ID CRCM_HUMAN Reviewed; 829 AA. AC P23508; D3DT05; Q6ZR04; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 24-JAN-2024, entry version 191. DE RecName: Full=Colorectal mutant cancer protein; DE Short=Protein MCC; GN Name=MCC; 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], AND VARIANTS ARG-190; GLN-506 AND VAL-698. RC TISSUE=Brain; RX PubMed=1848370; DOI=10.1126/science.1848370; RA Kinzler K.W., Nilbert M.C., Vogelstein B., Bryan T.M., Levy D.B., RA Smith K.J., Preisinger A.C., Hamilton S.R., Hedge P., Markham A., RA Carlson M., Joslyn G., Groden J., White R., Miki Y., Miyoshi Y., RA Nishisho I., Nakamura Y.; RT "Identification of a gene located at chromosome 5q21 that is mutated in RT colorectal cancers."; RL Science 251:1366-1370(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-190. RC TISSUE=Muscle; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-779 (ISOFORM 2), AND VARIANT RP ARG-190. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP FUNCTION IN WNT SIGNALING, SUBCELLULAR LOCATION, AND INTERACTION WITH RP CTNNB1. RX PubMed=18591935; DOI=10.1038/onc.2008.204; RA Fukuyama R., Niculaita R., Ng K.P., Obusez E., Sanchez J., Kalady M., RA Aung P.P., Casey G., Sizemore N.; RT "Mutated in colorectal cancer, a putative tumor suppressor for serrated RT colorectal cancer, selectively represses beta-catenin-dependent RT transcription."; RL Oncogene 27:6044-6055(2008). RN [7] RP FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, AND INTERACTION WITH RP SCRIB; EZR; SNX27; NHERF1 AND NHERF2. RX PubMed=19555689; DOI=10.1016/j.febslet.2009.06.034; RA Arnaud C., Sebbagh M., Nola S., Audebert S., Bidaut G., Hermant A., RA Gayet O., Dusetti N.J., Ollendorff V., Santoni M.J., Borg J.P., Lecine P.; RT "MCC, a new interacting protein for Scrib, is required for cell migration RT in epithelial cells."; RL FEBS Lett. 583:2326-2332(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP FUNCTION, PDZ-BINDING MOTIF, PHOSPHORYLATION AT SER-828, INTERACTION WITH RP SCRIB AND MYH10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-828. RX PubMed=22480440; DOI=10.1016/j.bbamcr.2012.03.011; RA Pangon L., Van Kralingen C., Abas M., Daly R.J., Musgrove E.A., RA Kohonen-Corish M.R.; RT "The PDZ-binding motif of MCC is phosphorylated at position -1 and controls RT lamellipodia formation in colon epithelial cells."; RL Biochim. Biophys. Acta 1823:1058-1067(2012). RN [10] RP IDENTIFICATION BY 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). RN [11] RP VARIANTS LEU-267; LEU-486; LEU-490; GLN-506 AND VAL-698. RX PubMed=1651563; DOI=10.1126/science.1651563; RA Nishisho I., Nakamura Y., Miyoshi Y., Miki Y., Ando H., Horii A., RA Koyama K., Utsunomiya J., Baba S., Hedge P., Markham A., Krush A.J., RA Petersen G.M., Hamilton S.R., Nilbert M.C., Levy D.B., Bryan T.M., RA Preisinger A.C., Smith K.J., Su L.-K., Kinzler K.W., Vogelstein B.; RT "Mutations of chromosome 5q21 genes in FAP and colorectal cancer RT patients."; RL Science 253:665-669(1991). RN [12] RP CHARACTERIZATION OF VARIANT GLN-506, FUNCTION, SUBCELLULAR LOCATION, RP INTERACTION WITH CCAR2, AND NUCLEAR LOCALIZATION SIGNAL. RX PubMed=24824780; DOI=10.1002/ijc.28967; RA Pangon L., Mladenova D., Watkins L., Van Kralingen C., Currey N., RA Al-Sohaily S., Lecine P., Borg J.P., Kohonen-Corish M.R.; RT "MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in RT the cytoplasm."; RL Int. J. Cancer 136:55-64(2015). RN [13] RP VARIANT LYS-142. RX PubMed=27932480; DOI=10.1681/asn.2016040387; RG NephroS; RG UK study of Nephrotic Syndrome; RA Bierzynska A., Soderquest K., Dean P., Colby E., Rollason R., Jones C., RA Inward C.D., McCarthy H.J., Simpson M.A., Lord G.M., Williams M., RA Welsh G.I., Koziell A.B., Saleem M.A.; RT "MAGI2 mutations cause congenital nephrotic syndrome."; RL J. Am. Soc. Nephrol. 