ID   C2D1A_HUMAN             Reviewed;         951 AA.
AC   Q6P1N0; Q7Z435; Q86XV0; Q8NF89; Q9H603; Q9NXI1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Coiled-coil and C2 domain-containing protein 1A;
DE   AltName: Full=Akt kinase-interacting protein 1;
DE   AltName: Full=Five prime repressor element under dual repression-binding protein 1;
DE            Short=FRE under dual repression-binding protein 1;
DE            Short=Freud-1;
DE   AltName: Full=Putative NF-kappa-B-activating protein 023N;
GN   Name=CC2D1A; Synonyms=AKI1, LGD2 {ECO:0000305};
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 2).
RC   TISSUE=Kidney;
RA   Guo J.H., Chen L., Yu L.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung fibroblast;
RX   PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA   Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA   Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT   "Large-scale identification and characterization of human genes that
RT   activate NF-kappaB and MAPK signaling pathways.";
RL   Oncogene 22:3307-3318(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-606 AND 622-951 (ISOFORM 1).
RC   TISSUE=Ovary;
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 MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Ovary;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INVOLVEMENT IN MRT3.
RX   PubMed=16033914; DOI=10.1136/jmg.2005.035709;
RA   Basel-Vanagaite L., Attia R., Yahav M., Ferland R.J., Anteki L.,
RA   Walsh C.A., Olender T., Straussberg R., Magal N., Taub E., Drasinover V.,
RA   Alkelai A., Bercovich D., Rechavi G., Simon A.J., Shohat M.;
RT   "The CC2D1A, a member of a new gene family with C2 domains, is involved in
RT   autosomal recessive non-syndromic mental retardation.";
RL   J. Med. Genet. 43:203-210(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204; SER-208; SER-253 AND
RP   SER-455, AND 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   [10]
RP   FUNCTION, PHOSPHORYLATION AT SER-208 BY CDK1, AND SUBCELLULAR LOCATION.
RX   PubMed=20171170; DOI=10.1016/j.bbrc.2010.02.103;
RA   Nakamura A., Naito M., Arai H., Fujita N.;
RT   "Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1 complex.";
RL   Biochem. Biophys. Res. Commun. 393:872-876(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-455, 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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206; SER-208 AND SER-455, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-455, AND
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).
CC   -!- FUNCTION: Transcription factor that binds specifically to the DRE (dual
CC       repressor element) and represses HTR1A gene transcription in neuronal
CC       cells. The combination of calcium and ATP specifically inactivates the
CC       binding with FRE. May play a role in the altered regulation of HTR1A
CC       associated with anxiety and major depression. Mediates HDAC-independent
CC       repression of HTR1A promoter in neuronal cell. Performs essential
CC       function in controlling functional maturation of synapses (By
CC       similarity). Plays distinct roles depending on its localization. When
CC       cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway.
CC       Repressor of HTR1A when nuclear. In the centrosome, regulates spindle
CC       pole localization of the cohesin subunit SCC1/RAD21, thereby mediating
CC       centriole cohesion during mitosis. {ECO:0000250,
CC       ECO:0000269|PubMed:20171170}.
CC   -!- INTERACTION:
CC       Q6P1N0; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-7112364, EBI-749627;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16033914}. Nucleus
CC       {ECO:0000250|UniProtKB:Q66HA5}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000303|PubMed:20171170}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P1N0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P1N0-2; Sequence=VSP_019242;
CC   -!- DOMAIN: The C2 domain is required for the repression. {ECO:0000250}.
CC   -!- PTM: Phosphorylation on Ser-208 by CDK1 promotes spindle pole
CC       localization and association with SCC1/RAD21.
CC       {ECO:0000269|PubMed:20171170}.
CC   -!- DISEASE: Intellectual developmental disorder, autosomal recessive 3
CC       (MRT3) [MIM:608443]: A disorder characterized by significantly below
CC       average general intellectual functioning associated with impairments in
CC       adaptive behavior and manifested during the developmental period.
CC       {ECO:0000269|PubMed:16033914}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the CC2D1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91029.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=BAB15464.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF536205; AAN04488.1; -; mRNA.
DR   EMBL; AB097002; BAC77355.1; -; mRNA.
DR   EMBL; AK000248; BAA91029.1; ALT_SEQ; mRNA.
DR   EMBL; AK026371; BAB15464.1; ALT_INIT; mRNA.
