O14936 (CSKP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peripheral plasma membrane protein CASK
Short name=hCASK
EC=2.7.11.1

Alternative name(s):
Calcium/calmodulin-dependent serine protein kinase
Protein lin-2 homolog

Gene names

Name:	CASK
Synonyms:	LIN2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	926 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TRB1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity. Ref.11
Enzyme regulation	Differs from archetypal CaMK members in that the kinase domain exhibits a constitutively active conformation and the autoinhibitory region does not engage in direct contact with the ATP-binding cleft, although it still binds Ca2+/CAM. Ref.11
Subunit structure	Binds WHRN and NRXN1 cytosolic tail. Interacts with CASKIN1, APBA1, LIN7(A/B/C) and L27 domain of DLG1 and isoform 2 of DLG4 By similarity. CASK and LIN7 form two mutually exclusive tripartite complexes with APBA1 or CASKIN1 By similarity. Interacts with FCHSD2. Interacts with TSPYL2. Part of a complex containing CASK, TRB1 and TSPYL2 By similarity. Identified in a complex with ACTN4, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 By similarity. Interacts with KIRREL3. Ref.1 Ref.9
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.
Tissue specificity	Ubiquitous. Expression is significantly greater in brain relative to kidney, lung, and liver and in fetal brain and kidney relative to lung and liver. Ref.8
Domain	The first L27 domain binds DLG1 and the second L27 domain probably binds LIN7 By similarity. The protein kinase domain mediates the interaction with FCHSD2.
Involvement in disease	Mental retardation and microcephaly with pontine and cerebellar hypoplasia (MICPCH) [MIM:300749]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Affected individuals can manifest a severe phenotype consisting of severe intellectual deficit, congenital or postnatal microcephaly, disproportionate brainstem and cerebellar hypoplasia. A milder phenotype consists of mental retardation alone or associated with nystagmus. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 FG syndrome 4 (FGS4) [MIM:300422]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15
Sequence similarities	In the N-terminal section; belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 2 L27 domains. Contains 1 PDZ (DHR) domain. Contains 1 protein kinase domain. Contains 1 SH3 domain.
Biophysicochemical properties	Kinetic parameters: Kinetics of autophosphorylation assay were measured, rather than phosphorylation of an exogenous substrate. KM=563 µM for ATP Ref.11

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Domain	Repeat SH3 domain
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion import Inferred from electronic annotation. Source: Compara cell adhesion Traceable author statement Ref.1. Source: ProtInc negative regulation of cell-matrix adhesion Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL negative regulation of cellular response to growth factor stimulus Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL negative regulation of keratinocyte proliferation Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL negative regulation of wound healing Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL positive regulation of calcium ion import Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara
Cellular_component	actin cytoskeleton Traceable author statement Ref.1. Source: ProtInc basement membrane Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from electronic annotation. Source: Compara cell-cell junction Inferred from direct assay PubMed 18664494. Source: BHF-UCL cilium membrane Inferred from sequence or structural similarity. Source: BHF-UCL cytoplasm Inferred from direct assay PubMed 18664494. Source: BHF-UCL cytosol Inferred from electronic annotation. Source: Compara nuclear lamina Inferred from direct assay PubMed 18664494. Source: BHF-UCL nuclear matrix Inferred from direct assay PubMed 18664494. Source: BHF-UCL nucleolus Inferred from direct assay PubMed 18664494. Source: BHF-UCL presynaptic membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate kinase activity Traceable author statement Ref.1. Source: ProtInc protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ID1	P41134	3	EBI-1215506,EBI-1215527
Nrxn1	Q63373	3	EBI-1215506,EBI-1780696	From a different organism.
RPH3A	Q9Y2J0	3	EBI-1215506,EBI-1216802
SDC2	P34741	2	EBI-1215506,EBI-1172957

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14936-1)

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: O14936-2)

The sequence of this isoform differs from the canonical sequence as follows:
     719-723: Missing.

Isoform 3 (identifier: O14936-3)

The sequence of this isoform differs from the canonical sequence as follows:
     340-345: Missing.
     580-602: Missing.

Isoform 4 (identifier: O14936-4)

The sequence of this isoform differs from the canonical sequence as follows:
     580-602: Missing.
     719-723: Missing.

