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CING_HUMAN
ID   CING_HUMAN              Reviewed;        1203 AA.
AC   Q9P2M7; A6H8L3; A7MD22; Q5T386; Q9NR25;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 3.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Cingulin {ECO:0000305};
GN   Name=CGN {ECO:0000312|HGNC:HGNC:17429}; Synonyms=KIAA1319;
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 1), AND SUBUNIT.
RC   TISSUE=Neuroepithelium;
RX   PubMed=11042084; DOI=10.1006/jsbi.2000.4284;
RA   Citi S., D'Atri F., Parry D.A.D.;
RT   "Human and Xenopus cingulin share a modular organization of the coiled-coil
RT   rod domain: predictions for intra- and intermolecular assembly.";
RL   J. Struct. Biol. 131:135-145(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [7]
RP   PROTEIN SEQUENCE OF 374-382.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   INTERACTION WITH TJP1.
RX   PubMed=12023291; DOI=10.1074/jbc.m203717200;
RA   D'Atri F., Nadalutti F., Citi S.;
RT   "Evidence for a functional interaction between cingulin and ZO-1 in
RT   cultured cells.";
RL   J. Biol. Chem. 277:27757-27764(2002).
RN   [9]
RP   IDENTIFICATION BY 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-1182, AND
RP   IDENTIFICATION BY 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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-165, AND
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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-579, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-258, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-140; SER-155;
RP   SER-165; SER-214; SER-217 AND THR-712, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-137; SER-140;
RP   SER-258; SER-276; SER-1175 AND SER-1176, AND IDENTIFICATION BY MASS
RP   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   [18]
RP   INTERACTION WITH SPEF1, AND SUBCELLULAR LOCATION.
RX   PubMed=31473225; DOI=10.1053/j.gastro.2019.08.031;
RA   Tapia R., Perez-Yepez E.A., Carlino M.J., Karandikar U.C., Kralicek S.E.,
RA   Estes M.K., Hecht G.A.;
RT   "Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and
RT   Contributes to Formation of Filopodia and Lamellipodia.";
RL   Gastroenterology 157:1544-1555(2019).
CC   -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC       tight junction (TJ) paracellular permeability barrier.
CC   -!- SUBUNIT: Homodimer (PubMed:11042084). Interacts with TJP1/ZO1
CC       (PubMed:12023291). Interacts with SPEF1 (PubMed:31473225).
CC       {ECO:0000269|PubMed:12023291, ECO:0000269|PubMed:31473225,
CC       ECO:0000303|PubMed:11042084}.
CC   -!- INTERACTION:
CC       Q9P2M7; P63104: YWHAZ; NbExp=3; IntAct=EBI-79537, EBI-347088;
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000250|UniProtKB:P59242}. Note=Localizes to the apical junction
CC       complex composed of tight and adherens junctions (By similarity).
CC       Colocalizes with SPEF1 at sites of cell-cell contact in intestinal
CC       epithelial cells (PubMed:12023291). {ECO:0000250|UniProtKB:P59242,
CC       ECO:0000269|PubMed:12023291}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9P2M7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P2M7-2; Sequence=VSP_037039, VSP_037040;
CC   -!- TISSUE SPECIFICITY: Localized on the cytoplasmic face of tight
CC       junctions of polarized epithelia and some endothelia. Expressed in
CC       pancreas, kidney, liver and lung, but not in skeletal muscle, placenta,
CC       brain or heart.
CC   -!- DOMAIN: Deletion of the TJP1/ZO1 interaction motif (ZIM) decreases but
CC       does not abolish colocalization with TJP1/ZO1.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cingulin family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI46658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA92557.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF263462; AAF74498.1; -; mRNA.
DR   EMBL; AB037740; BAA92557.1; ALT_INIT; mRNA.
DR   EMBL; AK290007; BAF82696.1; -; mRNA.
DR   EMBL; AL365436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53434.1; -; Genomic_DNA.
DR   EMBL; BC146657; AAI46658.1; ALT_INIT; mRNA.
