O70589 (CSKP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peripheral plasma membrane protein CASK
EC=2.7.11.1

Alternative name(s):
Calcium/calmodulin-dependent serine protein kinase

Gene names

Name:

Cask

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.4
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 By similarity.
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 By similarity.
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. Interacts with FCHSD2 By similarity. Interacts with KIRREL3 By similarity. Identified in a complex with ACTN4, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 By similarity. Interacts with TSPYL2. Part of a complex containing CASK, TRB1 and TSPYL2. Ref.4 Ref.5 Ref.7
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.
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 By similarity.
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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
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 mutant phenotype PubMed 18054859. Source: MGI negative regulation of cell-matrix adhesion Inferred from electronic annotation. Source: Compara negative regulation of cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara negative regulation of keratinocyte proliferation Inferred from electronic annotation. Source: Compara negative regulation of wound healing Inferred from electronic annotation. Source: Compara positive regulation of calcium ion import Inferred from direct assay PubMed 18054859. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 15584924. Source: MGI
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from direct assay PubMed 12351654PubMed 16105026. Source: MGI cell-cell junction Inferred from direct assay PubMed 18664494. Source: BHF-UCL cytosol Inferred from direct assay PubMed 12202822. Source: MGI nuclear lamina Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 18664494. Source: BHF-UCL synapse Inferred from direct assay PubMed 12202822PubMed 14622577PubMed 16186258PubMed 18054859. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW neurexin family protein binding Inferred from direct assay PubMed 18054859. Source: MGI protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O70589-1)

Also known as: CASK-B;

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: O70589-2)

Also known as: CASK-A;

The sequence of this isoform differs from the canonical sequence as follows:
     580-664: RDSPSTSRQS...NWWQGKLENS → VISLTSLSYP...KIKAKYRKLQ
     665-926: Missing.

Isoform 3 (identifier: O70589-3)

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

Isoform 4 (identifier: O70589-4)

The sequence of this isoform differs from the canonical sequence as follows:
     340-345: Missing.
     603-614: Missing.

Isoform 5 (identifier: O70589-5)

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

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_0000094569

Regions

Domain

12 – 276

265

Protein kinase

Domain

343 – 398

56

L27 1

Domain

402 – 455

54

L27 2

Domain

490 – 571

82

PDZ

Domain

612 – 682

71

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 By similarity

Modified residue

155

1

Phosphoserine; by autocatalysis By similarity

Modified residue

571

1

Phosphotyrosine Ref.6

Natural variations

Alternative sequence

340 – 345

6

Missing in isoform 3, isoform 4 and isoform 5.

VSP_024614

Alternative sequence

580 – 664

85

RDSPS…KLENS → VISLTSLSYPNLPISSEFLT NFLLMAECFCFLGNCFCCAV TTLHTNFTTKITEQKEVPPT SSALLACRYLQPFCSKIKAK YRKLQ in isoform 2.

VSP_003152

Alternative sequence

580 – 602

23

Missing in isoform 3.

VSP_024615

Alternative sequence

603 – 614

12

Missing in isoform 4.

VSP_024616

Alternative sequence

665 – 926

262

Missing in isoform 2.

