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O14936

- CSKP_HUMAN

UniProt

O14936 - CSKP_HUMAN

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Protein

Peripheral plasma membrane protein CASK

Gene

CASK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

Kinetics of autophosphorylation assay were measured, rather than phosphorylation of an exogenous substrate.

  1. KM=563 µM for ATP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411ATPPROSITE-ProRule annotation
Active sitei141 – 1411By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. guanylate kinase activity Source: ProtInc
  3. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. calcium ion import Source: Ensembl
  2. cell adhesion Source: ProtInc
  3. extracellular matrix organization Source: Reactome
  4. negative regulation of cell-matrix adhesion Source: BHF-UCL
  5. negative regulation of cellular response to growth factor stimulus Source: BHF-UCL
  6. negative regulation of keratinocyte proliferation Source: BHF-UCL
  7. negative regulation of wound healing Source: BHF-UCL
  8. nucleotide phosphorylation Source: GOC
  9. positive regulation of calcium ion import Source: Ensembl
  10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_163942. Syndecan interactions.
REACT_23832. Nephrin interactions.
SignaLinkiO14936.

Names & Taxonomyi

Protein namesi
Recommended name:
Peripheral plasma membrane protein CASK (EC:2.7.11.1)
Short name:
hCASK
Alternative name(s):
Calcium/calmodulin-dependent serine protein kinase
Protein lin-2 homolog
Gene namesi
Name:CASK
Synonyms:LIN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:1497. CASK.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. basement membrane Source: Ensembl
  3. basolateral plasma membrane Source: Ensembl
  4. cell-cell junction Source: BHF-UCL
  5. ciliary membrane Source: BHF-UCL
  6. cytoplasm Source: BHF-UCL
  7. cytosol Source: Ensembl
  8. focal adhesion Source: UniProtKB
  9. nuclear lamina Source: BHF-UCL
  10. nuclear matrix Source: BHF-UCL
  11. nucleolus Source: BHF-UCL
  12. plasma membrane Source: ProtInc
  13. presynaptic membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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 adaptive 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti268 – 2681Y → H in MICPCH. 1 Publication
VAR_062996
Natural varianti396 – 3961P → S in MICPCH. 1 Publication
VAR_062997
Natural varianti710 – 7101D → G in MICPCH. 1 Publication
VAR_062998
FG syndrome 4 (FGS4) [MIM:300422]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281R → L in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein. 1 Publication
VAR_058719

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300422. phenotype.
300749. phenotype.
Orphaneti1934. Early infantile epileptic encephalopathy.
323. FG syndrome.
163937. X-linked intellectual disability, Najm type.
PharmGKBiPA26081.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 926926Peripheral plasma membrane protein CASKPRO_0000094568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Phosphoserine; by autocatalysis1 Publication
Modified residuei155 – 1551Phosphoserine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14936.
PaxDbiO14936.
PRIDEiO14936.

PTM databases

PhosphoSiteiO14936.

Expressioni

Tissue specificityi

Ubiquitous. Expression is significantly greater in brain relative to kidney, lung, and liver and in fetal brain and kidney relative to lung and liver.1 Publication

Gene expression databases

BgeeiO14936.
CleanExiHS_CASK.
ExpressionAtlasiO14936. baseline and differential.
GenevestigatoriO14936.

Organism-specific databases

HPAiCAB001949.
HPA023857.

Interactioni

Subunit structurei

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, TBR1 and TSPYL2 By similarity. Identified in a complex with ACTN4, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 By similarity. Interacts with KIRREL3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASKIN1Q8WXD94EBI-1215506,EBI-970261
EPS8Q129293EBI-1215506,EBI-375576
ID1P411343EBI-1215506,EBI-1215527
LIN7AO149103EBI-1215506,EBI-2513988
Nrxn1Q633733EBI-1215506,EBI-1780696From a different organism.
RPH3AQ9Y2J03EBI-1215506,EBI-1216802
SDC2P347412EBI-1215506,EBI-1172957

Protein-protein interaction databases

BioGridi114141. 53 interactions.
DIPiDIP-38727N.
IntActiO14936. 34 interactions.
MINTiMINT-102444.

