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Keratin, type I cytoskeletal 13 (Cytokeratin-13) (CK-13) (Keratin-13) (K13)

 K1C13_HUMAN             Reviewed;         458 AA.
P13646; Q53G54; Q6AZK5; Q8N240;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 4.
13-FEB-2019, entry version 196.
RecName: Full=Keratin, type I cytoskeletal 13;
AltName: Full=Cytokeratin-13;
Short=CK-13;
AltName: Full=Keratin-13;
Short=K13;
Name=KRT13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-187 AND
ALA-298.
PubMed=2475110; DOI=10.1016/0006-291X(89)90847-4;
Schulz P., Wachter E., Hochstrasser K., Wild A.G., Mischke D.;
"Sequence of a human keratin 13 specific cDNA encompassing coil 1B
through the 3' end.";
Biochem. Biophys. Res. Commun. 162:1522-1527(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, PROTEIN
SEQUENCE OF 291-299, AND VARIANTS VAL-187 AND ALA-298.
PubMed=2477803; DOI=10.1093/nar/17.19.7984;
Mischke D., Schulz P., Wild A.G.;
"The N-, but not the C-terminal domains of human keratins 13 and 15
are closely related.";
Nucleic Acids Res. 17:7984-7984(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
VARIANTS VAL-187 AND ALA-298.
PubMed=2483837; DOI=10.1111/j.1432-0436.1989.tb00612.x;
Kuruc N., Leube R.E., Moll I., Bader B.L., Franke W.W.;
"Synthesis of cytokeratin 13, a component characteristic of internal
stratified epithelia, is not induced in human epidermal tumors.";
Differentiation 42:111-123(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANTS VAL-187
AND ALA-298.
PubMed=9714826; DOI=10.1016/S0378-1119(98)00297-2;
Waseem A., Alam Y., Dogan B., White K.N., Leigh I.M., Waseem N.H.;
"Isolation, sequence and expression of the gene encoding human keratin
13.";
Gene 215:269-279(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
VAL-187 AND ALA-298.
TISSUE=Tongue;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
VAL-187 AND ALA-298.
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[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] (ISOFORM 1), AND VARIANTS
VAL-187 AND ALA-298.
TISSUE=Brain, and Pancreas;
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]
PROTEIN SEQUENCE OF 124-135; 176-222; 291-318 AND 416-429,
PHOSPHORYLATION AT SER-427, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
Submitted (OCT-2008) to UniProtKB.
[10]
GLYCOSYLATION.
PubMed=2474541;
King I.A., Hounsell E.F.;
"Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine
residues.";
J. Biol. Chem. 264:14022-14028(1989).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, 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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27 AND ARG-35, 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).
[18]
VARIANT WSN2 PRO-119.
PubMed=7493031; DOI=10.1038/ng1295-453;
Richard G., de Laurenzi V., Didona B., Bale S.J., Compton J.G.;
"Keratin 13 point mutation underlies the hereditary mucosal epithelial
disorder white sponge nevus.";
Nat. Genet. 11:453-455(1995).
[19]
VARIANTS WSN2 THR-108 AND PRO-115.
PubMed=10561721;
Rugg E.L., Magee G., Wilson N., Brandrup F., Hamburger J., Lane E.B.;
"Identification of two novel mutations in keratin 13 as the cause of
white sponge naevus.";
Oral Dis. 5:321-324(1999).
[20]
VARIANT WSN2 SER-112.
PubMed=11379896; DOI=10.1177/00220345010800031401;
Terrinoni A., Rugg E.L., Lane E.B., Melino G., Felix D.H., Munro C.S.,
McLean W.H.I.;
"A novel mutation in the keratin 13 gene causing oral white sponge
nevus.";
J. Dent. Res. 80:919-923(2001).
[21]
VARIANT WSN2 PRO-111.
PubMed=14600690; DOI=10.1016/S1079-2104(03)00372-X;
Shibuya Y., Zhang J., Yokoo S., Umeda M., Komori T.;
"Constitutional mutation of keratin 13 gene in familial white sponge
nevus.";
Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod.
