Reviewed, UniProtKB/Swiss-Prot Q04759 (KPCT_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein kinase C theta type
    EC=2.7.11.13
Alternative name(s):
    nPKC-theta

Gene names

Name:	PRKCQ
Synonyms:	PRKCT

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	706 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. Essential for T-cell receptor (TCR)-mediated T-cell activation, but is dispensable during TCR-dependent thymocyte development. Links the TCR signaling complex to the activation of NF-kappa-B in mature T lymphocytes. Required for interleukin-2 (IL2) production. Ref.8 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. Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Three specific sites; Thr-538 (activation loop of the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic region), need to be phosphorylated for its full activation.
Subunit structure	Interacts with TXNL2/PICOT. Ref.7
Tissue specificity	Skeletal muscle, megakaryoblastic cells and platelets. Ref.1
Domain	The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
Post-translational modification	Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PKC upon antigen receptor ligation.
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
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	intracellular signaling cascade Ref.1 Non-traceable author statement. Source: UniProtKB membrane protein ectodomain proteolysis Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Non-traceable author statement. Source: UniProtKB regulation of cell growth Ref.3 Non-traceable author statement. Source: UniProtKB
Cellular component	intracellular Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Non-traceable author statement. Source: UniProtKB diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.7 Inferred from physical interaction. Source: IntAct protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BTK	Q06187	2	EBI-374762,EBI-624835
FYN	P06241	6	EBI-374762,EBI-515315
GLRX3	O76003	2	EBI-374762,EBI-374781
PRKCZ	Q05513	2	EBI-374762,EBI-295351

Alternative products

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

Isoform 1 (identifier: Q04759-1)

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 2 (identifier: Q04759-2)

The sequence of this isoform differs from the canonical sequence as follows:
     550-612: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 706

706

Protein kinase C theta type

PRO_0000055708

Regions

Domain

8 – 123

116

C2

Domain

380 – 634

255

Protein kinase

Domain

635 – 706

72

AGC-kinase C-terminal

Zinc finger

159 – 209

51

Phorbol-ester/DAG-type 1

Zinc finger

231 – 281

51

Phorbol-ester/DAG-type 2

Nucleotide binding

386 – 394

9

ATP By similarity

Sites

Active site

504

1

Proton acceptor By similarity

Binding site

409

1

ATP

Amino acid modifications

Modified residue

219

1

Phosphothreonine; by autocatalysis Ref.8

Modified residue

348

1

Phosphoserine Ref.10

Modified residue

538

1

Phosphothreonine Ref.8 Ref.9

Modified residue

676

1

Phosphoserine Ref.8 Ref.10

Modified residue

685

1

Phosphoserine Ref.10 Ref.9

Modified residue

695

1

Phosphoserine Ref.8 Ref.10 Ref.9

Natural variations

Alternative sequence

550 – 612

63

Missing in isoform 2.

VSP_017294

Natural variant

240

1

K → N in a colorectal adenocarcinoma sample; somatic mutation. Ref.12

VAR_042319

Natural variant

306

1

D → V Ref.12

VAR_042320

Natural variant

330

1

P → L: dbSNP rs2236379. Ref.1 Ref.12 Ref.4

VAR_020401

Natural variant

354

1

D → N Ref.12

VAR_042321

Experimental info

Mutagenesis

219

1

T → A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity. Ref.8

Mutagenesis

409

1

K → A: Loss of kinase activity.

