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CLIP2_MOUSE
ID   CLIP2_MOUSE             Reviewed;        1047 AA.
AC   Q9Z0H8; Q7TSI9; Q8CHU1; Q9EP81;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=CAP-Gly domain-containing linker protein 2;
DE   AltName: Full=Cytoplasmic linker protein 115;
DE            Short=CLIP-115;
DE   AltName: Full=Cytoplasmic linker protein 2;
GN   Name=Clip2; Synonyms=Cyln2, Kiaa0291;
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 [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=9799601; DOI=10.1006/geno.1998.5529;
RA   Hoogenraad C.C., Eussen B.H.J., Langeveld A., van Haperen R.,
RA   Winterberg S., Wouters C.H., Grosveld F., de Zeeuw C.I., Galjart N.;
RT   "The murine CYLN2 gene: genomic organization, chromosome localization, and
RT   comparison to the human gene that is located within the 7q11.23 Williams
RT   syndrome critical region.";
RL   Genomics 53:348-358(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RA   Green E.D.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   [4]
RP   INTERACTION WITH CLASP1 AND CLASP2.
RX   PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA   Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA   Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA   Galjart N.;
RT   "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT   regulation of microtubule dynamics in motile fibroblasts.";
RL   Cell 104:923-935(2001).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9427243; DOI=10.1016/s0896-6273(00)80411-0;
RA   de Zeeuw C.I., Hoogenraad C.C., Goedknegt E., Hertzberg E., Neubauer A.,
RA   Grosveld F.G., Galjart N.J.;
RT   "CLIP-115, a novel brain specific cytoplasmic linker protein, mediates the
RT   localisation of dendritic lamellar bodies.";
RL   Neuron 19:1187-1199(1997).
RN   [6]
RP   SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
RX   PubMed=16954346; DOI=10.1083/jcb.200512058;
RA   Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K.,
RA   Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J.,
RA   Andrieux A., Job D.;
RT   "Tubulin tyrosination is a major factor affecting the recruitment of CAP-
RT   Gly proteins at microtubule plus ends.";
RL   J. Cell Biol. 174:839-849(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-208; SER-212;
RP   SER-315; SER-974 AND SER-980, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC   Spleen;
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   -!- FUNCTION: Seems to link microtubules to dendritic lamellar body (DLB),
CC       a membranous organelle predominantly present in bulbous dendritic
CC       appendages of neurons linked by dendrodendritic gap junctions. May
CC       operate in the control of brain-specific organelle translocations (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CLASP1 and CLASP2 (PubMed:11290329). Binds
CC       preferentially to tyrosinated microtubules, and only marginally to
CC       detyrosinated microtubules (PubMed:16954346).
CC       {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:16954346}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55156}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Note=Localizes
CC       preferentially to the ends of tyrosinated microtubules.
CC       {ECO:0000269|PubMed:16954346}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z0H8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z0H8-2; Sequence=VSP_015683;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, and very low levels in
CC       kidneys. {ECO:0000269|PubMed:9427243}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 10.5 dpc, expression declines until
CC       birth after which it suddenly increases. Expression gradually decreases
CC       until postnatal day 10, (the day when DLBs start to occur), then again
CC       increases and reaches the levels present in adult brain.
CC       {ECO:0000269|PubMed:9427243}.
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DR   EMBL; AJ228863; CAA13068.1; -; Genomic_DNA.
DR   EMBL; AJ228865; CAA13069.1; -; Genomic_DNA.
DR   EMBL; AJ228868; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228869; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228870; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228872; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228876; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228880; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228867; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228875; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228871; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228873; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228877; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228866; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228879; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228878; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228874; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AF289667; AAF99340.1; -; Genomic_DNA.
DR   EMBL; AF289664; AAF99333.1; -; Genomic_DNA.
DR   EMBL; BC039162; AAH39162.1; -; mRNA.
DR   EMBL; BC053048; AAH53048.1; -; mRNA.
DR   CCDS; CCDS39309.1; -. [Q9Z0H8-2]
DR   CCDS; CCDS39310.1; -. [Q9Z0H8-1]
DR   PIR; T42720; T42720.
DR   RefSeq; NP_001034251.1; NM_001039162.2. [Q9Z0H8-2]
DR   RefSeq; NP_034120.2; NM_009990.3. [Q9Z0H8-1]
DR   AlphaFoldDB; Q9Z0H8; -.
DR   SMR; Q9Z0H8; -.
DR   BioGRID; 234703; 11.
DR   IntAct; Q9Z0H8; 7.
DR   MINT; Q9Z0H8; -.
DR   STRING; 10090.ENSMUSP00000098212; -.
DR   iPTMnet; Q9Z0H8; -.
DR   PhosphoSitePlus; Q9Z0H8; -.
DR   SwissPalm; Q9Z0H8; -.
DR   EPD; Q9Z0H8; -.
DR   jPOST; Q9Z0H8; -.
DR   MaxQB; Q9Z0H8; -.
DR   PaxDb; Q9Z0H8; -.
DR   PeptideAtlas; Q9Z0H8; -.
DR   PRIDE; Q9Z0H8; -.
DR   ProteomicsDB; 279107; -. [Q9Z0H8-1]
DR   ProteomicsDB; 279108; -. [Q9Z0H8-2]
DR   Antibodypedia; 14611; 168 antibodies from 25 providers.
DR   DNASU; 269713; -.
DR   Ensembl; ENSMUST00000036999; ENSMUSP00000037431; ENSMUSG00000063146. [Q9Z0H8-2]
DR   Ensembl; ENSMUST00000100647; ENSMUSP00000098212; ENSMUSG00000063146. [Q9Z0H8-1]
DR   GeneID; 269713; -.