Isoform 5 (identifier: O14936-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-385: Missing.
     386-386: L → M
     580-602: Missing.

Isoform 6 (identifier: O14936-6)

The sequence of this isoform differs from the canonical sequence as follows:
     603-614: Missing.
     719-723: Missing.

Note: Gene prediction confirmed by EST data.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 926

926

Peripheral plasma membrane protein CASK

PRO_0000094568

Regions

Domain

12 – 276

265

Protein kinase

Domain

343 – 398

56

L27 1

Domain

402 – 455

54

L27 2

Domain

489 – 564

76

PDZ

Domain

615 – 682

68

SH3

Domain

739 – 911

173

Guanylate kinase-like

Nucleotide binding

18 – 26

9

ATP By similarity

Region

305 – 315

11

Calmodulin-binding

Sites

Active site

141

1

By similarity

Binding site

41

1

ATP By similarity

Amino acid modifications

Modified residue

151

1

Phosphoserine; by autocatalysis Ref.11

Modified residue

155

1

Phosphoserine; by autocatalysis Ref.11

Modified residue

571

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 385

385

Missing in isoform 5.

VSP_024421

Alternative sequence

340 – 345

6

Missing in isoform 3.

VSP_024422

Alternative sequence

386

1

L → M in isoform 5.

VSP_024423

Alternative sequence

580 – 602

23

Missing in isoform 3, isoform 4 and isoform 5.

VSP_024424

Alternative sequence

603 – 614

12

Missing in isoform 6.

VSP_024425

Alternative sequence

719 – 723

5

Missing in isoform 2, isoform 4 and isoform 6.

VSP_024426

Natural variant

28

1

R → L in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein. Ref.15

VAR_058719

Natural variant

96

1

G → V in a lung large cell carcinoma sample; somatic mutation. Ref.12

VAR_041956

Natural variant

268

1

Y → H in MICPCH. Ref.16

VAR_062996

Natural variant

396

1

P → S in MICPCH. Ref.16

VAR_062997

Natural variant

710

1

D → G in MICPCH. Ref.16

VAR_062998

Experimental info

Sequence conflict

401

1

P → L in AAB88198. Ref.2

Sequence conflict

479

1

D → G in AAB88125. Ref.1

Sequence conflict

479

1

D → G in BAB12252. Ref.3

Sequence conflict

479

1

D → G in AAU10527. Ref.4

Sequence conflict

479

1

D → G in AAF72666. Ref.8

Sequence conflict

479

1

D → G in AAF72667. Ref.8

Sequence conflict

675

1

P → S in AAB88125. Ref.1

Sequence conflict

675

1

P → S in AAU10527. Ref.4

Sequence conflict

780

1

K → R in AAB88125. Ref.1

Sequence conflict

780

1

K → R in AAU10527. Ref.4

Secondary structure

1

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926

Helix Strand Turn

Details...

