Reviewed, UniProtKB/Swiss-Prot O96017 (CHK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase Chk2
    EC=2.7.11.1
Alternative name(s):
    Cds1

Gene names

Name:	CHEK2
Synonyms:	CHK2, RAD53

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

General annotation (Comments)

Function	Regulates cell cycle checkpoints and apoptosis in response to DNA damage, particularly to DNA double-strand breaks. Inhibits CDC25C phosphatase by phosphorylation on 'Ser-216', preventing the entry into mitosis. May also play a role in meiosis. Regulates the TP53 tumor suppressor through phosphorylation at 'Thr-18' and 'Ser-20'. Ref.2 Ref.3 Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Rapidly phosphorylated on Thr-68 by MLTK in response to DNA damage and to replication block. Kinase activity is also up-regulated by autophosphorylation. Ref.11
Subcellular location	Isoform 2: Nucleus. Note: Isoform 10 is present throughout the cell. Ref.4 Isoform 4: Nucleus. Ref.4 Isoform 7: Nucleus. Ref.4 Isoform 9: Nucleus. Ref.4 Isoform 12: Nucleus. Ref.4
Tissue specificity	High expression is found in testis, spleen, colon and peripheral blood leukocytes. Low expression is found in other tissues.
Involvement in disease	Defects in CHEK2 are associated with Li-Fraumeni syndrome 2 (LFS2) [MIM:609265]; a highly penetrant familial cancer phenotype usually associated with inherited mutations in p53/TP53. Ref.15 Defects in CHEK2 are found in some patients with prostate cancer (CaP) [MIM:176807]. Defects in CHEK2 are found in some patients with osteosarcoma (OSRC) [MIM:259500].
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHK2 subfamily. Contains 1 FHA domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Li-Fraumeni syndrome Proto-oncogene
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA damage checkpoint Ref.2 Ref.13 Traceable author statement. Source: UniProtKB DNA damage response, signal transduction resulting in induction of apoptosis Inferred from direct assay. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	PML body Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AATF	Q9NY61	3	EBI-1180783,EBI-372428
GINS2	Q9Y248	1	EBI-1180783,EBI-747491
PLK1	P53350	3	EBI-1180783,EBI-476768
PPP2R5A	Q15172	1	EBI-1180783,EBI-641666
PPP2R5B	Q15173	1	EBI-1180783,EBI-1369497
PPP2R5C	Q13362-1	3	EBI-1180783,EBI-1266170
PPP2R5C	Q13362-2	1	EBI-1180783,EBI-1266173
PPP2R5C	Q13362-3	3	EBI-1180783,EBI-1266176
PPP2R5E	Q16537	3	EBI-1180783,EBI-968374
Tp53	P02340	1	EBI-1180783,EBI-474016	From a different organism.
VCP	P55072	2	EBI-1180783,EBI-355164

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O96017-1)

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: O96017-2)

Also known as: ins2;

The sequence of this isoform differs from the canonical sequence as follows:
     198-224: VFVFFDLTVDDQSVYPKALRDEYIMSK → EKILKIYSLSRFSKIRRGAVAHVFNPS
     228-234: SGACGEV → GRGWQIT
     235-543: Missing.

Note: Isoform 10 is present throughout the cell. Ref.4 Catalytically inactive.

Isoform 3 (identifier: O96017-3)

Also known as: del2-12;

The sequence of this isoform differs from the canonical sequence as follows:
     107-487: Missing.

Isoform 4 (identifier: O96017-4)

Also known as: del2-3;

The sequence of this isoform differs from the canonical sequence as follows:
     107-197: Missing.

Note: Catalytically active.

Isoform 5 (identifier: O96017-5)

Also known as: del4;

The sequence of this isoform differs from the canonical sequence as follows:
     199-203: FVFFD → VPVER
     204-543: Missing.

Isoform 6 (identifier: O96017-6)

Also known as: sub3;

The sequence of this isoform differs from the canonical sequence as follows:
     150-165: VGPKNSYIAYIEDHSG → ENLSCPYRIWFNFCLF
     166-543: Missing.

Isoform 7 (identifier: O96017-7)

Also known as: del9-12;

The sequence of this isoform differs from the canonical sequence as follows:
     337-339: YLH → MKT
     340-543: Missing.

Note: Catalytically inactive.

Isoform 8 (identifier: O96017-8)

Also known as: del7;

The sequence of this isoform differs from the canonical sequence as follows:
     283-289: PCIIKIK → DGRGRAV
     290-543: Missing.