96:561-565(2003).
[22]
VARIANT [LARGE SCALE ANALYSIS] VAL-187, 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).
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
keratin-13 is generally associated with keratin-4.
-!- INTERACTION:
P14136:GFAP; NbExp=5; IntAct=EBI-1223876, EBI-744302;
A0A0S2Z4Q4:HGS; NbExp=3; IntAct=EBI-1223876, EBI-16429135;
O14964:HGS; NbExp=5; IntAct=EBI-1223876, EBI-740220;
P35908:KRT2; NbExp=3; IntAct=EBI-1223876, EBI-1247312;
P02538:KRT6A; NbExp=5; IntAct=EBI-1223876, EBI-702198;
P07196:NEFL; NbExp=3; IntAct=EBI-1223876, EBI-475646;
A0A0S2Z5X4:ZNF688; NbExp=3; IntAct=EBI-1223876, EBI-16429014;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=A;
IsoId=P13646-1; Sequence=Displayed;
Name=2;
IsoId=P13646-2; Sequence=VSP_016376, VSP_016377;
Note=No experimental confirmation available.;
Name=3;
IsoId=P13646-3; Sequence=VSP_038433;
-!- TISSUE SPECIFICITY: Expressed in some epidermal sweat gland ducts
(at protein level) and in exocervix, esophagus and placenta.
{ECO:0000269|PubMed:2483837}.
-!- PTM: O-glycosylated; glycans consist of single N-acetylglucosamine
residues. {ECO:0000269|PubMed:2474541}.
-!- DISEASE: White sponge nevus 2 (WSN2) [MIM:615785]: A rare disorder
characterized by the presence of soft, white, and spongy plaques
in the oral mucosa. The characteristic histopathologic features
are epithelial thickening, parakeratosis, and vacuolization of the
suprabasal layer of oral epithelial keratinocytes. Less frequently
the mucous membranes of the nose, esophagus, genitalia and rectum
are involved. {ECO:0000269|PubMed:10561721,
ECO:0000269|PubMed:11379896, ECO:0000269|PubMed:14600690,
ECO:0000269|PubMed:7493031}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-13 entry;
URL="https://en.wikipedia.org/wiki/Keratin_13";
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EMBL; X14640; CAA32786.1; -; mRNA.
EMBL; X52426; CAA36673.1; -; mRNA.
EMBL; AF049259; AAC35754.1; -; Genomic_DNA.
EMBL; AK092276; BAC03847.1; -; mRNA.
EMBL; AK223051; BAD96771.1; -; mRNA.
EMBL; AK223077; BAD96797.1; -; mRNA.
EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002661; AAH02661.3; -; mRNA.
EMBL; BC077718; AAH77718.2; -; mRNA.
CCDS; CCDS11396.1; -. [P13646-1]
CCDS; CCDS11397.1; -. [P13646-3]
PIR; A37343; A37343.
PIR; S06088; KRHU3.
RefSeq; NP_002265.2; NM_002274.3.
RefSeq; NP_705694.2; NM_153490.2.
UniGene; Hs.654550; -.
ProteinModelPortal; P13646; -.
SMR; P13646; -.
BioGrid; 110058; 68.
IntAct; P13646; 32.
STRING; 9606.ENSP00000246635; -.
GlyConnect; 311; -.
iPTMnet; P13646; -.
PhosphoSitePlus; P13646; -.
SwissPalm; P13646; -.
UniCarbKB; P13646; -.
BioMuta; KRT13; -.
DMDM; 269849755; -.
jPOST; P13646; -.
PaxDb; P13646; -.
PeptideAtlas; P13646; -.
PRIDE; P13646; -.
ProteomicsDB; 52951; -.
ProteomicsDB; 52952; -. [P13646-2]
ProteomicsDB; 52953; -. [P13646-3]
DNASU; 3860; -.
Ensembl; ENST00000246635; ENSP00000246635; ENSG00000171401. [P13646-1]
Ensembl; ENST00000336861; ENSP00000336604; ENSG00000171401. [P13646-3]
GeneID; 3860; -.
