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Cytoskeleton-associated protein 2 (CTCL tumor antigen se20-10) (Tumor- and microtubule-associated protein)

 CKAP2_HUMAN             Reviewed;         683 AA.
Q8WWK9; A2BDE0; A5YM58; B4DR35; E9PD90; Q3KRA5; Q5VXB4; Q8IWV5;
Q8IWV6; Q96FH9; Q9H012; Q9H0D0; Q9H988; Q9HC49; Q9NVG4;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 128.
RecName: Full=Cytoskeleton-associated protein 2;
AltName: Full=CTCL tumor antigen se20-10;
AltName: Full=Tumor- and microtubule-associated protein;
Name=CKAP2 {ECO:0000312|HGNC:HGNC:1990};
Synonyms=LB1 {ECO:0000312|EMBL:CAC17466.1},
TMAP {ECO:0000312|EMBL:AAL47212.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:CAC17466.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND VARIANT VAL-323.
TISSUE=T-cell {ECO:0000312|EMBL:CAC17466.1};
PubMed=9771967; DOI=10.1038/sj.onc.1202048;
Maouche-Chretien L., Deleu N., Badoual C., Fraissignes P., Berger R.,
Gaulard P., Romeo P.H., Leroy-Viard K.;
"Identification of a novel cDNA, encoding a cytoskeletal associated
protein, differentially expressed in diffuse large B-cell lymphomas.";
Oncogene 17:1245-1251(1998).
[2] {ECO:0000305, ECO:0000312|EMBL:CAD22295.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=11234418;
Udina I.G., Baranova A.V., Kompaniytsev A.A., Sulimova G.E.;
"Evolutionarily-conserved gene CKAP2,located in region 13q14.3 of the
human genome, is frequently rearranged in various tumors.";
Genetika 37:120-123(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:AAL47212.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
AND INDUCTION.
TISSUE=Cervix carcinoma {ECO:0000312|EMBL:AAL47212.1};
PubMed=12942315; DOI=10.1007/s00432-003-0484-0;
Bae C.-D., Sung Y.-S., Jeon S.-M., Suh Y., Yang H.-K., Kim Y.-I.,
Park K.-H., Choi J., Ahn G., Park J.;
"Up-regulation of cytoskeletal-associated protein 2 in primary human
gastric adenocarcinomas.";
J. Cancer Res. Clin. Oncol. 129:621-630(2003).
[4] {ECO:0000305, ECO:0000312|EMBL:BAB14345.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
VAL-323.
TISSUE=Teratocarcinoma {ECO:0000312|EMBL:BAB14345.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[7] {ECO:0000305, ECO:0000312|EMBL:AAH10901.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
VAL-323.
TISSUE=Bone marrow {ECO:0000312|EMBL:AAH10901.1}, Cerebellum, and
Testis {ECO:0000312|EMBL:AAI05807.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8] {ECO:0000305, ECO:0000312|EMBL:AAG33675.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 38-683 (ISOFORM 1), AND VARIANTS LYS-236
AND VAL-323.
TISSUE=Testis {ECO:0000312|EMBL:AAG33675.1};
PubMed=11149944; DOI=10.1073/pnas.98.2.629;
Eichmueller S., Usener D., Dummer R., Stein A., Thiel D.,
Schadendorf D.;
"Serological detection of cutaneous T-cell lymphoma-associated
antigens.";
Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
[9] {ECO:0000305, ECO:0000312|EMBL:CAB66782.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 135-683 (ISOFORM 1), AND
VARIANT VAL-323.
TISSUE=Testis {ECO:0000312|EMBL:CAB66782.2};
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[10]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=17376772; DOI=10.1074/jbc.M701688200;
Seki A., Fang G.;
"CKAP2 is a spindle-associated protein degraded by APC/C-Cdh1 during
mitotic exit.";
J. Biol. Chem. 282:15103-15113(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-579; THR-582; SER-595;
THR-596; THR-597; TYR-599 AND SER-602, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-597 AND SER-602, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534; SER-595; THR-597
AND SER-602, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-190, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Possesses microtubule stabilizing properties. Involved
in regulating aneuploidy, cell cycling, and cell death in a
p53/TP53-dependent manner (By similarity). {ECO:0000250}.
-!- SUBUNIT: Associates with alpha- and beta-tubulins. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole.
Note=Contrary to the ectopically expressed protein, endogenous
CKAP2 does not colocalize with microtubules in G1, S and early G2.
At late G2 and prophase after separation of duplicated
centrosomes, colocalizes with gamma-tubulin and centrosome-
proximal microtubules. From prometaphase through anaphase B,
colocalizes with mitotic spindle poles and spindle microtubules.
