MCMBP_HUMAN
ID MCMBP_HUMAN Reviewed; 642 AA.
AC Q9BTE3; B3KSP7; Q6IA56; Q9BVT9; Q9H916;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Mini-chromosome maintenance complex-binding protein;
DE Short=MCM-BP;
DE Short=MCM-binding protein;
GN Name=MCMBP; Synonyms=C10orf119;
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] (ISOFORM 1).
RC TISSUE=Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 340-642 (ISOFORMS 1/2).
RC TISSUE=Muscle, and Placenta;
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 SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION
RP WITH THE MCM COMPLEX.
RX PubMed=17296731; DOI=10.1128/mcb.02384-06;
RA Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.;
RT "Identification and characterization of a novel component of the human
RT minichromosome maintenance complex.";
RL Mol. Cell. Biol. 27:3044-3055(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-160 AND SER-298, 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 [7]
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 [8]
RP IDENTIFICATION BY MASS 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 [9]
RP INTERACTION WITH THE RPA COMPLEX.
RX PubMed=20679368; DOI=10.1093/jb/mvq085;
RA Nakaya R., Takaya J., Onuki T., Moritani M., Nozaki N., Ishimi Y.;
RT "Identification of proteins that may directly interact with human RPA.";
RL J. Biochem. 148:539-547(2010).
RN [10]
RP FUNCTION.
RX PubMed=20090939; DOI=10.1371/journal.pgen.1000817;
RA Takahashi N., Quimbaya M., Schubert V., Lammens T., Vandepoele K.,
RA Schubert I., Matsui M., Inze D., Berx G., De Veylder L.;
RT "The MCM-binding protein ETG1 aids sister chromatid cohesion required for
RT postreplicative homologous recombination repair.";
RL PLoS Genet. 6:E1000817-E1000817(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP FUNCTION.
RX PubMed=21196493; DOI=10.1101/gad.614411;
RA Nishiyama A., Frappier L., Mechali M.;
RT "MCM-BP regulates unloading of the MCM2-7 helicase in late S phase.";
RL Genes Dev. 25:165-175(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-167 AND SER-298, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, 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: Associated component of the MCM complex that acts as a
CC regulator of DNA replication. Binds to the MCM complex during late S
CC phase and promotes the disassembly of the MCM complex from chromatin,
CC thereby acting as a key regulator of pre-replication complex (pre-RC)
CC unloading from replicated DNA. Can dissociate the MCM complex without
CC addition of ATP; probably acts by destabilizing interactions of each
CC individual subunits of the MCM complex. Required for sister chromatid
CC cohesion. {ECO:0000269|PubMed:20090939, ECO:0000269|PubMed:21196493}.
CC -!- SUBUNIT: Interacts with the MCM complex: associates with the MCM3-7
CC complex which lacks MCM2, while it does not interact with the MCM
CC complex when MCM2 is present (MCM2-7 complex). Interacts with the RPA
CC complex, when composed of all RPA1, RPA2 and RPA3 components, but not
CC with RPA1 or RPA2 alone. {ECO:0000269|PubMed:17296731,
CC ECO:0000269|PubMed:20679368}.
