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RMD2_MOUSE
ID   RMD2_MOUSE              Reviewed;         410 AA.
AC   Q8BSE0; A9UN02; Q8CIF1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Regulator of microtubule dynamics protein 2;
DE            Short=RMD-2;
DE            Short=mRMD-2;
DE   AltName: Full=Protein FAM82A1;
GN   Name=Rmdn2; Synonyms=Fam82a, Fam82a1;
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; TISSUE=Brain cortex, and Embryo;
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   STRAIN=Czech II; TISSUE=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   [3]
RP   IDENTIFICATION.
RX   PubMed=18070910; DOI=10.1083/jcb.200705108;
RA   Oishi K., Okano H., Sawa H.;
RT   "RMD-1, a novel microtubule-associated protein, functions in chromosome
RT   segregation in Caenorhabditis elegans.";
RL   J. Cell Biol. 179:1149-1162(2007).
RN   [4]
RP   IDENTIFICATION BY 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND THR-154, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, 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: Interacts with microtubules. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Cytoplasm. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC       Note=In interphase localizes in the cytoplasm, and during mitosis
CC       localizes to the spindle microtubules and spindle poles. Also detected
CC       as large dots in the perinuclear region (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24059.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK034617; BAC28771.1; -; mRNA.
DR   EMBL; AK139382; BAE23985.1; -; mRNA.
DR   EMBL; BC024059; AAH24059.1; ALT_INIT; mRNA.
DR   EMBL; BR000694; FAA00419.1; -; mRNA.
DR   CCDS; CCDS28985.1; -.
DR   RefSeq; NP_958749.1; NM_201361.2.
DR   AlphaFoldDB; Q8BSE0; -.
DR   SMR; Q8BSE0; -.
DR   STRING; 10090.ENSMUSP00000044543; -.
DR   iPTMnet; Q8BSE0; -.
DR   PhosphoSitePlus; Q8BSE0; -.
DR   SwissPalm; Q8BSE0; -.
DR   EPD; Q8BSE0; -.
DR   jPOST; Q8BSE0; -.
DR   MaxQB; Q8BSE0; -.
DR   PaxDb; Q8BSE0; -.
DR   PRIDE; Q8BSE0; -.
DR   ProteomicsDB; 299865; -.
DR   Ensembl; ENSMUST00000040368; ENSMUSP00000044543; ENSMUSG00000036368.
DR   Ensembl; ENSMUST00000225357; ENSMUSP00000153443; ENSMUSG00000036368.
DR   GeneID; 381110; -.
DR   KEGG; mmu:381110; -.
DR   UCSC; uc008dpy.1; mouse.
DR   CTD; 151393; -.
DR   MGI; MGI:2147043; Rmdn2.
DR   VEuPathDB; HostDB:ENSMUSG00000036368; -.
DR   eggNOG; ENOG502QS2U; Eukaryota.
DR   GeneTree; ENSGT00950000182992; -.
DR   HOGENOM; CLU_046369_0_0_1; -.
DR   InParanoid; Q8BSE0; -.
DR   OMA; DLGQKNN; -.
DR   OrthoDB; 1380644at2759; -.
DR   PhylomeDB; Q8BSE0; -.
DR   TreeFam; TF315854; -.
DR   BioGRID-ORCS; 381110; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Rmdn2; mouse.
DR   PRO; PR:Q8BSE0; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8BSE0; protein.
DR   Bgee; ENSMUSG00000036368; Expressed in spermatid and 220 other tissues.
DR   ExpressionAtlas; Q8BSE0; baseline and differential.
DR   Genevisible; Q8BSE0; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR   GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR   GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..410
FT                   /note="Regulator of microtubule dynamics protein 2"
FT                   /id="PRO_0000287506"
FT   TRANSMEM        9..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          120..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          69..110
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        133..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q498D5"
FT   MOD_RES         139
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT   MOD_RES         152
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT   MOD_RES         154
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         157
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96LZ7"
FT   CONFLICT        40
FT                   /note="P -> S (in Ref. 2; AAH24059)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289
FT                   /note="Missing (in Ref. 2; AAH24059)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  47016 MW;  170C39E02C052B08 CRC64;
     MPHSTNKELI LGIMAGTAGI SLLAFWYHKV LKPRTTMNFP KLLSLGKKFG SLTLPEESHS
     AQGASVVFQR RQLQILEKLN ELLTNMEELK EEIRFLKETI PKLEECIQDE FGGKVTVHKI
     SPQHRARKKK GTTVQRSATS NSSEEAESEG GYITANTDTE EQNFPFPKAL NTHIEELKLD
     VLLQKADHLR TNESHKMESF ELLCDHKEKF SEETEFLWRL ARAYGDMYDL STSTQEKKHY
     ANIGKTLGER AITRAPMNGH CHLWYAVLCG YVSEFEGLQN KINCGHLFKK HLEIAIQLLP
     EEPLLYYLKG RYCYTVSRLS WIEKKMAATL FGEIPYSTVH EALHNFLKTE ELQPGYSMSN
     YMYTAKCYVE LGEPQEACKF CNLALLLPVV TKEDKDAHKE VKKMISSLKR
 
 
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