CMIP_HUMAN
ID CMIP_HUMAN Reviewed; 773 AA.
AC Q8IY22; Q9C0G9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=C-Maf-inducing protein;
DE Short=c-Mip;
DE AltName: Full=Truncated c-Maf-inducing protein;
DE Short=Tc-Mip;
GN Name=CMIP; Synonyms=KIAA1694, TCMIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12939343; DOI=10.1084/jem.20030566;
RA Grimbert P., Valanciute A., Audard V., Pawlak A., Le gouvelo S., Lang P.,
RA Niaudet P., Bensman A., Guellaen G., Sahali D.;
RT "Truncation of C-mip (Tc-mip), a new proximal signaling protein, induces c-
RT maf Th2 transcription factor and cytoskeleton reorganization.";
RL J. Exp. Med. 198:797-807(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-773 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [5]
RP FUNCTION, INTERACTION WITH FLNA, AND SUBCELLULAR LOCATION.
RX PubMed=15128042; DOI=10.1016/j.molimm.2003.11.035;
RA Grimbert P., Valanciute A., Audard V., Lang P., Guellaen G., Sahali D.;
RT "The Filamin-A is a partner of Tc-mip, a new adapter protein involved in c-
RT maf-dependent Th2 signaling pathway.";
RL Mol. Immunol. 40:1257-1261(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-382, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Plays a role in T-cell signaling pathway. Isoform 2 may play
CC a role in T-helper 2 (Th2) signaling pathway and seems to represent the
CC first proximal signaling protein that links T-cell receptor-mediated
CC signal to the activation of c-Maf Th2 specific factor.
CC {ECO:0000269|PubMed:12939343, ECO:0000269|PubMed:15128042}.
CC -!- SUBUNIT: Interacts with FLNA. {ECO:0000269|PubMed:15128042}.
CC -!- INTERACTION:
CC Q8IY22; P27986: PIK3R1; NbExp=2; IntAct=EBI-7689652, EBI-79464;
CC Q8IY22; Q80SY4: Mib1; Xeno; NbExp=2; IntAct=EBI-7689652, EBI-645227;
CC Q8IY22-3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-12149877, EBI-2130429;
CC Q8IY22-3; Q969E8: TSR2; NbExp=3; IntAct=EBI-12149877, EBI-746981;
CC Q8IY22-3; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-12149877, EBI-747993;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12939343}. Cytoplasm
CC {ECO:0000269|PubMed:12939343}. Note=Isoform 2 is translocated to the
CC nucleus and is specifically recruited during minimal change nephrotic
CC syndrome (MCNS) (PubMed:12939343) (PubMed:15616553). Detected in
CC nuclear and cytoplasmic compartments during MCNS relapse
CC (PubMed:12939343) (PubMed:15616553). Expressed in cytoplasm only during
CC MCNS remission and absent in normal patients (PubMed:12939343).
CC {ECO:0000269|PubMed:12939343, ECO:0000269|PubMed:15616553}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=C-Mip;
CC IsoId=Q8IY22-1; Sequence=Displayed;
CC Name=2; Synonyms=Tc-Mip;
CC IsoId=Q8IY22-2; Sequence=VSP_031109, VSP_031110;
CC Name=3;
CC IsoId=Q8IY22-3; Sequence=VSP_031108, VSP_031111;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in peripheral blood
CC mononuclear cells and kidney. Lower expression in brain and liver.
CC Expression is down-regulated in activated cells. Isoform 2 is expressed
CC in lymphocyte precursors, however, expression shuts down during
CC maturation and differentiation in thymus and fetal liver.
CC {ECO:0000269|PubMed:12939343}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver.
CC {ECO:0000269|PubMed:12939343}.
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DR EMBL; AY172689; AAO17720.1; -; mRNA.
DR EMBL; AC092135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038113; AAH38113.1; -; mRNA.
DR EMBL; AB051481; BAB21785.1; -; mRNA.
DR CCDS; CCDS54044.1; -. [Q8IY22-1]
DR CCDS; CCDS54045.1; -. [Q8IY22-2]
DR RefSeq; NP_085132.1; NM_030629.2. [Q8IY22-2]
DR RefSeq; NP_938204.2; NM_198390.2. [Q8IY22-1]
DR AlphaFoldDB; Q8IY22; -.
DR SMR; Q8IY22; -.
DR BioGRID; 123313; 28.
DR IntAct; Q8IY22; 10.
DR MINT; Q8IY22; -.
DR STRING; 9606.ENSP00000446100; -.
DR GlyGen; Q8IY22; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IY22; -.
DR PhosphoSitePlus; Q8IY22; -.
DR BioMuta; CMIP; -.
DR DMDM; 353526341; -.
DR EPD; Q8IY22; -.
DR jPOST; Q8IY22; -.
DR MassIVE; Q8IY22; -.
DR MaxQB; Q8IY22; -.
DR PaxDb; Q8IY22; -.
DR PeptideAtlas; Q8IY22; -.
DR PRIDE; Q8IY22; -.
