CSKI1_RAT
ID CSKI1_RAT Reviewed; 1430 AA.
AC Q8VHK2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Caskin-1;
DE AltName: Full=CASK-interacting protein 1;
GN Name=Caskin1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 183-193; 279-287; 308-319;
RP 727-743; 757-767; 769-782; 806-813; 888-894; 1265-1276 AND 1296-1303,
RP INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C AND NRXN1, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-722; THR-740;
RP SER-790; SER-890; SER-892 AND SER-1258, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May link the scaffolding protein CASK to downstream
CC intracellular effectors.
CC -!- SUBUNIT: Polymerizes, via the tandem SAM domains, to form long, 8 nM
CC wide fibers, upon which other proteins can assemble (By similarity).
CC Binds the CaM kinase domain of CASK. Forms a ternary complex with CASK
CC and LIN7A, LIN7B or LIN7C. Competes with APBA1 that forms a similar
CC complex with CASK and LIN7 proteins. The tripartite complex
CC CASKIN1/CASK/LIN7(A/B/C) binds the cytoplasmic tail of NRXN1.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8VHK2; Q9NYB9: ABI2; Xeno; NbExp=3; IntAct=EBI-7049475, EBI-743598;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12040031}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Localized primarily to the
CC neuropil and enriched in synaptic areas (at protein level).
CC {ECO:0000269|PubMed:12040031}.
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DR EMBL; AF451975; AAL49756.1; -; mRNA.
DR RefSeq; NP_542421.2; NM_080690.2.
DR AlphaFoldDB; Q8VHK2; -.
DR SMR; Q8VHK2; -.
DR BioGRID; 250839; 17.
DR CORUM; Q8VHK2; -.
DR IntAct; Q8VHK2; 12.
DR MINT; Q8VHK2; -.
DR STRING; 10116.ENSRNOP00000039956; -.
DR iPTMnet; Q8VHK2; -.
DR PhosphoSitePlus; Q8VHK2; -.
DR jPOST; Q8VHK2; -.
DR PaxDb; Q8VHK2; -.
DR PRIDE; Q8VHK2; -.
DR GeneID; 140722; -.
DR KEGG; rno:140722; -.
DR UCSC; RGD:620191; rat.
DR CTD; 57524; -.
DR RGD; 620191; Caskin1.
DR eggNOG; KOG0507; Eukaryota.
DR InParanoid; Q8VHK2; -.
DR OrthoDB; 75723at2759; -.
DR PhylomeDB; Q8VHK2; -.
DR PRO; PR:Q8VHK2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; IPI:UniProtKB.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR CDD; cd12062; SH3_Caskin1; 1.
DR DisProt; DP01127; -.
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 ANK repeat; Cytoplasm; Direct protein sequencing; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1430
FT /note="Caskin-1"
FT /id="PRO_0000066982"
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 474..537
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 543..607
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 348..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..471
FT /note="CASK-binding"
FT REGION 421..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1339
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:0000250|UniProtKB:Q8WXD9"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 1066
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1267
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9K8"
FT CONFLICT 782
FT /note="T -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="P -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1430 AA; 150347 MW; F2AE91EF10F5B746 CRC64;
MGKEQELVQA VKAEDVGTAQ RLLQRPRPGK AKLLGSTKKI NVNFQDPDGF SALHHAALNG
NTELISLLLE AQAAVDIKDN KGMRPLHYAA WQGRKEPMKL VLKAGSAVNV PSDEGHIPLH
LAAQHGHYDV SEMLLQHQSN PCIVDNSGKT PLDLACEFGR VGVVQLLLSS NMCAALLEPR
PGDTTDPNGT SPLHLAAKNG HIDIIRLLLQ AGIDINRQTK SGTALHEAAL CGKTEVVRLL
LDSGINAQVR NTYSQTALDI VHQFTTSQAS KEIKQLLREA SAALQVRATK DYCNNYDLTS
LNVKAGDIIT VLEQHPDGRW KGCIHDNRTG NDRVGYFPSS LGEAIVKRAG SRTGSEPSPP
QGGGSLGPSA PPEEIWVLRK PFAGGDRSGS LSNVAGGRST GGHALHAGAE GVKLLATVLS
QKSVSESSPG DSPVKPPEGS SGAARSQPPA AHAGQVYGEQ PPKKLESSSA SEGKSAEAVS
QWLATFQLQL YAPNFTSAGY DLPTISRMTP EDLTAIGVTK PGHRKKITAE ISGLNIPDCL
PEHKPANLAV WLSMIGLAQY YKVLVDNGYE NIDFITDITW EDLQEIGITK LGHQKKLMLA
VRKLAELQKA EYSKYEGGPL RRKAPQSLEM MAIESPPPSE PAAAECQSPK MTTFQDSELS
GELQAALSGP AEAGAAAAEK SSNHLPATPR TTSRQESSLS GRARHMSSSQ ELLGDGPQGP
GSPMSRSQEY LLDEGPAPGT PPKEVRSSRH GHSVKRASVP PVPGKPRQVL PSGVSHFTPP
QTPTKAQPGS PQALGGPHGP ATAKVKPTPQ LLPPTDRPMS PRSLPQSPTH RGFAYVLPQP
VEGEAGPPAP GPVPPPVPAA VPTLCLPPEA DVEPRRPKKR AHSLNRYAAS DSEPERDELL
VPAAAGPYAT VQRRVGRSHS VRAPAGTDKN VNRSQSFAVR PRKKGPPPPP PKRSSSAMAS
ANLADEPSPD VETEDGRLGV RAQRRRASDL AGSVDTGSAG SVKSIAAMLE LSSIGGGGRA
IRRPPEGHPT PRPASPDPGR VATVLASVKH KEAIGPDGEV VNRRRTLSGP VTGLLATARR
GPGEPAEQSH FMEDGTARQR LRGPAKGEAG VEGPPLARVE ASATLKRRIR AKQSQQENVK
FILTESDTVK RRPKAKEPDI GPEPPPPLSV YQNGTATIRR RPASEQAGPP ELPPPPPPAE
PPPTDLMPLP PLPLPDGSAR KPVKPPVSPK PILAQPVSKI QGSPTPASKK VPLPGPGSPE
VKRAHGTPPP VSPKPPPPPT APKPAKALAG LQSSSATPSP VPSPARQPPA ALIKPASSPP
SQSASPAKPP SPGAPALQVP TKPPRAAASV VSGPPVASDC ASPGDSARQK LEETSACLAA
ALQAVEEKIR QEDGQGPRPS SIEEKSTGSI LEDIGSMFDD LADQLDAMLE