DR   EMBL; BC048345; AAH48345.1; -; mRNA.
DR   EMBL; BC064981; AAH64981.1; -; mRNA.
DR   CCDS; CCDS42512.1; -. [Q6P1N0-1]
DR   CCDS; CCDS92537.1; -. [Q6P1N0-2]
DR   RefSeq; NP_060191.3; NM_017721.4. [Q6P1N0-1]
DR   RefSeq; XP_005260030.1; XM_005259973.2.
DR   AlphaFoldDB; Q6P1N0; -.
DR   SMR; Q6P1N0; -.
DR   BioGRID; 120212; 155.
DR   IntAct; Q6P1N0; 44.
DR   MINT; Q6P1N0; -.
DR   STRING; 9606.ENSP00000313601; -.
DR   GlyGen; Q6P1N0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6P1N0; -.
DR   PhosphoSitePlus; Q6P1N0; -.
DR   BioMuta; CC2D1A; -.
DR   DMDM; 74737148; -.
DR   EPD; Q6P1N0; -.
DR   jPOST; Q6P1N0; -.
DR   MassIVE; Q6P1N0; -.
DR   MaxQB; Q6P1N0; -.
DR   PaxDb; 9606-ENSP00000313601; -.
DR   PeptideAtlas; Q6P1N0; -.
DR   ProteomicsDB; 66855; -. [Q6P1N0-1]
DR   ProteomicsDB; 66856; -. [Q6P1N0-2]
DR   Pumba; Q6P1N0; -.
DR   Antibodypedia; 1689; 203 antibodies from 28 providers.
DR   DNASU; 54862; -.
DR   Ensembl; ENST00000318003.11; ENSP00000313601.6; ENSG00000132024.18. [Q6P1N0-1]
DR   Ensembl; ENST00000589606.5; ENSP00000467526.1; ENSG00000132024.18. [Q6P1N0-2]
DR   Ensembl; ENST00000672017.1; ENSP00000500461.1; ENSG00000288293.1. [Q6P1N0-1]
DR   Ensembl; ENST00000672339.1; ENSP00000500343.1; ENSG00000288293.1. [Q6P1N0-2]
DR   GeneID; 54862; -.
DR   KEGG; hsa:54862; -.
DR   MANE-Select; ENST00000318003.11; ENSP00000313601.6; NM_017721.5; NP_060191.3.
DR   UCSC; uc002mxo.3; human. [Q6P1N0-1]
DR   AGR; HGNC:30237; -.
DR   CTD; 54862; -.
DR   DisGeNET; 54862; -.
DR   GeneCards; CC2D1A; -.
DR   HGNC; HGNC:30237; CC2D1A.
DR   HPA; ENSG00000132024; Low tissue specificity.
DR   MalaCards; CC2D1A; -.
DR   MIM; 608443; phenotype.
DR   MIM; 610055; gene.
DR   neXtProt; NX_Q6P1N0; -.
DR   OpenTargets; ENSG00000132024; -.
DR   Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR   PharmGKB; PA142672197; -.
DR   VEuPathDB; HostDB:ENSG00000132024; -.
DR   eggNOG; KOG3837; Eukaryota.
DR   GeneTree; ENSGT00390000009595; -.
DR   HOGENOM; CLU_008808_0_0_1; -.
DR   InParanoid; Q6P1N0; -.
DR   OMA; LHRIKIM; -.
DR   OrthoDB; 2881278at2759; -.
DR   PhylomeDB; Q6P1N0; -.
DR   TreeFam; TF314229; -.
DR   PathwayCommons; Q6P1N0; -.
DR   SignaLink; Q6P1N0; -.
DR   SIGNOR; Q6P1N0; -.
DR   BioGRID-ORCS; 54862; 11 hits in 1160 CRISPR screens.
DR   ChiTaRS; CC2D1A; human.
DR   GeneWiki; CC2D1A; -.
DR   GenomeRNAi; 54862; -.
DR   Pharos; Q6P1N0; Tbio.
DR   PRO; PR:Q6P1N0; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q6P1N0; Protein.
DR   Bgee; ENSG00000132024; Expressed in right hemisphere of cerebellum and 91 other cell types or tissues.
DR   ExpressionAtlas; Q6P1N0; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR   GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR   GO; GO:1905381; P:negative regulation of snRNA transcription by RNA polymerase II; IDA:GO_Central.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd08690; C2_Freud-1; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037772; C2_Freud.
