Reviewed, UniProtKB/Swiss-Prot P05771 (KPCB_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein kinase C beta type
      Short name=PKC-beta
      Short name=PKC-B
    EC=2.7.11.13

Gene names

Name:	PRKCB
Synonyms:	PKCB, PRKCB1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	671 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	This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.
Subunit structure	Interacts with PDK1 By similarity. Interacts in vitro with PRKCBP1.
Subcellular location	Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.
Post-translational modification	Phosphorylation on Thr-500 of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosphorylated on 'Thr-640' and 'Ser-659', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on PKC activity By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 C2 domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipoprotein transport Traceable author statement. Source: UniProtKB protein amino acid phosphorylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein kinase C activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRL1	Q42384	1	EBI-706216,EBI-1382964	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta-I (identifier: P05771-1)

Also known as: PRKCB1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Beta-II (identifier: P05771-2)

Also known as: PRKCB2;

The sequence of this isoform differs from the canonical sequence as follows:
     622-671: RDKRDTSNFD...YTNPEFVINV → CGRNAENFDR...SEFLKPEVKS

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 671

670

Protein kinase C beta type

PRO_0000055684

Regions

Domain

173 – 260

88

C2

Domain

342 – 600

259

Protein kinase

Domain

601 – 671

71

AGC-kinase C-terminal

Zinc finger

36 – 86

51

Phorbol-ester/DAG-type 1

Zinc finger

101 – 151

51

Phorbol-ester/DAG-type 2

Nucleotide binding

348 – 356

9

ATP By similarity

Sites

Active site

466

1

Proton acceptor By similarity

Metal binding

186

1

Calcium 1; via carbonyl oxygen By similarity

Metal binding

187

1

Calcium 1 By similarity

Metal binding

187

1

Calcium 2 By similarity

Metal binding

193

1

Calcium 2 By similarity

Metal binding

246

1

Calcium 1 By similarity

Metal binding

246

1

Calcium 2 By similarity

Metal binding

247

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

248

1

Calcium 1 By similarity

Metal binding

248

1

Calcium 2 By similarity

Metal binding

248

1

Calcium 3 By similarity

Metal binding

251

1

Calcium 3 By similarity

Metal binding

252

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

254

1

Calcium 1 By similarity

Metal binding

254

1

Calcium 3 By similarity

Binding site

371

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Modified residue

16

1

Phosphoserine; by autocatalysis Potential

Modified residue

17

1

Phosphothreonine; by autocatalysis Potential

Modified residue

195

1

Phosphotyrosine By similarity

Modified residue

314

1

Phosphothreonine; by autocatalysis Potential

Modified residue

324

1

Phosphothreonine; by autocatalysis Potential

Modified residue

500

1

Phosphothreonine Ref.12 Ref.15

Modified residue

504

1

Phosphothreonine Ref.12

Modified residue

635

1

Phosphothreonine; by autocatalysis

Modified residue

642

1

Phosphothreonine Ref.15 Ref.13

Modified residue

661

1

Phosphoserine; by autocatalysis Ref.15

Natural variations

Alternative sequence

622 – 671

50

RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II.

VSP_004738

Natural variant

144

1

V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.16

VAR_042304

Natural variant

496

1

V → M in a glioblastoma multiforme sample; somatic mutation. Ref.16

VAR_042305

Natural variant

588

1

P → H Ref.16

VAR_042306

Experimental info

Sequence conflict

69

1

V → G Ref.5

Secondary structure

1

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671

Helix Strand Turn

Details...

