CRACD_HUMAN
ID CRACD_HUMAN Reviewed; 1233 AA.
AC Q6ZU35; Q9NTE2; Q9NTP8; Q9ULK9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Capping protein-inhibiting regulator of actin dynamics {ECO:0000312|HGNC:HGNC:29219};
DE AltName: Full=Cancer-related regulator of actin dynamics {ECO:0000303|PubMed:30361697};
GN Name=CRACD {ECO:0000312|HGNC:HGNC:29219};
GN Synonyms=CRAD {ECO:0000303|PubMed:30361697},
GN KIAA1211 {ECO:0000312|HGNC:HGNC:29219};
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 [LARGE SCALE MRNA], AND VARIANT PRO-655.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-655 AND LEU-776.
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-655.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-1233, AND VARIANT PRO-655.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 612-1233, AND VARIANT PRO-655.
RC TISSUE=Testis;
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 AND THR-559, 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].
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-971 AND SER-975, AND
RP IDENTIFICATION BY MASS 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 AND SER-1017, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, 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 [14]
RP VARIANT GLN-249.
RX PubMed=27717682; DOI=10.1016/j.jstrokecerebrovasdis.2016.09.003;
RA Mukawa M., Nariai T., Onda H., Yoneyama T., Aihara Y., Hirota K., Kudo T.,
RA Sumita K., Maehara T., Kawamata T., Kasuya H., Akagawa H.;
RT "Exome sequencing identified CCER2 as a novel candidate gene for Moyamoya
RT disease.";
RL J. Stroke Cerebrovasc. Dis. 26:150-161(2017).
RN [15]
RP FUNCTION, INTERACTION WITH CAPZA1; CAPZA2 AND CAPZB, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=30361697; DOI=10.1038/s41556-018-0215-z;
RA Jung Y.S., Wang W., Jun S., Zhang J., Srivastava M., Kim M.J., Lien E.M.,
RA Shang J., Chen J., McCrea P.D., Zhang S., Park J.I.;
RT "Deregulation of CRAD-controlled cytoskeleton initiates mucinous colorectal
RT cancer via beta-catenin.";
RL Nat. Cell Biol. 20:1303-1314(2018).
CC -!- FUNCTION: Involved in epithelial cell integrity by acting on the
CC maintenance of the actin cytoskeleton. Positively regulates the actin
CC polymerization, by inhibiting the interaction of actin-capping proteins
CC with actin. {ECO:0000269|PubMed:30361697}.
CC -!- SUBUNIT: Directly interacts with actin-capping proteins CAPZA1, CAPZA2
CC and CAPZB; this interaction decreases the binding of capping proteins
CC to actin. {ECO:0000269|PubMed:30361697}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:30361697}.
CC -!- TISSUE SPECIFICITY: Expressed in intestinal epithelial cells (at
CC protein level). {ECO:0000269|PubMed:30361697}.
CC -!- DISEASE: Note=In colorectal cancers, CRACD gene is observed to be often
CC the target of inactivating mutations. In the absence of genetic
CC mutations, expression levels tend to be down-regulated.
CC {ECO:0000269|PubMed:30361697}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86525.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=CAB61360.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033037; BAA86525.1; ALT_SEQ; mRNA.
DR EMBL; AK126014; BAC86392.1; -; mRNA.
DR EMBL; AC068620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05481.1; -; Genomic_DNA.
DR EMBL; AL133028; CAB61360.2; ALT_INIT; mRNA.
DR EMBL; AL137336; CAB70699.1; -; mRNA.
DR CCDS; CCDS43230.1; -.
DR PIR; T42702; T42702.
DR RefSeq; NP_065773.1; NM_020722.1.
DR RefSeq; XP_005265809.1; XM_005265752.2.
DR RefSeq; XP_011532699.1; XM_011534397.2.
DR AlphaFoldDB; Q6ZU35; -.
DR BioGRID; 121552; 41.
DR IntAct; Q6ZU35; 6.
DR MINT; Q6ZU35; -.
DR STRING; 9606.ENSP00000423366; -.
DR iPTMnet; Q6ZU35; -.
DR PhosphoSitePlus; Q6ZU35; -.
DR BioMuta; KIAA1211; -.
DR DMDM; 296439324; -.
DR EPD; Q6ZU35; -.
DR jPOST; Q6ZU35; -.
DR MassIVE; Q6ZU35; -.
DR MaxQB; Q6ZU35; -.
DR PaxDb; Q6ZU35; -.
DR PeptideAtlas; Q6ZU35; -.
DR PRIDE; Q6ZU35; -.
DR ProteomicsDB; 68308; -.
DR Antibodypedia; 56722; 17 antibodies from 8 providers.
DR DNASU; 57482; -.
DR Ensembl; ENST00000264229.11; ENSP00000264229.6; ENSG00000109265.15.
DR Ensembl; ENST00000504228.6; ENSP00000423366.1; ENSG00000109265.15.
DR Ensembl; ENST00000682029.1; ENSP00000507165.1; ENSG00000109265.15.
DR GeneID; 57482; -.
DR KEGG; hsa:57482; -.
DR MANE-Select; ENST00000682029.1; ENSP00000507165.1; NM_001393381.1; NP_001380310.1.
DR UCSC; uc003hbk.3; human.
DR CTD; 57482; -.
DR DisGeNET; 57482; -.
DR GeneCards; CRACD; -.
DR HGNC; HGNC:29219; CRACD.
DR HPA; ENSG00000109265; Tissue enhanced (brain, intestine, testis).
DR MIM; 618327; gene.
DR neXtProt; NX_Q6ZU35; -.