Isoform 9 (identifier: O96017-9)

Also known as: insx;

The sequence of this isoform differs from the canonical sequence as follows:
     107-107: E → ETESGHVTQSDLELLLSSDPPASASQSAGIRGVRHHPRPVCSLK

Note: Retains low level of catalytic activity.

Isoform 10 (identifier: O96017-10)

Also known as: iso2;

The sequence of this isoform differs from the canonical sequence as follows:
     131-147: KRTDKYRTYSKKHFRIF → EFRSYSFYLP
     148-543: Missing.

Note: Catalytically inactive.

Isoform 11 (identifier: O96017-11)

Also known as: iso1;

The sequence of this isoform differs from the canonical sequence as follows:
     75-392: Missing.

Isoform 12 (identifier: O96017-12)

Also known as: del9;

The sequence of this isoform differs from the canonical sequence as follows:
     337-365: Missing.

Note: Catalytically inactive.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 543

543

Serine/threonine-protein kinase Chk2

PRO_0000085858

Regions

Domain

113 – 175

63

FHA

Domain

220 – 486

267

Protein kinase

Nucleotide binding

226 – 234

9

ATP By similarity

Sites

Active site

347

1

Proton acceptor

Binding site

249

1

ATP By similarity

Amino acid modifications

Modified residue

68

1

Phosphothreonine; by MLTK Ref.11

Natural variations

Alternative sequence

75 – 392

318

Missing in isoform 11.

VSP_014556

Alternative sequence

107 – 487

381

Missing in isoform 3.

VSP_014559

Alternative sequence

107 – 197

91

Missing in isoform 4.

VSP_014558

Alternative sequence

107

1

E → ETESGHVTQSDLELLLSSDP PASASQSAGIRGVRHHPRPV CSLK in isoform 9.

VSP_014557

Alternative sequence

131 – 147

17

KRTDK…HFRIF → EFRSYSFYLP in isoform 10.

VSP_014560

Alternative sequence

148 – 543

396

Missing in isoform 10.

VSP_014561

Alternative sequence

150 – 165

16

VGPKN…EDHSG → ENLSCPYRIWFNFCLF in isoform 6.

VSP_014562

Alternative sequence

166 – 543

378

Missing in isoform 6.

VSP_014563

Alternative sequence

198 – 224

27

VFVFF…YIMSK → EKILKIYSLSRFSKIRRGAV AHVFNPS in isoform 2.

VSP_014564

Alternative sequence

199 – 203

5

FVFFD → VPVER in isoform 5.

VSP_014565

Alternative sequence

204 – 543

340

Missing in isoform 5.

VSP_014566

Alternative sequence

228 – 234

7

SGACGEV → GRGWQIT in isoform 2.

VSP_014567

Alternative sequence

235 – 543

309

Missing in isoform 2.

VSP_014568

Alternative sequence

283 – 289

7

PCIIKIK → DGRGRAV in isoform 8.

VSP_014569

Alternative sequence

290 – 543

254

Missing in isoform 8.

VSP_014570

Alternative sequence

337 – 365

29

Missing in isoform 12.

VSP_014571

Alternative sequence

337 – 339

3

YLH → MKT in isoform 7.

VSP_014572

Alternative sequence

340 – 543

204

Missing in isoform 7.

VSP_014573

Natural variant

17

1

A → S in osteosarcoma; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer. Ref.18

VAR_019101

Natural variant

59

1

T → K in multiple cancers. Ref.16

VAR_026630

Natural variant

64

1

E → K in prostate cancer; somatic mutation. Ref.19

VAR_019107

Natural variant

85

1

P → L in osteosarcoma; is a neutral allele among Ashkenazi Jewish women. dbSNP rs17883862. Ref.18 Ref.8 Ref.27

VAR_019102

Natural variant

117

1

R → G Might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer. Ref.17 Ref.20 Ref.29

VAR_022461

Natural variant

137

1

R → Q Might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer. Ref.17 Ref.29

VAR_022462

Natural variant

145

1

R → P in prostate cancer; somatic mutation. Ref.15 Ref.19 Ref.20 Ref.29 Ref.13 Ref.23

VAR_019108

Natural variant

145

1

R → W in colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer. Ref.15 Ref.19 Ref.20 Ref.29 Ref.13 Ref.23