KEGG; hsa:3860; -.
UCSC; uc002hwu.2; human. [P13646-1]
CTD; 3860; -.
DisGeNET; 3860; -.
EuPathDB; HostDB:ENSG00000171401.14; -.
GeneCards; KRT13; -.
HGNC; HGNC:6415; KRT13.
HPA; CAB000133; -.
HPA; HPA030877; -.
HPA; HPA069771; -.
MalaCards; KRT13; -.
MIM; 148065; gene.
MIM; 615785; phenotype.
neXtProt; NX_P13646; -.
OpenTargets; ENSG00000171401; -.
Orphanet; 171723; White sponge nevus.
PharmGKB; PA30202; -.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00940000165872; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; P13646; -.
KO; K07604; -.
OMA; DAKMTGF; -.
OrthoDB; 856254at2759; -.
PhylomeDB; P13646; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
ChiTaRS; KRT13; human.
GeneWiki; Keratin_13; -.
GenomeRNAi; 3860; -.
PRO; PR:P13646; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000171401; Expressed in 121 organ(s), highest expression level in esophagus mucosa.
ExpressionAtlas; P13646; baseline and differential.
Genevisible; P13646; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
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;
Alternative splicing; Coiled coil; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein;
Intermediate filament; Keratin; Methylation; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 458 Keratin, type I cytoskeletal 13.
/FTId=PRO_0000063647.
DOMAIN 104 416 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 103 Head.
REGION 104 139 Coil 1A.
REGION 140 158 Linker 1.
REGION 159 250 Coil 1B.
REGION 251 273 Linker 12.
REGION 274 412 Coil 2.
REGION 413 458 Tail.
COMPBIAS 13 102 Gly-rich.
MOD_RES 27 27 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 35 35 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.9}.
VAR_SEQ 62 73 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016376.
VAR_SEQ 351 458 ETECRYALQLQQIQGLISSIEAQLSELRSEMECQNQEYKML
LDIKTRLEQEIATYRSLLEGQDAKMIGFPSSAGSVSPRSTS
VTTTSSASVTTTSNASGRRTSDVRRP -> DPGTHQQHRGP
AERAPQ (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016377.
VAR_SEQ 416 458 MIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVR
RP -> KRQPP (in isoform 3).
{ECO:0000303|PubMed:2483837}.
/FTId=VSP_038433.
VARIANT 81 81 F -> Y (in dbSNP:rs12150581).
/FTId=VAR_059376.
VARIANT 108 108 M -> T (in WSN2; dbSNP:rs60364670).
{ECO:0000269|PubMed:10561721}.
/FTId=VAR_016035.
VARIANT 111 111 L -> P (in WSN2; dbSNP:rs59897026).
{ECO:0000269|PubMed:14600690}.
/FTId=VAR_023924.
VARIANT 112 112 N -> S (in WSN2; dbSNP:rs59970018).
{ECO:0000269|PubMed:11379896}.
/FTId=VAR_016036.
VARIANT 115 115 L -> P (in WSN2; dbSNP:rs60906702).
{ECO:0000269|PubMed:10561721}.
/FTId=VAR_016037.
VARIANT 119 119 L -> P (in WSN2; dbSNP:rs60440396).
{ECO:0000269|PubMed:7493031}.
/FTId=VAR_003836.
VARIANT 146 146 A -> G (in dbSNP:rs760134).
/FTId=VAR_024488.
VARIANT 187 187 A -> V (in dbSNP:rs9891361).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2475110,
ECO:0000269|PubMed:2477803,
ECO:0000269|PubMed:2483837,
ECO:0000269|PubMed:9714826,
ECO:0000269|Ref.6}.
/FTId=VAR_060724.
VARIANT 298 298 T -> A (in dbSNP:rs4796697).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2475110,
ECO:0000269|PubMed:2477803,
ECO:0000269|PubMed:2483837,
ECO:0000269|PubMed:9714826,
ECO:0000269|Ref.6}.
/FTId=VAR_059377.
