CYTSA_HUMAN
ID CYTSA_HUMAN Reviewed; 1117 AA.
AC Q69YQ0; B7Z758; F5H1H6; O15081;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytospin-A;
DE AltName: Full=Renal carcinoma antigen NY-REN-22;
DE AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1-like;
DE Short=SPECC1-like protein;
GN Name=SPECC1L; Synonyms=CYTSA, KIAA0376;
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 VARIANT MET-951.
RC TISSUE=Brain;
RA Huang C.-H., Ye T., Chen Y.;
RT "Characterization of cytospin A as a multiple coiled coil protein involved
RT in cytokinesis and spindle organization.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-951.
RC TISSUE=Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-951.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1041 (ISOFORM 1), AND VARIANT
RP MET-951.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [6]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-881, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868 AND SER-881, 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 [9]
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 [10]
RP FUNCTION, INTERACTION WITH MICROTUBULES AND ACTIN CYTOSKELETON, SUBCELLULAR
RP LOCATION, VARIANT OBLFC1 PRO-415, AND VARIANT MET-190.
RX PubMed=21703590; DOI=10.1016/j.ajhg.2011.05.023;
RA Saadi I., Alkuraya F.S., Gisselbrecht S.S., Goessling W., Cavallesco R.,
RA Turbe-Doan A., Petrin A.L., Harris J., Siddiqui U., Grix A.W. Jr.,
RA Hove H.D., Leboulch P., Glover T.W., Morton C.C., Richieri-Costa A.,
RA Murray J.C., Erickson R.P., Maas R.L.;
RT "Deficiency of the cytoskeletal protein SPECC1L leads to oblique facial
RT clefting.";
RL Am. J. Hum. Genet. 89:44-55(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-881 AND SER-887, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887, 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).
RN [13]
RP INVOLVEMENT IN TBHS1, AND VARIANTS TBHS1 400-ILE-HIS-401 DEL AND ASP-420.
RX PubMed=26111080; DOI=10.1002/ajmg.a.37217;
RA Bhoj E.J., Li D., Harr M.H., Tian L., Wang T., Zhao Y., Qiu H., Kim C.,
RA Hoffman J.D., Hakonarson H., Zackai E.H.;
RT "Expanding the SPECC1L mutation phenotypic spectrum to include Teebi
RT hypertelorism syndrome.";
RL Am. J. Med. Genet. A 167A:2497-2502(2015).
RN [14]
RP INVOLVEMENT IN TBHS1, VARIANTS TBHS1 PRO-397 AND SER-1083, AND
RP CHARACTERIZATION OF VARIANTS TBHS1 PRO-397 AND SER-1083.
RX PubMed=25412741; DOI=10.1136/jmedgenet-2014-102677;
RA Kruszka P., Li D., Harr M.H., Wilson N.R., Swarr D., McCormick E.M.,
RA Chiavacci R.M., Li M., Martinez A.F., Hart R.A., McDonald-McGinn D.M.,
RA Deardorff M.A., Falk M.J., Allanson J.E., Hudson C., Johnson J.P.,
RA Saadi I., Hakonarson H., Muenke M., Zackai E.H.;
RT "Mutations in SPECC1L, encoding sperm antigen with calponin homology and
RT coiled-coil domains 1-like, are found in some cases of autosomal dominant
RT Opitz G/BBB syndrome.";
RL J. Med. Genet. 52:104-110(2015).
CC -!- FUNCTION: Involved in cytokinesis and spindle organization. May play a
CC role in actin cytoskeleton organization and microtubule stabilization
CC and hence required for proper cell adhesion and migration.
CC {ECO:0000269|PubMed:21703590}.
CC -!- SUBUNIT: May interact with both microtubules and actin cytoskeleton.
CC -!- INTERACTION:
CC Q69YQ0; Q8N7B9-2: EFCAB3; NbExp=3; IntAct=EBI-351113, EBI-11958551;
CC Q69YQ0; Q14241: ELOA; NbExp=3; IntAct=EBI-351113, EBI-742350;
CC Q69YQ0; Q9BZL4: PPP1R12C; NbExp=3; IntAct=EBI-351113, EBI-721802;
CC Q69YQ0; Q13573: SNW1; NbExp=3; IntAct=EBI-351113, EBI-632715;
CC Q69YQ0; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-351113, EBI-10237226;
CC Q69YQ0; P15622-3: ZNF250; NbExp=3; IntAct=EBI-351113, EBI-10177272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21703590}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:21703590}. Cell junction, gap junction
CC {ECO:0000269|PubMed:21703590}. Note=Colocalizes with acetylated alpha-
CC tubulin, gamma-tubulin and F-actin. Also observed in a ring around
CC gamma-tubulin containing centrioles possibly in the microtubule
CC organizing center.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69YQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69YQ0-2; Sequence=VSP_047359;
CC -!- DISEASE: Facial clefting, oblique, 1 (OBLFC1) [MIM:600251]: A rare form
CC of facial clefting. A facial cleft is any of the fissures between the
CC embryonic prominences that normally unite to form the face.