DR   InterPro; IPR039725; CC2D1A/B.
DR   InterPro; IPR006608; CC2D1A/B_DM14.
DR   PANTHER; PTHR13076:SF8; COILED-COIL AND C2 DOMAIN-CONTAINING PROTEIN 1A; 1.
DR   PANTHER; PTHR13076; UNCHARACTERIZED; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF21528; CC2D1A-B_DM14; 3.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00685; DM14; 4.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   PROSITE; PS50004; C2; 1.
DR   Genevisible; Q6P1N0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW   Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..951
FT                   /note="Coiled-coil and C2 domain-containing protein 1A"
FT                   /id="PRO_0000239609"
FT   DOMAIN          637..771
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          80..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          346..392
FT                   /evidence="ECO:0000255"
FT   COILED          484..517
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        83..108
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..343
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         92
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q66HA5"
FT   MOD_RES         204
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         206
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         208
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000269|PubMed:20171170,
FT                   ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         455
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   VAR_SEQ         819
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_019242"
FT   VARIANT         339
FT                   /note="T -> P (in dbSNP:rs11883041)"
FT                   /id="VAR_026670"
FT   VARIANT         635
FT                   /note="T -> S (in dbSNP:rs2290663)"
FT                   /id="VAR_026671"
FT   VARIANT         801
FT                   /note="T -> M (in dbSNP:rs2305777)"
FT                   /id="VAR_026672"
FT   CONFLICT        646
FT                   /note="I -> V (in Ref. 1; AAN04488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        824
FT                   /note="K -> E (in Ref. 2; BAC77355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        837
FT                   /note="S -> P (in Ref. 2; BAC77355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        906
FT                   /note="A -> T (in Ref. 2; BAC77355)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        943
FT                   /note="E -> G (in Ref. 2; BAC77355)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   951 AA;  104062 MW;  04D80124FC47729A CRC64;
     MHKRKGPPGP PGRGAAAARQ LGLLVDLSPD GLMIPEDGAN DEELEAEFLA LVGGQPPALE
     KLKGKGPLPM EAIEKMASLC MRDPDEDEEE GTDEDDLEAD DDLLAELNEV LGEEQKASET
     PPPVAQPKPE APHPGLETTL QERLALYQTA IESARQAGDS AKMRRYDRGL KTLENLLASI
     RKGNAIDEAD IPPPVAIGKG PASTPTYSPA PTQPAPRIAS APEPRVTLEG PSATAPASSP
     GLAKPQMPPG PCSPGPLAQL QSRQRDYKLA ALHAKQQGDT TAAARHFRVA KSFDAVLEAL
     SRGEPVDLSC LPPPPDQLPP DPPSPPSQPP TPATAPSTTE VPPPPRTLLE ALEQRMERYQ
     VAAAQAKSKG DQRKARMHER IVKQYQDAIR AHKAGRAVDV AELPVPPGFP PIQGLEATKP
     TQQSLVGVLE TAMKLANQDE GPEDEEDEVP KKQNSPVAPT AQPKAPPSRT PQSGSAPTAK
     APPKATSTRA QQQLAFLEGR KKQLLQAALR AKQKNDVEGA KMHLRQAKGL EPMLEASRNG
     LPVDITKVPP APVNKDDFAL VQRPGPGLSQ EAARRYGELT KLIRQQHEMC LNHSNQFTQL
     GNITETTKFE KLAEDCKRSM DILKQAFVRG LPTPTARFEQ RTFSVIKIFP DLSSNDMLLF
     IVKGINLPTP PGLSPGDLDV FVRFDFPYPN VEEAQKDKTS VIKNTDSPEF KEQFKLCINR
     SHRGFRRAIQ TKGIKFEVVH KGGLFKTDRV LGTAQLKLDA LEIACEVREI LEVLDGRRPT
     GGRLEVMVRI REPLTAQQLE TTTERWLVID PVPAAVPTQV AGPKGKAPPV PAPARESGNR
     SARPLHSLSV LAFDQERLER KILALRQARR PVPPEVAQQY QDIMQRSQWQ RAQLEQGGVG
     IRREYAAQLE RQLQFYTEAA RRLGNDGSRD AAKEALYRRN LVESELQRLR R
//