位置:首页 > 蛋白库 > SHOC2_MOUSE
SHOC2_MOUSE
ID   SHOC2_MOUSE             Reviewed;         582 AA.
AC   O88520; Q3UJH6; Q8BVL0; Q91VH8;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Leucine-rich repeat protein SHOC-2;
DE   AltName: Full=Protein soc-2 homolog;
DE   AltName: Full=Protein sur-8 homolog;
GN   Name=Shoc2;
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 [MRNA].
RX   PubMed=9674433; DOI=10.1016/s0092-8674(00)81227-1;
RA   Sieburth D.S., Sun Q., Han M.;
RT   "SUR-8, a conserved Ras-binding protein with leucine-rich repeats,
RT   positively regulates Ras-mediated signaling in C. elegans.";
RL   Cell 94:119-130(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16682971; DOI=10.1038/ng1796;
RA   Clee S.M., Yandell B.S., Schueler K.M., Rabaglia M.E., Richards O.C.,
RA   Raines S.M., Kabara E.A., Klass D.M., Mui E.T.-K., Stapleton D.S.,
RA   Gray-Keller M.P., Young M.B., Stoehr J.P., Lan H., Boronenkov I.,
RA   Raess P.W., Flowers M.T., Attie A.D.;
RT   "Positional cloning of Sorcs1, a type 2 diabetes quantitative trait
RT   locus.";
RL   Nat. Genet. 38:688-693(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary gland;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Pancreas, 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: Regulatory subunit of protein phosphatase 1 (PP1c) that acts
CC       as a M-Ras/MRAS effector and participates in MAPK pathway activation.
CC       Upon M-Ras/MRAS activation, targets PP1c to specifically
CC       dephosphorylate the 'Ser-259' inhibitory site of RAF1 kinase and
CC       stimulate RAF1 activity at specialized signaling complexes.
CC       {ECO:0000250|UniProtKB:Q9UQ13}.
CC   -!- SUBUNIT: Interacts with M-Ras/MRAS, and RAF1. Forms a multiprotein
CC       complex with Ras (M-Ras/MRAS), Raf (RAF1) and protein phosphatase 1
CC       (PPP1CA, PPP1CB and PPP1CC). Interacts with ERBIN; disrupts the
CC       interaction with RAF1 and Ras, leading to prevent activation of the Ras
CC       signaling pathway. Specifically binds K-Ras/KRAS, M-Ras/MRAS and N-
CC       Ras/NRAS but not H-Ras/HRAS. Interacts with LZTR1.
CC       {ECO:0000250|UniProtKB:Q9UQ13}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UQ13}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9UQ13}. Note=Translocates from cytoplasm to
CC       nucleus upon growth factor stimulation. {ECO:0000250|UniProtKB:Q9UQ13}.
CC   -!- SIMILARITY: Belongs to the SHOC2 family. {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; AF068921; AAC40175.1; -; mRNA.
DR   EMBL; DQ479926; ABF48505.1; -; Genomic_DNA.
DR   EMBL; AK077798; BAC37016.1; -; mRNA.
DR   EMBL; AK146447; BAE27179.1; -; mRNA.
DR   EMBL; BC013722; AAH13722.1; -; mRNA.
DR   EMBL; BC049775; AAH49775.1; -; mRNA.
DR   EMBL; BC083060; AAH83060.1; -; mRNA.
DR   CCDS; CCDS29904.1; -.
DR   RefSeq; NP_001161977.1; NM_001168505.1.
DR   RefSeq; NP_062632.2; NM_019658.6.
DR   RefSeq; XP_006527291.1; XM_006527228.3.
DR   RefSeq; XP_011245601.1; XM_011247299.2.
DR   RefSeq; XP_017173749.1; XM_017318260.1.
DR   AlphaFoldDB; O88520; -.
DR   SMR; O88520; -.
DR   BioGRID; 207949; 53.
DR   IntAct; O88520; 50.
DR   MINT; O88520; -.
DR   STRING; 10090.ENSMUSP00000025932; -.
DR   iPTMnet; O88520; -.
DR   PhosphoSitePlus; O88520; -.
DR   EPD; O88520; -.
DR   MaxQB; O88520; -.
DR   PaxDb; O88520; -.
DR   PeptideAtlas; O88520; -.
DR   PRIDE; O88520; -.
DR   ProteomicsDB; 255414; -.
DR   Antibodypedia; 1953; 237 antibodies from 32 providers.
DR   DNASU; 56392; -.
DR   Ensembl; ENSMUST00000025932; ENSMUSP00000025932; ENSMUSG00000024976.