Structurei

Secondary structure

1
926
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Beta strandi12 – 209Combined sources
Beta strandi22 – 3110Combined sources
Turni32 – 343Combined sources
Beta strandi37 – 448Combined sources
Helixi45 – 495Combined sources
Beta strandi51 – 533Combined sources
Helixi56 – 6813Combined sources
Beta strandi77 – 837Combined sources
Beta strandi86 – 927Combined sources
Helixi99 – 10810Combined sources
Helixi115 – 13420Combined sources
Helixi144 – 1463Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi158 – 1603Combined sources
Helixi163 – 1653Combined sources
Beta strandi171 – 1733Combined sources
Helixi183 – 1853Combined sources
Helixi188 – 1914Combined sources
Helixi199 – 21416Combined sources
Helixi223 – 23210Combined sources
Helixi239 – 2424Combined sources
Helixi247 – 25610Combined sources
Turni261 – 2633Combined sources
Helixi267 – 2715Combined sources
Helixi274 – 2774Combined sources
Helixi279 – 2824Combined sources
Helixi289 – 30214Combined sources
Turni304 – 3063Combined sources
Helixi309 – 3124Combined sources
Helixi404 – 41613Combined sources
Helixi423 – 4319Combined sources
Helixi437 – 45014Combined sources
Beta strandi489 – 4957Combined sources
Beta strandi497 – 4993Combined sources
Beta strandi503 – 5064Combined sources
Helixi510 – 5123Combined sources
Beta strandi513 – 5186Combined sources
Helixi523 – 5275Combined sources
Beta strandi535 – 5395Combined sources
Helixi544 – 5463Combined sources
Helixi549 – 55810Combined sources
Beta strandi561 – 5688Combined sources
Beta strandi741 – 7455Combined sources
Helixi752 – 76211Combined sources
Turni764 – 7663Combined sources
Turni784 – 7863Combined sources
Helixi793 – 8019Combined sources
Beta strandi805 – 8117Combined sources
Beta strandi814 – 8196Combined sources
Helixi820 – 8289Combined sources
Beta strandi832 – 8365Combined sources
Helixi839 – 8413Combined sources
Helixi842 – 8454Combined sources
Turni848 – 8503Combined sources
Beta strandi852 – 8587Combined sources
Helixi870 – 88617Combined sources
Helixi887 – 8893Combined sources
Beta strandi891 – 8955Combined sources
Helixi899 – 91315Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KGDX-ray1.31A739-914[»]
1KWAX-ray1.93A/B487-572[»]
1ZL8NMR-B403-456[»]
3C0GX-ray2.19A/B1-337[»]
3C0HX-ray2.30A/B1-337[»]
3C0IX-ray1.85A1-337[»]
3MFRX-ray2.00A1-337[»]
3MFSX-ray2.10A1-337[»]
3MFTX-ray2.20A1-337[»]
3MFUX-ray2.30A1-337[»]
3TACX-ray2.20A1-345[»]
ProteinModelPortaliO14936.
SMRiO14936. Positions 5-394, 403-456, 487-572, 615-921.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14936.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 276265Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini343 – 39856L27 1PROSITE-ProRule annotationAdd
BLAST
Domaini402 – 45554L27 2PROSITE-ProRule annotationAdd
BLAST
Domaini489 – 56476PDZPROSITE-ProRule annotationAdd
BLAST
Domaini615 – 68268SH3PROSITE-ProRule annotationAdd
BLAST
Domaini739 – 911173Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni305 – 31511Calmodulin-bindingAdd
BLAST

Domaini

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.

Sequence similaritiesi

In the N-terminal section; belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.Curated
Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 2 L27 domains.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118866.
HOVERGENiHBG001858.
InParanoidiO14936.
KOiK06103.
OMAiRCINRET.
OrthoDBiEOG79CXZ5.
PhylomeDBiO14936.
TreeFamiTF314263.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR008145. 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.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00220. S_TKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00856. 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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14936-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS
60 70 80 90 100
SPGLSTEDLK REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC
110 120 130 140 150
FEIVKRADAG FVYSEAVASH YMRQILEALR YCHDNNIIHR DVKPHCVLLA
160 170 180 190 200
SKENSAPVKL GGFGVAIQLG ESGLVAGGRV GTPHFMAPEV VKREPYGKPV
210 220 230 240 250
DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR QWSHISESAK
260 270 280 290 300
DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA
310 320 330 340 350
RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV
360 370 380 390 400
LDSLEEIHAL TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN
410 420 430 440 450
PPSDAVQRAK EVLEEISCYP ENNDAKELKR ILTQPHFMAL LQTHDVVAHE
460 470 480 490 500
VYSDEALRVT PPPTSPYLNG DSPESANGDM DMENVTRVRL VQFQKNTDEP
510 520 530 540 550
MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN GISVANQTVE
560 570 580 590 600
QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS
610 620 630 640 650
VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS
660 670 680 690 700
KDDHNWWQGK LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW
710 720 730 740 750
FGKKKKQYKD KYLAKHNAVF DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV
760 770 780 790 800
GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK DEENGKNYYF VSHDQMMQDI
810 820 830 840 850
SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ ALKVLRTAEF
860 870 880 890 900
APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID
910 920
ETIRHLEEAV ELVCTAPQWV PVSWVY
Length:926
Mass (Da):105,123
Last modified:April 17, 2007 - v3
Checksum:i6C02008CE52728BA
GO
Isoform 2 (identifier: O14936-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:921
Mass (Da):104,520
Checksum:iC3C9FAE8D051AA27
GO
Isoform 3 (identifier: O14936-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:897
Mass (Da):102,114
Checksum:i8B3BC03D2EF717CA
GO
Isoform 4 (identifier: O14936-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:898
Mass (Da):102,165
Checksum:iB7BC96EB46CCD791
GO
Isoform 5 (identifier: O14936-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:518
Mass (Da):59,383
Checksum:i855EE0A1FC92D5B0
GO
Isoform 6 (identifier: O14936-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:909
Mass (Da):103,211
Checksum:iB0B98E6A73E36142
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011P → L in AAB88198. 1 PublicationCurated
Sequence conflicti479 – 4791D → G in AAB88125. (PubMed:9660868)Curated
Sequence conflicti479 – 4791D → G in BAB12252. 1 PublicationCurated
Sequence conflicti479 – 4791D → G in AAU10527. 1 PublicationCurated
Sequence conflicti479 – 4791D → G in AAF72666. (PubMed:11003712)Curated
Sequence conflicti479 – 4791D → G in AAF72667. (PubMed:11003712)Curated
Sequence conflicti675 – 6751P → S in AAB88125. (PubMed:9660868)Curated
Sequence conflicti675 – 6751P → S in AAU10527. 1 PublicationCurated
Sequence conflicti780 – 7801K → R in AAB88125. (PubMed:9660868)Curated
Sequence conflicti780 – 7801K → R in AAU10527. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281R → L in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein. 1 Publication
VAR_058719
Natural varianti96 – 961G → V in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_041956
Natural varianti268 – 2681Y → H in MICPCH. 1 Publication
VAR_062996
Natural varianti396 – 3961P → S in MICPCH. 1 Publication
VAR_062997
Natural varianti710 – 7101D → G in MICPCH. 1 Publication
VAR_062998

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 385385Missing in isoform 5. 1 PublicationVSP_024421Add
BLAST
Alternative sequencei340 – 3456Missing in isoform 3. 2 PublicationsVSP_024422
Alternative sequencei386 – 3861L → M in isoform 5. 1 PublicationVSP_024423
Alternative sequencei580 – 60223Missing in isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_024424Add
BLAST
Alternative sequencei603 – 61412Missing in isoform 6. CuratedVSP_024425Add
BLAST
Alternative sequencei719 – 7235Missing in isoform 2, isoform 4 and isoform 6. 4 PublicationsVSP_024426

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14257.1. [O14936-2]
CCDS48094.1. [O14936-3]
CCDS48095.1. [O14936-4]
RefSeqiNP_001119526.1. NM_001126054.2. [O14936-4]
NP_001119527.1. NM_001126055.2. [O14936-3]
NP_003679.2. NM_003688.3. [O14936-2]
UniGeneiHs.495984.