CC {ECO:0000269|PubMed:21703590}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Teebi hypertelorism syndrome 1 (TBHS1) [MIM:145420]: A form of
CC Teebi hypertelorism syndrome, a syndrome characterized by an abnormally
CC increased distance between ocular orbits, and facial features that can
CC resemble craniofrontonasal dysplasia such as prominent forehead,
CC widow's peak, heavy and broad eyebrows, long palpebral fissures,
CC ptosis, high and broad nasal bridge, short nose, low-set ears, natal
CC teeth, thin upper lip and a grooved chin. Some affected individuals
CC have limb, urogenital, umbilical and cardiac defects. Developmental
CC delay and/or impaired intellectual development have been observed in
CC some patients. TBHS1 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:25412741, ECO:0000269|PubMed:26111080}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the cytospin-A family. {ECO:0000305}.
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DR EMBL; AY884293; AAX84184.1; -; mRNA.
DR EMBL; AK301482; BAH13494.1; -; mRNA.
DR EMBL; AL832425; CAH10609.1; -; mRNA.
DR EMBL; AP000354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB002374; BAA21574.1; -; mRNA.
DR CCDS; CCDS33619.1; -. [Q69YQ0-1]
DR CCDS; CCDS58797.1; -. [Q69YQ0-2]
DR RefSeq; NP_001241661.2; NM_001254732.2.
DR RefSeq; NP_056145.4; NM_015330.4.
DR AlphaFoldDB; Q69YQ0; -.
DR BioGRID; 116960; 196.
DR DIP; DIP-33173N; -.
DR IntAct; Q69YQ0; 73.
DR MINT; Q69YQ0; -.
DR STRING; 9606.ENSP00000325785; -.
DR iPTMnet; Q69YQ0; -.
DR MetOSite; Q69YQ0; -.
DR PhosphoSitePlus; Q69YQ0; -.
DR BioMuta; SPECC1L; -.
DR DMDM; 300669640; -.
DR EPD; Q69YQ0; -.
DR jPOST; Q69YQ0; -.
DR MassIVE; Q69YQ0; -.
DR MaxQB; Q69YQ0; -.
DR PaxDb; Q69YQ0; -.
DR PeptideAtlas; Q69YQ0; -.
DR PRIDE; Q69YQ0; -.
DR ProteomicsDB; 25658; -.
DR ProteomicsDB; 66168; -. [Q69YQ0-1]
DR Antibodypedia; 45171; 136 antibodies from 21 providers.
DR DNASU; 23384; -.
DR Ensembl; ENST00000314328.14; ENSP00000325785.8; ENSG00000100014.20. [Q69YQ0-1]
DR Ensembl; ENST00000437398.5; ENSP00000393363.1; ENSG00000100014.20. [Q69YQ0-1]
DR Ensembl; ENST00000541492.1; ENSP00000439633.1; ENSG00000100014.20. [Q69YQ0-2]
DR GeneID; 23384; -.
DR KEGG; hsa:23384; -.
DR MANE-Select; ENST00000314328.14; ENSP00000325785.8; NM_015330.6; NP_056145.5.
DR UCSC; uc002zzv.6; human. [Q69YQ0-1]
DR CTD; 23384; -.
DR DisGeNET; 23384; -.
DR GeneCards; SPECC1L; -.
DR HGNC; HGNC:29022; SPECC1L.
DR HPA; ENSG00000100014; Low tissue specificity.
DR MalaCards; SPECC1L; -.
DR MIM; 145420; phenotype.
DR MIM; 600251; phenotype.
DR MIM; 614140; gene.
DR neXtProt; NX_Q69YQ0; -.
DR OpenTargets; ENSG00000100014; -.
DR Orphanet; 1519; SPECC1L-related hypertelorism syndrome.
DR Orphanet; 141258; Tessier number 4 facial cleft.
DR Orphanet; 141276; Tessier number 7 facial cleft.
DR PharmGKB; PA164718673; -.
DR VEuPathDB; HostDB:ENSG00000100014; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000153592; -.
DR HOGENOM; CLU_009328_1_0_1; -.
DR InParanoid; Q69YQ0; -.
DR PhylomeDB; Q69YQ0; -.
DR TreeFam; TF316716; -.
DR PathwayCommons; Q69YQ0; -.
DR SignaLink; Q69YQ0; -.
DR BioGRID-ORCS; 23384; 22 hits in 1071 CRISPR screens.
DR GenomeRNAi; 23384; -.
DR Pharos; Q69YQ0; Tbio.
DR PRO; PR:Q69YQ0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q69YQ0; protein.
DR Bgee; ENSG00000100014; Expressed in calcaneal tendon and 185 other tissues.
DR ExpressionAtlas; Q69YQ0; baseline and differential.
DR Genevisible; Q69YQ0; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR040166; CYTSA.
