Reviewed, UniProtKB/Swiss-Prot P19525 (E2AK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Interferon-induced, double-stranded RNA-activated protein kinase
    EC=2.7.11.1
Alternative name(s):
    Interferon-inducible RNA-dependent protein kinase
    Eukaryotic translation initiation factor 2-alpha kinase 2
      Short name=eIF-2A protein kinase 2
    Protein kinase RNA-activated
      Short name=PKR
    p68 kinase
    P1/eIF-2A protein kinase

Gene names

Name:	EIF2AK2
Synonyms:	PKR, PRKR

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

General annotation (Comments)

Function	Following activation by double-stranded RNA in the presence of ATP, the kinase becomes autophosphorylated and can catalyze the phosphorylation of the translation initiation factor EIF2S1, which leads to an inhibition of the initiation of protein synthesis. Double-stranded RNA is generated during the course of a viral infection.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activity is markedly stimulated by manganese ions. Besides dsRNA, heparin is a potent activator of the kinase. Binding to dsRNA is required for dimerization leading to autophosphorylation in the activation loop and stimulation of function. Inhibited by vaccinia virus protein E3, probably via dsRNA sequestering.
Subunit structure	Homodimer. Interacts with STRBP By similarity. Interacts with DNAJC3. Inhibited by direct interaction with viral proteins such as HCV E2, HCV NS5A and influenza A NS1. Activated by the interaction with HIV-1 Tat.
Induction	By interferon.
Post-translational modification	Autophosphorylated on several Ser and Thr residues. Autophosphorylation of Thr-451 is dependent on Thr-446 and is stimulated by dsRNA binding and dimerization. Autophosphorylation apparently leads to the activation of the kinase. Ref.15 Ref.16 Ref.18 Ref.21
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. Contains 2 DRBM (double-stranded RNA-binding) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Traceable author statement. Source: ProtInc response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA binding Traceable author statement. Source: ProtInc eukaryotic translation initiation factor 2alpha kinase activity Traceable author statement. Source: ProtInc protein binding Ref.10 Inferred from physical interaction. Source: IntAct protein phosphatase type 2A regulator activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DBNL	Q9UJU6	1	EBI-640775,EBI-751783
DNAJC3	Q27968	3	EBI-640775,EBI-640793	From a different organism.
EIF2S1	P05198	1	EBI-640775,EBI-1056162

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 551

551

Interferon-induced, double-stranded RNA-activated protein kinase

PRO_0000085945

Regions

Domain

9 – 77

69

DRBM 1

Domain

100 – 167

68

DRBM 2

Domain

267 – 538

272

Protein kinase

Repeat

331 – 343

13

1

Repeat

345 – 357

13

2

Nucleotide binding

273 – 281

9

ATP By similarity

Region

331 – 357

27

2 X 13 AA approximate repeats

Sites

Active site

414

1

Proton acceptor By similarity

Binding site

296

1

ATP

Amino acid modifications

Modified residue

83

1

Phosphoserine; by autocatalysis Probable

Modified residue

88

1

Phosphothreonine; by autocatalysis Probable

Modified residue

89

1

Phosphothreonine; by autocatalysis Probable

Modified residue

90

1

Phosphothreonine; by autocatalysis Probable

Modified residue

242

1

Phosphoserine; by autocatalysis Probable

Modified residue

255

1

Phosphothreonine; by autocatalysis Probable

Modified residue

258

1

Phosphothreonine; by autocatalysis Probable

Modified residue

446

1

Phosphothreonine; by autocatalysis Ref.16 Ref.21

Modified residue

451

1

Phosphothreonine; by autocatalysis Ref.16

Modified residue

456

1

Phosphoserine Ref.18

Natural variations

Natural variant

428

1

V → E Ref.22

VAR_040474

Natural variant

439

1

L → V in a lung adenocarcinoma sample; somatic mutation. Ref.22

VAR_040475

Natural variant

506

1

I → V Ref.22

VAR_040476

Experimental info

Mutagenesis

59 – 60

2

SK → AA in FL-PKR-2AI; moderate loss of activity but no effect on dsRNA binding.

