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Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)

 CD11A_HUMAN             Reviewed;         783 AA.
Q9UQ88; O95227; O95228; O96012; Q12821; Q12853; Q12854; Q2TAJ0;
Q5QPR0; Q5QPR1; Q5QPR2; Q9UBC4; Q9UBI3; Q9UEI1; Q9UEI2; Q9UP53;
Q9UP54; Q9UP55; Q9UP56; Q9UQ86; Q9UQ87; Q9UQ89;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
25-APR-2018, entry version 177.
RecName: Full=Cyclin-dependent kinase 11A;
EC=2.7.11.22;
AltName: Full=Cell division cycle 2-like protein kinase 2;
AltName: Full=Cell division protein kinase 11A;
AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA;
AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L2;
Name=CDK11A; Synonyms=CDC2L2, CDC2L3, PITSLREB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; SV2 AND 4), TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANT SER-402.
TISSUE=Cervix carcinoma;
PubMed=8195233;
Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J.;
"Molecular cloning and expression of alternatively spliced PITSLRE
protein kinase isoforms.";
J. Biol. Chem. 269:15786-15794(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; SV2; SV3; SV6; SV7; SV12 AND
SV13), TISSUE SPECIFICITY, AND VARIANT TRP-93.
TISSUE=Cervix carcinoma;
PubMed=9750192;
Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I.,
Ambros P.F., Kidd V.J.;
"Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22
genes on human chromosome 1p36.3 and their linkage to D1Z2.";
Genome Res. 8:929-939(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-93.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SV7).
TISSUE=Skin;
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).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNL1 AND SFRS7.
PubMed=12501247; DOI=10.1074/jbc.M210057200;
Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.;
"CDK11 complexes promote pre-mRNA splicing.";
J. Biol. Chem. 278:8623-8629(2003).
[6]
ALTERNATIVE INITIATION (ISOFORM 4), AND INDUCTION.
PubMed=10882096; DOI=10.1016/S1097-2765(00)80239-7;
Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S.,
Beyaert R.;
"Identification and characterization of a novel cell cycle-regulated
internal ribosome entry site.";
Mol. Cell 5:597-605(2000).
[7]
FUNCTION, AND INTERACTION WITH PAK1.
PubMed=12624090; DOI=10.1074/jbc.M300818200;
Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S.,
Zong H., Hu Y., Yuan Z., Shen Z., Gu J.;
"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein
kinase (p110C) associates with p21-activated kinase 1 and inhibits its
activity during anoikis.";
J. Biol. Chem. 278:20029-20036(2003).
-!- FUNCTION: Appears to play multiple roles in cell cycle
progression, cytokinesis and apoptosis. The p110 isoforms have
been suggested to be involved in pre-mRNA splicing, potentially by
phosphorylating the splicing protein SFRS7. The p58 isoform may
act as a negative regulator of normal cell cycle progression.
{ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Phosphorylation at Thr-436 or Tyr-437
inactivates the enzyme, while phosphorylation at Thr-583 activates
it. {ECO:0000250}.
-!- SUBUNIT: The cleaved p110 isoform, p110C, binds to the
serine/threonine kinase PAK1. The p58 isoform but not the p110
isoform or p110C interacts with CCND3. The p110 isoforms are found
in large molecular weight complexes containing CCNL1 and SFRS7.
{ECO:0000269|PubMed:12501247, ECO:0000269|PubMed:12624090}.
-!- INTERACTION:
O96017:CHEK2; NbExp=2; IntAct=EBI-11579223, EBI-1180783;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=SV6; Synonyms=p110;
IsoId=Q9UQ88-1; Sequence=Displayed;
Name=SV1; Synonyms=Pbeta21, Beta 2-1;
IsoId=Q9UQ88-2; Sequence=VSP_008286, VSP_008288;
Note=Ref.1 (AAA19594) sequence is in conflict in position:
109:C->R. Ref.1 (AAA19594) sequence is in conflict in position:
112:H->R. {ECO:0000305};
Name=SV2; Synonyms=Pbeta22;
IsoId=Q9UQ88-3; Sequence=VSP_008287, VSP_008288;
Note=Ref.1 (AAA19595) sequence is in conflict in position:
158:F->V. {ECO:0000305};
Name=SV3;
IsoId=Q9UQ88-4; Sequence=VSP_008288;
Name=SV7; Synonyms=SV8;
IsoId=Q9UQ88-5; Sequence=VSP_008283, VSP_008289;
Name=SV12;
IsoId=Q9UQ88-8; Sequence=VSP_008284, VSP_008292;
Name=SV13;
IsoId=Q9UQ88-9; Sequence=VSP_008281, VSP_008287, VSP_008288,
VSP_008290, VSP_008291;
Name=4; Synonyms=Beta 1, p58;
IsoId=Q9UQ88-10; Sequence=VSP_018836;
Note=Produced by alternative initiation at Met-345 of isoform
SV6.;
-!- TISSUE SPECIFICITY: Expressed ubiquitously. Some evidence of
isoform-specific tissue distribution. {ECO:0000269|PubMed:8195233,
ECO:0000269|PubMed:9750192}.