DR   EMBL; BC152445; AAI52446.1; -; mRNA.
DR   CCDS; CCDS999.1; -. [Q9P2M7-1]
DR   RefSeq; NP_065821.1; NM_020770.2.
DR   RefSeq; XP_005245422.1; XM_005245365.4.
DR   AlphaFoldDB; Q9P2M7; -.
DR   BioGRID; 121589; 137.
DR   DIP; DIP-30947N; -.
DR   IntAct; Q9P2M7; 38.
DR   MINT; Q9P2M7; -.
DR   STRING; 9606.ENSP00000271636; -.
DR   iPTMnet; Q9P2M7; -.
DR   MetOSite; Q9P2M7; -.
DR   PhosphoSitePlus; Q9P2M7; -.
DR   BioMuta; CGN; -.
DR   DMDM; 27923755; -.
DR   EPD; Q9P2M7; -.
DR   jPOST; Q9P2M7; -.
DR   MassIVE; Q9P2M7; -.
DR   MaxQB; Q9P2M7; -.
DR   PaxDb; Q9P2M7; -.
DR   PeptideAtlas; Q9P2M7; -.
DR   PRIDE; Q9P2M7; -.
DR   ProteomicsDB; 83849; -. [Q9P2M7-1]
DR   ProteomicsDB; 83850; -. [Q9P2M7-2]
DR   Antibodypedia; 34064; 106 antibodies from 23 providers.
DR   DNASU; 57530; -.
DR   Ensembl; ENST00000271636.12; ENSP00000271636.7; ENSG00000143375.15. [Q9P2M7-1]
DR   GeneID; 57530; -.
DR   KEGG; hsa:57530; -.
DR   MANE-Select; ENST00000271636.12; ENSP00000271636.7; NM_020770.3; NP_065821.1.
DR   UCSC; uc009wmw.4; human. [Q9P2M7-1]
DR   CTD; 57530; -.
DR   DisGeNET; 57530; -.
DR   GeneCards; CGN; -.
DR   HGNC; HGNC:17429; CGN.
DR   HPA; ENSG00000143375; Tissue enhanced (intestine).
DR   MIM; 609473; gene.
DR   neXtProt; NX_Q9P2M7; -.
DR   OpenTargets; ENSG00000143375; -.
DR   PharmGKB; PA134938123; -.
DR   VEuPathDB; HostDB:ENSG00000143375; -.
DR   eggNOG; ENOG502R9EI; Eukaryota.
DR   GeneTree; ENSGT00940000154489; -.
DR   HOGENOM; CLU_002036_0_0_1; -.
DR   InParanoid; Q9P2M7; -.
DR   OrthoDB; 110948at2759; -.
DR   PhylomeDB; Q9P2M7; -.
DR   TreeFam; TF332247; -.
DR   PathwayCommons; Q9P2M7; -.
DR   Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   SignaLink; Q9P2M7; -.
DR   BioGRID-ORCS; 57530; 12 hits in 1069 CRISPR screens.
DR   ChiTaRS; CGN; human.
DR   GeneWiki; Cingulin; -.
DR   GenomeRNAi; 57530; -.
DR   Pharos; Q9P2M7; Tbio.
DR   PRO; PR:Q9P2M7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9P2M7; protein.
DR   Bgee; ENSG00000143375; Expressed in pancreatic ductal cell and 146 other tissues.
DR   ExpressionAtlas; Q9P2M7; baseline and differential.
DR   Genevisible; Q9P2M7; HS.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF01576; Myosin_tail_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell junction; Coiled coil;
KW   Direct protein sequencing; Phosphoprotein; Reference proteome;
KW   Tight junction.
