

KEGG

hsa:60.

UCSC

uc003sos.2. human.

Organism-specific databases

CTD

60.

GeneCards

GC07M005566.

H-InvDB

HIX0006454.

HGNC

HGNC:132. ACTB.

HPA

CAB002621.

MIM

102630. gene.
607371. phenotype.

neXtProt

NX_P60709.

Orphanet

79107. Developmental malformations - deafness - dystonia.

PharmGKB

PA24457.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18221.

HOVERGEN

HBG003771.

InParanoid

P60709.

OMA

IKNLMER.

OrthoDB

EOG41JZC9.

PhylomeDB

P60709.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P60709.

Bgee

P60709.

CleanEx

HS_ACTB.

Genevestigator

P60709.

GermOnline

ENSG00000075624. Homo sapiens.

Family and domain databases

InterPro

IPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]

KO

K05692.

PANTHER

PTHR11937. Actin_like. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

PRINTS

PR00190. ACTIN.

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

PROSITE

PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

253.

SOURCE

Search...

Entry information

Entry name

ACTB_HUMAN

Accession

Primary (citable) accession number: P60709
Secondary accession number(s): P02570 , P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 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.