Helix

8 – 11

4

Beta strand

12 – 20

9

Beta strand

22 – 31

10

Turn

32 – 34

3

Beta strand

37 – 44

8

Helix

45 – 49

5

Beta strand

51 – 53

3

Helix

56 – 68

13

Beta strand

77 – 83

7

Beta strand

86 – 92

7

Helix

99 – 108

10

Helix

115 – 134

20

Helix

144 – 146

3

Beta strand

147 – 149

3

Beta strand

151 – 153

3

Beta strand

158 – 160

3

Helix

163 – 165

3

Beta strand

171 – 173

3

Helix

183 – 185

3

Helix

188 – 191

4

Helix

199 – 214

16

Helix

223 – 232

10

Helix

239 – 242

4

Helix

247 – 256

10

Turn

261 – 263

3

Helix

267 – 271

5

Helix

274 – 277

4

Helix

279 – 282

4

Helix

289 – 302

14

Turn

304 – 306

3

Helix

309 – 312

4

Helix

404 – 416

13

Helix

423 – 431

9

Helix

437 – 450

14

Beta strand

489 – 495

7

Beta strand

497 – 499

3

Beta strand

503 – 506

4

Helix

510 – 512

3

Beta strand

513 – 518

6

Helix

523 – 527

5

Beta strand

535 – 539

5

Helix

544 – 546

3

Helix

549 – 558

10

Beta strand

561 – 568

8

Beta strand

741 – 745

5

Helix

752 – 762

11

Turn

764 – 766

3

Turn

784 – 786

3

Helix

793 – 801

9

Beta strand

805 – 811

7

Beta strand

814 – 819

6

Helix

820 – 828

9

Beta strand

832 – 836

5

Helix

839 – 841

3

Helix

842 – 845

4

Turn

848 – 850

3

Beta strand

852 – 858

7

Helix

870 – 886

17

Helix

887 – 889

3

Beta strand

891 – 895

5

Helix

899 – 909

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 17, 2007. Version 3. Checksum: 6C02008CE52728BA	FASTA	926	105,123
	10 20 30 40 50 60 MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK 70 80 90 100 110 120 REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH 130 140 150 160 170 180 YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV 190 200 210 220 230 240 GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR 250 260 270 280 290 300 QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 310 320 330 340 350 360 RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL 370 380 390 400 410 420 TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP 430 440 450 460 470 480 ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM 490 500 510 520 530 540 DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN 550 560 570 580 590 600 GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS 610 620 630 640 650 660 VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK 670 680 690 700 710 720 LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNAVF 730 740 750 760 770 780 DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK 790 800 810 820 830 840 DEENGKNYYF VSHDQMMQDI SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ 850 860 870 880 890 900 ALKVLRTAEF APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID 910 920 ETIRHLEEAV ELVCTAPQWV PVSWVY
	Isoform 2 [UniParc]. Checksum: C3C9FAE8D051AA27	FASTA	921	104,520
	10 20 30 40 50 60 MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK 70 80 90 100 110 120 REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH 130 140 150 160 170 180 YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV 190 200 210 220 230 240 GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR 250 260 270 280 290 300 QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 310 320 330 340 350 360 RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL 370 380 390 400 410 420 TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP 430 440 450 460 470 480 ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM 490 500 510 520 530 540 DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN 550 560 570 580 590 600 GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS 610 620 630 640 650 660 VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK 670 680 690 700 710 720 LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNADL 730 740 750 760 770 780 VTYEEVVKLP AFKRKTLVLL GAHGVGRRHI KNTLITKHPD RFAYPIPHTT RPPKKDEENG 790 800 810 820 830 840 KNYYFVSHDQ MMQDISNNEY LEYGSHEDAM YGTKLETIRK IHEQGLIAIL DVEPQALKVL 850 860 870 880 890 900 RTAEFAPFVV FIAAPTITPG LNEDESLQRL QKESDILQRT YAHYFDLTII NNEIDETIRH 910 920 LEEAVELVCT APQWVPVSWV Y
	Isoform 3 [UniParc]. Checksum: 8B3BC03D2EF717CA	FASTA	897	102,114
	10 20 30 40 50 60 MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK 70 80 90 100 110 120 REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH 130 140 150 160 170 180 YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV 190 200 210 220 230 240 GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR 250 260 270 280 290 300 QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 310 320 330 340 350 360 RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGA VSQVLDSLEE IHALTDCSEK 370 380 390 400 410 420 DLDFLHSVFQ DQHLHTLLDL YDKINTKSSP QIRNPPSDAV QRAKEVLEEI SCYPENNDAK 430 440 450 460 470 480 ELKRILTQPH FMALLQTHDV VAHEVYSDEA LRVTPPPTSP YLNGDSPESA NGDMDMENVT 490 500 510 520 530 540 RVRLVQFQKN TDEPMGITLK MNELNHCIVA RIMHGGMIHR QGTLHVGDEI REINGISVAN 550 560 570 580 590 600 QTVEQLQKML REMRGSITFK IVPSYRTQSS SCEDLPSTTQ PKGRQIYVRA QFEYDPAKDD 610 620 630 640 650 660 LIPCKEAGIR FRVGDIIQII SKDDHNWWQG KLENSKNGTA GLIPSPELQE WRVACIAMEK 670 680 690 700 710 720 TKQEQQASCT WFGKKKKQYK DKYLAKHNAV FDQLDLVTYE EVVKLPAFKR KTLVLLGAHG 730 740 750 760 770 780 VGRRHIKNTL ITKHPDRFAY PIPHTTRPPK KDEENGKNYY FVSHDQMMQD ISNNEYLEYG 790 800 810 820 830 840 SHEDAMYGTK LETIRKIHEQ GLIAILDVEP QALKVLRTAE FAPFVVFIAA PTITPGLNED 850 860 870 880 890 ESLQRLQKES DILQRTYAHY FDLTIINNEI DETIRHLEEA VELVCTAPQW VPVSWVY