Mutagenesis

60

1

K → A: Impairs dsRNA binding but not dimerization or activity.

Mutagenesis

67

1

A → E: Significant loss of activity; loss of dsRNA binding and dimerization.

Mutagenesis

83

1

S → A: No effect on enzymatic activity; when associated with A-88; A-89 and A-90. Ref.15

Mutagenesis

88

1

T → A: No effect on enzymatic activity; when associated with A-83; A-89 and A-90. Ref.15

Mutagenesis

89

1

T → A: No effect on enzymatic activity; when associated with A-83; A-88 and A-90. Ref.15

Mutagenesis

90

1

T → A: No effect on enzymatic activity; when associated with A-83; A-88 and A-89. Ref.15

Mutagenesis

149 – 150

2

TK → AA in FL-PKR-2AII; no effect on activity.

Mutagenesis

242

1

S → A: Moderate loss of activity; when associated with A-255 and A-258. Ref.15

Mutagenesis

244 – 296

53

Missing: Loss of activity. Ref.15

Mutagenesis

255

1

T → A: Moderate loss of activity; when associated with A-242 and A-255. Ref.15

Mutagenesis

258

1

T → A: Moderate loss of activity. Ref.15

Mutagenesis

296

1

K → R: Loss of activity. Ref.15

Mutagenesis

446

1

T → A: Significant loss of activity and impairs autophosphorylation of T-451.

Mutagenesis

451

1

T → A: Loss of activity.

