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STRP2_MOUSE
ID   STRP2_MOUSE             Reviewed;         844 AA.
AC   Q8C9H6; Q3TQB7; Q80TI6; Q8C7A2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Striatin-interacting proteins 2;
DE   AltName: Full=Protein FAM40B;
GN   Name=Strip2; Synonyms=Fam40b, Kiaa1170, Stripb;
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=Cerebellum, and Thymus;
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] OF 46-844 (ISOFORM 3).
RC   TISSUE=Brain;
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   [3]
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-339 AND SER-364, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, 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 control of cell shape (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
CC       (STRIPAK) complex. Interacts with CTTNBP2NL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Enriched in
CC       lamellipodia. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C9H6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C9H6-4; Sequence=VSP_019001, VSP_019002;
CC       Name=3;
CC         IsoId=Q8C9H6-3; Sequence=VSP_014870;
CC   -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
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DR   EMBL; AK042073; BAC31154.1; -; mRNA.
DR   EMBL; AK163706; BAE37467.1; -; mRNA.
DR   EMBL; AK122459; BAC65741.1; -; mRNA.
DR   CCDS; CCDS19967.1; -. [Q8C9H6-1]
DR   CCDS; CCDS85025.1; -. [Q8C9H6-3]
DR   RefSeq; NP_001032829.1; NM_001037740.1. [Q8C9H6-3]
DR   RefSeq; NP_796178.2; NM_177204.3. [Q8C9H6-1]
DR   AlphaFoldDB; Q8C9H6; -.
DR   SMR; Q8C9H6; -.
DR   BioGRID; 236153; 37.
DR   STRING; 10090.ENSMUSP00000036477; -.
DR   iPTMnet; Q8C9H6; -.
DR   PhosphoSitePlus; Q8C9H6; -.
DR   jPOST; Q8C9H6; -.
DR   MaxQB; Q8C9H6; -.
DR   PaxDb; Q8C9H6; -.
DR   PRIDE; Q8C9H6; -.
DR   ProteomicsDB; 257501; -. [Q8C9H6-1]
DR   ProteomicsDB; 257502; -. [Q8C9H6-4]
DR   ProteomicsDB; 257503; -. [Q8C9H6-3]
DR   Antibodypedia; 17893; 59 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000046028; ENSMUSP00000036477; ENSMUSG00000039629. [Q8C9H6-1]
DR   Ensembl; ENSMUST00000151738; ENSMUSP00000119506; ENSMUSG00000039629. [Q8C9H6-3]
DR   GeneID; 320609; -.
DR   KEGG; mmu:320609; -.
DR   UCSC; uc009bem.1; mouse. [Q8C9H6-1]
DR   UCSC; uc009beo.1; mouse. [Q8C9H6-3]
DR   CTD; 57464; -.
DR   MGI; MGI:2444363; Strip2.
DR   VEuPathDB; HostDB:ENSMUSG00000039629; -.
DR   eggNOG; KOG3680; Eukaryota.
DR   GeneTree; ENSGT00400000022095; -.
DR   InParanoid; Q8C9H6; -.
DR   OMA; RHNNFLL; -.
DR   PhylomeDB; Q8C9H6; -.
DR   TreeFam; TF314205; -.
DR   BioGRID-ORCS; 320609; 5 hits in 74 CRISPR screens.
DR   PRO; PR:Q8C9H6; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8C9H6; protein.
DR   Bgee; ENSMUSG00000039629; Expressed in olfactory tubercle and 146 other tissues.
DR   ExpressionAtlas; Q8C9H6; baseline and differential.
DR   Genevisible; Q8C9H6; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; 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   Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..844
FT                   /note="Striatin-interacting proteins 2"
FT                   /id="PRO_0000187023"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         659..662
FT                   /note="EAGD -> GLSV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_019001"
FT   VAR_SEQ         663..844
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_019002"
FT   VAR_SEQ         694..721
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_014870"
FT   CONFLICT        47
FT                   /note="Q -> L (in Ref. 2; BAC65741)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   844 AA;  96294 MW;  78E4D64476A7B097 CRC64;
     MDDPAAPGPA GSPANDNGNG NGNGNGNGNG GKGKPAVPKG RETFRNQRRE SEGSVDCPTL
     EFEYGDSDGH AAELSELYSY TENLEFTTNR KCFEEDFRTQ VQDTKEWLEL EEDAQKTYVM
     GLLDRLEVVS REKRLKVARA VLYLAQGTFG ECDSEVDVLH WSRYNCFLLY QMGTFSAFLE
     LLHMEIDNSQ ASSSALRKPA VSIADSTELR VLLSVMYLMV ENIRLEREID PCGWRTARET
     FRTELSFSTH NEEPFALLLF SMVTKFCSGL APHFPIKKVL LLLWKVVMFT LGGFEHLQAL
     KIQKRAELGL PPLAEDSIQV VKSMRAASPP SYTLDLGESQ LAPPPSKLRG RRGSRRQLLT
     KQDSLDIYNE RDLFKTEEPA TEEEEESAAD GERTLDGELD LLEQDPLVPP PPSQTPLSTD
     RVAFPKGLPW APKVRQKDIE HFLEMSRNKF IGFTLGQDTD TLVGLPRPIH ESVKTLKQHK
     YISIADIQIK NEEELEKCPL SLGEEVVPET PSEILYQGML YSLPQYMIAL LKILLAAAPT
     SKAKTDSINI LADVLPEEMP VTVLQSMKLG IDVNRHKEII VKSISALLLL LLKHFKLNHI
     YQFEYVSQHL VFANCIPLIL KFFNQNILSY ITAKNSISVL DYPCCTIQDL PELTTESLEA
     GDNSQFCWRN LFSCINLLRL LNKLTKWKHS RTMMLVVFKS APILKRALKV KQAMLQLYVL
     KLLKIQTKYL GRQWRKSNMK TMSAIYQKVR HRMNDDWAYG NDIDARPWDF QAEECTLRAN
     IEAFNSRRYD KPQDSEFSPV DNCLQSVLGQ RLDLPEDFHY SYELWLEREV FSQPICWEEL
     LQNH
 
 
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