VAR_008554

Natural variant

157

1

I → T Might influence susceptibility to diffferent types of cancer; does not cause protein abrogation in familial colorectal cancer. dbSNP rs17879961. Ref.19 Ref.8 Ref.20 Ref.29 Ref.13 Ref.23 Ref.14 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.28

VAR_008555

Natural variant

167

1

G → R in prostate cancer; somatic mutation. Ref.19

VAR_019109

Natural variant

180

1

R → C in prostate cancer; somatic mutation. Ref.19 Ref.17 Ref.29

VAR_019103

Natural variant

180

1

R → H in prostate cancer; somatic mutation. Ref.19 Ref.17 Ref.29

VAR_019110

Natural variant

181

1

R → C in prostate cancer; somatic mutation. Ref.19

VAR_019104

Natural variant

181

1

R → H in prostate cancer; somatic mutation. Ref.19

VAR_019105

Natural variant

239

1

E → K in prostate cancer; germline mutation. Ref.19

VAR_019106

Natural variant

251

1

I → F in prostate cancer; germline mutation. Ref.19

VAR_019111

Natural variant

318

1

R → H in prostate cancer; somatic mutation. Ref.19

VAR_019112

Natural variant

323

1

T → P in prostate cancer; somatic mutation. Ref.19

VAR_019113

Natural variant

327

1

Y → C in prostate cancer; somatic mutation. Ref.19

VAR_019114

Natural variant

347

1

D → N: dbSNP rs28909980.

VAR_029154

Natural variant

406

1

R → H: dbSNP rs299671.

VAR_024572

Natural variant

428

1

S → F Increases breast cancer risk approximately 2-fold among Ashkenazi Jewish women. Ref.27

VAR_022463

Natural variant

436

1

L → M: dbSNP rs17882922. Ref.8

VAR_021117

Natural variant

446

1

N → K: dbSNP rs17880867. Ref.8

VAR_021118

Natural variant

447

1

F → I: dbSNP rs17881473. Ref.8

VAR_021119

Natural variant

448

1

I → S: dbSNP rs17886163. Ref.8

VAR_021120

Natural variant

476

1

T → K in prostate cancer; somatic mutation. Ref.19

VAR_019115

Natural variant

500

1

S → C: dbSNP rs28909981.

VAR_029155

Natural variant

501

1

E → K: dbSNP rs17883172. Ref.8

VAR_021121

Natural variant

512

1

L → V: dbSNP rs17882942. Ref.8

VAR_021122

Experimental info

Mutagenesis

68

1

T → A: Loss of activation and phosphorylation. Ref.11

Mutagenesis

347

1

D → A: Loss of kinase activity. Ref.1

Mutagenesis

368

1

D → N: Loss of autophosphorylation activity. Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

543

Helix Strand Turn

Details...