VSP_003153

Experimental info

Sequence conflict

298

1

F → L in CAA76646. Ref.1

Sequence conflict

298

1

F → L in CAA76647. Ref.1

Sequence conflict

666

1

N → K in CAA76646. Ref.1

Sequence conflict

666

1

N → K in CAA76647. Ref.1

Sequence conflict

677 – 679

3

LQE → IQG in CAA76646. Ref.1

Sequence conflict

677 – 679

3

LQE → IQG in CAA76647. Ref.1

Sequence conflict

720 – 723

4

FDQL → LII in CAA76646. Ref.1

Sequence conflict

720 – 723

4

FDQL → LII in CAA76647. Ref.1

Sequence conflict

742

1

L → S in CAA76646. Ref.1

Sequence conflict

742

1

L → S in CAA76647. Ref.1

Sequence conflict

769

1

Y → C in CAA76646. Ref.1

Sequence conflict

769

1

Y → C in CAA76647. Ref.1

Sequence conflict

798

1

Q → R in CAA76646. Ref.1

Sequence conflict

798

1

Q → R in CAA76647. Ref.1

Sequence conflict

816

1

Y → F in CAA76646. Ref.1

Sequence conflict

816

1

Y → F in CAA76647. Ref.1

Sequence conflict

821 – 823

3

ETI → DH in CAA76646. Ref.1

Sequence conflict

821 – 823

3

ETI → DH in CAA76647. Ref.1

Sequence conflict

851

1

A → P in CAA76646. Ref.1

Sequence conflict

851

1

A → P in CAA76647. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

926

Helix Strand Turn

Details...

Helix

406 – 417

12

Helix

423 – 433

11

Helix

435 – 452

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CASK-B) [UniParc]. Last modified April 17, 2007. Version 2. Checksum: ADD2008CE53E0018	FASTA	926	105,109
	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 VLQRTYAHYF DLTIINNEID 910 920 ETIRHLEEAV ELVCTAPQWV PVSWVY
	Isoform 2 (CASK-A) [UniParc]. Checksum: B60B1EB9E3091CB6	FASTA	664	74,907
	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 YRTQSSSCEV ISLTSLSYPN LPISSEFLTN 610 620 630 640 650 660 FLLMAECFCF LGNCFCCAVT TLHTNFTTKI TEQKEVPPTS SALLACRYLQ PFCSKIKAKY RKLQ
	Isoform 3 [UniParc]. Checksum: 4AEBC03D2EEE3F68	FASTA	897	102,100
	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 DVLQRTYAHY FDLTIINNEI DETIRHLEEA VELVCTAPQW VPVSWVY
	Isoform 4 [UniParc]. Checksum: 0413DFBEA74F4E37	FASTA	908	103,145
	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 SCERDSPSTS RQSPANGHSS TNNSVSIYVR 610 620 630 640 650 660 AQFEYDPAKD DLIPCKEAGI RFRVGDIIQI ISKDDHNWWQ GKLENSKNGT AGLIPSPELQ 670 680 690 700 710 720 EWRVACIAME KTKQEQQASC TWFGKKKKQY KDKYLAKHNA VFDQLDLVTY EEVVKLPAFK 730 740 750 760 770 780 RKTLVLLGAH GVGRRHIKNT LITKHPDRFA YPIPHTTRPP KKDEENGKNY YFVSHDQMMQ 790 800 810 820 830 840 DISNNEYLEY GSHEDAMYGT KLETIRKIHE QGLIAILDVE PQALKVLRTA EFAPFVVFIA 850 860 870 880 890 900 APTITPGLNE DESLQRLQKE SDVLQRTYAH YFDLTIINNE IDETIRHLEE AVELVCTAPQ WVPVSWVY
	Isoform 5 [UniParc]. Checksum: DD0E0B86503865A6	FASTA	920	104,455
	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 SCERDSPSTS RQSPANGHSS TNNSVSDLPS 610 620 630 640 650 660 TTQPKGRQIY VRAQFEYDPA KDDLIPCKEA GIRFRVGDII QIISKDDHNW WQGKLENSKN 670 680 690 700 710 720 GTAGLIPSPE LQEWRVACIA MEKTKQEQQA SCTWFGKKKK QYKDKYLAKH NAVFDQLDLV 730 740 750 760 770 780 TYEEVVKLPA FKRKTLVLLG AHGVGRRHIK NTLITKHPDR FAYPIPHTTR PPKKDEENGK 790 800 810 820 830 840 NYYFVSHDQM MQDISNNEYL EYGSHEDAMY GTKLETIRKI HEQGLIAILD VEPQALKVLR 850 860 870 880 890 900 TAEFAPFVVF IAAPTITPGL NEDESLQRLQ KESDVLQRTY AHYFDLTIIN NEIDETIRHL 910 920 EEAVELVCTA PQWVPVSWVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Murine CASK is disrupted in a sex-linked cleft palate mouse mutant." Laverty H.G., Wilson J.B. Genomics 53:29-41(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6. Tissue: Embryo.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-926 (ISOFORM 3). Strain: C57BL/6J. Tissue: Cecum.
[4]	"Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2." Hsueh Y.P., Wang T.F., Yang F.C., Sheng M. Nature 404:298-302(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TBR1.
[5]	"Transcriptional modification by a CASK-interacting nucleosome assembly protein." Wang G.-S., Hong C.-J., Yen T.-Y., Huang H.-Y., Ou Y., Huang T.-N., Jung W.-G., Kuo T.-Y., Sheng M., Wang T.-F., Hsueh Y.-P. Neuron 42:113-128(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TSPYL2, IDENTIFICATION IN COMPLEX WITH TSPYL2 AND TBR1. Strain: C57BL/6.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins." Feng W., Long J.-F., Zhang M. Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 405-454, INTERACTION WITH LIN7B.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y17138 mRNA. Translation: CAA76647.1.
Y17137 mRNA. Translation: CAA76646.1.
AL671117, AL672204, BX005215 Genomic DNA. Translation: CAM19440.1.
AL671117, AL672204, BX005215 Genomic DNA. Translation: CAM19441.1.
AL671117, AL672204 Genomic DNA. Translation: CAM19446.1.
AL672204, AL671117, BX005215 Genomic DNA. Translation: CAM20906.1.
AL672204, BX005215, AL671117 Genomic DNA. Translation: CAM20907.1.
AL672204, AL671117 Genomic DNA. Translation: CAM20909.1.
BX005215, AL672204, AL671117 Genomic DNA. Translation: CAM19528.1.
BX005215, AL672204, AL671117 Genomic DNA. Translation: CAM19529.1.
AK136523 mRNA. Translation: BAE23024.1.