CC -!- INTERACTION:
CC Q9BTE3; O00311: CDC7; NbExp=2; IntAct=EBI-749378, EBI-374980;
CC Q9BTE3; Q9Y248: GINS2; NbExp=2; IntAct=EBI-749378, EBI-747491;
CC Q9BTE3; Q9BRT9: GINS4; NbExp=2; IntAct=EBI-749378, EBI-747500;
CC Q9BTE3; P49736: MCM2; NbExp=4; IntAct=EBI-749378, EBI-374819;
CC Q9BTE3; P25205: MCM3; NbExp=11; IntAct=EBI-749378, EBI-355153;
CC Q9BTE3; P33991: MCM4; NbExp=14; IntAct=EBI-749378, EBI-374938;
CC Q9BTE3; P33992: MCM5; NbExp=13; IntAct=EBI-749378, EBI-359410;
CC Q9BTE3; Q14566: MCM6; NbExp=15; IntAct=EBI-749378, EBI-374900;
CC Q9BTE3; P33993: MCM7; NbExp=21; IntAct=EBI-749378, EBI-355924;
CC Q9BTE3; Q9UJA3: MCM8; NbExp=3; IntAct=EBI-749378, EBI-8756095;
CC Q9BTE3; Q9NRG1: PRTFDC1; NbExp=3; IntAct=EBI-749378, EBI-739759;
CC Q9BTE3; Q9UQE7: SMC3; NbExp=6; IntAct=EBI-749378, EBI-80718;
CC Q9BTE3-2; P04424: ASL; NbExp=6; IntAct=EBI-9384556, EBI-750131;
CC Q9BTE3-2; P35638: DDIT3; NbExp=3; IntAct=EBI-9384556, EBI-742651;
CC Q9BTE3-2; Q13451: FKBP5; NbExp=4; IntAct=EBI-9384556, EBI-306914;
CC Q9BTE3-2; Q14145: KEAP1; NbExp=3; IntAct=EBI-9384556, EBI-751001;
CC Q9BTE3-2; P33993: MCM7; NbExp=6; IntAct=EBI-9384556, EBI-355924;
CC Q9BTE3-2; Q9NRG1: PRTFDC1; NbExp=6; IntAct=EBI-9384556, EBI-739759;
CC Q9BTE3-2; Q9UIY3: RWDD2A; NbExp=3; IntAct=EBI-9384556, EBI-17677006;
CC Q9BTE3-2; Q13573: SNW1; NbExp=3; IntAct=EBI-9384556, EBI-632715;
CC Q9BTE3-2; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-9384556, EBI-17269964;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17296731}.
CC Note=Associates with chromatin. Highly associated with chromatin in
CC G1/S and S phases, reduced binding to chromatin in G2, and further
CC decreased binding in early M phase. It then reassociates with chromatin
CC in late M phase. Dissociates from chromatin later than component of the
CC MCM complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BTE3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTE3-2; Sequence=VSP_014707;
CC Name=3;
CC IsoId=Q9BTE3-3; Sequence=VSP_040721, VSP_014707;
CC -!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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DR EMBL; AK023143; BAB14427.1; -; mRNA.
DR EMBL; AK094075; BAG52809.1; -; mRNA.
DR EMBL; CR457299; CAG33580.1; -; mRNA.
DR EMBL; AC027672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000935; AAH00935.1; -; mRNA.
DR EMBL; BC004183; AAH04183.1; -; mRNA.
DR EMBL; BC007219; AAH07219.1; -; mRNA.
DR CCDS; CCDS58099.1; -. [Q9BTE3-2]
DR CCDS; CCDS7617.1; -. [Q9BTE3-1]
DR RefSeq; NP_001243307.1; NM_001256378.1. [Q9BTE3-2]
DR RefSeq; NP_001243308.1; NM_001256379.1. [Q9BTE3-3]
DR RefSeq; NP_079110.1; NM_024834.3. [Q9BTE3-1]
DR PDB; 4KG9; X-ray; 1.70 A; B=152-161.
DR PDBsum; 4KG9; -.
DR AlphaFoldDB; Q9BTE3; -.
DR SMR; Q9BTE3; -.
DR BioGRID; 122976; 107.
DR IntAct; Q9BTE3; 46.
DR MINT; Q9BTE3; -.
DR STRING; 9606.ENSP00000353098; -.
DR GlyGen; Q9BTE3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BTE3; -.
DR MetOSite; Q9BTE3; -.
DR PhosphoSitePlus; Q9BTE3; -.
DR BioMuta; MCMBP; -.
DR DMDM; 71153001; -.
DR EPD; Q9BTE3; -.
DR jPOST; Q9BTE3; -.
DR MassIVE; Q9BTE3; -.
DR MaxQB; Q9BTE3; -.
DR PaxDb; Q9BTE3; -.
DR PeptideAtlas; Q9BTE3; -.
DR PRIDE; Q9BTE3; -.
DR ProteomicsDB; 78982; -. [Q9BTE3-1]
DR ProteomicsDB; 78983; -. [Q9BTE3-2]
DR ProteomicsDB; 78984; -. [Q9BTE3-3]
DR ABCD; Q9BTE3; 2 sequenced antibodies.