Beta strand

94 – 98

5

Beta strand

106 – 108

3

Beta strand

110 – 118

9

Beta strand

122 – 124

3

Helix

128 – 132

5

Helix

135 – 138

4

Beta strand

144 – 150

7

Beta strand

154 – 162

9

Beta strand

168 – 170

3

Beta strand

180 – 182

3

Beta strand

187 – 193

7

Beta strand

197 – 203

7

Helix

214 – 219

6

Beta strand

220 – 228

9

Beta strand

230 – 239

10

Turn

240 – 243

4

Beta strand

244 – 252

9

Helix

270 – 279

10

Beta strand

288 – 302

15

Helix

309 – 312

4

Helix

321 – 340

20

Helix

350 – 352

3

Beta strand

353 – 361

9

Beta strand

364 – 366

3

Helix

378 – 384

7

Helix

388 – 390

3

Helix

393 – 397

5

Turn

398 – 403

6

Helix

407 – 422

16

Beta strand

429 – 431

3

Helix

436 – 442

7

Helix

449 – 452

4

Helix

457 – 466

10

Turn

471 – 473

3

Helix

477 – 481

5

Helix

484 – 486

3

Helix

489 – 502

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 28890ACF3C1F3408	FASTA	543	60,915
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 170 180 CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR 190 200 210 220 230 240 RPLNNNSEIA LSLSRNKVFV FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER 250 260 270 280 290 300 KTCKKVAIKI ISKRKFAIGS AREADPALNV ETEIEILKKL NHPCIIKIKN FFDAEDYYIV 310 320 330 340 350 360 LELMEGGELF DKVVGNKRLK EATCKLYFYQ MLLAVQYLHE NGIIHRDLKP ENVLLSSQEE 370 380 390 400 410 420 DCLIKITDFG HSKILGETSL MRTLCGTPTY LAPEVLVSVG TAGYNRAVDC WSLGVILFIC 430 440 450 460 470 480 LSGYPPFSEH RTQVSLKDQI TSGKYNFIPE VWAEVSEKAL DLVKKLLVVD PKARFTTEEA 490 500 510 520 530 540 LRHPWLQDED MKRKFQDLLS EENESTALPQ VLAQPSTSRK RPREGEAEGA ETTKRPAVCA AVL
	Isoform 2 (ins2). Checksum: 46766F331DD13DA8	FASTA	234	26,084
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 170 180 CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR 190 200 210 220 230 RPLNNNSEIA LSLSRNKEKI LKIYSLSRFS KIRRGAVAHV FNPSTLGGRG WQIT
	Isoform 3 (del2-12). Checksum: D3BF7E0BC0DB0EC1	FASTA	162	17,370
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLDEDM KRKFQDLLSE 130 140 150 160 ENESTALPQV LAQPSTSRKR PREGEAEGAE TTKRPAVCAA VL
	Isoform 4 (del2-3). Checksum: 96F7C353E4F3C85B	FASTA	452	50,203
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLVFVF FDLTVDDQSV 130 140 150 160 170 180 YPKALRDEYI MSKTLGSGAC GEVKLAFERK TCKKVAIKII SKRKFAIGSA READPALNVE 190 200 210 220 230 240 TEIEILKKLN HPCIIKIKNF FDAEDYYIVL ELMEGGELFD KVVGNKRLKE ATCKLYFYQM 250 260 270 280 290 300 LLAVQYLHEN GIIHRDLKPE NVLLSSQEED CLIKITDFGH SKILGETSLM RTLCGTPTYL 310 320 330 340 350 360 APEVLVSVGT AGYNRAVDCW SLGVILFICL SGYPPFSEHR TQVSLKDQIT SGKYNFIPEV 370 380 390 400 410 420 WAEVSEKALD LVKKLLVVDP KARFTTEEAL RHPWLQDEDM KRKFQDLLSE ENESTALPQV 430 440 450 LAQPSTSRKR PREGEAEGAE TTKRPAVCAA VL
	Isoform 5 (del4). Checksum: 9D1ED8844633607E	FASTA	203	22,594
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 170 180 CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR 190 200 RPLNNNSEIA LSLSRNKVVP VER
	Isoform 6 (sub3). Checksum: 795CC81539178CF0	FASTA	165	18,706
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 CEYCFDEPLL KRTDKYRTYS KKHFRIFREE NLSCPYRIWF NFCLF
	Isoform 7 (del9-12). Checksum: CAE0E58DF0308393	FASTA	339	38,125
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 170 180 CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR 190 200 210 220 230 240 RPLNNNSEIA LSLSRNKVFV FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER 250 260 270 280 290 300 KTCKKVAIKI ISKRKFAIGS AREADPALNV ETEIEILKKL NHPCIIKIKN FFDAEDYYIV 310 320 330 LELMEGGELF DKVVGNKRLK EATCKLYFYQ MLLAVQMKT
	Isoform 8 (del7). Checksum: 630D0AF3AE5114E6	FASTA	289	32,142
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 170 180 CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR 190 200 210 220 230 240 RPLNNNSEIA LSLSRNKVFV FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER 250 260 270 280 KTCKKVAIKI ISKRKFAIGS AREADPALNV ETEIEILKKL NHDGRGRAV
	Isoform 9 (insx). Checksum: 55BDE42C9A0F98A7	FASTA	586	65,419