-!- INDUCTION: The p58 isoform is specifically induced in G2/M phase
of the cell cycle. {ECO:0000269|PubMed:10882096}.
-!- PTM: During apoptosis, induced by Fas or tumor necrosis factor,
specific CKD11 p110 isoforms are cleaved by caspases to produce a
protein (p110C) that contains the C-terminal kinase domain of the
CDK11 proteins.
-!- MISCELLANEOUS: Duplicated gene. CDK11A and CDK11B encode almost
identical protein kinases of 110 kDa that contain at their C-
termini the open reading frame of a smaller 58 kDa isoform which
is expressed following IRES-mediated alternative initiation of
translation.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- CAUTION: Many references talk about 'p110 isoforms' but it is not
yet known if this refers to CDK11A and/or CDK11B or one/some of
the isoforms of each. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC95297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC95298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC95299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC95300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC95302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC95303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; U04819; AAA19585.1; -; mRNA.
EMBL; U07704; AAA19594.1; -; mRNA.
EMBL; U07705; AAA19595.1; -; mRNA.
EMBL; AF067518; AAC72083.1; -; mRNA.
EMBL; AF067519; AAC72084.1; -; mRNA.
EMBL; AF067520; AAC72085.1; -; mRNA.
EMBL; AF067521; AAC72086.1; -; mRNA.
EMBL; AF067522; AAC72087.1; -; mRNA.
EMBL; AF067523; AAC72088.1; -; mRNA.
EMBL; AF067524; AAC72089.1; -; mRNA.
EMBL; AF067525; AAC72090.1; -; mRNA.
EMBL; AF067526; AAC72091.1; -; mRNA.
EMBL; AF067527; AAC72092.1; -; mRNA.
EMBL; AF067528; AAC72093.1; -; mRNA.
EMBL; AF067529; AAC72094.1; -; mRNA.
EMBL; AF080694; AAC95297.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080695; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF105714; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080696; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080697; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF092427; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF092428; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080689; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080690; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080691; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080692; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080693; AAC95297.1; JOINED; Genomic_DNA.
EMBL; AF080694; AAC95298.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080695; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF105714; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080696; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080697; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF092427; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF092428; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080689; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080690; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080691; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080692; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080693; AAC95298.1; JOINED; Genomic_DNA.
EMBL; AF080694; AAC95299.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080695; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF105714; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080696; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080697; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF092427; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF092428; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080689; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080690; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080691; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080692; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080693; AAC95299.1; JOINED; Genomic_DNA.
EMBL; AF080694; AAC95300.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080695; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF105714; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080696; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080697; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF092427; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF092428; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080689; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080690; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080691; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080692; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080693; AAC95300.1; JOINED; Genomic_DNA.
EMBL; AF080697; AAC95302.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080695; AAC95302.1; JOINED; Genomic_DNA.
EMBL; AF105714; AAC95302.1; JOINED; Genomic_DNA.
EMBL; AF080696; AAC95302.1; JOINED; Genomic_DNA.
EMBL; AF080697; AAC95303.1; ALT_SEQ; Genomic_DNA.
EMBL; AF080695; AAC95303.1; JOINED; Genomic_DNA.
EMBL; AF105714; AAC95303.1; JOINED; Genomic_DNA.
EMBL; AF080696; AAC95303.1; JOINED; Genomic_DNA.
EMBL; AL031282; CAI20032.1; -; Genomic_DNA.
EMBL; AL031282; CAI20033.1; -; Genomic_DNA.
EMBL; AL031282; CAI20034.1; -; Genomic_DNA.
EMBL; BC110905; AAI10906.1; -; mRNA.
CCDS; CCDS44042.1; -. [Q9UQ88-2]
CCDS; CCDS44043.1; -. [Q9UQ88-4]
CCDS; CCDS81253.1; -. [Q9UQ88-1]
CCDS; CCDS81254.1; -. [Q9UQ88-3]
PIR; B54024; B54024.