28:1614-1621(2017). CC -!- FUNCTION: Candidate for the putative colorectal tumor suppressor gene CC located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin CC pathway in colorectal cancer cells. Inhibits DNA binding of b- CC catenin/TCF/LEF transcription factors. Involved in cell migration CC independently of RAC1, CDC42 and p21-activated kinase (PAK) activation CC (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the CC beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2- CC dependent manner by sequestering CCAR2 to the cytoplasm, thereby CC impairing its ability to inhibit SIRT1 which is involved in the CC deacetylation and negative regulation of beta-catenin (CTNB1) CC transcriptional activity (PubMed:24824780). CC {ECO:0000269|PubMed:18591935, ECO:0000269|PubMed:19555689, CC ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:24824780}. CC -!- SUBUNIT: Interacts with SCRIB (via phosphorylated PDZ-binding motif), CC EZR, SNX27, NHERF1 and NHERF2. Interacts with CTNNB1; the interaction CC is enhanced upon Wnt stimulation. Interacts with MYH10. Interacts with CC CCAR2. {ECO:0000269|PubMed:18591935, ECO:0000269|PubMed:19555689, CC ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:24824780}. CC -!- INTERACTION: CC P23508; O95696: BRD1; NbExp=3; IntAct=EBI-307531, EBI-714754; CC P23508; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-307531, EBI-715389; CC P23508; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-307531, EBI-751596; CC P23508; Q9HC52: CBX8; NbExp=3; IntAct=EBI-307531, EBI-712912; CC P23508; Q8NEF3-2: CCDC112; NbExp=3; IntAct=EBI-307531, EBI-12095166; CC P23508; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-307531, EBI-10749669; CC P23508; Q8N715: CCDC185; NbExp=3; IntAct=EBI-307531, EBI-740814; CC P23508; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-307531, EBI-3919850; CC P23508; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-307531, EBI-1104570; CC P23508; Q96GE4: CEP95; NbExp=3; IntAct=EBI-307531, EBI-372775; CC P23508; Q5T655: CFAP58; NbExp=3; IntAct=EBI-307531, EBI-10245749; CC P23508; P49674: CSNK1E; NbExp=4; IntAct=EBI-307531, EBI-749343; CC P23508; Q8WXU2-2: DNAAF4; NbExp=3; IntAct=EBI-307531, EBI-9381887; CC P23508; Q14241: ELOA; NbExp=3; IntAct=EBI-307531, EBI-742350; CC P23508; P62508-3: ESRRG; NbExp=3; IntAct=EBI-307531, EBI-12001340; CC P23508; Q3B820: FAM161A; NbExp=3; IntAct=EBI-307531, EBI-719941; CC P23508; O43320: FGF16; NbExp=3; IntAct=EBI-307531, EBI-11479104; CC P23508; P29084: GTF2E2; NbExp=2; IntAct=EBI-307531, EBI-2853321; CC P23508; Q9NV31: IMP3; NbExp=3; IntAct=EBI-307531, EBI-747481; CC P23508; Q92993: KAT5; NbExp=3; IntAct=EBI-307531, EBI-399080; CC P23508; O14782: KIF3C; NbExp=3; IntAct=EBI-307531, EBI-1104854; CC P23508; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-307531, EBI-14069005; CC P23508; Q96CN5: LRRC45; NbExp=3; IntAct=EBI-307531, EBI-2805176; CC P23508; Q9HCI5: MAGEE1; NbExp=3; IntAct=EBI-307531, EBI-949966; CC