	Isoform 4 [UniParc]. Checksum: B7BC96EB46CCD791	FASTA	898	102,165
	10 20 30 40 50 60 MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK 70 80 90 100 110 120 REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH 130 140 150 160 170 180 YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV 190 200 210 220 230 240 GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR 250 260 270 280 290 300 QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 310 320 330 340 350 360 RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL 370 380 390 400 410 420 TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP 430 440 450 460 470 480 ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM 490 500 510 520 530 540 DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN 550 560 570 580 590 600 GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCED LPSTTQPKGR QIYVRAQFEY 610 620 630 640 650 660 DPAKDDLIPC KEAGIRFRVG DIIQIISKDD HNWWQGKLEN SKNGTAGLIP SPELQEWRVA 670 680 690 700 710 720 CIAMEKTKQE QQASCTWFGK KKKQYKDKYL AKHNADLVTY EEVVKLPAFK RKTLVLLGAH 730 740 750 760 770 780 GVGRRHIKNT LITKHPDRFA YPIPHTTRPP KKDEENGKNY YFVSHDQMMQ DISNNEYLEY 790 800 810 820 830 840 GSHEDAMYGT KLETIRKIHE QGLIAILDVE PQALKVLRTA EFAPFVVFIA APTITPGLNE 850 860 870 880 890 DESLQRLQKE SDILQRTYAH YFDLTIINNE IDETIRHLEE AVELVCTAPQ WVPVSWVY
	Isoform 5 [UniParc]. Checksum: 855EE0A1FC92D5B0	FASTA	518	59,383
	10 20 30 40 50 60 MYDKINTKSS PQIRNPPSDA VQRAKEVLEE ISCYPENNDA KELKRILTQP HFMALLQTHD 70 80 90 100 110 120 VVAHEVYSDE ALRVTPPPTS PYLNGDSPES ANGDMDMENV TRVRLVQFQK NTDEPMGITL 130 140 150 160 170 180 KMNELNHCIV ARIMHGGMIH RQGTLHVGDE IREINGISVA NQTVEQLQKM LREMRGSITF 190 200 210 220 230 240 KIVPSYRTQS SSCEDLPSTT QPKGRQIYVR AQFEYDPAKD DLIPCKEAGI RFRVGDIIQI 250 260 270 280 290 300 ISKDDHNWWQ GKLENSKNGT AGLIPSPELQ EWRVACIAME KTKQEQQASC TWFGKKKKQY 310 320 330 340 350 360 KDKYLAKHNA VFDQLDLVTY EEVVKLPAFK RKTLVLLGAH GVGRRHIKNT LITKHPDRFA 370 380 390 400 410 420 YPIPHTTRPP KKDEENGKNY YFVSHDQMMQ DISNNEYLEY GSHEDAMYGT KLETIRKIHE 430 440 450 460 470 480 QGLIAILDVE PQALKVLRTA EFAPFVVFIA APTITPGLNE DESLQRLQKE SDILQRTYAH 490 500 510 YFDLTIINNE IDETIRHLEE AVELVCTAPQ WVPVSWVY
	Isoform 6 [UniParc]. Checksum: B0B98E6A73E36142	FASTA	909	103,211
	10 20 30 40 50 60 MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK 70 80 90 100 110 120 REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH 130 140 150 160 170 180 YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV 190 200 210 220 230 240 GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR 250 260 270 280 290 300 QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 310 320 330 340 350 360 RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL 370 380 390 400 410 420 TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP 430 440 450 460 470 480 ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM 490 500 510 520 530 540 DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN 550 560 570 580 590 600 GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS 610 620 630 640 650 660 VSIYVRAQFE YDPAKDDLIP CKEAGIRFRV GDIIQIISKD DHNWWQGKLE NSKNGTAGLI 670 680 690 700 710 720 PSPELQEWRV ACIAMEKTKQ EQQASCTWFG KKKKQYKDKY LAKHNADLVT YEEVVKLPAF 730 740 750 760 770 780 KRKTLVLLGA HGVGRRHIKN TLITKHPDRF AYPIPHTTRP PKKDEENGKN YYFVSHDQMM 790 800 810 820 830 840 QDISNNEYLE YGSHEDAMYG TKLETIRKIH EQGLIAILDV EPQALKVLRT AEFAPFVVFI 850 860 870 880 890 900 AAPTITPGLN EDESLQRLQK ESDILQRTYA HYFDLTIINN EIDETIRHLE EAVELVCTAP QWVPVSWVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells." Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., Anderson J.M. J. Cell Biol. 142:129-138(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SDC2 AND EPB41. Tissue: Brain, Liver and Lung.
[2]	"The human homolog of the rat CASK, Drosophila Camguk and C.elegans Lin-2 genes." Zha D., Hu G. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]	"Putative alternative splicing form of human CASK mRNA (partial codes)." Ding L., Saijo K., Kawai K., Akaza H., Ugai H., Yokoyama K.K., Ohno T. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Kidney.
[4]	"Caco2-BBE calcium/calmodulin-dependent serine protein kinase." Yan Y., Merlin D. Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Colon carcinoma.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[7]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-926 (ISOFORM 2). Tissue: Brain.