Mutagenesis

538

1

T → A: Loss of kinase activity. Ref.8

Mutagenesis

676

1

S → A: Reduction in kinase activity. Ref.8

Mutagenesis

695

1

S → A: Reduction in kinase activity. Ref.8

Sequence conflict

700

1

G → R Ref.1

Sequence conflict

700

1

G → R Ref.4

Secondary structure

1

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706

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Beta strand

28 – 39

12

Beta strand

42 – 52

11

Beta strand

56 – 62

7

Beta strand

69 – 75

7

Beta strand

83 – 89

7

Helix

90 – 98

9

Turn

99 – 101

3

Beta strand

103 – 108

6

Beta strand

110 – 112

3

Beta strand

114 – 121

8

Beta strand

155 – 159

5

Beta strand

161 – 165

5

Beta strand

174 – 176

3

Beta strand

187 – 189

3

Beta strand

191 – 193

3

Beta strand

196 – 199

4

Helix

200 – 202

3

Beta strand

234 – 236

3

Beta strand

246 – 248

3

Beta strand

255 – 257

3

Beta strand

259 – 265

7

Turn

271 – 276

6

Turn

281 – 283

3

Beta strand

380 – 388

9

Beta strand

390 – 399

10

Turn

400 – 402

3

Beta strand

405 – 412

8

Helix

413 – 418

6

Helix

422 – 435

14

Beta strand

444 – 449

6

Beta strand

451 – 459

9

Helix

466 – 473

8

Helix

478 – 497

20

Helix

507 – 509

3

Beta strand

510 – 512

3

Beta strand

518 – 520

3

Helix

543 – 545

3

Helix

548 – 551

4

Helix

559 – 574

16

Helix

584 – 593

10

Helix

604 – 613

10

Helix

618 – 620

3

Helix

628 – 630

3

Helix

632 – 634

3

Helix

639 – 643

5

Turn

690 – 693

4

Helix

701 – 706

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 27, 2002. Version 3. Checksum: B3C53AB892D5210A	FASTA	706	81,865
	10 20 30 40 50 60 MSPFLRIGLS NFDCGSCQSC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF 70 80 90 100 110 120 DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GKTEIWLELK PQGRMLMNAR 130 140 150 160 170 180 YFLEMSDTKD MNEFETEGFF ALHQRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV 190 200 210 220 230 240 WGLNKQGYQC RQCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK 250 260 270 280 290 300 SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ 310 320 330 340 350 360 ARCLRDTEQI FREGPVEIGL PCSIKNEARP PCLPTPGKRE PQGISWESPL DEVDKMCHLP 370 380 390 400 410 420 EPELNKERPS LQIKLKIEDF ILHKMLGKGS FGKVFLAEFK KTNQFFAIKA LKKDVVLMDD 430 440 450 460 470 480 DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR 490 500 510 520 530 540 ATFYAAEIIL GLQFLHSKGI VYRDLKLDNI LLDKDGHIKI ADFGMCKENM LGDAKTNTFC 550 560 570 580 590 600 GTPDYIAPEI LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR 610 620 630 640 650 660 WLEKEAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP FRPKVKSPFD 670 680 690 700 CSNFDKEFLN EKPRLSFADR ALINSMDQNM FRNFSFMNPG MERLIS
	Isoform 2. Checksum: A3B688EBE8809B9E	FASTA	643	74,287
	10 20 30 40 50 60 MSPFLRIGLS NFDCGSCQSC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF 70 80 90 100 110 120 DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GKTEIWLELK PQGRMLMNAR 130 140 150 160 170 180 YFLEMSDTKD MNEFETEGFF ALHQRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV 190 200 210 220 230 240 WGLNKQGYQC RQCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK 250 260 270 280 290 300 SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ 310 320 330 340 350 360 ARCLRDTEQI FREGPVEIGL PCSIKNEARP PCLPTPGKRE PQGISWESPL DEVDKMCHLP 370 380 390 400 410 420 EPELNKERPS LQIKLKIEDF ILHKMLGKGS FGKVFLAEFK KTNQFFAIKA LKKDVVLMDD 430 440 450 460 470 480 DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR 490 500 510 520 530 540 ATFYAAEIIL GLQFLHSKGI VYRDLKLDNI LLDKDGHIKI ADFGMCKENM LGDAKTNTFC 550 560 570 580 590 600 GTPDYIAPEL FVREPEKRLG VRGDIRQHPL FREINWEELE RKEIDPPFRP KVKSPFDCSN 610 620 630 640 FDKEFLNEKP RLSFADRALI NSMDQNMFRN FSFMNPGMER LIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets." Chang J.D., Xu Y., Raychowdhury M.K., Ware J.A. J. Biol. Chem. 268:14208-14214(1993) [PubMed: 7686153] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT LEU-330.
[2]	Erratum Chang J.D., Xu Y., Raychowdhury M.K., Ware J.A. J. Biol. Chem. 269:31322-31322(1994) [PubMed: 7983077] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells." Baier G., Telford D., Giampa L., Coggeshall K.M., Baier-Bitterlich G., Isakov N., Altman A. J. Biol. Chem. 268:4997-5004(1993) [PubMed: 8444877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Blood.
[4]	Li H., Ke R., Zhou G., Shen C., Zhong G., Lin L., Yang S. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-330.
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [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] (ISOFORM 1). Tissue: Brain.
[7]	"Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain." Witte S., Villalba M., Bi K., Liu Y., Isakov N., Altman A. J. Biol. Chem. 275:1902-1909(2000) [PubMed: 10636891] [Abstract] Cited for: INTERACTION WITH TXNL2/PICOT.
[8]	"Critical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes." Thuille N., Heit I., Fresser F., Krumbock N., Bauer B., Leuthaeusser S., Dammeier S., Graham C., Copeland T.D., Shaw S., Baier G. EMBO J. 24:3869-3880(2005) [PubMed: 16252004] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-219; THR-538; SER-676 AND SER-695, MUTAGENESIS OF THR-219; THR-538; SER-676 AND SER-695.
[9]	"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-538; SER-685 AND SER-695, MASS SPECTROMETRY.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-676; SER-685 AND SER-695, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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] ASN-240; VAL-306; LEU-330 AND ASN-354.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L01087 mRNA. Translation: AAA75571.1.
L07032 mRNA. Translation: AAA60101.1.
AY702977 mRNA. Translation: AAU29340.1.
AL158043 Genomic DNA. Translation: CAC12904.2.
AL137145 Genomic DNA. Translation: CAC10200.2.
BC101465 mRNA. Translation: AAI01466.1.
BC113359 mRNA. Translation: AAI13360.1.

