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 10-OCT-2003 (Rel. 42, 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 CASK OR LIN2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain, Liver, and Lung; RX MEDLINE=98327121; PubMed=9660868; 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 SEQUENCE FROM N.A. RA Zha D., Hu G.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 173-926 FROM N.A. RC TISSUE=Fetal; RX MEDLINE=20458875; PubMed=11003712; 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: Bind 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 -!- SUBCELLULAR LOCATION: Cytoplasmic (Potential). CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE SER/THR CC FAMILY OF PROTEIN KINASES. CAMK SUBFAMILY. CC -!- SIMILARITY: Belongs to the MAGUK family. CC LIN-27/CASK SUBFAMILY. CC -!- SIMILARITY: Contains 1 PDZ/DHR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SIMILARITY: Contains 1 guanylate kinase-like 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; -. DR EMBL; AF035582; AAB88198.1; -. DR EMBL; AF262404; AAF72666.1; -. DR PDB; 1KWA; 27-MAY-98. DR PDB; 1KGD; 13-FEB-02. DR Genew; 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:0004384; F:membrane-associated guanylate kinase; 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; IPR001245; Tyr_pkinase. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00069; pkinase; 1. DR Pfam; PF00018; SH3; 1. 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 SMART; SM00219; TyrKc; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. 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 Transferase; Serine/threonine-protein kinase; ATP-binding; SH3 domain; KW Membrane; Calmodulin-binding; 3D-structure. FT DOMAIN 12 276 PROTEIN KINASE. FT DOMAIN 305 315 CALMODULIN-BINDING. FT DOMAIN 489 564 PDZ. FT DOMAIN 615 682 SH3. FT DOMAIN 739 926 GUANYLATE KINASE. FT NP_BIND 18 26 ATP (BY SIMILARITY). FT BINDING 41 41 ATP (BY SIMILARITY). FT ACT_SITE 141 141 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 SQ SEQUENCE 926 AA; 105064 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 //