PIR; E54024; E54024.
PIR; F54024; F54024.
PIR; H54024; H54024.
RefSeq; NP_001300825.1; NM_001313896.1. [Q9UQ88-1]
RefSeq; NP_001300911.1; NM_001313982.1.
RefSeq; NP_076916.2; NM_024011.3. [Q9UQ88-2]
RefSeq; NP_277071.2; NM_033529.3. [Q9UQ88-4]
UniGene; Hs.651228; -.
UniGene; Hs.709182; -.
ProteinModelPortal; Q9UQ88; -.
SMR; Q9UQ88; -.
BioGrid; 609064; 68.
IntAct; Q9UQ88; 39.
MINT; Q9UQ88; -.
BindingDB; Q9UQ88; -.
ChEMBL; CHEMBL5416; -.
GuidetoPHARMACOLOGY; 1963; -.
iPTMnet; Q9UQ88; -.
PhosphoSitePlus; Q9UQ88; -.
BioMuta; CDK11A; -.
DMDM; 317373559; -.
PeptideAtlas; Q9UQ88; -.
PRIDE; Q9UQ88; -.
Ensembl; ENST00000358779; ENSP00000351629; ENSG00000008128. [Q9UQ88-4]
Ensembl; ENST00000378633; ENSP00000367900; ENSG00000008128. [Q9UQ88-1]
Ensembl; ENST00000404249; ENSP00000384442; ENSG00000008128. [Q9UQ88-2]
GeneID; 728642; -.
KEGG; hsa:728642; -.
UCSC; uc009vkr.4; human. [Q9UQ88-1]
CTD; 728642; -.
DisGeNET; 728642; -.
EuPathDB; HostDB:ENSG00000008128.22; -.
GeneCards; CDK11A; -.
HGNC; HGNC:1730; CDK11A.
HPA; CAB010467; -.
HPA; HPA025061; -.
HPA; HPA073626; -.
MIM; 116951; gene.
neXtProt; NX_Q9UQ88; -.
OpenTargets; ENSG00000008128; -.
PharmGKB; PA26263; -.
eggNOG; KOG0663; Eukaryota.
eggNOG; ENOG410XQ50; LUCA.
GeneTree; ENSGT00910000144030; -.
HOVERGEN; HBG014652; -.
InParanoid; Q9UQ88; -.
KO; K08818; -.
OMA; CRIMHAD; -.
OrthoDB; EOG091G048P; -.
TreeFam; TF101035; -.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
SignaLink; Q9UQ88; -.
SIGNOR; Q9UQ88; -.
GeneWiki; CDC2L2; -.
GenomeRNAi; 728642; -.
PRO; PR:Q9UQ88; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000008128; -.
ExpressionAtlas; Q9UQ88; baseline and differential.
Genevisible; Q9UQ88; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; NAS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IEP:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Apoptosis; ATP-binding;
Cell cycle; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 783 Cyclin-dependent kinase 11A.
/FTId=PRO_0000024315.
DOMAIN 427 647 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 432 440 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 15 381 Glu-rich.
ACT_SITE 550 550 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 455 455 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 470 470 Phosphoserine; by CDK7.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 476 476 Phosphothreonine; by CDK7.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 577 577 Phosphoserine.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 582 582 Phosphotyrosine.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 583 583 Phosphothreonine.
{ECO:0000250|UniProtKB:P21127}.
MOD_RES 739 739 Phosphothreonine.
{ECO:0000250|UniProtKB:P24788}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000250|UniProtKB:P24788}.
VAR_SEQ 1 616 Missing (in isoform SV12).
{ECO:0000303|PubMed:9750192}.
/FTId=VSP_008284.
VAR_SEQ 1 386 Missing (in isoform SV7).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9750192}.
/FTId=VSP_008283.
VAR_SEQ 1 344 Missing (in isoform 4).
{ECO:0000303|PubMed:8195233}.
/FTId=VSP_018836.
VAR_SEQ 1 57 Missing (in isoform SV13).
{ECO:0000303|PubMed:9750192}.
/FTId=VSP_008281.
VAR_SEQ 109 109 W -> CRHHSHSAEGG (in isoform SV1).
{ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192}.
/FTId=VSP_008286.
VAR_SEQ 153 153 R -> RGNDGFCLFR (in isoform SV2 and
isoform SV13).
{ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192}.
/FTId=VSP_008287.
VAR_SEQ 240 253 GEARPAPAQKPAQL -> V (in isoform SV1,
isoform SV2, isoform SV3 and isoform
SV13). {ECO:0000303|PubMed:8195233,
ECO:0000303|PubMed:9750192}.
