CISH_MOUSE
ID CISH_MOUSE Reviewed; 257 AA.
AC Q62225; Q3TC70;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cytokine-inducible SH2-containing protein;
DE Short=CIS;
DE AltName: Full=CIS-1;
DE AltName: Full=Suppressor of cytokine signaling;
DE Short=SOCS;
GN Name=Cish; Synonyms=Cis;
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=7796808; DOI=10.1002/j.1460-2075.1995.tb07281.x;
RA Yoshimura A., Ohkubo T., Kiguchi T., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Hara T., Miyajima A.;
RT "A novel cytokine-inducible gene CIS encodes an SH2-containing protein that
RT binds to tyrosine-phosphorylated interleukin 3 and erythropoietin
RT receptors.";
RL EMBO J. 14:2816-2826(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Salivary 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 [4]
RP FUNCTION.
RX PubMed=9129017;
RA Matsumoto A., Masuhara M., Mitsui K., Yokouchi M., Ohtsubo M., Misawa H.,
RA Miyajima A., Yoshimura A.;
RT "CIS, a cytokine inducible SH2 protein, is a target of the JAK-STAT5
RT pathway and modulates STAT5 activation.";
RL Blood 89:3148-3154(1997).
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. CIS is
CC involved in the negative regulation of cytokines that signal through
CC the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin
CC 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its
CC tyrosine phosphorylation. May be a substrate-recognition component of a
CC SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein
CC ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:9129017}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Stably associated with the tyrosine-phosphorylated IL3
CC receptor beta chain and tyrosine-phosphorylated EPO receptor (EPOR).
CC -!- INTERACTION:
CC Q62225; P19235: EPOR; Xeno; NbExp=4; IntAct=EBI-617489, EBI-617321;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung and liver. Detected to a
CC lower extent in stomach and heart.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, expressed at low levels
CC from 10 dpc stages to young adulthood (P25) with peak levels from 14
CC dpc to P8.
CC -!- INDUCTION: By a subset of cytokines including interleukins 2, 3 and 6,
CC granulocyte-macrophage colony-stimulating factor (GM-CSF) and
CC erythropoietin (EPO).
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DR EMBL; D31943; BAA06713.1; -; mRNA.
DR EMBL; AK077338; BAC36758.1; -; mRNA.
DR EMBL; AK170554; BAE41877.1; -; mRNA.
DR EMBL; AK170877; BAE42087.1; -; mRNA.
DR EMBL; AK171431; BAE42448.1; -; mRNA.
DR EMBL; BC003783; AAH03783.1; -; mRNA.
DR EMBL; BC022178; AAH22178.1; -; mRNA.
DR CCDS; CCDS40761.1; -.
DR PIR; S55551; S55551.
DR RefSeq; NP_001304283.1; NM_001317354.1.
DR RefSeq; NP_034025.1; NM_009895.4.
DR AlphaFoldDB; Q62225; -.
DR SMR; Q62225; -.
DR BioGRID; 198717; 12.
DR DIP; DIP-907N; -.
DR IntAct; Q62225; 3.
DR MINT; Q62225; -.
DR STRING; 10090.ENSMUSP00000082183; -.
DR iPTMnet; Q62225; -.
DR PhosphoSitePlus; Q62225; -.
DR EPD; Q62225; -.
DR PaxDb; Q62225; -.
DR PRIDE; Q62225; -.
DR ProteomicsDB; 281627; -.
DR Antibodypedia; 14135; 187 antibodies from 31 providers.
DR DNASU; 12700; -.
DR Ensembl; ENSMUST00000085102; ENSMUSP00000082183; ENSMUSG00000032578.
DR GeneID; 12700; -.
DR KEGG; mmu:12700; -.
DR UCSC; uc009rlc.1; mouse.
DR CTD; 1154; -.
DR MGI; MGI:103159; Cish.
DR VEuPathDB; HostDB:ENSMUSG00000032578; -.
DR eggNOG; KOG4566; Eukaryota.
DR GeneTree; ENSGT00940000157392; -.
DR HOGENOM; CLU_079452_4_1_1; -.
DR InParanoid; Q62225; -.
DR OMA; LCVQGPH; -.
DR OrthoDB; 1135696at2759; -.
DR PhylomeDB; Q62225; -.
DR TreeFam; TF321368; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 12700; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cish; mouse.
DR PRO; PR:Q62225; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q62225; protein.
DR Bgee; ENSMUSG00000032578; Expressed in interventricular septum and 206 other tissues.
DR ExpressionAtlas; Q62225; baseline and differential.
DR Genevisible; Q62225; MM.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd10718; SH2_CIS; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR028425; CIS.
DR InterPro; IPR035887; CIS_SH2.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR10155:SF9; PTHR10155:SF9; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Growth regulation; Reference proteome; SH2 domain;
KW Signal transduction inhibitor; Ubl conjugation pathway.
FT CHAIN 1..257
FT /note="Cytokine-inducible SH2-containing protein"
FT /id="PRO_0000181232"
FT DOMAIN 82..163
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 208..256
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 170..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 257 AA; 28537 MW; F14FD8B370B9A005 CRC64;
MVLCVQGSCP LLAVEQIGRR PLWAQSLELP GPAMQPLPTG AFPEEVTEET PVQAENEPKV
LDPEGDLLCI AKTFSYLRES GWYWGSITAS EARQHLQKMP EGTFLVRDST HPSYLFTLSV
KTTRGPTNVR IEYADSSFRL DSNCLSRPRI LAFPDVVSLV QHYVASCAAD TRSDSPDPAP
TPALPMSKQD APSDSVLPIP VATAVHLKLV QPFVRRSSAR SLQHLCRLVI NRLVADVDCL
PLPRRMADYL RQYPFQL