DR Antibodypedia; 46307; 157 antibodies from 26 providers.
DR DNASU; 79892; -.
DR Ensembl; ENST00000360003.7; ENSP00000353098.3; ENSG00000197771.13. [Q9BTE3-1]
DR Ensembl; ENST00000369077.4; ENSP00000358073.3; ENSG00000197771.13. [Q9BTE3-2]
DR GeneID; 79892; -.
DR KEGG; hsa:79892; -.
DR MANE-Select; ENST00000369077.4; ENSP00000358073.3; NM_001256378.2; NP_001243307.1. [Q9BTE3-2]
DR UCSC; uc001leq.3; human. [Q9BTE3-1]
DR CTD; 79892; -.
DR DisGeNET; 79892; -.
DR GeneCards; MCMBP; -.
DR HGNC; HGNC:25782; MCMBP.
DR HPA; ENSG00000197771; Low tissue specificity.
DR MIM; 610909; gene.
DR neXtProt; NX_Q9BTE3; -.
DR OpenTargets; ENSG00000197771; -.
DR PharmGKB; PA134862625; -.
DR VEuPathDB; HostDB:ENSG00000197771; -.
DR eggNOG; KOG2545; Eukaryota.
DR GeneTree; ENSGT00390000017265; -.
DR HOGENOM; CLU_029811_0_0_1; -.
DR InParanoid; Q9BTE3; -.
DR OMA; HTEMIQQ; -.
DR OrthoDB; 1011739at2759; -.
DR PhylomeDB; Q9BTE3; -.
DR TreeFam; TF324793; -.
DR PathwayCommons; Q9BTE3; -.
DR SignaLink; Q9BTE3; -.
DR BioGRID-ORCS; 79892; 481 hits in 1087 CRISPR screens.
DR ChiTaRS; MCMBP; human.
DR GenomeRNAi; 79892; -.
DR Pharos; Q9BTE3; Tbio.
DR PRO; PR:Q9BTE3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BTE3; protein.
DR Bgee; ENSG00000197771; Expressed in oocyte and 190 other tissues.
DR ExpressionAtlas; Q9BTE3; baseline and differential.
DR Genevisible; Q9BTE3; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.
DR InterPro; IPR019140; MCM_complex-bd.
DR PANTHER; PTHR13489; PTHR13489; 1.
DR Pfam; PF09739; MCM_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW DNA replication; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..642
FT /note="Mini-chromosome maintenance complex-binding protein"
FT /id="PRO_0000089827"
FT REGION 151..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040721"
FT VAR_SEQ 334..335
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_014707"
FT CONFLICT 164
FT /note="H -> Y (in Ref. 2; CAG33580)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="E -> V (in Ref. 2; CAG33580)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="T -> A (in Ref. 1; BAG52809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 72980 MW; D9EA81646F1D50E2 CRC64;
MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP SLNEVPLHYL
KPNSFVKFRC MIQDMFDPEF YMGVYETVNQ NTKAHVLHFG KYRDVAECGP QQELDLNSPR
NTTLERQTFY CVPVPGESTW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DDDMDLQPNK
QKDQHAGARQ AGSVGGLQWC GEPKRLETEA STGQQLNSLN LSSPFDLNFP LPGEKGPACL
VKVYEDWDCF KVNDILELYG ILSVDPVLSI LNNDERDASA LLDPMECTDT AEEQRVHSPP
ASLVPRIHVI LAQKLQHINP LLPACLNKEE SKTCKFVSSF MSELSPVRAE LLGFLTHALL
GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPRNS TFTEHLYRII QHLVPASFRL
QMTIENMNHL KFIPHKDYTA NRLVSGLLQL PSNTSLVIDE TLLEQGQLDT PGVHNVTALS
NLITWQKVDY DFSYHQMEFP CNINVFITSE GRSLLPADCQ IHLQPQLIPP NMEEYMNSLL
SAVLPSVLNK FRIYLTLLRF LEYSISDEIT KAVEDDFVEM RKNDPQSITA DDLHQLLVVA
RCLSLSAGQT TLSRERWLRA KQLESLRRTR LQQQKCVNGN EL