IPI

IPI00029196.
IPI00470691.

PIR

A45416.

RefSeq

NP_006248.1.

UniGene

Hs.498570

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XJD	X-ray	2.00	A	362-706	[»]
2ENJ	NMR	-	A	1-126	[»]
2ENN	NMR	-	A	144-213	[»]
2ENZ	NMR	-	A	227-284	[»]
2JED	X-ray	2.32	A/B	361-706	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q04759. 7 interactions.

PTM databases

PhosphoSite

Q04759.

Proteomic databases

PRIDE

Q04759.

Genome annotation databases

Ensembl

ENSG00000065675. Homo sapiens. [Contig view]

GeneID

5588.

KEGG

hsa:5588.

Organism-specific databases

GeneCards

GC10M006509.

H-InvDB

HIX0025956.

HGNC

HGNC:9410. PRKCQ.

MIM

600448. gene.

PharmGKB

PA33773.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q04759.

HOVERGEN

Q04759.

OMA

Q04759. REPQGIS.

Enzyme and pathway databases

BRENDA

2.7.11.13. 247.

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
endothelinpathway. Endothelins.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_578. Apoptosis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

Q04759.

Bgee

Q04759.

CleanEx

HS_PRKCQ.

GermOnline

ENSG00000065675. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR002219. DAG_PE_bd.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
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.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000551. PKC_delta. 1 hit.

ProDom

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

SMART

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

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. False negative.
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

NextBio

21674.

PMAP-CutDB

Q04759.

SOURCE

Search...

Entry information

Entry name

KPCT_HUMAN

Accession

Primary (citable) accession number: Q04759
Secondary accession number(s): Q14DH6 , Q3MJF1, Q64FY5, Q9H508, Q9H549

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	March 27, 2002
Last modified:	June 16, 2009
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)