FT   CHAIN           1..1203
FT                   /note="Cingulin"
FT                   /id="PRO_0000089763"
FT   REGION          7..357
FT                   /note="Head"
FT   REGION          25..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..67
FT                   /note="Interaction with TJP1/ZO1"
FT                   /evidence="ECO:0000269|PubMed:12023291"
FT   REGION          89..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1161..1203
FT                   /note="Tail"
FT   COILED          358..1160
FT                   /evidence="ECO:0000255"
FT   MOTIF           48..62
FT                   /note="ZIM"
FT   COMPBIAS        109..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P59242"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P59242"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P59242"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P59242"
FT   MOD_RES         579
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         712
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         704..777
FT                   /note="KMVAEAEATVLGQRRAAVETTLRETQEENDEFRRRILGLEQQLKETRGLVDG
FT                   GEAVEARLRDKLQRLEAEKQQL -> RGVGTGLRRWRLRVSGGLRSQRVWKVTCHGYVL
FT                   TSSWVLGMWFKEARIWQGEDTCICVGVGFSEKRLAGGSCSL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037039"
FT   VAR_SEQ         778..1203
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037040"
FT   VARIANT         485
FT                   /note="R -> Q (in dbSNP:rs12038198)"
FT                   /id="VAR_057809"
SQ   SEQUENCE   1203 AA;  137057 MW;  0AE294110E605765 CRC64;
     MEQAPNMAEP RGPVDHGVQI RFITEPVSGA EMGTLRRGGR RPAKDARAST YGVAVRVQGI
     AGQPFVVLNS GEKGGDSFGV QIKGANDQGA SGALSSDLEL PENPYSQVKG FPAPSQSSTS
     DEEPGAYWNG KLLRSHSQAS LAGPGPVDPS NRSNSMLELA PKVASPGSTI DTAPLSSVDS
     LINKFDSQLG GQARGRTGRR TRMLPPEQRK RSKSLDSRLP RDTFEERERQ STNHWTSSTK
     YDNHVGTSKQ PAQSQNLSPL SGFSRSRQTQ DWVLQSFEEP RRSAQDPTML QFKSTPDLLR
     DQQEAAPPGS VDHMKATIYG ILREGSSESE TSVRRKVSLV LEKMQPLVMV SSGSTKAVAG
     QGELTRKVEE LQRKLDEEVK KRQKLEPSQV GLERQLEEKT EECSRLQELL ERRKGEAQQS
     NKELQNMKRL LDQGEDLRHG LETQVMELQN KLKHVQGPEP AKEVLLKDLL ETRELLEEVL
     EGKQRVEEQL RLRERELTAL KGALKEEVAS RDQEVEHVRQ QYQRDTEQLR RSMQDATQDH
     AVLEAERQKM SALVRGLQRE LEETSEETGH WQSMFQKNKE DLRATKQELL QLRMEKEEME
     EELGEKIEVL QRELEQARAS AGDTRQVEVL KKELLRTQEE LKELQAERQS QEVAGRHRDR
     ELEKQLAVLR VEADRGRELE EQNLQLQKTL QQLRQDCEEA SKAKMVAEAE ATVLGQRRAA
     VETTLRETQE ENDEFRRRIL GLEQQLKETR GLVDGGEAVE ARLRDKLQRL EAEKQQLEEA
     LNASQEEEGS LAAAKRALEA RLEEAQRGLA RLGQEQQTLN RALEEEGKQR EVLRRGKAEL
     EEQKRLLDRT VDRLNKELEK IGEDSKQALQ QLQAQLEDYK EKARREVADA QRQAKDWASE
     AEKTSGGLSR LQDEIQRLRQ ALQASQAERD TARLDKELLA QRLQGLEQEA ENKKRSQDDR
     ARQLKGLEEK VSRLETELDE EKNTVELLTD RVNRGRDQVD QLRTELMQER SARQDLECDK
     ISLERQNKDL KTRLASSEGF QKPSASLSQL ESQNQLLQER LQAEEREKTV LQSTNRKLER
     KVKELSIQIE DERQHVNDQK DQLSLRVKAL KRQVDEAEEE IERLDGLRKK AQREVEEQHE
     VNEQLQARIK SLEKDSWRKA SRSAAESALK NEGLSSDEEF DSVYDPSSIA SLLTESNLQT
     SSC
 
 
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