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLETES GHVTQSDLEL 130 140 150 160 170 180 LLSSDPPASA SQSAGIRGVR HHPRPVCSLK CVNDNYWFGR DKSCEYCFDE PLLKRTDKYR 190 200 210 220 230 240 TYSKKHFRIF REVGPKNSYI AYIEDHSGNG TFVNTELVGK GKRRPLNNNS EIALSLSRNK 250 260 270 280 290 300 VFVFFDLTVD DQSVYPKALR DEYIMSKTLG SGACGEVKLA FERKTCKKVA IKIISKRKFA 310 320 330 340 350 360 IGSAREADPA LNVETEIEIL KKLNHPCIIK IKNFFDAEDY YIVLELMEGG ELFDKVVGNK 370 380 390 400 410 420 RLKEATCKLY FYQMLLAVQY LHENGIIHRD LKPENVLLSS QEEDCLIKIT DFGHSKILGE 430 440 450 460 470 480 TSLMRTLCGT PTYLAPEVLV SVGTAGYNRA VDCWSLGVIL FICLSGYPPF SEHRTQVSLK 490 500 510 520 530 540 DQITSGKYNF IPEVWAEVSE KALDLVKKLL VVDPKARFTT EEALRHPWLQ DEDMKRKFQD 550 560 570 580 LLSEENESTA LPQVLAQPST SRKRPREGEA EGAETTKRPA VCAAVL
	Isoform 10 (iso2). Checksum: 54BBB0152B5668D5	FASTA	140	15,420
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 CEYCFDEPLL EFRSYSFYLP
	Isoform 11 (iso1). Checksum: 57F0155780C96BA2	FASTA	225	24,396
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEVLVS VGTAGYNRAV DCWSLGVILF ICLSGYPPFS EHRTQVSLKD 130 140 150 160 170 180 QITSGKYNFI PEVWAEVSEK ALDLVKKLLV VDPKARFTTE EALRHPWLQD EDMKRKFQDL 190 200 210 220 LSEENESTAL PQVLAQPSTS RKRPREGEAE GAETTKRPAV CAAVL
	Isoform 12 (del9). Checksum: 8B99B81830B8092F	FASTA	514	57,526
	10 20 30 40 50 60 MSRESDVEAQ QSHGSSACSQ PHGSVTQSQG SSSQSQGISS SSTSTMPNSS QSSHSSSGTL 70 80 90 100 110 120 SSLETVSTQE LYSIPEDQEP EDQEPEEPTP APWARLWALQ DGFANLECVN DNYWFGRDKS 130 140 150 160 170 180 CEYCFDEPLL KRTDKYRTYS KKHFRIFREV GPKNSYIAYI EDHSGNGTFV NTELVGKGKR 190 200 210 220 230 240 RPLNNNSEIA LSLSRNKVFV FFDLTVDDQS VYPKALRDEY IMSKTLGSGA CGEVKLAFER 250 260 270 280 290 300 KTCKKVAIKI ISKRKFAIGS AREADPALNV ETEIEILKKL NHPCIIKIKN FFDAEDYYIV 310 320 330 340 350 360 LELMEGGELF DKVVGNKRLK EATCKLYFYQ MLLAVQITDF GHSKILGETS LMRTLCGTPT 370 380 390 400 410 420 YLAPEVLVSV GTAGYNRAVD CWSLGVILFI CLSGYPPFSE HRTQVSLKDQ ITSGKYNFIP 430 440 450 460 470 480 EVWAEVSEKA LDLVKKLLVV DPKARFTTEE ALRHPWLQDE DMKRKFQDLL SEENESTALP 490 500 510 QVLAQPSTSR KRPREGEAEG AETTKRPAVC AAVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Linkage of ATM to cell cycle regulation by the Chk2 protein kinase." Matsuoka S., Huang M., Elledge S.J. Science 282:1893-1897(1998) [PubMed: 9836640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASP-347.
[2]	"A human homologue of the checkpoint kinase Cds1 directly inhibits Cdc25 phosphatase." Blasina A., van de Weyer I., Laus M.C., Luyten W.H.M.L., Parker A.E., McGowan C.H. Curr. Biol. 9:1-10(1999) [PubMed: 9889122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[3]	"A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage." Brown A.L., Lee C.-H., Schwarz J.K., Mitiku N., Piwnica-Worms H., Chung J.H. Proc. Natl. Acad. Sci. U.S.A. 96:3745-3750(1999) [PubMed: 10097108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
[4]	"Alternative splicing and mutation status of CHEK2 in stage III breast cancer." Staalesen V., Falck J., Geisler S., Bartkova J., Boerresen-Dale A.-L., Lukas J., Lillehaug J.R., Bartek J., Lonning P.E. Oncogene 23:8535-8544(2004) [PubMed: 15361853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12), FUNCTION, SUBCELLULAR LOCATION. Tissue: Mammary gland.
[5]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
[6]	"Chk2/HuCds1 cell cycle checkpoint protein kinase from human colon carcinoma HT29 cells: regulation by autophosphorylation and DNA-dependent protein kinase and inhibition by cell cycle regulatory drugs." Shao R.-G., Zhang H., Yu Q., Pommier Y. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon carcinoma.
[7]	"An alternative spliced Chk2." Ogawa A., Okabe-Nakamura A. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12). Tissue: T-cell.
[8]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-85; THR-157; MET-436; LYS-446; ILE-447; SER-448; LYS-501 AND VAL-512.
[9]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: Muscle.