Sequence conflict

512

1

K → E in AAF13156. Ref.6

Secondary structure

1

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551

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Helix

10 – 21

12

Beta strand

26 – 32

7

Turn

35 – 37

3

Beta strand

41 – 50

10

Beta strand

54 – 56

3

Helix

61 – 76

16

Helix

102 – 111

10

Beta strand

115 – 123

9

Beta strand

125 – 138

14

Beta strand

144 – 149

6

Helix

150 – 167

18

Helix

261 – 266

6

Beta strand

267 – 274

8

Beta strand

276 – 278

3

Beta strand

281 – 286

6

Turn

287 – 289

3

Beta strand

292 – 299

8

Helix

303 – 305

3

Helix

306 – 314

9

Beta strand

323 – 332

10

Beta strand

358 – 366

9

Helix

374 – 380

7

Helix

381 – 383

3

Helix

388 – 407

20

Helix

417 – 419

3

Beta strand

420 – 424

5

Beta strand

427 – 430

4

Beta strand

437 – 440

4

Helix

457 – 461

5

Helix

468 – 482

15

Helix

488 – 499

12

Helix

509 – 518

10

Helix

523 – 525

3

Helix

529 – 539

11

Sequences

	Sequence		Length	Mass (Da)
	P19525-1 [UniParc]. Last modified May 1, 1991. Version 2. Checksum: 815AD83ACAB45DA3	FASTA	551	62,094
	10 20 30 40 50 60 MAGDLSAGFF MEELNTYRQK QGVVLKYQEL PNSGPPHDRR FTFQVIIDGR EFPEGEGRSK 70 80 90 100 110 120 KEAKNAAAKL AVEILNKEKK AVSPLLLTTT NSSEGLSMGN YIGLINRIAQ KKRLTVNYEQ 130 140 150 160 170 180 CASGVHGPEG FHYKCKMGQK EYSIGTGSTK QEAKQLAAKL AYLQILSEET SVKSDYLSSG 190 200 210 220 230 240 SFATTCESQS NSLVTSTLAS ESSSEGDFSA DTSEINSNSD SLNSSSLLMN GLRNNQRKAK 250 260 270 280 290 300 RSLAPRFDLP DMKETKYTVD KRFGMDFKEI ELIGSGGFGQ VFKAKHRIDG KTYVIKRVKY 310 320 330 340 350 360 NNEKAEREVK ALAKLDHVNI VHYNGCWDGF DYDPETSDDS LESSDYDPEN SKNSSRSKTK 370 380 390 400 410 420 CLFIQMEFCD KGTLEQWIEK RRGEKLDKVL ALELFEQITK GVDYIHSKKL IHRDLKPSNI 430 440 450 460 470 480 FLVDTKQVKI GDFGLVTSLK NDGKRTRSKG TLRYMSPEQI SSQDYGKEVD LYALGLILAE 490 500 510 520 530 540 LLHVCDTAFE TSKFFTDLRD GIISDIFDKK EKTLLQKLLS KKPEDRPNTS EILRTLTVWK 550 KSPEKNERHT C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon." Meurs E., Chong K., Galabru J., Thomas N.S.B., Kerr I.M., Williams B.R.G., Hovanessian A.G. Cell 62:379-390(1990) [PubMed: 1695551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 101-118 AND 309-325.
[2]	Meurs E. Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Mechanism of interferon action: cDNA structure, expression, and regulation of the interferon-induced, RNA-dependent P1/eIF-2 alpha protein kinase from human cells." Thomis D.C., Doohan J.P., Samuel C.E. Virology 188:33-46(1992) [PubMed: 1373553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Mechanism of interferon action sequence of the human interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones." Kuhen K.L., Shen X., Samuel C.E. Gene 178:191-193(1996) [PubMed: 8921913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[5]	"Structural organization of the human gene (PKR) encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog." Kuhen K.L., Shen X., Carlisle E.R., Richardson A.L., Weier H.-U.G., Tanaka H., Samuel C.E. Genomics 36:197-201(1996) [PubMed: 8812437] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[6]	"Genomic features of human PKR: alternative splicing and a polymorphic CGG repeat in the 5'-untranslated region." Xu Z., Williams B.R. J. Interferon Cytokine Res. 18:609-616(1998) [PubMed: 9726442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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.
[10]	"The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity." Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G. J. Biol. Chem. 271:1702-1707(1996) [PubMed: 8576172] [Abstract] Cited for: INTERACTION WITH DNAJC3.
[11]	"The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR." Brand S.R., Kobayashi R., Mathews M.B. J. Biol. Chem. 272:8388-8395(1997) [PubMed: 9079663] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[12]	"Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein." Gale M.J. Jr., Korth M.J., Tang N.M., Tan S.-L., Hopkins D.A., Dever T.E., Polyak S.J., Gretch D.R., Katze M.G. Virology 230:217-227(1997) [PubMed: 9143277] [Abstract] Cited for: INTERACTION WITH HCV NS5A.
[13]	"Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase." Tan S.L., Katze M.G. J. Interferon Cytokine Res. 18:757-766(1998) [PubMed: 9781815] [Abstract] Cited for: INTERACTION WITH INFLUENZA A NS1 PROTEIN.
[14]	"Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein." Taylor D.R., Shi S.T., Romano P.R., Barber G.N., Lai M.M.C. Science 285:107-110(1999) [PubMed: 10390359] [Abstract] Cited for: INTERACTION WITH HCV E2 ENVELOPE PROTEIN.
[15]	"Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain." Taylor D.R., Tian B., Romano P.R., Hinnebusch A.G., Lai M.M.C., Mathews M.B. J. Virol. 75:1265-1273(2001) [PubMed: 11152499] [Abstract] Cited for: PHOSPHORYLATION AT SER-83; THR-88; THR-89; THR-90; SER-242; THR-255 AND THR-258, MUTAGENESIS OF SER-83; THR-88; THR-89; THR-90; SER-242; THR-255; THR-258 AND LYS-296, INHIBITION BY HCV E2 ENVELOPE PROTEIN.
[16]	"Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop." Zhang F., Romano P.R., Nagamura-Inoue T., Tian B., Dever T.E., Mathews M.B., Ozato K., Hinnebusch A.G. J. Biol. Chem. 276:24946-24958(2001) [PubMed: 11337501] [Abstract] Cited for: MUTAGENESIS, PHOSPHORYLATION AT THR-446 AND THR-451.
[17]	"Inhibition of PKR by vaccinia virus: role of the N- and C-terminal domains of E3L." Langland J.O., Jacobs B.L. Virology 324:419-429(2004) [PubMed: 15207627] [Abstract] Cited for: INHIBITION BY VACCINIA VIRUS PROTEIN E3.
[18]	"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-83 AND SER-456, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation." Nanduri S., Carpick B.W., Yang Y., Williams B.R.G., Qin J. EMBO J. 17:5458-5465(1998) [PubMed: 9736623] [Abstract] Cited for: STRUCTURE BY NMR OF 1-175.
[21]	"Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR." Dar A.C., Dever T.E., Sicheri F. Cell 122:887-900(2005) [PubMed: 16179258] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 258-550 IN COMPLEX WITH EIF2ALPHA, PHOSPHORYLATION AT THR-446.
[22]	"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] GLU-428; VAL-439 AND VAL-506.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M35663 mRNA. Translation: AAA36409.1.
M85294 mRNA. Translation: AAA18253.1.
U50648 , U50634, U50635, U50636, U50637, U50638, U50639, U50640, U50641, U50642, U50643, U50644, U50645, U50646, U50647 Genomic DNA. Translation: AAC50768.1.
AF167472 , AF167460, AF167462, AF167463, AF167464, AF167465, AF167466, AF167468, AF167470 Genomic DNA. Translation: AAF13156.1.
AY228338 Genomic DNA. Translation: AAO38055.1.
AC007899 Genomic DNA. Translation: AAY24317.1.
BC093676 mRNA. Translation: AAH93676.1.
BC101475 mRNA. Translation: AAI01476.1.