P23508; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-307531, EBI-14086479; CC P23508; Q9UGY1: NOL12; NbExp=3; IntAct=EBI-307531, EBI-716098; CC P23508; P05165: PCCA; NbExp=3; IntAct=EBI-307531, EBI-2211679; CC P23508; Q96T60: PNKP; NbExp=3; IntAct=EBI-307531, EBI-1045072; CC P23508; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-307531, EBI-10320765; CC P23508; Q99633: PRPF18; NbExp=3; IntAct=EBI-307531, EBI-2798416; CC P23508; P26045: PTPN3; NbExp=2; IntAct=EBI-307531, EBI-1047946; CC P23508; Q9UJF2-2: RASAL2; NbExp=3; IntAct=EBI-307531, EBI-12171247; CC P23508; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-307531, EBI-1504830; CC P23508; Q14160: SCRIB; NbExp=14; IntAct=EBI-307531, EBI-357345; CC P23508; Q9NWH9: SLTM; NbExp=3; IntAct=EBI-307531, EBI-2814558; CC P23508; O95391: SLU7; NbExp=3; IntAct=EBI-307531, EBI-750559; CC P23508; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-307531, EBI-745392; CC P23508; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-307531, EBI-10246152; CC P23508; Q15560: TCEA2; NbExp=3; IntAct=EBI-307531, EBI-710310; CC P23508; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-307531, EBI-11955057; CC P23508; Q9BT49: THAP7; NbExp=3; IntAct=EBI-307531, EBI-741350; CC P23508; Q8IZ69: TRMT2A; NbExp=3; IntAct=EBI-307531, EBI-2515774; CC P23508; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-307531, EBI-10687282; CC P23508; P40222: TXLNA; NbExp=3; IntAct=EBI-307531, EBI-359793; CC P23508; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-307531, EBI-11737646; CC P23508; P10074: ZBTB48; NbExp=3; IntAct=EBI-307531, EBI-744864; CC P23508; P17014: ZNF12; NbExp=3; IntAct=EBI-307531, EBI-11278550; CC P23508; O95125: ZNF202; NbExp=3; IntAct=EBI-307531, EBI-751960; CC P23508; O43296: ZNF264; NbExp=3; IntAct=EBI-307531, EBI-4395808; CC P23508; P17036: ZNF3; NbExp=3; IntAct=EBI-307531, EBI-1640965; CC P23508; P13682: ZNF35; NbExp=3; IntAct=EBI-307531, EBI-11041653; CC P23508; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-307531, EBI-740727; CC P23508; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-307531, EBI-11962468; CC P23508; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-307531, EBI-10486136; CC P23508; Q08ER8: ZNF543; NbExp=3; IntAct=EBI-307531, EBI-10226133; CC P23508; Q5T619: ZNF648; NbExp=3; IntAct=EBI-307531, EBI-11985915; CC P23508; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-307531, EBI-10240849; CC -!- SUBCELLULAR LOCATION: Cell membrane. Cell projection, lamellipodium. CC Nucleus {ECO:0000269|PubMed:24824780}. Cytoplasm CC {ECO:0000269|PubMed:24824780}. Note=Colocalizes with actin at the CC leading edge of polarized cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P23508-1; Sequence=Displayed; CC Name=2; CC IsoId=P23508-2; Sequence=VSP_037660; CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. CC -!- SIMILARITY: Belongs to the MCC 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; M62397; AAA52069.1; -; mRNA. DR EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010431; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093208; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC106750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC126917; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471086; EAW48984.1; -; Genomic_DNA. DR EMBL; CH471086; EAW48986.1; -; Genomic_DNA. DR EMBL; BC009279; AAH09279.1; -; mRNA. DR