ID CSKI1_HUMAN Reviewed; 1431 AA. AC Q8WXD9; Q9P2P0; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Caskin-1; DE AltName: Full=CASK-interacting protein 1; GN Name=CASKIN1; Synonyms=KIAA1306; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12040031; DOI=10.1523/jneurosci.22-11-04264.2002; RA Tabuchi K., Biederer T., Butz S., Suedhof T.C.; RT "CASK participates in alternative tripartite complexes in which Mint 1 RT competes for binding with Caskin 1, a novel CASK-binding protein."; RL J. Neurosci. 22:4264-4273(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-1431. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787 AND SER-1257, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [4] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-398, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 470-605, AND SUBUNIT. RX PubMed=22153505; DOI=10.1016/j.str.2011.09.018; RA Stafford R.L., Hinde E., Knight M.J., Pennella M.A., Ear J., Digman M.A., RA Gratton E., Bowie J.U.; RT "Tandem SAM domain structure of human Caskin1: a presynaptic, self- RT assembling scaffold for CASK."; RL Structure 19:1826-1836(2011). CC -!- FUNCTION: May link the scaffolding protein CASK to downstream CC intracellular effectors. {ECO:0000250}. CC -!- SUBUNIT: Binds the CaM kinase domain of CASK. Forms a ternary complex CC with CASK and LIN7A, LIN7B or LIN7C. Competes with APBA1 that forms a CC similar complex with CASK and LIN7 proteins. The tripartite complex CC CASKIN1/CASK/LIN7(A/B/C) binds the cytoplasmic tail of NRXN1 (By CC similarity). Polymerizes, via the tandem SAM domains, to form long, 8 CC nM wide fibers, upon which other proteins can assemble. {ECO:0000250, CC ECO:0000269|PubMed:22153505}. CC -!- INTERACTION: CC Q8WXD9; O14936: CASK; NbExp=4; IntAct=EBI-970261, EBI-1215506; CC Q8WXD9; O14936-2: CASK; NbExp=2; IntAct=EBI-970261, EBI-15957318; CC Q8WXD9; Q8WXD9: CASKIN1; NbExp=8; IntAct=EBI-970261, EBI-970261; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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; AF451977; AAL49758.1; -; mRNA. DR EMBL; AB037727; BAA92544.1; -; mRNA. DR CCDS; CCDS42103.1; -. DR RefSeq; NP_065815.1; NM_020764.3. DR PDB; 3SEI; X-ray; 2.40 A; A/B=470-605. DR PDB; 3SEN; X-ray; 3.10 A; A/B/C/D=470-613. DR PDB; 7ATY; NMR; -; A=284-346. DR PDBsum; 3SEI; -. DR PDBsum; 3SEN; -. DR PDBsum; 7ATY; -. DR AlphaFoldDB; Q8WXD9; -. DR SMR; Q8WXD9; -. DR BioGRID; 121585; 5. DR DIP; DIP-34890N; -. DR IntAct; Q8WXD9; 4. DR STRING; 9606.ENSP00000345436; -. DR GlyCosmos; Q8WXD9; 2 sites, 1 glycan. DR GlyGen; Q8WXD9; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8WXD9; -. DR PhosphoSitePlus; Q8WXD9; -. DR BioMuta; CASKIN1; -. DR DMDM; 61213003; -. DR EPD; Q8WXD9; -. DR jPOST; Q8WXD9; -. DR MassIVE; Q8WXD9; -. DR MaxQB; Q8WXD9; -. DR PaxDb; 9606-ENSP00000345436; -. DR PeptideAtlas; Q8WXD9; -. DR ProteomicsDB; 75015; -. DR Antibodypedia; 61351; 27 antibodies from 15 providers. DR DNASU; 57524; -. DR Ensembl; ENST00000343516.8; ENSP00000345436.6; ENSG00000167971.16. DR GeneID; 57524; -. DR KEGG; hsa:57524; -. DR MANE-Select; ENST00000343516.8; ENSP00000345436.6; NM_020764.4; NP_065815.1. DR UCSC; uc010bsg.2; human. DR AGR; HGNC:20879; -. DR CTD; 57524; -. DR DisGeNET; 57524; -. DR GeneCards; CASKIN1; -. DR HGNC; HGNC:20879; CASKIN1. DR HPA; ENSG00000167971; Tissue enriched (brain). DR MIM; 612184; gene. DR neXtProt; NX_Q8WXD9; -. DR OpenTargets; ENSG00000167971; -. DR PharmGKB; PA134878267; -. DR VEuPathDB; HostDB:ENSG00000167971; -. DR eggNOG; KOG0507; Eukaryota. DR GeneTree; ENSGT00940000158025; -. DR HOGENOM; CLU_003619_1_1_1; -. DR