CSKI1_HUMAN
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 03-AUG-2022, entry version 156.
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}.
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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; 3.
DR DIP; DIP-34890N; -.
DR IntAct; Q8WXD9; 3.
DR STRING; 9606.ENSP00000345436; -.
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; Q8WXD9; -.
DR PeptideAtlas; Q8WXD9; -.
DR PRIDE; Q8WXD9; -.
DR ProteomicsDB; 75015; -.
DR Antibodypedia; 61351; 26 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 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; KPPNHLP; -.
DR OrthoDB; 75723at2759; -.
DR PhylomeDB; Q8WXD9; -.
DR TreeFam; TF320582; -.
DR PathwayCommons; Q8WXD9; -.
DR SignaLink; Q8WXD9; -.
DR SIGNOR; Q8WXD9; -.
DR BioGRID-ORCS; 57524; 14 hits in 1069 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 tissues.
DR Genevisible; Q8WXD9; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; 1.10.150.50; -; 2.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR027013; Caskin-1/2.
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:SF11; PTHR24174:SF11; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 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; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 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.
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