[11]	"The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway." Tosti E., Waldbaum L., Warshaw G., Gross E.A., Ruggieri R. J. Biol. Chem. 279:47652-47660(2004) [PubMed: 15342622] [Abstract] Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-68, MUTAGENESIS OF THR-68 AND ASP-368.
[12]	"Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2." Li J., Williams B.L., Haire L.F., Goldberg M., Wilker E., Durocher D., Yaffe M.B., Jackson S.P., Smerdon S.J. Mol. Cell 9:1045-1054(2002) [PubMed: 12049740] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 64-212.
[13]	"Heterozygous germ line hCHK2 mutations in Li-Fraumeni syndrome." Bell D.W., Varley J.M., Szydlo T.E., Kang D.H., Wahrer D.C.R., Shannon K.E., Lubratovich M., Versalis S.J., Isselbacher K.J., Fraumeni J.F. Jr., Birch J.M., Li F.P., Garber J.E., Haber D.A. Science 286:2528-2531(1999) [PubMed: 10617473] [Abstract] Cited for: VARIANT THR-157, VARIANT COLON CANCER TRP-145.
[14]	"Mutation analysis of the CHK2 gene in families with hereditary breast cancer." Allinen M., Huusko P., Maentyniemi S., Launonen V., Winqvist R. Br. J. Cancer 85:209-212(2001) [PubMed: 11461078] [Abstract] Cited for: VARIANT THR-157.
[15]	"Destabilization of CHK2 by a missense mutation associated with Li-Fraumeni Syndrome." Lee S.B., Kim S.H., Bell D.W., Wahrer D.C.R., Schiripo T.A., Jorczak M.M., Sgroi D.C., Garber J.E., Li F.P., Nichols K.E., Varley J.M., Godwin A.K., Shannon K.M., Harlow E., Haber D.A. Cancer Res. 61:8062-8067(2001) [PubMed: 11719428] [Abstract] Cited for: VARIANT LFS2 TRP-145.
[16]	"Mutation analysis of the CHK2 gene in breast carcinoma and other cancers." Ingvarsson S., Sigbjornsdottir B.I., Huiping C., Hafsteinsdottir S.H., Ragnarsson G., Barkardottir R.B., Arason A., Egilsson V., Bergthorsson J.T. Breast Cancer Res. 4:R4-R4(2002) [PubMed: 12052256] [Abstract] Cited for: VARIANT MULTIPLE CANCERS LYS-59.
[17]	"CHEK2 variants in susceptibility to breast cancer and evidence of retention of the wild type allele in tumours." Sodha N., Bullock S., Taylor R., Mitchell G., Guertl-Lackner B., Williams R.D., Bevan S., Bishop K., McGuire S., Houlston R.S., Eeles R.A. Br. J. Cancer 87:1445-1448(2002) [PubMed: 12454775] [Abstract] Cited for: VARIANTS GLY-117; GLN-137 AND HIS-180.
[18]	"Mutations of the CHK2 gene are found in some osteosarcomas, but are rare in breast, lung, and ovarian tumors." Miller C.W., Ikezoe T., Krug U., Hofmann W.K., Tavor S., Vegesna V., Tsukasaki K., Takeuchi S., Koeffler H.P. Genes Chromosomes Cancer 33:17-21(2002) [PubMed: 11746983] [Abstract] Cited for: VARIANTS OSTEOSARCOMA SER-17 AND LEU-85.
[19]	"Mutations in CHEK2 associated with prostate cancer risk." Dong X., Wang L., Taniguchi K., Wang X., Cunningham J.M., McDonnell S.K., Qian C., Marks A.F., Slager S.L., Peterson B.J., Smith D.I., Cheville J.C., Blute M.L., Jacobsen S.J., Schaid D.J., Tindall D.J., Thibodeau S.N., Liu W. Am. J. Hum. Genet. 72:270-280(2003) [PubMed: 12533788] [Abstract] Cited for: VARIANTS PROSTATE CANCER LYS-64; PRO-145; ARG-167; CYS-180; HIS-180; CYS-181; HIS-181; LYS-239; PHE-251; HIS-318; PRO-323; CYS-327 AND LYS-476, VARIANT THR-157.
[20]	"Variants in CHEK2 other than 1100delC do not make a major contribution to breast cancer susceptibility." Schutte M., Seal S., Barfoot R., Meijers-Heijboer H., Wasielewski M., Evans D.G., Eccles D., Meijers C., Lohman F., Klijn J., van den Ouweland A., Brady A., Cole T., Collins A., Cox H., Donaldson A., Eeles R., Evans G. , Gregory H., Gray J., Houlston R., Lalloo F., Lucassen A., Mackay J., Mitchell G., Morrison P., Murday V., Narod S., Patterson J., Peretz T., Phelan C.M., Rogers M., Schofield A., Tonin P., Weber B., Weber W., Futreal P.A., Nathanson K.L., Weber B.L., Easton D.F., Stratton M.R., Rahman N. Am. J. Hum. Genet. 72:1023-1028(2003) [PubMed: 12610780] [Abstract] Cited for: VARIANTS GLY-117; TRP-145 AND THR-157.
[21]	"CHEK2 variants associate with hereditary prostate cancer." Seppaelae E.H., Ikonen T., Mononen N., Autio V., Roekman A., Matikainen M.P., Tammela T.L.J., Schleutker J. Br. J. Cancer 89:1966-1970(2003) [PubMed: 14612911] [Abstract] Cited for: VARIANT THR-157.