InParanoid; Q8WXD9; -. DR OMA; LFCLHGQ; -. DR OrthoDB; 25046at2759; -. DR PhylomeDB; Q8WXD9; -. DR TreeFam; TF320582; -. DR PathwayCommons; Q8WXD9; -. DR SignaLink; Q8WXD9; -. DR SIGNOR; Q8WXD9; -. DR BioGRID-ORCS; 57524; 14 hits in 1147 CRISPR screens. DR ChiTaRS; CASKIN1; human. DR GenomeRNAi; 57524; -. DR Pharos; Q8WXD9; Tdark. DR PRO; PR:Q8WXD9; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q8WXD9; Protein. DR Bgee; ENSG00000167971; Expressed in right frontal lobe and 120 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB. DR CDD; cd09497; SAM_caskin1_2_repeat1; 1. DR CDD; cd09498; SAM_caskin1_2_repeat2; 1. DR CDD; cd12062; SH3_Caskin1; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2. DR InterPro; IPR033635; ANKS1/Caskin. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR032232; Caskin1-CID. DR InterPro; IPR035497; Caskin1/2_SAM_1. DR InterPro; IPR035498; Caskin1/2_SAM_2. DR InterPro; IPR035495; Caskin1_SH3. DR InterPro; IPR032117; Caskin_C. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR24174:SF11; CASKIN-1; 1. DR Pfam; PF12796; Ank_2; 2. DR Pfam; PF13637; Ank_4; 1. DR Pfam; PF16907; Caskin-Pro-rich; 1. DR Pfam; PF16632; Caskin-tail; 1. DR Pfam; PF16600; Caskin1-CID; 1. DR Pfam; PF00536; SAM_1; 2. DR Pfam; PF07653; SH3_2; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 6. DR SMART; SM00454; SAM; 2. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 2. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 6. DR PROSITE; PS50105; SAM_DOMAIN; 2. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q8WXD9; HS. PE 1: Evidence at protein level; KW 3D-structure; ANK repeat; Cytoplasm; Methylation; Phosphoprotein; KW Reference proteome; Repeat; SH3 domain. FT CHAIN 1..1431 FT /note="Caskin-1" FT /id="PRO_0000066980" FT REPEAT 48..77 FT /note="ANK 1" FT REPEAT 81..110 FT /note="ANK 2" FT REPEAT 114..143 FT /note="ANK 3" FT REPEAT 147..176 FT /note="ANK 4" FT REPEAT 188..217 FT /note="ANK 5" FT REPEAT 220..249 FT /note="ANK 6" FT DOMAIN 281..347 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 472..535 FT /note="SAM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT DOMAIN 541..605 FT /note="SAM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT REGION 348..373 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..469 FT /note="CASK-binding" FT /evidence="ECO:0000250" FT REGION 387..406 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 421..447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 630..977 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1014..1039 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1072..1377 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1390..1416 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 356..370 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 644..660 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 681..702 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..862 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 871..897 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1143..1160 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1186..1232 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1265..1284 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1296..1338 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 253 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 358 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 398 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 432 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 633 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 646 