ID CSKI2_MOUSE Reviewed; 1201 AA.
AC Q8VHK1; B1ATA2; Q6ZPX1; Q7TS77;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Caskin-2;
GN Name=Caskin2; Synonyms=Kiaa1139;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371; SER-403; SER-406;
RP SER-409; SER-874; SER-875 AND THR-880, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: May not bind CASK.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98107.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF451978; AAL49759.1; -; mRNA.
DR EMBL; AK129297; BAC98107.1; ALT_INIT; mRNA.
DR EMBL; AL645852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053083; AAH53083.1; -; mRNA.
DR CCDS; CCDS25647.1; -.
DR RefSeq; NP_542374.2; NM_080643.2.
DR AlphaFoldDB; Q8VHK1; -.
DR BMRB; Q8VHK1; -.
DR SMR; Q8VHK1; -.
DR STRING; 10090.ENSMUSP00000041328; -.
DR GlyGen; Q8VHK1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8VHK1; -.
DR PhosphoSitePlus; Q8VHK1; -.
DR MaxQB; Q8VHK1; -.
DR PaxDb; 10090-ENSMUSP00000041328; -.
DR PeptideAtlas; Q8VHK1; -.
DR ProteomicsDB; 285322; -.
DR Pumba; Q8VHK1; -.
DR Antibodypedia; 53193; 199 antibodies from 26 providers.
DR DNASU; 140721; -.
DR Ensembl; ENSMUST00000041684.11; ENSMUSP00000041328.5; ENSMUSG00000034471.13.
DR GeneID; 140721; -.
DR KEGG; mmu:140721; -.
DR UCSC; uc007mip.1; mouse.
DR AGR; MGI:2157062; -.
DR CTD; 57513; -.
DR MGI; MGI:2157062; Caskin2.
DR VEuPathDB; HostDB:ENSMUSG00000034471; -.
DR eggNOG; KOG0507; Eukaryota.
DR eggNOG; KOG4384; Eukaryota.
DR GeneTree; ENSGT00940000158256; -.
DR HOGENOM; CLU_003619_2_0_1; -.
DR InParanoid; Q8VHK1; -.
DR OMA; PRCKERE; -.
DR OrthoDB; 25046at2759; -.
DR PhylomeDB; Q8VHK1; -.
DR TreeFam; TF320582; -.
DR BioGRID-ORCS; 140721; 4 hits in 77 CRISPR screens.
DR PRO; PR:Q8VHK1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VHK1; Protein.
DR Bgee; ENSMUSG00000034471; Expressed in brain blood vessel and 242 other cell types or tissues.
DR ExpressionAtlas; Q8VHK1; baseline and differential.
DR Genevisible; Q8VHK1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR CDD; cd12063; SH3_Caskin2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
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; IPR035499; Caskin2_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:SF18; CASKIN-2; 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; 7.
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; 5.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..1201
FT /note="Caskin-2"
FT /id="PRO_0000066984"
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 488..551
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 557..621
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 355..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE0"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 880
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 29
FT /note="A -> T (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="S -> P (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..381
FT /note="AADDPLPS -> PAEEPPHP (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> G (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="G -> V (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="A -> P (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="P -> L (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="H -> Q (in Ref. 1; AAL49759)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="G -> S (in Ref. 1; AAL49759 and 2; BAC98107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1201 AA; 126779 MW; B930742E6D407DB3 CRC64;
MGREQDLILA VKNGDVTCVQ KLVAKVKAAK TKLLGSTKRL NINYQDADGF SALHHAALGG
SLELIALLLE AQATVDIKDS NGMRPLHYAA WQGRLEPVRL LLRASAAVNA ASLDGQIPLH
LAAQYGHYEV SEMLLQHQSN PCLVNKLKKT PLDLACEFGR LKVAQLLLNS HLCVALLEGE
AKDPCDPNYT TPLHLAAKNG HREVIRQLLK AGIEINRQTK TGTALHEAAL YGKTEVVRLL
LEGGVDVNIR NTYNQTALDI VNQFTTSQAS REIKQLLREA SGILKVRALK DFWNLHDPTA
LNVRAGDVIT VLEQHPDGRW KGHIHESQRG TDRVGYFPPG IVEVVSKRVG IPVARLPSAP
TPLRPSFSRI SQPAADDPLP SVPYGQLPRV GLSPDSPAGD RNSVGSEGSV GSIRSAGSGQ
SSEGTNGHGT GLLIENAQPL PSASEDQGLP GLHAPSPADN LSHRPLAGYR SGEIFTQDVR
PEQLLEGKDA QAIHNWLSEF QLEGYTAHFL QAGYDVPTIS RMTPEDLTAI GVTKPGHRKK
IASEIAQLSI AEWLPNYIPV DLLEWLCALG LPQYHKQLVS SGYDSMGLVA DLTWEELQEI
GVNKLGHQKK LMLGVKRLAE LRRGLLHGEA LGEGGRRMTR GPELMAIEGL ENGEGPTTAG
PRLLTFQGSE LSPELQAAMA GGGSEPLPLP PARSPSQESI GARSRGSGHS QEQPVPQPSV
GDPSAPQERN LPEGTERPSK LCSPLPGQGP APYVFMCPQN LPSSPAPGPP PGVPRAFSYL
AGSPAAPPDP PRPKRRSHSL SRPGPAEGEA EGEAEGPVGS ALGSYATLTR RPGRSTLART
SPSLTPTRGT PRSQSFALRA RRKGPPPPPP KRLSSVSGST EPPSLDGTSG PKEGATGPRR
RTLSEPTGPS ESPGPSAPTG PVSDTEEEPG PEGTPPSRGS SGEGLPFAEE GNLTIKQRPK
PAGPPPRETP VPPGLDFNLT ESDTVKRRPK CKEREPLQTA LLAFGVVGSD TPGPSNPLST
QAPCDPPSAS SNPPQRSEPS VLPSQGTSAS SLSSVTQSPG HPGPSAGPAL ANSTGSKPNV
ETEPPAPPAA LLKVPGAGTA PKPVSVACTQ LAFSGPKLAP RLGPRPVPPP RPENTGPVCP
GRAQQRLEQT SSSLEAALRA AEKSIGTEER DGPTGTSTKH ILDDISTMFD ALADQLDAML
D
//