EMBL; BC018919; AAH18919.1; -; mRNA. DR EMBL; AK128596; BAC87521.1; -; mRNA. DR CCDS; CCDS4111.1; -. [P23508-1] DR CCDS; CCDS43351.1; -. [P23508-2] DR PIR; A38434; A33166. DR RefSeq; NP_001078846.1; NM_001085377.1. [P23508-2] DR RefSeq; NP_002378.1; NM_002387.2. [P23508-1] DR PDB; 6MTU; X-ray; 2.14 A; C/D=822-829. DR PDB; 6MTV; X-ray; 2.60 A; D/E=822-829. DR PDBsum; 6MTU; -. DR PDBsum; 6MTV; -. DR AlphaFoldDB; P23508; -. DR SMR; P23508; -. DR BioGRID; 110333; 215. DR CORUM; P23508; -. DR DIP; DIP-27599N; -. DR IntAct; P23508; 96. DR MINT; P23508; -. DR STRING; 9606.ENSP00000386227; -. DR GlyGen; P23508; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P23508; -. DR PhosphoSitePlus; P23508; -. DR BioMuta; MCC; -. DR DMDM; 317373352; -. DR EPD; P23508; -. DR jPOST; P23508; -. DR MassIVE; P23508; -. DR MaxQB; P23508; -. DR PaxDb; 9606-ENSP00000386227; -. DR PeptideAtlas; P23508; -. DR ProteomicsDB; 54120; -. [P23508-1] DR ProteomicsDB; 54121; -. [P23508-2] DR Pumba; P23508; -. DR Antibodypedia; 25386; 256 antibodies from 27 providers. DR DNASU; 4163; -. DR Ensembl; ENST00000302475.9; ENSP00000305617.4; ENSG00000171444.19. [P23508-1] DR Ensembl; ENST00000408903.7; ENSP00000386227.3; ENSG00000171444.19. [P23508-2] DR GeneID; 4163; -. DR KEGG; hsa:4163; -. DR MANE-Select; ENST00000408903.7; ENSP00000386227.3; NM_001085377.2; NP_001078846.2. [P23508-2] DR UCSC; uc003kqj.5; human. [P23508-1] DR AGR; HGNC:6935; -. DR CTD; 4163; -. DR DisGeNET; 4163; -. DR GeneCards; MCC; -. DR HGNC; HGNC:6935; MCC. DR HPA; ENSG00000171444; Tissue enhanced (ovary). DR MalaCards; MCC; -. DR MIM; 159350; gene. DR neXtProt; NX_P23508; -. DR OpenTargets; ENSG00000171444; -. DR PharmGKB; PA30679; -. DR VEuPathDB; HostDB:ENSG00000171444; -. DR eggNOG; ENOG502QPWE; Eukaryota. DR GeneTree; ENSGT00530000063974; -. DR InParanoid; P23508; -. DR OMA; RCRMQLI; -. DR OrthoDB; 2917181at2759; -. DR PhylomeDB; P23508; -. DR TreeFam; TF333056; -. DR PathwayCommons; P23508; -. DR SignaLink; P23508; -. DR SIGNOR; P23508; -. DR BioGRID-ORCS; 4163; 10 hits in 1151 CRISPR screens. DR ChiTaRS; MCC; human. DR GeneWiki; MCC_(gene); -. DR GenomeRNAi; 4163; -. DR Pharos; P23508; Tbio. DR PRO; PR:P23508; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P23508; Protein. DR Bgee; ENSG00000171444; Expressed in gingival epithelium and 188 other cell types or tissues. DR ExpressionAtlas; P23508; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0045184; P:establishment of protein localization; IDA:CACAO. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 6.10.250.3110; -; 1. DR InterPro; IPR040171; USBP1-like. DR InterPro; IPR019536; USHBP1_PDZ-bd. DR PANTHER; PTHR23347:SF4; COLORECTAL MUTANT CANCER PROTEIN; 1. DR PANTHER; PTHR23347; COLORECTAL MUTANT CANCER PROTEIN MCC PROTEIN -RELATED; 1. DR Pfam; PF10506; USHBP1_PDZ-bd; 2. DR Genevisible; P23508; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Cytoplasm; Membrane; Nucleus; Phosphoprotein; Reference proteome; KW Tumor suppressor; Wnt signaling pathway. FT CHAIN 1..829 FT /note="Colorectal mutant cancer protein" FT /id="PRO_0000079333" FT REGION 114..