DR OpenTargets; ENSG00000109265; -.
DR VEuPathDB; HostDB:ENSG00000109265; -.
DR eggNOG; ENOG502QQWT; Eukaryota.
DR GeneTree; ENSGT00940000161471; -.
DR HOGENOM; CLU_008508_0_0_1; -.
DR InParanoid; Q6ZU35; -.
DR OMA; ECKFAKD; -.
DR OrthoDB; 446624at2759; -.
DR PhylomeDB; Q6ZU35; -.
DR TreeFam; TF335584; -.
DR PathwayCommons; Q6ZU35; -.
DR SignaLink; Q6ZU35; -.
DR BioGRID-ORCS; 57482; 90 hits in 1068 CRISPR screens.
DR ChiTaRS; KIAA1211; human.
DR GenomeRNAi; 57482; -.
DR Pharos; Q6ZU35; Tdark.
DR PRO; PR:Q6ZU35; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6ZU35; protein.
DR Bgee; ENSG00000109265; Expressed in ileal mucosa and 146 other tissues.
DR ExpressionAtlas; Q6ZU35; baseline and differential.
DR Genevisible; Q6ZU35; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISS:UniProtKB.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IDA:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR InterPro; IPR028030; DUF4592.
DR Pfam; PF15262; DUF4592; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1233
FT /note="Capping protein-inhibiting regulator of actin
FT dynamics"
FT /id="PRO_0000342475"
FT REGION 92..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..472
FT /note="Required for interaction with actin-capping
FT proteins"
FT /evidence="ECO:0000269|PubMed:30361697"
FT REGION 560..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PR69"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PR69"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PR69"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 971
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 249
FT /note="E -> Q (in dbSNP:rs1379374919)"
FT /evidence="ECO:0000269|PubMed:27717682"
FT /id="VAR_079174"
FT VARIANT 269
FT /note="L -> I (in dbSNP:rs6823339)"
FT /id="VAR_044205"
FT VARIANT 655
FT /note="R -> P (in dbSNP:rs7672073)"
FT /evidence="ECO:0000269|PubMed:10574462,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4"
FT /id="VAR_044206"
FT VARIANT 710
FT /note="R -> Q (in dbSNP:rs3796546)"
FT /id="VAR_044207"
FT VARIANT 776
FT /note="S -> L (in dbSNP:rs3796547)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_044208"
FT CONFLICT 299
FT /note="G -> R (in Ref. 2; BAC86392)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="P -> L (in Ref. 2; BAC86392)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="E -> G (in Ref. 2; BAC86392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1233 AA; 136760 MW; 277958DCD15528C4 CRC64;
MGTRAFSHDS IFIPDGGAES EQTVQAMSQD NILGKVKTLQ QQLGKNIKFG QRSPNAIPMN
KANSGEASLE EDLFLTSPME IVTQQDIVLS DAENKSSDTP SSLSPLNLPG AGSEMEEKVA
PVKPSRPKRH FSSAGTIESV NLDAIPLAIA RLDNSAAKHK LAVKPKKQRV SKKHRRLAQD
PQHEQGGLES RPCLDQNGHP GEDKPTWHEE EPNPLDSEEE RRRQEDYWRE LEAKCKRQKA
EAAEKRRLEE QRLQALERRL WEENRRQELL EEEGEGQEPP LEAERAPREE QQRSLEAPGW
EDAERREREE RERLEAEEER RRLQAQAQAE ERRRLEEDAR LEERRRQEEE EGRCAEELKR
QEEEEAEGWE ELEQQEAEVQ GPPEALEETG EGRRGAEEED LGEEEEEGQA HLEDWRGQLS
ELLNDFEERL EDQERLKPEG QREHSEEPGI CEEQNPEAER RREQQGRSGD FQGADRPGPE
EKREEGDTEP LLKQEGPVEA AQPPVERKEA AALEQGRKVE ELRWQEVDER QTMPRPYTFQ
VSSGGKQILF PKVNLSPVTP AKDTGLTAAP QEPKAPKASP VQHALPSSLS VPHTAILVTG
AQLCGPAVNL SQIKDTACKS LLGLEEKKHA EAPAGENPPR GPGDARAGSG KAKPRQESPS
SASALAEWAS IRSRILKNAE SDPRSSERDQ LRPGDESTPR GRCDSRGNQR KTPPVNAKFS
IMPAWQKFSD GGTETSKQST EAESIRKRPM LGPSEETAPQ PPPAGVRELG KGPEKSEMHR
EPADTTEGCK FAKDLPSFLV PSLPYPPQKV VAHTEFTTSS DSETANGIAK PDPVMPGGEE
KASPFGIKLR RTNYSLRFNC DQQAEQKKKK RHSSTGDSAD AGPPAAGSAR GEKEMEGVAL
KHGPSLPQER KQAPSTRRDS AEPSSSRSVP VAHPGPPPAS SQTPAPEHDK AANKMPLAQK
PALAPKPTSQ TPPASPLSKL SRPYLVELLS RRAGRPDPEP SEPSKEDQES SDRRPPSPPG
PEERKGQKRD EEEEATERKP ASPPLPATQQ EKPSQTPEAG RKEKPMLQSR HSLDGSKLTE
KVETAQPLWI TLALQKQKGF REQQATREER KQAREAKQAE KLSKENVSVS VQPGSSSVSR
AGSLHKSTAL PEEKRPETAV SRLERREQLK KANTLPTSVT VEISDSAPPA PLVKEVTKRF
STPDAAPVST EPAWLALAKR KAKAWSDCPQ IIK
