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Keratin, type I cytoskeletal 19 (Cytokeratin-19) (CK-19) (Keratin-19) (K19)

 K1C19_HUMAN             Reviewed;         400 AA.
P08727; B2R874; Q5XG83; Q6NW33; Q7L5M9; Q96A53; Q96FV1; Q9BYF9;
Q9P1Y4;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 4.
23-MAY-2018, entry version 190.
RecName: Full=Keratin, type I cytoskeletal 19;
AltName: Full=Cytokeratin-19;
Short=CK-19;
AltName: Full=Keratin-19;
Short=K19;
Name=KRT19;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-60.
TISSUE=Placenta;
PubMed=2447559; DOI=10.1093/nar/15.23.10058;
Stasiak P.C., Lane E.B.;
"Sequence of cDNA coding for human keratin 19.";
Nucleic Acids Res. 15:10058-10058(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=2468493;
Bader B.L., Jahn L., Franke W.W.;
"Low level expression of cytokeratins 8, 18 and 19 in vascular smooth
muscle cells of human umbilical cord and in cultured cells derived
therefrom, with an analysis of the chromosomal locus containing the
cytokeratin 19 gene.";
Eur. J. Cell Biol. 47:300-319(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-60.
PubMed=2448790; DOI=10.1073/pnas.85.4.1114;
Eckert R.L.;
"Sequence of the human 40-kDa keratin reveals an unusual structure
with very high sequence identity to the corresponding bovine
keratin.";
Proc. Natl. Acad. Sci. U.S.A. 85:1114-1118(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
AND VARIANT GLY-60.
TISSUE=Placenta;
PubMed=2469734; DOI=10.1111/1523-1747.ep12721500;
Stasiak P.C., Purkis P.E., Leigh I.M., Lane E.B.;
"Keratin 19: predicted amino acid sequence and broad tissue
distribution suggest it evolved from keratinocyte keratins.";
J. Invest. Dermatol. 92:707-716(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-60.
PubMed=10623642; DOI=10.1006/bbrc.1999.1966;
Whittock N.V., Eady R.A.J., McGrath J.A.;
"Genomic organization and amplification of the human keratin 15 and 19
genes.";
Biochem. Biophys. Res. Commun. 267:462-465(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-60.
TISSUE=Placenta;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-60.
TISSUE=Mammary gland, Pancreas, and Placenta;
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
TISSUE=Peripheral blood leukocyte;
PubMed=11682035; DOI=10.1016/S0168-8278(01)00167-2;
Kagaya M., Kaneko S., Ohno H., Inamura K., Kobayashi K.;
"Cloning and characterization of the 5'-flanking region of human
cytokeratin 19 gene in human cholangiocarcinoma cell line.";
J. Hepatol. 35:504-511(2001).
[10]
PROTEIN SEQUENCE OF 25-31; 151-158 AND 227-237.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 145-352.
TISSUE=Lymph node;
Sato T., Weerasinghe A., Kuwano Y., Kaneko T., Ikeda T., Nagai T.,
Makino H., Sano M., Honma K., Nemoto K., Abo T., Shima Y.;
"Diversity of keratin 19 gene expressed in lymph nodes of breast
cancer patients -- strategy to clear the discrepancy between
histological findings and RT-PCR results in the detection of
micrometastasis.";
Seibutsu Butsuri Kagaku 44:201-204(2000).
[12]
PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF SER-10 AND SER-35.
PubMed=10212274; DOI=10.1074/jbc.274.18.12861;
Zhou X., Liao J., Hu L., Feng L., Omary M.B.;
"Characterization of the major physiologic phosphorylation site of
human keratin 19 and its role in filament organization.";
J. Biol. Chem. 274:12861-12866(1999).
[13]
INTERACTION WITH PNN.
PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
Shi J., Sugrue S.P.;
"Dissection of protein linkage between keratins and pinin, a protein
with dual location at desmosome-intermediate filament complex and in
the nucleus.";
J. Biol. Chem. 275:14910-14915(2000).
[14]
FUNCTION, INTERACTION WITH DMD, AND TISSUE SPECIFICITY.
PubMed=16000376; DOI=10.1091/mbc.E05-02-0112;
Stone M.R., O'Neill A., Catino D., Bloch R.J.;
"Specific interaction of the actin-binding domain of dystrophin with
intermediate filaments containing keratin 19.";
Mol. Biol. Cell 16:4280-4293(2005).
[15]
PHOSPHORYLATION AT TYR-391.
PubMed=21049038; DOI=10.1371/journal.pone.0013538;
Zhou Q., Snider N.T., Liao J., Li D.H., Hong A., Ku N.O.,
Cartwright C.A., Omary M.B.;
"Characterization of in vivo keratin 19 phosphorylation on tyrosine-
391.";
PLoS ONE 5:E13538-E13538(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-22; THR-323;
SER-395 AND SER-397, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7; ARG-24; ARG-32; ARG-43
AND ARG-51, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[19]
VARIANT [LARGE SCALE ANALYSIS] GLY-60, AND 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).