IPI

IPI00019463.

PIR

JC5225.

RefSeq

NP_001129123.1.
NP_002750.1.

UniGene

Hs.131431

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QU6	NMR	-	A	1-170	[»]
2A19	X-ray	2.50	B/C	258-550	[»]
2A1A	X-ray	2.80	B	258-550	[»]

SMR

P19525. Positions 257-541.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2657N.

IntAct

P19525. 3 interactions.

PTM databases

PhosphoSite

P19525.

Proteomic databases

PRIDE

P19525.

Genome annotation databases

Ensembl

ENSG00000055332. Homo sapiens. [Contig view]

GeneID

5610.

KEGG

hsa:5610.

NMPDR

fig|9606.3.peg.17745.

Organism-specific databases

GeneCards

GC02M037246.

H-InvDB

HIX0029806.

HGNC

HGNC:9437. EIF2AK2.

HPA

CAB003845.

MIM

176871. gene.

PharmGKB

PA33779.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P19525.

HOVERGEN

P19525.

OMA

P19525. GPEGFHY.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Reactome

REACT_6167. Influenza Infection.

Gene expression databases

ArrayExpress

P19525.

Bgee

P19525.

CleanEx

HS_EIF2AK2.

GermOnline

ENSG00000055332. Homo sapiens.

Family and domain databases

InterPro

IPR001159. Ds-RNA_bd.
IPR014720. dsRNA-bd-like.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
[Graphical view]

Gene3D

G3DSA:3.30.160.20. dsRNA-bd-like. 2 hits.

Pfam

PF00035. dsrm. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

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

SMART

SM00358. DSRM. 2 hits.
[Graphical view]

PROSITE

PS50137. DS_RBD. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

21806.

PMAP-CutDB

P19525.

SOURCE

Search...

Entry information

Entry name

E2AK2_HUMAN

Accession

Primary (citable) accession number: P19525
Secondary accession number(s): Q52M43, Q9UIR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 1, 1991
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)