[8]	"Mapping and expression analysis of the human CASK gene." Stevenson D., Laverty H.G., Wenwieser S., Douglas M., Wilson J.B. Mamm. Genome 11:934-937(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-926 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 27-926 (ISOFORM 3), TISSUE SPECIFICITY. Tissue: Fetus.
[9]	"Alterations in CDH15 and KIRREL3 in patients with mild to severe intellectual disability." Bhalla K., Luo Y., Buchan T., Beachem M.A., Guzauskas G.F., Ladd S., Bratcher S.J., Schroer R.J., Balsamo J., DuPont B.R., Lilien J., Srivastava A.K. Am. J. Hum. Genet. 83:703-713(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIRREL3.
[10]	"Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition." Daniels D.L., Cohen A.R., Anderson J.M., Bruenger A.T. Nat. Struct. Biol. 5:317-325(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-572.
[11]	"CASK functions as a Mg2+-independent neurexin kinase." Mukherjee K., Sharma M., Urlaub H., Bourenkov G.P., Jahn R., Suedhof T.C., Wahl M.C. Cell 133:328-339(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-337 IN COMPLEX WITH AMP, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION OF NRXN1, AUTOPHOSPHORYLATION AT SER-151 AND SER-155.
[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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-96.
[13]	"Mutations of CASK cause an X-linked brain malformation phenotype with microcephaly and hypoplasia of the brainstem and cerebellum." Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., Sudi J., Christian S.L., Ullmann R., Kuechler A., Haas C.A., Flubacher A., Charnas L.R., Uyanik G., Frank U., Klopocki E., Dobyns W.B., Kutsche K. Nat. Genet. 40:1065-1067(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MICPCH SYNDROME.
[14]	Erratum Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., Sudi J., Christian S.L., Ullmann R., Kuechler A., Haas C.A., Flubacher A., Charnas L.R., Uyanik G., Frank U., Klopocki E., Dobyns W.B., Kutsche K. Nat. Genet. 40:1384-1384(2008)
[15]	"A missense mutation in CASK causes FG syndrome in an Italian family." Piluso G., D'Amico F., Saccone V., Bismuto E., Rotundo I.L., Di Domenico M., Aurino S., Schwartz C.E., Neri G., Nigro V. Am. J. Hum. Genet. 84:162-177(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FGS4 LEU-28, CHARACTERIZATION OF VARIANT FGS4 LEU-28.
[16]	"A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation." Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J. , Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P., Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R., Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R., de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M., Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U., Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M., Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T., Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C., Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., Futreal P.A., Stratton M.R. Nat. Genet. 41:535-543(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] MICPCH HIS-268; SER-396 AND GLY-710.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF032119 mRNA. Translation: AAB88125.1.
AF035582 mRNA. Translation: AAB88198.1.
AB039327 mRNA. Translation: BAB12252.2.
AY705392 mRNA. Translation: AAU10527.1.
AL627402 , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71237.1.
AL627402 , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71238.1.
AL627402 , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71239.1.
AL627402 , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71240.1.
AL445239 , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41092.1.
AL445239 , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41093.1.
AL445239 , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41094.1.
AL445239 , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41095.1.
AL603754 , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41634.1.
AL603754 , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41635.1.
AL603754 , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41636.1.
AL603754 , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41637.1.
AL353691 , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42244.1.
AL353691 , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42245.1.
AL353691 , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42246.1.
AL353691 , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42247.1.
AL158144 , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42762.1.
AL158144 , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42763.1.
AL158144 , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42764.1.
AL158144 , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42765.1.
BC117311 mRNA. Translation: AAI17312.1.
BC143454 mRNA. Translation: AAI43455.1.
AB208859 mRNA. Translation: BAD92096.1.
AF262404 mRNA. Translation: AAF72666.1.
AF262405 mRNA. Translation: AAF72667.1.