[22]	"CHEK2 is a multiorgan cancer susceptibility gene." Cybulski C., Gorski B., Huzarski T., Masojc B., Mierzejewski M., Debniak T., Teodorczyk U., Byrski T., Gronwald J., Matyjasik J., Zlowocka E., Lenner M., Grabowska E., Nej K., Castaneda J., Medrek K., Szymanska A., Szymanska J. , Kurzawski G., Suchy J., Oszurek O., Witek A., Narod S.A., Lubinski J. Am. J. Hum. Genet. 75:1131-1135(2004) [PubMed: 15492928] [Abstract] Cited for: VARIANT THR-157.
[23]	"Frequency of CHEK2 mutations in a population based, case-control study of breast cancer in young women." Friedrichsen D.M., Malone K.E., Doody D.R., Daling J.R., Ostrander E.A. Breast Cancer Res. 6:R629-R635(2004) [PubMed: 15535844] [Abstract] Cited for: VARIANTS TRP-145 AND THR-157.
[24]	"A novel founder CHEK2 mutation is associated with increased prostate cancer risk." Cybulski C., Huzarski T., Gorski B., Masojc B., Mierzejewski M., Debniak T., Gliniewicz B., Matyjasik J., Zlowocka E., Kurzawski G., Sikorski A., Posmyk M., Szwiec M., Czajka R., Narod S.A., Lubinski J. Cancer Res. 64:2677-2679(2004) [PubMed: 15087378] [Abstract] Cited for: VARIANT THR-157.
[25]	"Limited relevance of the CHEK2 gene in hereditary breast cancer." Dufault M.R., Betz B., Wappenschmidt B., Hofmann W., Bandick K., Golla A., Pietschmann A., Nestle-Kraemling C., Rhiem K., Huettner C., von Lindern C., Dall P., Kiechle M., Untch M., Jonat W., Meindl A., Scherneck S., Niederacher D., Schmutzler R.K., Arnold N. Int. J. Cancer 110:320-325(2004) [PubMed: 15095295] [Abstract] Cited for: VARIANT THR-157.
[26]	"CHEK2 variant I157T may be associated with increased breast cancer risk." Kilpivaara O., Vahteristo P., Falck J., Syrjaekoski K., Eerola H., Easton D., Bartkova J., Lukas J., Heikkilae P., Aittomaeki K., Holli K., Blomqvist C., Kallioniemi O.-P., Bartek J., Nevanlinna H. Int. J. Cancer 111:543-547(2004) [PubMed: 15239132] [Abstract] Cited for: VARIANT THR-157.
[27]	"Functional and genomic approaches reveal an ancient CHEK2 allele associated with breast cancer in the Ashkenazi Jewish population." Shaag A., Walsh T., Renbaum P., Kirchhoff T., Nafa K., Shiovitz S., Mandell J.B., Welcsh P., Lee M.K., Ellis N., Offit K., Levy-Lahad E., King M.-C. Hum. Mol. Genet. 14:555-563(2005) [PubMed: 15649950] [Abstract] Cited for: VARIANTS LEU-85 AND PHE-428.
[28]	"Association of two mutations in the CHEK2 gene with breast cancer." Bogdanova N., Enbetaen-Dubrowinskaja N., Feshchenko S., Lazjuk G.I., Rogov Y.I., Dammann O., Bremer M., Karstens J.H., Sohn C., Doerk T. Int. J. Cancer 116:263-266(2005) [PubMed: 15810020] [Abstract] Cited for: VARIANT THR-157.
[29]	"Homozygosity for a CHEK2*1100delC mutation identified in familial colorectal cancer does not lead to a severe clinical phenotype." van Puijenbroek M., van Asperen C.J., van Mil A., Devilee P., van Wezel T., Morreau H. J. Pathol. 206:198-204(2005) [PubMed: 15818573] [Abstract] Cited for: VARIANTS GLY-117; GLN-137; TRP-145; THR-157 AND HIS-180.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF086904 mRNA. Translation: AAC83693.1.
AJ131197 mRNA. Translation: CAA10319.1.
AF096279 mRNA. Translation: AAD11784.1.
AY551295 mRNA. Translation: AAS58456.1.
AY551296 mRNA. Translation: AAS58457.1.
AY551297 mRNA. Translation: AAS58458.1.
AY551298 mRNA. Translation: AAS58459.1.
AY551299 mRNA. Translation: AAS58460.1.
AY551300 mRNA. Translation: AAS58461.1.
AY551301 mRNA. Translation: AAS58462.1.
AY551302 mRNA. Translation: AAS58463.1.
AY551303 mRNA. Translation: AAS58464.1.
AY551304 mRNA. Translation: AAS58465.1.
AY551305 mRNA. Translation: AAS58466.1.
CR456418 mRNA. Translation: CAG30304.1.
AF174135 mRNA. Translation: AAD48504.1.
AB040105 mRNA. Translation: BAB17231.1.
AY800241 Genomic DNA. Translation: AAV41895.1.
AL121825, AL117330 Genomic DNA. Translation: CAH73823.1.
AL117330, AL121825 Genomic DNA. Translation: CAH73875.1.
BC004207 mRNA. Translation: AAH04207.1.