IPI

IPI00119517.
IPI00227910.
IPI00776307.
IPI00776341.
IPI00844763.

RefSeq

NP_033936.2. NM_009806.2.

UniGene

Mm.327591.
Mm.474948.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y74	NMR	-	B/D	405-454	[»]

ProteinModelPortal

O70589.

SMR

O70589. Positions 5-394, 403-456, 487-572, 615-921.

ModBase

Search...

Protein-protein interaction databases

IntAct

O70589. 16 interactions.

PTM databases

PhosphoSite

O70589.

Proteomic databases

PaxDb

O70589.

PRIDE

O70589.

Protocols and materials databases

DNASU

12361.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000033321; ENSMUSP00000033321; ENSMUSG00000031012.
ENSMUST00000115436; ENSMUSP00000111096; ENSMUSG00000031012.
ENSMUST00000115438; ENSMUSP00000111098; ENSMUSG00000031012.
ENSMUST00000156096; ENSMUSP00000120299; ENSMUSG00000031012.

GeneID

12361.

KEGG

mmu:12361.

UCSC

uc009srp.1. mouse.
uc009srq.1. mouse.
uc012hez.1. mouse.

Organism-specific databases

CTD

8573.

MGI

MGI:1309489. Cask.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00560000077048.

HOGENOM

HOG000233034.

HOVERGEN

HBG001858.

InParanoid

O70589.

KO

K06103.

OrthoDB

EOG4FBHS6.

Enzyme and pathway databases

BRENDA

2.7.11.1. 3474.

Gene expression databases

ArrayExpress

O70589.

Bgee

O70589.

Genevestigator

O70589.

GermOnline

ENSMUSG00000031012. Mus musculus.

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.
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.

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

ChiTaRS

CASK. mouse.

EvolutionaryTrace

O70589.

NextBio

281028.

SOURCE

Search...

Entry information

Entry name

CSKP_MOUSE

Accession

Primary (citable) accession number: O70589
Secondary accession number(s): A2ADP8 , A2ADP9, A2ADQ4, O70588, Q3UW92

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	April 17, 2007
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program