Beta strand

342 – 351

10

Beta strand

354 – 361

8

Beta strand

364 – 374

11

Helix

375 – 380

6

Helix

384 – 394

11

Beta strand

406 – 411

6

Beta strand

413 – 421

9

Helix

428 – 435

8

Helix

440 – 459

20

Helix

469 – 471

3

Beta strand

472 – 474

3

Beta strand

480 – 482

3

Helix

505 – 507

3

Helix

510 – 513

4

Helix

521 – 536

16

Helix

546 – 555

10

Helix

566 – 575

10

Helix

590 – 595

6

Helix

598 – 600

3

Helix

605 – 609

5

Helix

629 – 636

8

Helix

646 – 651

6

Turn

654 – 657

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-I (PRKCB1) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 3937E7B667108C68	FASTA	671	76,869
	10 20 30 40 50 60 MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF 70 80 90 100 110 120 GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS 130 140 150 160 170 180 LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR DVLIVLVRDA 190 200 210 220 230 240 KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL 250 260 270 280 290 300 SVEIWDWDLT SRNDFMGSLS FGISELQKAS VDGWFKLLSQ EEGEYFNVPV PPEGSEANEE 310 320 330 340 350 360 LRQKFERAKI SQGTKVPEEK TTNTVSKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE 370 380 390 400 410 420 RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM 430 440 450 460 470 480 EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI 490 500 510 520 530 540 KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP 550 560 570 580 590 600 FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF 610 620 630 640 650 660 RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF 670 SYTNPEFVIN V
	Isoform Beta-II (PRKCB2). Checksum: 03D42B0E4164B48F	FASTA	673	77,012
	10 20 30 40 50 60 MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF 70 80 90 100 110 120 GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS 130 140 150 160 170 180 LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR DVLIVLVRDA 190 200 210 220 230 240 KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL 250 260 270 280 290 300 SVEIWDWDLT SRNDFMGSLS FGISELQKAS VDGWFKLLSQ EEGEYFNVPV PPEGSEANEE 310 320 330 340 350 360 LRQKFERAKI SQGTKVPEEK TTNTVSKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE 370 380 390 400 410 420 RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM 430 440 450 460 470 480 EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI 490 500 510 520 530 540 KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP 550 560 570 580 590 600 FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF 610 620 630 640 650 660 RYIDWEKLER KEIQPPYKPK ACGRNAENFD RFFTRHPPVL TPPDQEVIRN IDQSEFEGFS 670 FVNSEFLKPE VKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways." Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A. Science 233:859-866(1986) [PubMed: 3755548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
[2]	"Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences." Kubo K., Ohno S., Suzuki K. FEBS Lett. 223:138-142(1987) [PubMed: 3666134] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
[3]	"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q." Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D. Genomics 60:295-308(1999) [PubMed: 10493829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Hippocampus.
[5]	"Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells." Mahajna J., King P., Parker P., Haley J. DNA Cell Biol. 14:213-222(1995) [PubMed: 7880442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
[6]	"Positive and negative regulation of the transcription of the human protein kinase C beta gene." Niino Y.S., Ohno S., Suzuki K. J. Biol. Chem. 267:6158-6163(1992) [PubMed: 1556124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
[7]	"Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters." Obeid L.M., Blobe G.C., Karolak L.A., Hannun Y.A. J. Biol. Chem. 267:20804-20810(1992) [PubMed: 1400396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
[8]	"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 2-19, ACETYLATION AT ALA-2. Tissue: Platelet.
[9]	"The genomic structure of the human protein kinase C beta gene (PRKCB)." Greenham J.A., Adams M.D., Doggett N.A., Mole S.E. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-176.
[10]	"Alternative splicing increases the diversity of the human protein kinase C family." Coussens L., Rhee L., Parker P.J., Ullrich A. DNA 6:389-394(1987) [PubMed: 3677994] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-671. Tissue: Fetal brain.
[11]	"Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta-I/beta-II." Kubo K., Ohno S., Suzuki K. Nucleic Acids Res. 15:7179-7180(1987) [PubMed: 3658678] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-671.
[12]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-500 AND THR-504, MASS SPECTROMETRY.
[13]	"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-642, MASS SPECTROMETRY. Tissue: Platelet.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor." Grodsky N., Li Y., Bouzida D., Love R., Jensen J., Nodes B., Nonomiya J., Grant S. Biochemistry 45:13970-13981(2006) [PubMed: 17115692] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 321-660 IN COMPLEX WITH INHIBITOR, PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
[16]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-144; MET-496 AND HIS-588.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M13975 mRNA. Translation: AAA60095.1.
X06318 mRNA. Translation: CAA29634.1.
X07109 mRNA. Translation: CAA30130.1.
AC130454 Genomic DNA. No translation available.
AC002299 Genomic DNA. Translation: AAB97933.1.
AC002299 Genomic DNA. Translation: AAB97934.1.
BC036472 mRNA. Translation: AAH36472.1.
X62532 Genomic DNA. Translation: CAA44393.1.
S47311 Genomic DNA. Translation: AAD13852.1.
D10022 Genomic DNA. Translation: BAA00912.1.
AJ002799, AJ002800 Genomic DNA. Translation: CAA05725.1.
M18254 Genomic DNA. Translation: AAA60096.1.
M18255 Genomic DNA. Translation: AAA60097.1.
X05972 Genomic DNA. Translation: CAA29396.1.
X05971 Genomic DNA. Translation: CAA29395.1.

IPI

IPI00010466.
IPI00219628.

PIR

KIHUC2. B24664.
KIHUC1. S00159.

RefSeq

NP_002729.2.
NP_997700.1.

UniGene

Hs.460355

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I0E	X-ray	2.60	A/B	321-661	[»]

SMR

P05771. Positions 94-158, 95-159, 156-287, 157-288, 339-668.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05771. 5 interactions.

PTM databases

PhosphoSite

P05771.

Proteomic databases

PRIDE

P05771.

Genome annotation databases

Ensembl

ENSG00000166501. Homo sapiens. [Contig view]

GeneID

5579.

KEGG

hsa:5579.

UCSC

uc002dmc.1. human.
uc002dmd.1. human.

Organism-specific databases

GeneCards

GC16P023755.

H-InvDB

HIX0012899.

HGNC

HGNC:9395. PRKCB.

HPA

CAB003843.

MIM

176970. gene.

PharmGKB

PA33761.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P05771.

OMA

P05771. SKFDNNG.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
endothelinpathway. Endothelins.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
il2_1pathway. IL2-mediated signaling events.
tcrjnkpathway. JNK signaling in the CD4+ TCR pathway.
tcrraspathway. Ras signaling in the CD4+ TCR pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
txa2pathway. Thromboxane A2 receptor signaling.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P05771.

Bgee

P05771.

GermOnline

ENSG00000166501. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR002219. DAG_PE_bd.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

PANTHER

PTHR22985:SF86. PKC. 1 hit.

Pfam

PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000550. PKC_alpha. 1 hit.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00163. Vitamin E.

NextBio

21632.

PMAP-CutDB

P05771.

SOURCE

Search...

Entry information

Entry name

KPCB_HUMAN

Accession

Primary (citable) accession number: P05771
Secondary accession number(s): O43744 , P05127, Q15138, Q93060, Q9UE49, Q9UE50, Q9UEH8, Q9UJ30, Q9UJ33

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 131 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)