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O70589 (CSKP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peripheral plasma membrane protein CASK

EC=2.7.11.1
Alternative name(s):
Calcium/calmodulin-dependent serine protein kinase
Gene names
Name:Cask
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Protein existenceEvidence 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 TBR1. 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, TBR1 and TSPYL2. Ref.4 Ref.5 Ref.6

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 componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion import

Inferred from mutant phenotype PubMed 18054859. Source: MGI

negative regulation of cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of wound healing

Inferred from electronic annotation. Source: Ensembl

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_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from direct assay PubMed 12351654PubMed 16105026. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 12202822. Source: MGI

membrane

Inferred from direct assay PubMed 18054859. Source: MGI

nuclear lamina

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

synapse

Inferred from direct assay PubMed 12202822PubMed 14622577PubMed 16186258PubMed 18054859. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

neurexin family protein binding

Inferred from direct assay PubMed 18054859. Source: MGI

protein binding

Inferred from physical interaction PubMed 12093160PubMed 12202822PubMed 16105026PubMed 16186258PubMed 16874800PubMed 18054859PubMed 23791195. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 926926Peripheral plasma membrane protein CASK
PRO_0000094569

Regions

Domain12 – 276265Protein kinase
Domain343 – 39856L27 1
Domain402 – 45554L27 2
Domain490 – 57182PDZ
Domain612 – 68271SH3
Domain739 – 911173Guanylate kinase-like
Nucleotide binding18 – 269ATP By similarity
Region305 – 31511Calmodulin-binding

Sites

Active site1411 By similarity
Binding site411ATP By similarity

Amino acid modifications

Modified residue1511Phosphoserine; by autocatalysis By similarity
Modified residue1551Phosphoserine; by autocatalysis By similarity

Natural variations

Alternative sequence340 – 3456Missing in isoform 3, isoform 4 and isoform 5.
VSP_024614
Alternative sequence580 – 66485RDSPS…KLENS → VISLTSLSYPNLPISSEFLT NFLLMAECFCFLGNCFCCAV TTLHTNFTTKITEQKEVPPT SSALLACRYLQPFCSKIKAK YRKLQ in isoform 2.
VSP_003152
Alternative sequence580 – 60223Missing in isoform 3.
VSP_024615
Alternative sequence603 – 61412Missing in isoform 4.
VSP_024616
Alternative sequence665 – 926262Missing in isoform 2.
VSP_003153

Experimental info

Sequence conflict2981F → L in CAA76646. Ref.1
Sequence conflict2981F → L in CAA76647. Ref.1
Sequence conflict6661N → K in CAA76646. Ref.1
Sequence conflict6661N → K in CAA76647. Ref.1
Sequence conflict677 – 6793LQE → IQG in CAA76646. Ref.1
Sequence conflict677 – 6793LQE → IQG in CAA76647. Ref.1
Sequence conflict720 – 7234FDQL → LII in CAA76646. Ref.1
Sequence conflict720 – 7234FDQL → LII in CAA76647. Ref.1
Sequence conflict7421L → S in CAA76646. Ref.1
Sequence conflict7421L → S in CAA76647. Ref.1
Sequence conflict7691Y → C in CAA76646. Ref.1
Sequence conflict7691Y → C in CAA76647. Ref.1
Sequence conflict7981Q → R in CAA76646. Ref.1
Sequence conflict7981Q → R in CAA76647. Ref.1
Sequence conflict8161Y → F in CAA76646. Ref.1
Sequence conflict8161Y → F in CAA76647. Ref.1
Sequence conflict821 – 8233ETI → DH in CAA76646. Ref.1
Sequence conflict821 – 8233ETI → DH in CAA76647. Ref.1
Sequence conflict8511A → P in CAA76646. Ref.1
Sequence conflict8511A → P in CAA76647. Ref.1

Secondary structure

....... 926
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CASK-B) [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: ADD2008CE53E0018

FASTA926105,109
        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 

« Hide

Isoform 2 (CASK-A) [UniParc].

Checksum: B60B1EB9E3091CB6
Show »

FASTA66474,907
Isoform 3 [UniParc].

Checksum: 4AEBC03D2EEE3F68
Show »

FASTA897102,100
Isoform 4 [UniParc].

Checksum: 0413DFBEA74F4E37
Show »

FASTA908103,145
Isoform 5 [UniParc].

Checksum: DD0E0B86503865A6
Show »

FASTA920104,455

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
CCDSCCDS40878.1. [O70589-3]
CCDS72343.1. [O70589-5]
RefSeqNP_001271432.1. NM_001284503.1. [O70589-1]
NP_001271433.1. NM_001284504.1.
NP_001271434.1. NM_001284505.1. [O70589-5]
NP_033936.2. NM_009806.3. [O70589-3]
UniGeneMm.327591.
Mm.474948.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y74NMR-B/D405-454[»]
ProteinModelPortalO70589.
SMRO70589. Positions 5-394, 403-456, 487-572, 615-921.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198491. 4 interactions.
IntActO70589. 18 interactions.
MINTMINT-4092125.

PTM databases

PhosphoSiteO70589.

Proteomic databases

MaxQBO70589.
PaxDbO70589.
PRIDEO70589.

Protocols and materials databases

DNASU12361.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033321; ENSMUSP00000033321; ENSMUSG00000031012. [O70589-4]
ENSMUST00000115436; ENSMUSP00000111096; ENSMUSG00000031012. [O70589-3]
ENSMUST00000115438; ENSMUSP00000111098; ENSMUSG00000031012. [O70589-5]
GeneID12361.
KEGGmmu:12361.
UCSCuc009srp.1. mouse. [O70589-3]
uc009srq.1. mouse. [O70589-1]
uc012hez.1. mouse. [O70589-5]

Organism-specific databases

CTD8573.
MGIMGI:1309489. Cask.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000077048.
HOGENOMHOG000233034.
HOVERGENHBG001858.
InParanoidO70589.
KOK06103.
OMARCINRET.
OrthoDBEOG79CXZ5.
PhylomeDBO70589.
TreeFamTF314263.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressO70589.
BgeeO70589.
GenevestigatorO70589.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR011009. Kinase-like_dom.
IPR004172. L27.
IPR014775. L27_C.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00220. S_TKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCASK. mouse.
EvolutionaryTraceO70589.
NextBio281028.
PROO70589.
SOURCESearch...

Entry information

Entry nameCSKP_MOUSE
AccessionPrimary (citable) accession number: O70589
Secondary accession number(s): A2ADP8 expand/collapse secondary AC list , A2ADP9, A2ADQ4, O70588, Q3UW92
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot