ID CSKP_HUMAN STANDARD; PRT; 926 AA. AC O14936; O43215; Q9NYB3; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 19-SEP-2006, entry version 73. DE Peripheral plasma membrane protein CASK (EC 2.7.11.1) (hCASK) DE (Calcium/calmodulin-dependent serine protein kinase) (Lin-2 homolog). GN Name=CASK; Synonyms=LIN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain, Liver, and Lung; RX MEDLINE=98327121; PubMed=9660868; DOI=10.1083/jcb.142.1.129; RA Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., RA Anderson J.M.; RT "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to RT the basolateral membrane of epithelial cells."; RL J. Cell Biol. 142:129-138(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zha D., Hu G.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 173-926. RC TISSUE=Fetus; RX MEDLINE=20458875; PubMed=11003712; DOI=10.1007/s003350010170; RA Stevenson D., Laverty H.G., Wenwieser S., Douglas M., Wilson J.B.; RT "Mapping and expression analysis of the human CASK gene."; RL Mamm. Genome 11:934-937(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-572. RX MEDLINE=98206299; PubMed=9546224; RA Daniels D.L., Cohen A.R., Anderson J.M., Bruenger A.T.; RT "Crystal structure of the hCASK PDZ domain reveals the structural RT basis of class II PDZ domain target recognition."; RL Nat. Struct. Biol. 5:317-325(1998). CC -!- FUNCTION: Binds to cell-surface proteins, including amyloid CC precursor protein, neurexins, and syndecans. May mediate a link CC between the extracellular matrix and the actin cytoskeleton via CC its interaction with syndecan and with the actin/spectrin-binding CC protein 4.1. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Binds WHRN and NRXN1 cytosolic tail. Interacts with CC CASKIN1, APBA1, LIN7(A/B/C) and L27 domain of DLG1 and isoform 2 CC of DLG4 (By similarity). CASK and LIN7 form two mutually exclusive CC tripartite complexes with APBA1 or CASKIN1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: The first L27 domain binds DLG1 and the second L27 domain CC probably binds LIN7 (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the Ser/Thr CC protein kinase family. CaMK subfamily. CC -!- SIMILARITY: Belongs to the MAGUK family. CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. CC -!- SIMILARITY: Contains 2 L27 domains. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF032119; AAB88125.1; -; mRNA. DR EMBL; AF035582; AAB88198.1; -; mRNA. DR EMBL; AF262404; AAF72666.1; -; mRNA. DR PDB; 1KGD; X-ray; A=739-914. DR PDB; 1KWA; X-ray; A/B=487-572. DR PDB; 1ZL8; NMR; B=403-456. DR SMR; O14936; 339-394. DR Ensembl; ENSG00000147044; Homo sapiens. DR KEGG; hsa:8573; -. DR HGNC; HGNC:1497; CASK. DR MIM; 300172; gene. DR LinkHub; O14936; -. DR ArrayExpress; O14936; -. DR GO; GO:0015629; C:actin cytoskeleton; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0004385; F:guanylate kinase activity; TAS. DR GO; GO:0007155; P:cell adhesion; TAS. DR InterPro; IPR008144; Guanylate_kin. DR InterPro; IPR008145; Guanylt/Ca. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR004172; L27. DR InterPro; IPR001478; PDZ. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR001452; SH3. DR InterPro; IPR011511; SH3_2. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF07653; SH3_2; 1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50002; SH3; 1. KW 3D-structure; ATP-binding; Calmodulin-binding; Kinase; Membrane; KW Nucleotide-binding; Repeat; Serine/threonine-protein kinase; KW SH3 domain; Transferase. FT CHAIN 1 926 Peripheral plasma membrane protein CASK. FT /FTId=PRO_0000094568. FT DOMAIN 12 276 Protein kinase. FT DOMAIN 343 398 L27 1. FT DOMAIN 402 455 L27 2. FT DOMAIN 489 564 PDZ. FT DOMAIN 615 682 SH3. FT DOMAIN 739 911 Guanylate kinase-like. FT NP_BIND 18 26 ATP (By similarity). FT REGION 305 315 Calmodulin-binding. FT ACT_SITE 141 141 By similarity. FT BINDING 41 41 ATP (By similarity). FT CONFLICT 340 345 Missing (in Ref. 2). FT CONFLICT 401 401 P -> L (in Ref. 2). FT CONFLICT 479 479 G -> D (in Ref. 2). FT CONFLICT 580 602 Missing (in Ref. 2). FT CONFLICT 675 675 P -> S (in Ref. 1). FT CONFLICT 719 723 Missing (in Ref. 1). FT CONFLICT 780 780 K -> R (in Ref. 1). FT STRAND 736 740 FT TURN 743 744 FT STRAND 745 746 FT HELIX 747 757 FT TURN 759 761 FT STRAND 762 763 FT STRAND 768 769 FT STRAND 771 771 FT TURN 779 781 FT STRAND 782 782 FT STRAND 784 785 FT HELIX 788 796 FT TURN 797 798 FT STRAND 800 806 FT TURN 807 808 FT STRAND 809 814 FT HELIX 815 823 FT TURN 824 825 FT STRAND 827 831 FT HELIX 834 840 FT STRAND 841 842 FT TURN 843 845 FT STRAND 847 853 FT STRAND 856 856 FT TURN 859 860 FT STRAND 861 861 FT STRAND 864 864 FT HELIX 865 884 FT STRAND 886 890 FT STRAND 892 893 SQ SEQUENCE 926 AA; 105065 MW; D08D4372B8B60435 CRC64; MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGGM DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNAVF DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK DEENGKNYYF VSHDQMMQDI SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ ALKVLRTAEF APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID ETIRHLEEAV ELVCTAPQWV PVSWVY //