-!- FUNCTION: Involved in the organization of myofibers. Together with
KRT8, helps to link the contractile apparatus to dystrophin at the
costameres of striated muscle. {ECO:0000269|PubMed:16000376}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Interacts with PNN and the actin-binding domain of DMD. Interacts
with HCV core protein. {ECO:0000269|PubMed:10809736,
ECO:0000269|PubMed:16000376}.
-!- INTERACTION:
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-742756, EBI-10187270;
Q9NX04:C1orf109; NbExp=5; IntAct=EBI-742756, EBI-8643161;
Q9H257:CARD9; NbExp=3; IntAct=EBI-742756, EBI-751319;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-742756, EBI-10247802;
Q8TD31-3:CCHCR1; NbExp=4; IntAct=EBI-742756, EBI-10175300;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-742756, EBI-10181988;
Q9BT78:COPS4; NbExp=3; IntAct=EBI-742756, EBI-742413;
P11532:DMD; NbExp=2; IntAct=EBI-742756, EBI-295827;
O60573:EIF4E2; NbExp=3; IntAct=EBI-742756, EBI-398610;
Q9NRA8:EIF4ENIF1; NbExp=3; IntAct=EBI-742756, EBI-301024;
Q8IYI6:EXOC8; NbExp=3; IntAct=EBI-742756, EBI-742102;
Q9H5Z6:FAM124B; NbExp=3; IntAct=EBI-742756, EBI-741626;
P14136:GFAP; NbExp=5; IntAct=EBI-742756, EBI-744302;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-742756, EBI-2514791;
O14964:HGS; NbExp=3; IntAct=EBI-742756, EBI-740220;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-742756, EBI-747204;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-742756, EBI-2125614;
P35908:KRT2; NbExp=8; IntAct=EBI-742756, EBI-1247312;
P13647:KRT5; NbExp=4; IntAct=EBI-742756, EBI-702187;
P04259:KRT6B; NbExp=3; IntAct=EBI-742756, EBI-740907;
P05787:KRT8; NbExp=4; IntAct=EBI-742756, EBI-297852;
Q6KB66-2:KRT80; NbExp=4; IntAct=EBI-742756, EBI-11999246;
O15160:POLR1C; NbExp=3; IntAct=EBI-742756, EBI-1055079;
Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-742756, EBI-2557469;
Q9P0N9:TBC1D7; NbExp=5; IntAct=EBI-742756, EBI-3258000;
P0C1Z6-2:TFPT; NbExp=3; IntAct=EBI-742756, EBI-10178002;
P21980:TGM2; NbExp=2; IntAct=EBI-742756, EBI-727668;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-742756, EBI-10180829;
Q1A5X7:WHAMMP3; NbExp=4; IntAct=EBI-742756, EBI-11956783;
-!- TISSUE SPECIFICITY: Expressed in a defined zone of basal
keratinocytes in the deep outer root sheath of hair follicles.
Also observed in sweat gland and mammary gland ductal and
secretory cells, bile ducts, gastrointestinal tract, bladder
urothelium, oral epithelia, esophagus, ectocervical epithelium (at
protein level). Expressed in epidermal basal cells, in nipple
epidermis and a defined region of the hair follicle. Also seen in
a subset of vascular wall cells in both the veins and artery of
human umbilical cord, and in umbilical cord vascular smooth
muscle. Observed in muscle fibers accumulating in the costameres
of myoplasm at the sarcolemma in structures that contain
dystrophin and spectrin. {ECO:0000269|PubMed:16000376,
ECO:0000269|PubMed:2468493, ECO:0000269|PubMed:2469734}.
-!- DEVELOPMENTAL STAGE: Present in hair follicles at all stages of
development. {ECO:0000269|PubMed:2469734}.
-!- DOMAIN: This keratin differs from all other IF proteins in lacking
the C-terminal tail domain.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; J03607; AAA36044.1; -; Genomic_DNA.
EMBL; Y00503; CAA68556.1; -; mRNA.
EMBL; AF202321; AAF27048.1; -; Genomic_DNA.
EMBL; AK313261; BAG36071.1; -; mRNA.
EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002539; AAH02539.3; -; mRNA.
EMBL; BC007628; AAH07628.1; -; mRNA.
EMBL; BC010409; AAH10409.3; -; mRNA.
EMBL; BC067744; AAH67744.2; -; mRNA.
EMBL; BC084574; AAH84574.2; -; mRNA.
EMBL; AB045973; BAB40770.1; -; Genomic_DNA.
EMBL; AB041267; BAA94607.1; -; mRNA.
CCDS; CCDS11399.1; -.