IPI

IPI00014072.
IPI00030746.
IPI00423146.
IPI00423149.
IPI00423156.
IPI00423157.
IPI00607619.
IPI00607680.
IPI00607709.
IPI00607739.
IPI00607753.
IPI00607851.

RefSeq

NP_001005735.1.
NP_009125.1.
NP_665861.1.

UniGene

Hs.291363
Hs.505297

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GXC	X-ray	2.70	A/D/G/J	64-212	[»]
2CN5	X-ray	2.25	A	210-531	[»]
2CN8	X-ray	2.70	A	210-531	[»]
2W0J	X-ray	2.05	A	210-531	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:24270N.

IntAct

O96017. 15 interactions.

PTM databases

PhosphoSite

O96017.

Proteomic databases

PRIDE

O96017.

Genome annotation databases

Ensembl

ENSG00000183765. Homo sapiens. [Contig view]

GeneID

11200.

KEGG

hsa:11200.

Organism-specific databases

GeneCards

GC0YP012028.
GC22M027408.
GC22M027413.
GC22M027414.
GC22M027415.
GC22P015366.

H-InvDB

HIX0016341.
HIX0038241.

HGNC

HGNC:16627. CHEK2.

HPA

CAB002030.
HPA001878.

MIM

176807. phenotype.
259500. phenotype.
604373. gene+phenotype.
609265. phenotype.

Orphanet

145. Breast cancer, familial.
524. Li-Fraumeni syndrome.
668. Osteosarcoma.
1331. Prostate cancer, familial.

PharmGKB

PA404.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O96017.

OMA

O96017. KARFTTE.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpress

O96017.

Bgee

O96017.

GermOnline

ENSG00000183765. Homo sapiens.

Family and domain databases

InterPro

IPR000253. FHA.
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]

Gene3D

G3DSA:2.60.200.20. FHA. 1 hit.

Pfam

PF00498. FHA. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

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

SMART

SM00240. FHA. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS50006. FHA_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

42629.

SOURCE

Search...

Entry information

Entry name

CHK2_HUMAN

Accession

Primary (citable) accession number: O96017
Secondary accession number(s): Q6QA03 , Q6QA04, Q6QA05, Q6QA06, Q6QA07, Q6QA08, Q6QA10, Q6QA11, Q6QA12, Q6QA13, Q9HCQ8, Q9UGF0, Q9UGF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)