Genome annotation databases

EnsembliENST00000378158; ENSP00000367400; ENSG00000147044. [O14936-6]
ENST00000378163; ENSP00000367405; ENSG00000147044. [O14936-1]
ENST00000378166; ENSP00000367408; ENSG00000147044. [O14936-2]
ENST00000421587; ENSP00000400526; ENSG00000147044. [O14936-3]
ENST00000442742; ENSP00000398007; ENSG00000147044. [O14936-4]
GeneIDi8573.
KEGGihsa:8573.
UCSCiuc004dfk.4. human. [O14936-1]
uc004dfl.4. human. [O14936-2]
uc004dfm.4. human. [O14936-4]
uc004dfn.4. human. [O14936-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14257.1. [O14936-2 ]
CCDS48094.1. [O14936-3 ]
CCDS48095.1. [O14936-4 ]
RefSeqi NP_001119526.1. NM_001126054.2. [O14936-4 ]
NP_001119527.1. NM_001126055.2. [O14936-3 ]
NP_003679.2. NM_003688.3. [O14936-2 ]
UniGenei Hs.495984.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KGD X-ray 1.31 A 739-914 [» ]
1KWA X-ray 1.93 A/B 487-572 [» ]
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 [» ]
ProteinModelPortali O14936.
SMRi O14936. Positions 5-394, 403-456, 487-572, 615-921.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114141. 53 interactions.
DIPi DIP-38727N.
IntActi O14936. 34 interactions.
MINTi MINT-102444.

Chemistry

BindingDBi O14936.
ChEMBLi CHEMBL1908381.
GuidetoPHARMACOLOGYi 1959.

PTM databases

PhosphoSitei O14936.

Proteomic databases

MaxQBi O14936.
PaxDbi O14936.
PRIDEi O14936.

Protocols and materials databases

DNASUi 8573.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378158 ; ENSP00000367400 ; ENSG00000147044 . [O14936-6 ]
ENST00000378163 ; ENSP00000367405 ; ENSG00000147044 . [O14936-1 ]
ENST00000378166 ; ENSP00000367408 ; ENSG00000147044 . [O14936-2 ]
ENST00000421587 ; ENSP00000400526 ; ENSG00000147044 . [O14936-3 ]
ENST00000442742 ; ENSP00000398007 ; ENSG00000147044 . [O14936-4 ]
GeneIDi 8573.
KEGGi hsa:8573.
UCSCi uc004dfk.4. human. [O14936-1 ]
uc004dfl.4. human. [O14936-2 ]
uc004dfm.4. human. [O14936-4 ]
uc004dfn.4. human. [O14936-3 ]

Organism-specific databases

CTDi 8573.
GeneCardsi GC0XM041374.
GeneReviewsi CASK.
HGNCi HGNC:1497. CASK.
HPAi CAB001949.
HPA023857.
MIMi 300172. gene.
300422. phenotype.
300749. phenotype.
neXtProti NX_O14936.
Orphaneti 1934. Early infantile epileptic encephalopathy.
323. FG syndrome.
163937. X-linked intellectual disability, Najm type.
PharmGKBi PA26081.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118866.
HOVERGENi HBG001858.
InParanoidi O14936.
KOi K06103.
OMAi RCINRET.
OrthoDBi EOG79CXZ5.
PhylomeDBi O14936.
TreeFami TF314263.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_163942. Syndecan interactions.
REACT_23832. Nephrin interactions.
SignaLinki O14936.

Miscellaneous databases

ChiTaRSi CASK. human.
EvolutionaryTracei O14936.
GeneWikii CASK.
GenomeRNAii 8573.
NextBioi 32157.
PROi O14936.
SOURCEi Search...

Gene expression databases

Bgeei O14936.
CleanExi HS_CASK.
ExpressionAtlasi O14936. baseline and differential.
Genevestigatori O14936.

Family and domain databases

Gene3Di 2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR008145. 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.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
SMARTi SM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00220. S_TKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00856. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-337 IN COMPLEX WITH AMP, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION OF NRXN1, PHOSPHORYLATION 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. Cited for: VARIANT FGS4 LEU-28, CHARACTERIZATION OF VARIANT FGS4 LEU-28.
  15. "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.

Entry informationi

Entry nameiCSKP_HUMAN
AccessioniPrimary (citable) accession number: O14936
Secondary accession number(s): A6NES1
, B7ZKY0, O43215, Q17RI4, Q59HA0, Q5VT16, Q5VT17, Q5VT18, Q5VT19, Q66T42, Q9BYH6, Q9NYB2, Q9NYB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 17, 2007
Last modified: October 29, 2014
This is version 167 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3