/FTId=VSP_008288.
VAR_SEQ 387 418 SALTEGDYVPDSPALLPIELKQELPKYLPALQ -> MKNEK
MKTTSWLFQSHGSTEIPGRVKKQRKKW (in isoform
SV7). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9750192}.
/FTId=VSP_008289.
VAR_SEQ 567 600 GDFGLAREYGSPLKAYTPVVVTQWYRAPELLLGA -> SPP
PSGPSQGDPPGPTHSRPSVVAGG (in isoform
SV13). {ECO:0000303|PubMed:9750192}.
/FTId=VSP_008290.
VAR_SEQ 601 783 Missing (in isoform SV13).
{ECO:0000303|PubMed:9750192}.
/FTId=VSP_008291.
VAR_SEQ 617 658 GELLTQKPLFPGNSEIDQINKVFKELGTPSEKIWPGYSELP
V -> MGKTEEKGNGKGAFQERKGPLGAVRKEAGAGAQDAG
AAEGAA (in isoform SV12).
{ECO:0000303|PubMed:9750192}.
/FTId=VSP_008292.
VARIANT 57 57 C -> R (in dbSNP:rs1059832).
/FTId=VAR_060152.
VARIANT 92 92 S -> P (in dbSNP:rs7531938).
/FTId=VAR_062200.
VARIANT 93 93 R -> W (in dbSNP:rs1059831).
{ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:9750192}.
/FTId=VAR_031716.
VARIANT 402 402 L -> S (in dbSNP:rs1059828).
{ECO:0000269|PubMed:8195233}.
/FTId=VAR_031717.
VARIANT 658 658 V -> A (in dbSNP:rs1059811).
/FTId=VAR_060153.
CONFLICT 109 109 Missing (in Ref. 1; AAA19594/AAA19595).
{ECO:0000305}.
CONFLICT 246 246 P -> R (in Ref. 2; AAC72087).
{ECO:0000305}.
CONFLICT 312 314 Missing (in Ref. 1; AAA19594/AAA19595 and
2; AAC72084/AAC72085/AAC72086/AAC72087/
AAC72090). {ECO:0000305}.
CONFLICT 424 424 E -> D (in Ref. 1; AAA19585/AAA19594/
AAA19595). {ECO:0000305}.
CONFLICT 463 463 K -> N (in Ref. 1; AAA19585/AAA19594/
AAA19595). {ECO:0000305}.
CONFLICT 666 666 E -> R (in Ref. 1; AAA19585/AAA19594/
AAA19595). {ECO:0000305}.
CONFLICT 682 682 D -> E (in Ref. 1; AAA19585/AAA19594/
AAA19595). {ECO:0000305}.
SEQUENCE 783 AA; 91362 MW; 1BCF67EB180F37C6 CRC64;
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHCMEI
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKVHHR KDEKRKEKWK HARVKEREHE
RRKRHREEQD KARREWERQK RREMAREHSR RERDRLEQLE RKRERERKMR EQQKEQREQK
ERERRAEERR KEREARREVS AHHRTMREDY SDKVKASHWS RSPPRPPRER FELGDGRKPG
EARPAPAQKP AQLKEEKMEE RDLLSDLQDI SDSERKTSSA ESSSAESGSG SEEEEEEEEE
EEEEGSTSEE SEEEEEEEEE EEEETGSNSE EASEQSAEEV SEEEMSEDEE RENENHLLVV
PESRFDRDSG ESEEAEEEVG EGTPQSSALT EGDYVPDSPA LLPIELKQEL PKYLPALQGC
RSVEEFQCLN RIEEGTYGVV YRAKDKKTDE IVALKRLKME KEKEGFPITS LREINTILKA
QHPNIVTVRE IVVGSNMDKI YIVMNYVEHD LKSLMETMKQ PFLPGEVKTL MIQLLRGVKH
LHDNWILHRD LKTSNLLLSH AGILKVGDFG LAREYGSPLK AYTPVVVTQW YRAPELLLGA
KEYSTAVDMW SVGCIFGELL TQKPLFPGNS EIDQINKVFK ELGTPSEKIW PGYSELPVVK
KMTFSEHPYN NLRKRFGALL SDQGFDLMNK FLTYFPGRRI SAEDGLKHEY FRETPLPIDP
SMFPTWPAKS EQQRVKRGTS PRPPEGGLGY SQLGDDDLKE TGFHLTTTNQ GASAAGPGFS
LKF


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