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SH24A_MOUSE
ID   SH24A_MOUSE             Reviewed;         421 AA.
AC   Q9D7V1; Q14AV2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=SH2 domain-containing protein 4A;
GN   Name=Sh2d4a;
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=Stomach;
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].
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17251388; DOI=10.1681/asn.2006060675;
RA   Patrakka J., Xiao Z., Nukui M., Takemoto M., He L., Oddsson A., Perisic L.,
RA   Kaukinen A., Szigyarto C.A.-K., Uhlen M., Jalanko H., Betsholtz C.,
RA   Tryggvason K.;
RT   "Expression and subcellular distribution of novel glomerulus-associated
RT   proteins Dendrin, Ehd3, Sh2d4a, Plekhh2, and 2310066E14Rik.";
RL   J. Am. Soc. Nephrol. 18:689-697(2007).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=18641339; DOI=10.4049/jimmunol.181.3.2019;
RA   Lapinski P.E., Oliver J.A., Kamen L.A., Hughes E.D., Saunders T.L.,
RA   King P.D.;
RT   "Genetic analysis of SH2D4A, a novel adapter protein related to T cell-
RT   specific adapter and adapter protein in lymphocytes of unknown function,
RT   reveals a redundant function in T cells.";
RL   J. Immunol. 181:2019-2027(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Pancreas, and Spleen;
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: Inhibits estrogen-induced cell proliferation by competing
CC       with PLCG for binding to ESR1, blocking the effect of estrogen on PLCG
CC       and repressing estrogen-induced proliferation (By similarity). May play
CC       a role in T-cell development and function. {ECO:0000250,
CC       ECO:0000269|PubMed:18641339}.
CC   -!- SUBUNIT: Interacts with ESR1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17251388}.
CC       Note=Located at podocyte foot processes.
CC   -!- TISSUE SPECIFICITY: In the kidney, expressed only in the glomerulus.
CC       Expressed in T-cells, B-cells, macrophages and dendritic cells (at
CC       protein level). In adult, highest levels are found in muscle and lung
CC       with lower levels in kidney. {ECO:0000269|PubMed:17251388,
CC       ECO:0000269|PubMed:18641339}.
CC   -!- INDUCTION: Upon CD3/CD28 stimulation in CD4 T-cells.
CC       {ECO:0000269|PubMed:18641339}.
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DR   EMBL; AK008803; BAB25905.1; -; mRNA.
DR   EMBL; BC116682; AAI16683.1; -; mRNA.
DR   CCDS; CCDS52564.1; -.
DR   RefSeq; NP_082458.1; NM_028182.1.
DR   RefSeq; XP_006509814.1; XM_006509751.3.
DR   AlphaFoldDB; Q9D7V1; -.
DR   SMR; Q9D7V1; -.
DR   STRING; 10090.ENSMUSP00000070825; -.
DR   iPTMnet; Q9D7V1; -.
DR   PhosphoSitePlus; Q9D7V1; -.
DR   MaxQB; Q9D7V1; -.
DR   PaxDb; Q9D7V1; -.
DR   PeptideAtlas; Q9D7V1; -.
DR   PRIDE; Q9D7V1; -.
DR   ProteomicsDB; 261209; -.
DR   Antibodypedia; 968; 226 antibodies from 33 providers.
DR   Ensembl; ENSMUST00000066594; ENSMUSP00000070825; ENSMUSG00000053886.
DR   GeneID; 72281; -.
DR   KEGG; mmu:72281; -.
DR   UCSC; uc009lwe.2; mouse.
DR   CTD; 63898; -.
DR   MGI; MGI:1919531; Sh2d4a.
DR   VEuPathDB; HostDB:ENSMUSG00000053886; -.
DR   eggNOG; ENOG502QVV5; Eukaryota.
DR   GeneTree; ENSGT00940000157357; -.
DR   HOGENOM; CLU_029296_1_0_1; -.
DR   InParanoid; Q9D7V1; -.
DR   OMA; YPCGQQG; -.
DR   OrthoDB; 782492at2759; -.
DR   PhylomeDB; Q9D7V1; -.
DR   TreeFam; TF336893; -.
DR   BioGRID-ORCS; 72281; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Sh2d4a; mouse.
DR   PRO; PR:Q9D7V1; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9D7V1; protein.
DR   Bgee; ENSMUSG00000053886; Expressed in epithelium of stomach and 162 other tissues.
DR   ExpressionAtlas; Q9D7V1; baseline and differential.
DR   Genevisible; Q9D7V1; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; SH2 domain.
FT   CHAIN           1..421
FT                   /note="SH2 domain-containing protein 4A"
FT                   /id="PRO_0000233134"
FT   DOMAIN          315..407
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          132..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H788"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H788"
FT   CONFLICT        283
FT                   /note="I -> T (in Ref. 2; AAI16683)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  48460 MW;  EED076D6A1AE32D8 CRC64;
     MLRQILSDMF IDPDLLAELS EEQKQILFYK MREEQIRRWK EREAAMERKE SLPVKSRPKK
     ENGKSVHWKL GADKQVWVWV MGEHHLDKPY DVLCDEILAE REHLRAAKDS ELRKTQSLEL
     ANSLKIKSQN CDLQAMKKTE PQNVTRKAAS EEASGQGPRA IPTRKDDKAQ TKPVKEKDHE
     EMKQTEDEKT KQIYKSWKED SEWQASLRKS KAADEKRRSL AKQAREDYKR LSQRGRSGDG
     LQNPLTGPQK PRRPPLPPKP QFLQPLGIPP KSLGNQGVIR TEISSAQMDT IRWFKEEQLP
     FRAGYQKNSD TIAPWFHGIL TLKKANELLS TGVPGSFLIR VSEKIKGYAL SYLSEEGCKH
     FLIDASANSY SFLGVDQLQH ATLADLVEYH KEEPITSLGK ELLLYPCGQQ DKLPDYLELF
     Q
 
 
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