DR   KEGG; mmu:269713; -.
DR   UCSC; uc008zwi.2; mouse. [Q9Z0H8-1]
DR   UCSC; uc008zwj.2; mouse. [Q9Z0H8-2]
DR   CTD; 7461; -.
DR   MGI; MGI:1313136; Clip2.
DR   VEuPathDB; HostDB:ENSMUSG00000063146; -.
DR   eggNOG; KOG4568; Eukaryota.
DR   GeneTree; ENSGT00940000159426; -.
DR   HOGENOM; CLU_001753_0_0_1; -.
DR   InParanoid; Q9Z0H8; -.
DR   OMA; GTQYFAC; -.
DR   OrthoDB; 1110101at2759; -.
DR   PhylomeDB; Q9Z0H8; -.
DR   TreeFam; TF326096; -.
DR   BioGRID-ORCS; 269713; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Clip2; mouse.
DR   PRO; PR:Q9Z0H8; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9Z0H8; protein.
DR   Bgee; ENSMUSG00000063146; Expressed in cortical plate and 125 other tissues.
DR   Genevisible; Q9Z0H8; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR   GO; GO:1901588; C:dendritic microtubule; ISO:MGI.
DR   GO; GO:0042599; C:lamellar body; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   Gene3D; 2.30.30.190; -; 2.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR028394; CLIP2.
DR   PANTHER; PTHR18916:SF10; PTHR18916:SF10; 1.
DR   Pfam; PF01302; CAP_GLY; 2.
DR   SMART; SM01052; CAP_GLY; 2.
DR   SUPFAM; SSF74924; SSF74924; 2.
DR   PROSITE; PS00845; CAP_GLY_1; 2.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1047
FT                   /note="CAP-Gly domain-containing linker protein 2"
FT                   /id="PRO_0000083516"
FT   DOMAIN          100..142
FT                   /note="CAP-Gly 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   DOMAIN          240..282
FT                   /note="CAP-Gly 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          355..525
FT                   /evidence="ECO:0000255"
FT   COILED          564..637
FT                   /evidence="ECO:0000255"
FT   COILED          677..1017
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        22..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O55156"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         924
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UDT6"
FT   MOD_RES         974
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         980
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         462..496
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015683"
FT   CONFLICT        25
FT                   /note="V -> I (in Ref. 3; AAH39162)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="T -> A (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="D -> H (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="G -> A (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334..335
FT                   /note="RP -> PA (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="T -> I (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        559
FT                   /note="R -> D (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        713..719
FT                   /note="SQHRLEL -> AASAEA (in Ref. 1; CAA13068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        733
FT                   /note="A -> V (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        856
FT                   /note="A -> V (in Ref. 1; CAA13068/CAA13069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1003
FT                   /note="N -> D (in Ref. 3; AAH39162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1047 AA;  115910 MW;  8F46948122F58872 CRC64;
     MQKPSGLKPP GRGGKHSSPV GRPSVGSASS SVVASTSGSK EGSPLHKQAS GPSSSGAATT
     VSEKPGPKAA EVGDDFLGDF VVGERVWVNG VKPGVVQYLG ETQFAPGQWA GVVLDDPVGK
     NDGAVGGVRY FECPALQGIF TRPSKLTRQP TAEGSGSDTH SVESLTAQNL SLHSGTATPP
     LTGRVIPLRE SVLNSSVKTG NESGSNLSDS GSVKRGDKDL HLGDRVLVGG TKTGVVRYVG
     ETDFAKGEWC GVELDEPLGK NDGAVAGTRY FQCPPKFGLF APIHKVIRIG FPSTSPAKAK
     KTKRMAMGVS ALTHSPSSSS ISSVSSVASS VGGRPSRSGL LTETSSRYAR KISGTTALQE
     ALKEKQQHIE QLLAERDLER AEVAKATSHI CEVEKEIALL KAQHEQYVAE AEEKLQRARL
     LVENVRKEKV DLSNQLEEER RKVEDLQFRV EEESITKGDL ETQTQLEHAR IGELEQSLLL
     EKAQAERLLR ELADNRLTTV AEKSRVLQLE EELSLRRGEI EELQHCLLQS GPPPADHPEA
     AETLRLRERL LSASKEHQRD STLLQDKYEH MLKTYQTEVD KLRAANEKYA QEVADLKAKV
     QQATTENMGL MDNWKSKLDS LASDHQKSLE DLKATLNSGP GAQQKEIGEL KALVEGIKME
     HQLELGNLQA KHDLETAMHG KEKEGLRQKL QEVQEELAGL QQHWREQLEE QASQHRLELQ
     EAQDQCRDAQ LRAQELEGLD VEYRGQAQAI EFLKEQISLA EKKMLDYEML QRAEAQSRQE
     AERLREKLLV AENRLQAAES LCSAQHSHVI ESSDLSEETI RMKETVEGLQ DKLNKRDKEV
     TALTSQMDML RAQVSALENK CKSGEKKIDS LLKEKRRLEA ELEAVSRKTH DASGQLVHIS
     QELLRKERSL NELRVLLLEA NRHSPGPERD LSREVHKAEW RIKEQKLKDD IRGLREKLTG
     LDKEKSLSEQ RRYSLIDPAS PPELLKLQHQ LVSTEDALRD ALNQAQQVER LVEALRGCSD
     RTQTISNSGS ANGIHQPDKA HKQEDKH
 
 
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