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RASEF_MOUSE
ID   RASEF_MOUSE             Reviewed;         627 AA.
AC   Q5RI75; B2RQ59; Q5RI76;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Ras and EF-hand domain-containing protein homolog;
GN   Name=Rasef;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266 AND SER-272, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
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: Binds predominantly GDP, and also GTP (By similarity). Acts
CC       as a dynein adapter protein that activates dynein-mediated transport
CC       and dynein-dynactin motility on microtubules (By similarity).
CC       {ECO:0000250|UniProtKB:Q8IZ41}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with the dynein-dynactin
CC       complex (By similarity). {ECO:0000250|UniProtKB:Q8IZ41}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8IZ41}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5RI75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RI75-2; Sequence=VSP_027768;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AK132691; BAE21304.1; -; mRNA.
DR   EMBL; BX294159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC125539; AAI25540.1; -; mRNA.
DR   EMBL; BC137774; AAI37775.1; -; mRNA.
DR   CCDS; CCDS18281.1; -. [Q5RI75-1]
DR   RefSeq; NP_001017427.1; NM_001017427.1. [Q5RI75-1]
DR   RefSeq; XP_017175690.1; XM_017320201.1. [Q5RI75-1]
DR   AlphaFoldDB; Q5RI75; -.
DR   SMR; Q5RI75; -.
DR   STRING; 10090.ENSMUSP00000062771; -.
DR   iPTMnet; Q5RI75; -.
DR   PhosphoSitePlus; Q5RI75; -.
DR   EPD; Q5RI75; -.
DR   jPOST; Q5RI75; -.
DR   PaxDb; Q5RI75; -.
DR   PeptideAtlas; Q5RI75; -.
DR   PRIDE; Q5RI75; -.
DR   ProteomicsDB; 300353; -. [Q5RI75-1]
DR   ProteomicsDB; 300354; -. [Q5RI75-2]
DR   Antibodypedia; 13004; 103 antibodies from 25 providers.
DR   DNASU; 242505; -.
DR   Ensembl; ENSMUST00000058292; ENSMUSP00000062771; ENSMUSG00000043003. [Q5RI75-1]
DR   Ensembl; ENSMUST00000102837; ENSMUSP00000099901; ENSMUSG00000043003. [Q5RI75-2]
DR   GeneID; 242505; -.
DR   KEGG; mmu:242505; -.
DR   UCSC; uc008tiw.1; mouse. [Q5RI75-1]
DR   CTD; 158158; -.
DR   MGI; MGI:2448565; Rasef.
DR   VEuPathDB; HostDB:ENSMUSG00000043003; -.
DR   eggNOG; KOG0078; Eukaryota.
DR   GeneTree; ENSGT00940000159488; -.
DR   HOGENOM; CLU_023178_1_0_1; -.
DR   InParanoid; Q5RI75; -.
DR   PhylomeDB; Q5RI75; -.
DR   TreeFam; TF313106; -.
DR   BioGRID-ORCS; 242505; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Rasef; mouse.
DR   PRO; PR:Q5RI75; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q5RI75; protein.
DR   Bgee; ENSMUSG00000043003; Expressed in epithelium of stomach and 63 other tissues.
DR   ExpressionAtlas; Q5RI75; baseline and differential.
DR   Genevisible; Q5RI75; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0019003; F:GDP binding; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; ISO:MGI.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; GTP-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..627
FT                   /note="Ras and EF-hand domain-containing protein homolog"
FT                   /id="PRO_0000299578"
FT   COILED          55..245
FT                   /evidence="ECO:0000255"
FT   BINDING         438..443
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT   BINDING         541..544
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT   BINDING         578..579
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZ41"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         272
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027768"
SQ   SEQUENCE   627 AA;  70752 MW;  3D9530B81BDF339D CRC64;
     MAQEVSSSVA FIHRLLYTAL RGLLGDRLKR GLKKEQVSTL YQNITLVEPR LLQPYERVIR
     NFLREIKLQS TEMENLAIAV KRAQDKAAIQ LSELEEEMDQ RIQAVENESR KDEKRKAEEA
     LTDLRRQYET EVGDLQVTIK RLKKLEEQSR QISQKQDVTA LKKQIHDLTM ENQKLKKELL
     EAQTNVAFLQ SELDALKSDY ADQSLNSERD LEIIREYTED RSSLERQIEI LQTANRKLHD
     SNDGLRSALE NTYSKLNRSL RINNISPGNT ISRSSPKFNH HSSQPLAYDR SFHSSYADED
     CDSLALCDPL QKMNYEVDSL PESCFDSGLS TLRDNECDSE VDYKHQGEFQ TLHRTEESLG
     GDASDTDVPD IRDEEAFDSE SVASVLHWQP QGSAGEGSTL SSSRKPISAL SLQTDMVDNT
     SKVTSQKAYK IVLAGDAAVG KSSFLMRLCK NEFQGNTSAT LGVDFQMKTL IVDGEQTVLQ
     LWDTAGQERF RSIAKSYFRK ADGVLLLYDV TCEKSFLNVR EWVDMVEDGT HRTIPIMLVG
     NKADLRDVDN AENQKCISAY LGEKLAMTYG ALFCETSAKD GSNVVEAVLH LAREVKKRTE
     DDDSRSITSL AGSTSKKSLQ MKNCCNG
 
 
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