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 282..320 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 672..700 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 766..782 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:24824780" FT MOTIF 826..829 FT /note="PDZ-binding" FT COMPBIAS 114..130 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 828 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22480440" FT VAR_SEQ 1..19 FT /note="MNSGVAMKYGNDSSAELSE -> MMAAAAAAAAGSSSSGGGGGGSGSSSSSS FT DTSSTGEEERMRRLFQTCDGDGDGYISRNDLLMVCRQLNMEESVAEIMNQLGADENGKI FT SFQDFTRCRMQLVREIRKEEVDLSAKSDNSCTKKLRDRIASWPTSSDNSLGALSAARES FT WEYDSGARDLQSPDVQSQSALQKLLEYGGSSLHQQAALHKLLTQSPHIGNSVGGSYLEL FT ANT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037660" FT VARIANT 142 FT /note="E -> K (in dbSNP:rs185322500)" FT /evidence="ECO:0000269|PubMed:27932480" FT /id="VAR_079267" FT VARIANT 190 FT /note="K -> R (in dbSNP:rs6594681)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1848370" FT /id="VAR_050905" FT VARIANT 267 FT /note="R -> L (in a colorectal cancer sample)" FT /evidence="ECO:0000269|PubMed:1651563" FT /id="VAR_005141" FT VARIANT 486 FT /note="P -> L (in a colorectal cancer sample; FT dbSNP:rs35269015)" FT /evidence="ECO:0000269|PubMed:1651563" FT /id="VAR_005142" FT VARIANT 490 FT /note="S -> L (in a colorectal cancer sample; FT dbSNP:rs760495893)" FT /evidence="ECO:0000269|PubMed:1651563" FT /id="VAR_005143" FT VARIANT 506 FT /note="R -> Q (in colorectal cancer samples; somatic FT mutation; decreased binding to CCAR2; significant decrease FT in its ability to induce the relocalization of CCAR2 to the FT cytoplasm; loss of its ability to repress the beta-catenin FT pathway; loss of its ability to induce the SIRT1-mediated FT deacetylation of beta-catenin; dbSNP:rs121917732)" FT /evidence="ECO:0000269|PubMed:1651563, FT ECO:0000269|PubMed:1848370, ECO:0000269|PubMed:24824780" FT /id="VAR_005144" FT VARIANT 698 FT /note="A -> V (in colorectal cancer samples; somatic FT mutation; dbSNP:rs121917731)" FT /evidence="ECO:0000269|PubMed:1651563, FT ECO:0000269|PubMed:1848370" FT /id="VAR_005145" FT VARIANT 751 FT /note="S -> C (in dbSNP:rs17313892)" FT /id="VAR_033753" FT MUTAGEN 828 FT /note="S->A: Reduced binding to SCRIB." FT /evidence="ECO:0000269|PubMed:22480440" FT MUTAGEN 828 FT /note="S->D: Higher membrane localization, reduced FT formation of lamellipodia, accumulation of MYH10 at the FT cell cortex." FT /evidence="ECO:0000269|PubMed:22480440" FT CONFLICT 353 FT /note="S -> G (in Ref. 5; BAC87521)" FT /evidence="ECO:0000305" FT STRAND 825..829 FT /evidence="ECO:0007829|PDB:6MTU" FT CONFLICT P23508-2:25 FT /note="S -> GSSSG (in Ref. 5; BAC87521)" FT /evidence="ECO:0000305" SQ SEQUENCE 829 AA; 93027 MW; C90611B2E91A7F60 CRC64; MNSGVAMKYG NDSSAELSEL HSAALASLKG DIVELNKRLQ QTERERDLLE KKLAKAQCEQ SHLMREHEDV QERTTLRYEE RITELHSVIA ELNKKIDRLQ GTTIREEDEY SELRSELSQS QHEVNEDSRS MDQDQTSVSI PENQSTMVTA DMDNCSDLNS ELQRVLTGLE NVVCGRKKSS CSLSVAEVDK HIEQLTTASE HCDLAIKTVE EIEGVLGRDL YPNLAEERSR WEKELAGLRE ENESLTAMLC SKEEELNRTK ATMNAIREER DRLRRRVREL QTRLQSVQAT GPSSPGRLTS TNRPINPSTG ELSTSSSSND IPIAKIAERV KLSKTRSESS SSDRPVLGSE ISSIGVSSSV AEHLAHSLQD CSNIQEIFQT LYSHGSAISE SKIREFEVET ERLNSRIEHL KSQNDLLTIT LEECKSNAER MSMLVGKYES NATALRLALQ YSEQCIEAYE LLLALAESEQ SLILGQFRAA GVGSSPGDQS GDENITQMLK RAHDCRKTAE NAAKALLMKL DGSCGGAFAV AGCSVQPWES LSSNSHTSTT SSTASSCDTE FTKEDEQRLK DYIQQLKNDR AAVKLTMLEL ESIHIDPLSY DVKPRGDSQR LDLENAVLMQ ELMAMKEEMA ELKAQLYLLE KEKKALELKL STREAQEQAY LVHIEHLKSE VEEQKEQRMR SLSSTSSGSK DKPGKECADA ASPALSLAEL RTTCSENELA AEFTNAIRRE KKLKARVQEL VSALERLTKS SEIRHQQSAE FVNDLKRANS NLVAAYEKAK KKHQNKLKKL ESQMMAMVER HETQVRMLKQ RIALLEEENS RPHTNETSL //