ID Q9NYB2_HUMAN PRELIMINARY; PRT; 871 AA. AC Q9NYB2; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Calcium/calmodulin-dependent serine protein kinase membrane-associated DE guanylate kinase (Fragment). GN Name=CASK; 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. 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). 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 (By similarity). CC -!- SUBUNIT: Binds WHRN. Interacts with APBA1, LIN7 and DLG1 (By CC similarity). CC -!- DOMAIN: The first L27 domain binds DLG1 and the second L27 domain CC probably binds LIN7 (By similarity). 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; AF262405; AAF72667.1; -. DR HSSP; O14936; 1KGD. DR Ensembl; ENSG00000147044; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA. DR GO; GO:0005515; F:protein binding; IEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA. 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; 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 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; SM00326; SH3; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50002; SH3; 1. KW Calmodulin-binding; Kinase; Membrane; Repeat; SH3 domain. FT NON_TER 1 1 SQ SEQUENCE 871 AA; 99183 MW; 5682D4EB24FC81AA CRC64; RRCINRETGQ QFAVKIVDVA KFTSSPGLST EDLKREASIC HMLKHPHIVE LLETYSSDGM LYMVFEFMDG ADLCFEIVKR ADAGFVYSEA VASHYMRQIL EALRYCHDNN IIHRDVKPHC VLLASKENSA PVKLGGFGVA IQLGESGLVA GGRVGTPHFM APEVVKREPY GKPVDVWGCG VILFILLSGC LPFYGTKERL FEGIIKGKYK MNPRQWSHIS ESAKDLVRRM LMLDPAERIT VYEALNHPWL KERDRYAYKI HLPETVEQLR KFNARRKLKG AVLAAVSSHK FNSFYGDPPE ELPDFSEDPT SSGAVSQVLD SLEEIHALTD CSEKDLDFLH SVFQDQHLHT LLDLYDKINT KSSPQIRNPP SDAVQRAKEV LEEISCYPEN NDAKELKRIL TQPHFMALLQ THDVVAHEVY SDEALRVTPP PTSPYLNGDS PESANGGMDM ENVTRVRLVQ FQKNTDEPMG ITLKMNELNH CIVARIMHGG MIHRQGTLHV GDEIREINGI SVANQTVEQL QKMLREMRGS ITFKIVPSYR TQSSSCEDLP STTQPKGRQI YVRAQFEYDP AKDDLIPCKE AGIRFRVGDI IQIISKDDHN WWQGKLENSK NGTAGLIPSP ELQEWRVACI AMEKTKQEQQ ASCTWFGKKK KQYKDKYLAK HNAVFDQLDL VTYEEVVKLP AFKRKTLVLL GAHGVGRRHI KNTLITKHPD RFAYPIPHTT RPPKKDEENG KNYYFVSHDQ MMQDISNNEY LEYGSHEDAM YGTKLETIRK IHEQGLIAIL DVEPQALKVL RTAEFAPFVV FIAAPTITPG LNEDESLQRL QKESDILQRT YAHYFDLTII NNEIDETIRH LEEAVELVCT APQWVPVSWV Y //