DR   Ensembl; ENSMUST00000169861; ENSMUSP00000127932; ENSMUSG00000024976.
DR   GeneID; 56392; -.
DR   KEGG; mmu:56392; -.
DR   UCSC; uc008hxg.2; mouse.
DR   CTD; 8036; -.
DR   MGI; MGI:1927197; Shoc2.
DR   VEuPathDB; HostDB:ENSMUSG00000024976; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000156270; -.
DR   HOGENOM; CLU_000288_18_23_1; -.
DR   InParanoid; O88520; -.
DR   OMA; NQFTSYP; -.
DR   OrthoDB; 287114at2759; -.
DR   PhylomeDB; O88520; -.
DR   TreeFam; TF315742; -.
DR   Reactome; R-MMU-5673000; RAF activation.
DR   BioGRID-ORCS; 56392; 15 hits in 76 CRISPR screens.
DR   ChiTaRS; Shoc2; mouse.
DR   PRO; PR:O88520; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; O88520; protein.
DR   Bgee; ENSMUSG00000024976; Expressed in undifferentiated genital tubercle and 254 other tissues.
DR   ExpressionAtlas; O88520; baseline and differential.
DR   Genevisible; O88520; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; ISS:UniProtKB.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 3.80.10.10; -; 4.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027036; SHOC2.
DR   PANTHER; PTHR48051:SF9; PTHR48051:SF9; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   SMART; SM00369; LRR_TYP; 16.
DR   PROSITE; PS51450; LRR; 17.
PE   1: Evidence at protein level;
KW   Cytoplasm; Leucine-rich repeat; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..582
FT                   /note="Leucine-rich repeat protein SHOC-2"
FT                   /id="PRO_0000097738"
FT   REPEAT          101..122
FT                   /note="LRR 1"
FT   REPEAT          124..145
FT                   /note="LRR 2"
FT   REPEAT          147..169
FT                   /note="LRR 3"
FT   REPEAT          170..191
FT                   /note="LRR 4"
FT   REPEAT          193..215
FT                   /note="LRR 5"
FT   REPEAT          216..237
FT                   /note="LRR 6"
FT   REPEAT          239..260
FT                   /note="LRR 7"
FT   REPEAT          262..283
FT                   /note="LRR 8"
FT   REPEAT          285..307
FT                   /note="LRR 9"
FT   REPEAT          308..329
FT                   /note="LRR 10"
FT   REPEAT          332..353
FT                   /note="LRR 11"
FT   REPEAT          356..377
FT                   /note="LRR 12"
FT   REPEAT          380..400
FT                   /note="LRR 13"
FT   REPEAT          403..424
FT                   /note="LRR 14"
FT   REPEAT          426..448
FT                   /note="LRR 15"
FT   REPEAT          449..470
FT                   /note="LRR 16"
FT   REPEAT          472..494
FT                   /note="LRR 17"
FT   REPEAT          495..516
FT                   /note="LRR 18"
FT   REPEAT          518..540
FT                   /note="LRR 19"
FT   REPEAT          542..563
FT                   /note="LRR 20"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        11
FT                   /note="S -> F (in Ref. 1; AAC40175)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   582 AA;  64893 MW;  154B38C4909FB0AD CRC64;
     MSSSLGKEKD SKEKDPKVPS AKEREKESKA SGGFGKESKE KEPKAKGKDA KDGKKESSAA
     QPGVAFSVDN TIKRPNPAPG TRKKSSNAEV IKELNKCREE NSMRLDLSKR SIHILPPSVK
     ELTQLTELYL YSNKLQSLPA EVGCLVNLMT LALSENSLTS LPDSLDNLKK LRMLDLRHNK
     LREIPSVVYR LDSLTTLYLR FNRITTVEKD IKNLPKLSML SIRENKIKQL PAEIGELCNL
     ITLDVAHNQL EHLPKEIGNC TQITNLDLQH NDLLDLPDTI GNLSSLNRLG LRYNRLSAIP
     RSLAKCSALE ELNLENNNIS TLPESLLSSL VKLNSLTLAR NCFQLYPVGG PSQFSTIYSL
     NMEHNRINKI PFGIFSRAKV LSKLNMKDNQ LTSLPLDFGT WTSMVELNLA TNQLTKIPED
     VSGLVSLEVL ILSNNLLKKL PHGLGNLRKL RELDLEENKL ESLPNEIAYL KDLQKLVLTN
     NQLSTLPRGI GHLTNLTHLG LGENLLTHLP EEIGTLENLE ELYLNDNPNL HSLPFELALC
     SKLSIMSIEN CPLSHLPPQI VAGGPSFIIQ FLKMQGPYRA MV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024