DR ProteomicsDB; 71089; -. [Q8IY22-1]
DR ProteomicsDB; 71090; -. [Q8IY22-2]
DR ProteomicsDB; 71091; -. [Q8IY22-3]
DR Antibodypedia; 44799; 88 antibodies from 20 providers.
DR DNASU; 80790; -.
DR Ensembl; ENST00000398040.8; ENSP00000381120.4; ENSG00000153815.18. [Q8IY22-3]
DR Ensembl; ENST00000537098.8; ENSP00000446100.2; ENSG00000153815.18. [Q8IY22-1]
DR Ensembl; ENST00000539778.6; ENSP00000440401.2; ENSG00000153815.18. [Q8IY22-2]
DR GeneID; 80790; -.
DR KEGG; hsa:80790; -.
DR MANE-Select; ENST00000537098.8; ENSP00000446100.2; NM_198390.3; NP_938204.2.
DR UCSC; uc002fgp.5; human. [Q8IY22-1]
DR CTD; 80790; -.
DR DisGeNET; 80790; -.
DR GeneCards; CMIP; -.
DR HGNC; HGNC:24319; CMIP.
DR HPA; ENSG00000153815; Low tissue specificity.
DR MIM; 610112; gene.
DR neXtProt; NX_Q8IY22; -.
DR OpenTargets; ENSG00000153815; -.
DR VEuPathDB; HostDB:ENSG00000153815; -.
DR eggNOG; ENOG502QRSV; Eukaryota.
DR GeneTree; ENSGT00390000018220; -.
DR InParanoid; Q8IY22; -.
DR OMA; CEVHTAV; -.
DR OrthoDB; 355421at2759; -.
DR PhylomeDB; Q8IY22; -.
DR TreeFam; TF328575; -.
DR PathwayCommons; Q8IY22; -.
DR SignaLink; Q8IY22; -.
DR BioGRID-ORCS; 80790; 127 hits in 1086 CRISPR screens.
DR ChiTaRS; CMIP; human.
DR GenomeRNAi; 80790; -.
DR Pharos; Q8IY22; Tbio.
DR PRO; PR:Q8IY22; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8IY22; protein.
DR Bgee; ENSG00000153815; Expressed in kidney epithelium and 173 other tissues.
DR ExpressionAtlas; Q8IY22; baseline and differential.
DR Genevisible; Q8IY22; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..773
FT /note="C-Maf-inducing protein"
FT /id="PRO_0000317628"
FT DOMAIN 54..163
FT /note="PH"
FT REPEAT 663..686
FT /note="LRR 1"
FT REPEAT 687..707
FT /note="LRR 2"
FT REPEAT 712..732
FT /note="LRR 3"
FT REPEAT 736..756
FT /note="LRR 4"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031108"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12939343"
FT /id="VSP_031109"
FT VAR_SEQ 95..100
FT /note="SLASAT -> MGQAAE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12939343"
FT /id="VSP_031110"
FT VAR_SEQ 154..159
FT /note="HSLQWK -> MASVAQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031111"
SQ SEQUENCE 773 AA; 86331 MW; D8C25A853A93E9DD CRC64;
MDVTSSSGGG GDPRQIEETK PLLGGDVSAP EGTKMGAVPC RRALLLCNGM RYKLLQEGDI
QVCVIRHPRT FLSKILTSKF LRRWEPHHLT LADNSLASAT PTGYMENSVS YSAIEDVQLL
SWENAPKYCL QLTIPGGTVL LQAANSYLRD QWFHSLQWKK KIYKYKKVLS NPSRWEVVLK
EIRTLVDMAL TSPLQDDSIN QAPLEIVSKL LSENTNLTTQ EHENIIVAIA PLLENNHPPP
DLCEFFCKHC RERPRSMVVI EVFTPVVQRI LKHNMDFGKC PRLRLFTQEY ILALNELNAG
MEVVKKFIQS MHGPTGHCPH PRVLPNLVAV CLAAIYSCYE EFINSRDNSP SLKEIRNGCQ
QPCDRKPTLP LRLLHPSPDL VSQEATLSEA RLKSVVVASS EIHVEVERTS TAKPALTASA
GNDSEPNLID CLMVSPACST MSIELGPQAD RTLGCYVEIL KLLSDYDDWR PSLASLLQPI
PFPKEALAHE KFTKELKYVI QRFAEDPRQE VHSCLLSVRA GKDGWFQLYS PGGVACDDDG
ELFASMVHIL MGSCYKTKKF LLSLAENKLG PCMLLALRGN QTMVEILCLM LEYNIIDNND
TQLQIISTLE STDVGKRMYE QLCDRQRELK ELQRKGGPTR LTLPSKSTDA DLARLLSSGS
FGNLENLSLA FTNVTSACAE HLIKLPSLKQ LNLWSTQFGD AGLRLLSEHL TMLQVLNLCE
TPVTDAGLLA LSSMKSLCSL NMNSTKLSAD TYEDLKAKLP NLKEVDVRYT EAW