During cytokinesis, absent from midbody microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:12942315,
ECO:0000269|PubMed:9771967};
IsoId=Q8WWK9-1; Sequence=Displayed;
Name=2;
IsoId=Q8WWK9-4; Sequence=VSP_047100, VSP_047101, VSP_047102;
Note=No experimental confirmation available. {ECO:0000305};
Name=4;
IsoId=Q8WWK9-6; Sequence=VSP_055686;
Name=3;
IsoId=Q8WWK9-5; Sequence=VSP_047100;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Abundant in testis, thymus, and in tumor
derived cell lines, while barely detectable in liver, prostate,
and kidney. {ECO:0000269|PubMed:9771967}.
-!- DEVELOPMENTAL STAGE: Present at the G1/S boundary. Accumulates as
cells progress from S to G2 into mitosis. Rapidly degraded during
mitosis exit by CDH1-activated anaphase promoting
complex/cyclosome (APC/C). {ECO:0000269|PubMed:17376772}.
-!- INDUCTION: Up-regulated in primary human gastric cancers.
{ECO:0000269|PubMed:12942315}.
-!- SIMILARITY: Belongs to the CKAP2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG33675.1; Type=Frameshift; Positions=604; Evidence={ECO:0000305};
Sequence=AAG33675.1; Type=Frameshift; Positions=607; Evidence={ECO:0000305};
Sequence=AAH10901.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI05807.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA91788.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; Y15758; CAC17466.1; -; mRNA.
EMBL; AJ429398; CAD22295.1; -; Genomic_DNA.
EMBL; AY062261; AAL47212.1; -; mRNA.
EMBL; AY062262; AAL47213.1; -; mRNA.
EMBL; AK001611; BAA91788.1; ALT_INIT; mRNA.
EMBL; AK022982; BAB14345.1; -; mRNA.
EMBL; AK299083; BAG61147.1; -; mRNA.
EMBL; EF560732; ABQ59042.1; -; mRNA.
EMBL; AL359513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010901; AAH10901.1; ALT_INIT; mRNA.
EMBL; BC105806; AAI05807.1; ALT_SEQ; mRNA.
EMBL; BC130296; AAI30297.1; -; mRNA.
EMBL; AF177227; AAG33675.1; ALT_FRAME; mRNA.
EMBL; AL136848; CAB66782.2; -; mRNA.
CCDS; CCDS41893.1; -. [Q8WWK9-1]
CCDS; CCDS66557.1; -. [Q8WWK9-6]
CCDS; CCDS73578.1; -. [Q8WWK9-4]
CCDS; CCDS9435.1; -. [Q8WWK9-5]
RefSeq; NP_001091995.1; NM_001098525.2. [Q8WWK9-1]
RefSeq; NP_001273615.1; NM_001286686.1. [Q8WWK9-6]
RefSeq; NP_001273616.1; NM_001286687.1. [Q8WWK9-4]
RefSeq; NP_060674.3; NM_018204.4. [Q8WWK9-5]
UniGene; Hs.444028; -.
UniGene; Hs.594461; -.
ProteinModelPortal; Q8WWK9; -.
BioGrid; 117755; 35.
ELM; Q8WWK9; -.
IntAct; Q8WWK9; 27.
MINT; MINT-4989610; -.
STRING; 9606.ENSP00000367276; -.
iPTMnet; Q8WWK9; -.
PhosphoSitePlus; Q8WWK9; -.
BioMuta; CKAP2; -.
DMDM; 74751579; -.
EPD; Q8WWK9; -.
MaxQB; Q8WWK9; -.
PaxDb; Q8WWK9; -.
PeptideAtlas; Q8WWK9; -.
PRIDE; Q8WWK9; -.
DNASU; 26586; -.
Ensembl; ENST00000258607; ENSP00000258607; ENSG00000136108. [Q8WWK9-5]
Ensembl; ENST00000378034; ENSP00000367273; ENSG00000136108. [Q8WWK9-4]
Ensembl; ENST00000378037; ENSP00000367276; ENSG00000136108. [Q8WWK9-1]
Ensembl; ENST00000490903; ENSP00000417830; ENSG00000136108. [Q8WWK9-6]
GeneID; 26586; -.
KEGG; hsa:26586; -.
UCSC; uc001vgt.4; human. [Q8WWK9-1]
CTD; 26586; -.
DisGeNET; 26586; -.
EuPathDB; HostDB:ENSG00000136108.14; -.
GeneCards; CKAP2; -.
HGNC; HGNC:1990; CKAP2.
HPA; HPA008410; -.
HPA; HPA027821; -.
MIM; 611569; gene.
neXtProt; NX_Q8WWK9; -.
