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CAMKV_MOUSE
ID   CAMKV_MOUSE             Reviewed;         512 AA.
AC   Q3UHL1; Q8VD20;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=CaM kinase-like vesicle-associated protein;
GN   Name=Camkv;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Liver;
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: Does not appear to have detectable kinase activity.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with calmodulin, in the presence of calcium.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Predominantly observed
CC       in association with the plasma membrane of soma and in neurites, both
CC       axons and dendrites. May be associated with vesicular structures (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AK147323; BAE27846.1; -; mRNA.
DR   EMBL; BC017634; AAH17634.1; -; mRNA.
DR   EMBL; BC111033; AAI11034.1; -; mRNA.
DR   CCDS; CCDS40763.1; -.
DR   RefSeq; NP_663596.1; NM_145621.2.
DR   RefSeq; XP_006511785.1; XM_006511722.2.
DR   AlphaFoldDB; Q3UHL1; -.
DR   SMR; Q3UHL1; -.
DR   BioGRID; 231689; 7.
DR   IntAct; Q3UHL1; 5.
DR   STRING; 10090.ENSMUSP00000040430; -.
DR   iPTMnet; Q3UHL1; -.
DR   PhosphoSitePlus; Q3UHL1; -.
DR   SwissPalm; Q3UHL1; -.
DR   MaxQB; Q3UHL1; -.
DR   PaxDb; Q3UHL1; -.
DR   PeptideAtlas; Q3UHL1; -.
DR   PRIDE; Q3UHL1; -.
DR   ProteomicsDB; 273907; -.
DR   Antibodypedia; 2091; 209 antibodies from 29 providers.
DR   DNASU; 235604; -.
DR   Ensembl; ENSMUST00000035700; ENSMUSP00000040430; ENSMUSG00000032936.
DR   GeneID; 235604; -.
DR   KEGG; mmu:235604; -.
DR   UCSC; uc009rnk.1; mouse.
DR   CTD; 79012; -.
DR   MGI; MGI:2384296; Camkv.
DR   VEuPathDB; HostDB:ENSMUSG00000032936; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   GeneTree; ENSGT00940000156468; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q3UHL1; -.
DR   OMA; CVTLGEK; -.
DR   OrthoDB; 330091at2759; -.
DR   PhylomeDB; Q3UHL1; -.
DR   TreeFam; TF314166; -.
DR   BioGRID-ORCS; 235604; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Camkv; mouse.
DR   PRO; PR:Q3UHL1; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q3UHL1; protein.
DR   Bgee; ENSMUSG00000032936; Expressed in dentate gyrus of hippocampal formation granule cell and 107 other tissues.
DR   ExpressionAtlas; Q3UHL1; baseline and differential.
DR   Genevisible; Q3UHL1; MM.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0099159; P:regulation of modification of postsynaptic structure; IDA:SynGO.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cell membrane; Cytoplasmic vesicle; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..512
FT                   /note="CaM kinase-like vesicle-associated protein"
FT                   /id="PRO_0000250095"
FT   DOMAIN          24..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          328..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         446
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63092"
FT   MOD_RES         470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:15345747"
FT   CONFLICT        479
FT                   /note="D -> G (in Ref. 1; BAE27846)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  54819 MW;  CFEFD4C43CC889A9 CRC64;
     MPFGCVTLGD KKNYNQPSEV TDRYDLGQVI KTEEFCEIFR AKDKTTGKLH TCKKFQKRDG
     RKVRKAAKNE IGILKMVKHP NILQLVDVFV TRKEYFIFLE LATGREVFDW ILDQGYYSER
     DTSNVVRQVL EAVAYLHSLK IVHRNLKLEN LVYYNRLKNS KIVISDFHLA KLENGLIKEP
     CGTPEYLAPE VVGRQRYGRP VDCWAIGVIM YILLSGNPPF YEEVEEDDYE NHDKNLFRKI
     LAGDYEFDSP YWDDISQAAK DLVTRLMEVE QDQRITAEEA ISHEWISGNA ASDKNIKDGV
     CAQIEKNFAR AKWKKAVRVT TLMKRLRAPE QSGTAATQSA SDAATPGAAG GAIAAAAAAA
     AAGGAASASG ASATAATEGG AGCAAKSDDI ASADRSATPA TDGSATPATD GSVTPATDGS
     ITPATDGSVT PATDRSATPA TDGRATPATE ESTVPATQSS ALPAAKAAAT PEPAVAQPDS
     TALEGATGQA PPSSKGEEAT GCAQESQRVE TS
 
 
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