PIR; A31370; KRHU9.
RefSeq; NP_002267.2; NM_002276.4.
UniGene; Hs.654568; -.
ProteinModelPortal; P08727; -.
SMR; P08727; -.
BioGrid; 110078; 53.
DIP; DIP-35655N; -.
IntAct; P08727; 83.
MINT; P08727; -.
STRING; 9606.ENSP00000355124; -.
iPTMnet; P08727; -.
PhosphoSitePlus; P08727; -.
SwissPalm; P08727; -.
BioMuta; KRT19; -.
DMDM; 311033484; -.
SWISS-2DPAGE; P08727; -.
EPD; P08727; -.
MaxQB; P08727; -.
PaxDb; P08727; -.
PeptideAtlas; P08727; -.
PRIDE; P08727; -.
DNASU; 3880; -.
Ensembl; ENST00000361566; ENSP00000355124; ENSG00000171345.
GeneID; 3880; -.
KEGG; hsa:3880; -.
UCSC; uc002hxd.5; human.
CTD; 3880; -.
DisGeNET; 3880; -.
EuPathDB; HostDB:ENSG00000171345.13; -.
GeneCards; KRT19; -.
HGNC; HGNC:6436; KRT19.
HPA; CAB000031; -.
HPA; HPA002465; -.
MIM; 148020; gene.
neXtProt; NX_P08727; -.
OpenTargets; ENSG00000171345; -.
PharmGKB; PA30225; -.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00900000140820; -.
HOVERGEN; HBG013015; -.
InParanoid; P08727; -.
KO; K07604; -.
OMA; AHYNNLP; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; P08727; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P08727; -.
ChiTaRS; KRT19; human.
GeneWiki; Keratin_19; -.
GenomeRNAi; 3880; -.
PRO; PR:P08727; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000171345; -.
ExpressionAtlas; P08727; baseline and differential.
Genevisible; P08727; HS.
GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0043034; C:costamere; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:CACAO.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:1990357; C:terminal web; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IEA:Ensembl.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEP:UniProtKB.
GO; GO:0045214; P:sarcomere organization; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Direct protein sequencing;
Host-virus interaction; Intermediate filament; Keratin; Methylation;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 400 Keratin, type I cytoskeletal 19.
/FTId=PRO_0000063671.
DOMAIN 80 391 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 79 Head.
REGION 80 115 Coil 1A.
REGION 116 133 Linker 1.
REGION 134 225 Coil 1B.
REGION 226 248 Linker 12.
REGION 244 390 Necessary for interaction with PNN.
{ECO:0000269|PubMed:10809736}.
REGION 249 387 Coil 2.
REGION 388 400 Rod-like helical tail.
SITE 267 267 Stutter.
SITE 327 327 Stutter.
MOD_RES 7 7 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 24 24 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 24 24 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 32 32 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000269|PubMed:10212274}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:Q63279}.
MOD_RES 43 43 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 51 51 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:Q63279}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000250|UniProtKB:P19001}.
MOD_RES 323 323 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 391 391 Phosphotyrosine.
{ECO:0000269|PubMed:21049038}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 60 60 A -> G (in dbSNP:rs4602).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:10623642,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2447559,
ECO:0000269|PubMed:2448790,
ECO:0000269|PubMed:2469734}.
/FTId=VAR_014629.
MUTAGEN 10 10 S->A: No effect on phosphorylation; no
functional effect.
{ECO:0000269|PubMed:10212274}.
MUTAGEN 35 35 S->A: Abolishes phosphorylation; induces
perinuclear collapse or short cytoplasmic
filaments. {ECO:0000269|PubMed:10212274}.
CONFLICT 350 350 G -> A (in Ref. 1; CAA68556 and 5;
AAF27048). {ECO:0000305}.
SEQUENCE 400 AA; 44106 MW; C559BBBACCE32DCB CRC64;
MTSYSYRQSS ATSSFGGLGG GSVRFGPGVA FRAPSIHGGS GGRGVSVSSA RFVSSSSSGA
YGGGYGGVLT ASDGLLAGNE KLTMQNLNDR LASYLDKVRA LEAANGELEV KIRDWYQKQG
PGPSRDYSHY YTTIQDLRDK ILGATIENSR IVLQIDNARL AADDFRTKFE TEQALRMSVE
ADINGLRRVL DELTLARTDL EMQIEGLKEE LAYLKKNHEE EISTLRGQVG GQVSVEVDSA
PGTDLAKILS DMRSQYEVMA EQNRKDAEAW FTSRTEELNR EVAGHTEQLQ MSRSEVTDLR
RTLQGLEIEL QSQLSMKAAL EDTLAETEAR FGAQLAHIQA LISGIEAQLG DVRADSERQN
QEYQRLMDIK SRLEQEIATY RSLLEGQEDH YNNLSASKVL


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