OpenTargets; ENSG00000136108; -.
PharmGKB; PA26526; -.
eggNOG; ENOG410IF2W; Eukaryota.
eggNOG; ENOG4111T8P; LUCA.
GeneTree; ENSGT00530000063691; -.
HOGENOM; HOG000290636; -.
HOVERGEN; HBG107703; -.
InParanoid; Q8WWK9; -.
KO; K16769; -.
OMA; RRHTIAK; -.
OrthoDB; EOG091G05HU; -.
PhylomeDB; Q8WWK9; -.
TreeFam; TF333003; -.
SIGNOR; Q8WWK9; -.
GeneWiki; CKAP2; -.
GenomeRNAi; 26586; -.
PRO; PR:Q8WWK9; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136108; -.
ExpressionAtlas; Q8WWK9; baseline and differential.
Genevisible; Q8WWK9; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000281; P:mitotic cytokinesis; IGI:MGI.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
InterPro; IPR029197; CKAP2_C.
InterPro; IPR026165; CKAP2_fam.
PANTHER; PTHR16076; PTHR16076; 1.
Pfam; PF15297; CKAP2_C; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Cell cycle; Complete proteome;
Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 683 Cytoskeleton-associated protein 2.
/FTId=PRO_0000245774.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 534 534 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 579 579 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 582 582 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 595 595 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 596 596 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 597 597 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 599 599 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 602 602 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 51 MSTPAVPQDLQLPPSQRAQSAFKEQRRQKLKEHLLRRKTLF
AYKQENEMLS -> ML (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055686.
VAR_SEQ 53 53 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:12942315,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_047100.
VAR_SEQ 494 495 PI -> VR (in isoform 2).
{ECO:0000303|PubMed:12942315}.
/FTId=VSP_047101.
VAR_SEQ 496 683 Missing (in isoform 2).
{ECO:0000303|PubMed:12942315}.
/FTId=VSP_047102.
VARIANT 236 236 M -> K (in dbSNP:rs35975899).
{ECO:0000269|PubMed:11149944}.
/FTId=VAR_054018.
VARIANT 323 323 I -> V (in dbSNP:rs7335867).
{ECO:0000269|PubMed:11149944,
ECO:0000269|PubMed:11230166,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9771967}.
/FTId=VAR_069359.
CONFLICT 402 402 P -> L (in Ref. 9; CAB66782).
{ECO:0000305}.
CONFLICT 531 531 K -> Q (in Ref. 4; BAA91788).
{ECO:0000305}.
CONFLICT 531 531 K -> R (in Ref. 4; BAB14345).
{ECO:0000305}.
CONFLICT 559 559 F -> L (in Ref. 4; BAB14345).
{ECO:0000305}.
CONFLICT 577 577 V -> A (in Ref. 4; BAB14345).
{ECO:0000305}.
CONFLICT 643 643 K -> R (in Ref. 4; BAA91788).
{ECO:0000305}.
SEQUENCE 683 AA; 76987 MW; 15287A7D860A4B23 CRC64;
MSTPAVPQDL QLPPSQRAQS AFKEQRRQKL KEHLLRRKTL FAYKQENEML SSSRDQRVVT
SEDQVQEGTK VLKLKTKMAD KENMKRPAES KNNTVVGKHC IPLKPSNELT NSTVVIDTHK
PKDSNQTPHL LLTEDDPQSQ HMTLSQAFHL KNNSKKKQMT TEKQKQDANM PKKPVLGSYR
GQIVQSKINS FRKPLQVKDE SSAATKKLSA TIPKATKPQP VNTSSVTVKS NRSSNMTATT
KFVSTTSQNT QLVRPPIRSH HSNTRDTVKQ GISRTSANVT IRKGPHEKEL LQSKTALSSV
KTSSSQGIIR NKTLSRSIAS EVIARPASLS NDKLMEKSEP VDQRRHTAGK AIVDSRSAQP
KETSEERKAR LSEWKAGKGR VLKRPPNSVV TQHEPAGQNE KPVGSFWTTM AEEDEQRLFT
EKVNNTFSEC LNLINEGCPK EDILVTLNDL IKNIPDAKKL VKYWICLALI EPITSPIENI
IAIYEKAILA GAQPIEEMRH TIVDILTMKS QEKANLGENM EKSCASKEEV KEVSIEDTGV
DVDPEKLEME SKLHRNLLFQ DCEKEQDNKT KDPTHDVKTP NTETRTSCLI KYNVSTTPYL
QSVKKKVQFD GTNSAFKELK FLTPVRRSRR LQEKTSKLPD MLKDHYPCVS SLEQLTELGR
ETDAFVCRPN AALCRVYYEA DTT


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