ID CSKP_HUMAN STANDARD; PRT; 926 AA. AC O14936; O43215; Q9NYB3; DT 15-JUL-1999 (Rel. 38, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Peripheral plasma membrane protein CASK (EC 2.7.1.-) (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; Catarrhini; Hominidae; OC 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=Fetal; 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 -!- 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: Cytoplasmic (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 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=489-572. DR SMR; O14936; 339-394, 487-572, 739-914. DR Ensembl; ENSG00000147044; Homo sapiens. DR HGNC; HGNC:1497; CASK. DR MIM; 300172; -. 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; 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 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 489 495 FT STRAND 503 506 FT HELIX 510 512 FT STRAND 513 518 FT TURN 520 521 FT HELIX 523 527 FT TURN 528 528 FT TURN 532 533 FT STRAND 535 539 FT TURN 540 541 FT STRAND 542 543 FT HELIX 544 546 FT HELIX 549 558 FT STRAND 561 568 FT STRAND 741 745 FT TURN 748 749 FT HELIX 752 762 FT TURN 764 766 FT STRAND 767 768 FT STRAND 773 774 FT STRAND 784 784 FT TURN 785 787 FT STRAND 788 790 FT HELIX 793 801 FT TURN 802 803 FT STRAND 805 811 FT TURN 812 813 FT STRAND 814 819 FT HELIX 820 828 FT TURN 829 830 FT STRAND 832 836 FT HELIX 839 841 FT HELIX 842 845 FT TURN 848 850 FT STRAND 852 858 FT TURN 864 865 FT HELIX 870 886 FT HELIX 887 889 FT STRAND 892 895 FT HELIX 899 913 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 //