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 719 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VHK2" FT MOD_RES 724 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 737 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8VHK2" FT MOD_RES 787 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 889 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VHK2" FT MOD_RES 891 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VHK2" FT MOD_RES 987 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 1065 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 1067 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 1257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1266 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT MOD_RES 1364 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P9K8" FT CONFLICT 278 FT /note="R -> P (in Ref. 2; BAA92544)" FT /evidence="ECO:0000305" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 303..311 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 320..325 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 334..339 FT /evidence="ECO:0007829|PDB:7ATY" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:7ATY" FT HELIX 470..482 FT /evidence="ECO:0007829|PDB:3SEI" FT TURN 483..485 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 487..489 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 490..495 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 500..503 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 508..513 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 519..530 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 546..552 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 556..558 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 559..564 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 570..573 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 578..584 FT /evidence="ECO:0007829|PDB:3SEI" FT HELIX 589..605 FT /evidence="ECO:0007829|PDB:3SEI" SQ SEQUENCE 1431 AA; 149814 MW; CDF60E68B81E884A CRC64; MGKEQELVQA VKAEDVGTAQ RLLQRPRPGK AKLLGSTKKI NVNFQDPDGF SALHHAALNG NTELISLLLE AQAAVDIKDN KGMRPLHYAA WQGRKEPMKL VLKAGSAVNI PSDEGHIPLH LAAQHGHYDV SEMLLQHQSN PCMVDNSGKT PLDLACEFGR VGVVQLLLSS NMCAALLEPR PGDATDPNGT SPLHLAAKNG HIDIIRLLLQ AGIDINRQTK SGTALHEAAL CGKTEVVRLL LDSGINAHVR NTYSQTALDI VHQFTTSQAS REIKQLLREA SAALQVRATK DYCNNYDLTS LNVKAGDIIT VLEQHPDGRW KGCIHDNRTG NDRVGYFPSS LGEAIVKRAG SRAGTEPSLP QGSSSSGPSA PPEEIWVLRK PFAGGDRSGS ISGMAGGRGS GGHALHAGSE GVKLLATVLS QKSVSESGPG DSPAKPPEGS AGVARSQPPV AHAGQVYGEQ PPKKLEPASE GKSSEAVSQW LTAFQLQLYA PNFISAGYDL PTISRMTPED LTAIGVTKPG HRKKIAAEIS GLSIPDWLPE HKPANLAVWL SMIGLAQYYK VLVDNGYENI DFITDITWED LQEIGITKLG HQKKLMLAVR KLAELQKAEY AKYEGGPLRR KAPQSLEVMA IESPPPPEPT PADCQSPKMT TFQDSELSDE LQAAMTGPAE VGPTTEKPSS HLPPTPRATT RQDSSLGGRA RHMSSSQELL GDGPPGPSSP MSRSQEYLLD EGPAPGTPPR EARPGRHGHS IKRASVPPVP GKPRQVLPPG TSHFTPPQTP TKTRPGSPQA LGGPHGPAPA TAKVKPTPQL LPPTERPMSP RSLPQSPTHR GFAYVLPQPV EGEVGPAAPG PAPPPVPTAV PTLCLPPEAD AEPGRPKKRA HSLNRYAASD SEPERDELLV PAAAGPYATV QRRVGRSHSV RAPAGADKNV NRSQSFAVRP RKKGPPPPPP KRSSSALASA NLADEPVPDA EPEDGLLGVR AQCRRASDLA GSVDTGSAGS VKSIAAMLEL SSIGGGGRAA RRPPEGHPTP RPASPEPGRV ATVLASVKHK EAIGPGGEVV NRRRTLSGPV TGLLATARRG PGESADPGPF VEDGTGRQRP RGPSKGEAGV EGPPLAKVEA SATLKRRIRA KQNQQENVKF ILTESDTVKR RPKAKEREAG PEPPPPLSVY HNGTGTVRRR PASEQAGPPE LPPPPPPAEP PPTDLAHLPP LPPPEGEARK PAKPPVSPKP VLTQPVPKLQ GSPTPTSKKV PLPGPGSPEV KRAHGTPPPV SPKPPPPPTA PKPVKAVAGL PSGSAGPSPA PSPARQPPAA LAKPPGTPPS LGASPAKPPS PGAPALHVPA KPPRAAAAAA AAAAAPPAPP EGASPGDSAR QKLEETSACL AAALQAVEEK IRQEDAQGPR DSAAEKSTGS ILDDIGSMFD DLADQLDAML E //