IPI

IPI00514301.
IPI00555605.
IPI00641315.
IPI00646452.
IPI00877929.
IPI00937304.

RefSeq

NP_001119526.1. NM_001126054.2.
NP_001119527.1. NM_001126055.2.
NP_003679.2. NM_003688.3.

UniGene

Hs.495984.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KGD	X-ray	1.31	A	739-909	[»]
1KWA	X-ray	1.93	A/B	489-572	[»]
1ZL8	NMR	-	B	403-456	[»]
3C0G	X-ray	2.19	A/B	1-337	[»]
3C0H	X-ray	2.30	A/B	1-337	[»]
3C0I	X-ray	1.85	A	1-337	[»]
3MFR	X-ray	2.00	A	1-337	[»]
3MFS	X-ray	2.10	A	1-337	[»]
3MFT	X-ray	2.20	A	1-337	[»]
3MFU	X-ray	2.30	A	1-337	[»]
3TAC	X-ray	2.20	A	1-345	[»]

ProteinModelPortal

O14936.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38727N.

IntAct

O14936. 25 interactions.

MINT

MINT-102444.

PTM databases

PhosphoSite

O14936.

Proteomic databases

PaxDb

O14936.

PRIDE

O14936.

Protocols and materials databases

DNASU

8573.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000378158; ENSP00000367400; ENSG00000147044.
ENST00000378163; ENSP00000367405; ENSG00000147044.
ENST00000378166; ENSP00000367408; ENSG00000147044.
ENST00000421587; ENSP00000400526; ENSG00000147044.
ENST00000442742; ENSP00000398007; ENSG00000147044.

GeneID

8573.

KEGG

hsa:8573.

UCSC

uc004dfk.4. human.
uc004dfl.4. human.
uc004dfm.4. human.
uc004dfn.4. human.

Organism-specific databases

CTD

8573.

GeneCards

GC0XM041374.

HGNC

HGNC:1497. CASK.

HPA

CAB001949.
HPA023857.

MIM

300172. gene.
300422. phenotype.
300749. phenotype.

neXtProt

NX_O14936.

PharmGKB

PA26081.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG001858.

KO

K06103.

OMA

AIELVCT.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Pathway_Interaction_DB

syndecan_1_pathway. Syndecan-1-mediated signaling events.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_3_pathway. Syndecan-3-mediated signaling events.

Reactome

REACT_111155. Cell-Cell communication.

SignaLink

O14936.

Gene expression databases

ArrayExpress

O14936.

Bgee

O14936.

CleanEx

HS_CASK.

Genevestigator

O14936.

GermOnline

ENSG00000147044. Homo sapiens.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR011009. Kinase-like_dom.
IPR004172. L27.
IPR014775. L27_C.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR000719. Prot_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00220. S_TKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50156. PDZ. 1 hit.
SSF50044. SH3. 1 hit.
SSF52540. SSF52540. 1 hit.

PROSITE

PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O14936.

ChEMBL

CHEMBL1908381.

ChiTaRS

CASK. human.

EvolutionaryTrace

O14936.

GenomeRNAi

8573.

NextBio

32157.

SOURCE

Search...

Entry information

Entry name

CSKP_HUMAN

Accession

Primary (citable) accession number: O14936
Secondary accession number(s): A6NES1 , B7ZKY0, O43215, Q17RI4, Q59HA0, Q5VT16, Q5VT17, Q5VT18, Q5VT19, Q66T42, Q9BYH6, Q9NYB2, Q9NYB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	April 17, 2007
Last modified:	May 29, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.