位置:首页 > 蛋白库 > STRP1_MOUSE
STRP1_MOUSE
ID   STRP1_MOUSE             Reviewed;         837 AA.
AC   Q8C079; Q80T92; Q8BZC6; Q8CIF7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Striatin-interacting protein 1;
DE   AltName: Full=Protein FAM40A;
GN   Name=Strip1; Synonyms=Fam40a, Kiaa1761;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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] (ISOFORM 4).
RC   STRAIN=FVB/N; 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-837 (ISOFORM 3).
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, 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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   IDENTIFICATION IN THE STRIATIN-INTERACTING PHOSPHATASE AND KINASE (STRIPAK)
RP   COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA   Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA   Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA   Aebersold R., Raught B., Gingras A.C.;
RT   "A PP2A phosphatase high density interaction network identifies a novel
RT   striatin-interacting phosphatase and kinase complex linked to the cerebral
RT   cavernous malformation 3 (CCM3) protein.";
RL   Mol. Cell. Proteomics 8:157-171(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-339, AND
RP   IDENTIFICATION BY MASS 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   -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. Required in the cortical actin filament
CC       dynamics and cell shape (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
CC       (STRIPAK) complex (PubMed:18782753). Interacts with CDC42BPB. Interacts
CC       with CTTNBP2NL. {ECO:0000250|UniProtKB:Q5VSL9,
CC       ECO:0000269|PubMed:18782753}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Enriched on the
CC       plasma membrane. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8C079-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C079-2; Sequence=VSP_014865;
CC       Name=3;
CC         IsoId=Q8C079-3; Sequence=VSP_014866;
CC       Name=4;
CC         IsoId=Q8C079-4; Sequence=VSP_014863;
CC   -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION: [Isoform 2]:
CC       Sequence=BAC29206.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK032065; BAC27678.1; -; mRNA.
DR   EMBL; AK035833; BAC29206.1; ALT_FRAME; mRNA.
DR   EMBL; BC023952; AAH23952.1; -; mRNA.
DR   EMBL; AK122553; BAC65835.1; -; Unassigned_RNA.
DR   CCDS; CCDS51043.1; -. [Q8C079-1]
DR   RefSeq; NP_705791.2; NM_153563.2. [Q8C079-1]
DR   AlphaFoldDB; Q8C079; -.
DR   SMR; Q8C079; -.
DR   BioGRID; 230890; 15.
DR   CORUM; Q8C079; -.
DR   IntAct; Q8C079; 16.
DR   MINT; Q8C079; -.
DR   STRING; 10090.ENSMUSP00000068587; -.
DR   iPTMnet; Q8C079; -.
DR   PhosphoSitePlus; Q8C079; -.
DR   EPD; Q8C079; -.
DR   jPOST; Q8C079; -.
DR   MaxQB; Q8C079; -.
DR   PaxDb; Q8C079; -.
DR   PeptideAtlas; Q8C079; -.
DR   PRIDE; Q8C079; -.
DR   ProteomicsDB; 254602; -. [Q8C079-1]
DR   ProteomicsDB; 254603; -. [Q8C079-2]
DR   ProteomicsDB; 254604; -. [Q8C079-3]
DR   ProteomicsDB; 254605; -. [Q8C079-4]
DR   Antibodypedia; 53747; 184 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000064759; ENSMUSP00000068587; ENSMUSG00000014601. [Q8C079-1]
DR   GeneID; 229707; -.
DR   KEGG; mmu:229707; -.
DR   UCSC; uc008qxg.2; mouse. [Q8C079-1]
DR   CTD; 85369; -.
DR   MGI; MGI:2443884; Strip1.
DR   VEuPathDB; HostDB:ENSMUSG00000014601; -.
DR   eggNOG; KOG3680; Eukaryota.
DR   GeneTree; ENSGT00400000022095; -.
DR   HOGENOM; CLU_011008_1_0_1; -.
DR   InParanoid; Q8C079; -.
DR   OMA; KPYSWRN; -.
DR   PhylomeDB; Q8C079; -.
DR   TreeFam; TF314205; -.
DR   BioGRID-ORCS; 229707; 15 hits in 73 CRISPR screens.
DR   ChiTaRS; Strip1; mouse.
DR   PRO; PR:Q8C079; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8C079; protein.
DR   Bgee; ENSMUSG00000014601; Expressed in ear vesicle and 230 other tissues.
DR   Genevisible; Q8C079; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR040185; Far11/STRP.
DR   InterPro; IPR021819; Far11/STRP_C.
DR   InterPro; IPR012486; Far11/STRP_N.
DR   PANTHER; PTHR13239; PTHR13239; 1.
DR   Pfam; PF11882; DUF3402; 2.
DR   Pfam; PF07923; N1221; 1.
DR   SMART; SM01293; DUF3402; 1.
DR   SMART; SM01292; N1221; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..837
FT                   /note="Striatin-interacting protein 1"
FT                   /id="PRO_0000187019"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..33
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VSL9"
FT   VAR_SEQ         1..126
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014863"
FT   VAR_SEQ         430..837
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014865"
FT   VAR_SEQ         555..629
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_014866"
FT   CONFLICT        104
FT                   /note="D -> A (in Ref. 1; BAC27678)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="Q -> H (in Ref. 1; BAC27678)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   837 AA;  95585 MW;  BD984594F049D3F4 CRC64;
     MEPAAAGPGP LIVNNKQPQP PPPPPPATAQ PPPGAPRAAG GLLPGGKARE FNRNQRKDSE
     GYSESPDLEF EYADTDKWAA ELAELYSYTE GPEFLMNRKC FEEDFRIHVS DKKWTELDTN
     QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQFWMR YNIFLLLEVG
     TFNALVELLN MEIDNSAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQDCDGDKAE
     WRTMRQTFRA ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG
     FEELQSMKAE KRTLLGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR GRREHKALIK
     QDNLDAFNER DPYKADDSRE EEEENDDDSS LEGEAFPLER DEVMPPPLQH PQTDRLTCPK
     GLPWAPKVRE KDIEMFLESS RSKFIGYTLG SDTNTVVGLP RPIHESIKTL KQHKYTSIAE
     VQAQMEEEYL RSPLSGGEEE VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD
     SINILADVLP EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHIYQFEYM
     AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VNELPELTAE SLEAGDNNQF
     CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR ALKVKQAMMQ LYVLKLLKVQ
     TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD WAYGNDLDAR PWDFQAEECA LRANIERFNA
     RRYDRTHSNP DFLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024