DR PANTHER; PTHR23167:SF18; PTHR23167:SF18; 1.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell junction;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Gap junction;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1117
FT /note="Cytospin-A"
FT /id="PRO_0000231018"
FT DOMAIN 1011..1116
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..280
FT /evidence="ECO:0000255"
FT COILED 394..449
FT /evidence="ECO:0000255"
FT COILED 487..807
FT /evidence="ECO:0000255"
FT COMPBIAS 11..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2KN98"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1030..1068
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047359"
FT VARIANT 190
FT /note="T -> M (no effect on the stabilization of
FT microtubules; dbSNP:rs142144652)"
FT /evidence="ECO:0000269|PubMed:21703590"
FT /id="VAR_066872"
FT VARIANT 301
FT /note="G -> D (in dbSNP:rs204710)"
FT /id="VAR_060448"
FT VARIANT 397
FT /note="T -> P (in TBHS1; has an abnormal punctate
FT expression pattern; has a drastically reduced ability to
FT stabilize microtubules; dbSNP:rs786201030)"
FT /evidence="ECO:0000269|PubMed:25412741"
FT /id="VAR_073384"
FT VARIANT 400..401
FT /note="Missing (in TBHS1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26111080"
FT /id="VAR_081478"
FT VARIANT 415
FT /note="Q -> P (in OBLFC1; severely impairs the
FT stabilization of microtubules; dbSNP:rs387907108)"
FT /evidence="ECO:0000269|PubMed:21703590"
FT /id="VAR_066873"
FT VARIANT 420
FT /note="E -> D (in TBHS1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26111080"
FT /id="VAR_081479"
FT VARIANT 712
FT /note="S -> F (in dbSNP:rs5760340)"
FT /id="VAR_060449"
FT VARIANT 717
FT /note="T -> A (in dbSNP:rs6004132)"
FT /id="VAR_060450"
FT VARIANT 943
FT /note="V -> A (in dbSNP:rs11704759)"
FT /id="VAR_060451"
FT VARIANT 951
FT /note="V -> M (in dbSNP:rs204718)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:9205841,
FT ECO:0000269|Ref.1"
FT /id="VAR_060452"
FT VARIANT 1083
FT /note="G -> S (in TBHS1; has an abnormal punctate
FT expression pattern; has a drastically reduced ability to
FT stabilize microtubules; dbSNP:rs786201031)"
FT /evidence="ECO:0000269|PubMed:25412741"
FT /id="VAR_073385"
FT CONFLICT 375
FT /note="P -> L (in Ref. 1; AAX84184 and 2; CAH10609)"
FT /evidence="ECO:0000305"
FT CONFLICT 1041
FT /note="N -> K (in Ref. 4; BAA21574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1117 AA; 124544 MW; 9FA1BB5B2DC92C96 CRC64;
MKKASRSVGS VPKVSAISKT QTAEKIKPEN SSSASTGGKL VKPGTAASLS KTKSSDDLLA
GMAGGVTVTN GVKGKKSTCP SAAPSASAPA MTTVENKSKI STGTASSTKR STSTGNKESS
STRERLRERT RLNQSKKLPS AGQGANDMAL AKRSRSRTAT ECDVRMSKSK SDNQISDRAA
LEAKVKDLLT LAKTKDVEIL HLRNELRDMR AQLGINEDHS EGDEKSEKET IMAHQPTDVE
STLLQLQEQN TAIREELNQL KNENRMLKDR LNALGFSLEQ RLDNSEKLFG YQSLSPEITP
GNQSDGGGTL TSSVEGSAPG SVEDLLSQDE NTLMDHQHSN SMDNLDSECS EVYQPLTSSD
DALDAPSSSE SEGIPSIERS RKGSSGNASE VSVACLTERI HQMEENQHST SEELQATLQE
LADLQQITQE LNSENERLGE EKVILMESLC QQSDKLEHFS RQIEYFRSLL DEHHISYVID
EDVKSGRYME LEQRYMDLAE NARFEREQLL GVQQHLSNTL KMAEQDNKEA QEMIGALKER
SHHMERIIES EQKGKAALAA TLEEYKATVA SDQIEMNRLK AQLENEKQKV AELYSIHNSG
DKSDIQDLLE SVRLDKEKAE TLASSLQEDL AHTRNDANRL QDAIAKVEDE YRAFQEEAKK
QIEDLNMTLE KLRSDLDEKE TERSDMKETI FELEDEVEQH RAVKLHDNLI ISDLENTVKK
LQDQKHDMER EIKTLHRRLR EESAEWRQFQ ADLQTAVVIA NDIKSEAQEE IGDLKRRLHE
AQEKNEKLTK ELEEIKSRKQ EEERGRVYNY MNAVERDLAA LRQGMGLSRR SSTSSEPTPT
VKTLIKSFDS ASQVPNPAAA AIPRTPLSPS PMKTPPAAAV SPMQRHSISG PISTSKPLTA
LSDKRPNYGE IPVQEHLLRT SSASRPASLP RVPAMESAKT LSVSRRSSEE VKRDISAQEG
ASPASLMAMG TTSPQLSLSS SPTASVTPTT RSRIREERKD PLSALAREYG GSKRNALLKW
CQKKTEGYQN IDITNFSSSW NDGLAFCALL HTYLPAHIPY QELNSQDKRR NFMLAFQAAE
SVGIKSTLDI NEMVRTERPD WQNVMLYVTA IYKYFET