CONFLICT 46 46 G -> R (in Ref. 6; BAD96771/BAD96797).
{ECO:0000305}.
CONFLICT 58 58 G -> D (in Ref. 1; CAA32786 and 2).
{ECO:0000305}.
SEQUENCE 458 AA; 49588 MW; A51AECFD6195ACB4 CRC64;
MSLRLQSSSA SYGGGFGGGS CQLGGGRGVS TCSTRFVSGG SAGGYGGGVS CGFGGGAGSG
FGGGYGGGLG GGYGGGLGGG FGGGFAGGFV DFGACDGGLL TGNEKITMQN LNDRLASYLE
KVRALEEANA DLEVKIRDWH LKQSPASPER DYSPYYKTIE ELRDKILTAT IENNRVILEI
DNARLAADDF RLKYENELAL RQSVEADING LRRVLDELTL SKTDLEMQIE SLNEELAYMK
KNHEEEMKEF SNQVVGQVNV EMDATPGIDL TRVLAEMREQ YEAMAERNRR DAEEWFHTKS
AELNKEVSTN TAMIQTSKTE ITELRRTLQG LEIELQSQLS MKAGLENTVA ETECRYALQL
QQIQGLISSI EAQLSELRSE MECQNQEYKM LLDIKTRLEQ EIATYRSLLE GQDAKMIGFP
SSAGSVSPRS TSVTTTSSAS VTTTSNASGR RTSDVRRP


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1017: Type II interferon signaling (IFNG)
WP1136: Type II interferon signaling (IFNG)
WP1253: Type II interferon signaling (IFNG)
WP1289: Type II interferon signaling (IFNG)
WP1350: Type II interferon signaling (IFNG)
WP1584: Type II diabetes mellitus
WP2113: Type III interferon signaling
WP2272: Pathogenic Escherichia coli infection
WP585: Interferon type I
WP619: Type II interferon signaling (IFNG)
WP786: Type II interferon signaling (IFNG)
WP900: Type II interferon signaling (IFNG)

Related Genes :
[per CG2647] Period circadian protein (Protein clock-6) (CLK-6)
[Krt71 K6irs1 Kb34 Krt2-6g Krt6g] Keratin, type II cytoskeletal 71 (Cytokeratin-6G) (CK-6G) (Cytokeratin-71) (CK-71) (Keratin-6G) (K6G) (Keratin-71) (K71) (Type II inner root sheath-specific keratin-K6irs1) (mK6irs) (mK6irs1/Krt2-6g) (Type-II keratin Kb34)
[KRT1 KRTA] Keratin, type II cytoskeletal 1 (67 kDa cytokeratin) (Cytokeratin-1) (CK-1) (Hair alpha protein) (Keratin-1) (K1) (Type-II keratin Kb1)
[Krt18 Kerd Krt1-18] Keratin, type I cytoskeletal 18 (Cytokeratin endo B) (Keratin D) (Cytokeratin-18) (CK-18) (Keratin-18) (K18)
[KRT6C KRT6E] Keratin, type II cytoskeletal 6C (Cytokeratin-6C) (CK-6C) (Cytokeratin-6E) (CK-6E) (Keratin K6h) (Keratin-6C) (K6C) (Type-II keratin Kb12)
[KRT6A K6A KRT6D] Keratin, type II cytoskeletal 6A (Cytokeratin-6A) (CK-6A) (Cytokeratin-6D) (CK-6D) (Keratin-6A) (K6A) (Type-II keratin Kb6) (allergen Hom s 5)
[KRT18 CYK18 PIG46] Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18)
[KRT71 K6IRS1 KB34 KRT6IRS1] Keratin, type II cytoskeletal 71 (Cytokeratin-71) (CK-71) (Keratin-71) (K71) (Type II inner root sheath-specific keratin-K6irs1) (Keratin 6 irs) (hK6irs) (hK6irs1) (Type-II keratin Kb34)
[KRT10 KPP] Keratin, type I cytoskeletal 10 (Cytokeratin-10) (CK-10) (Keratin-10) (K10)
[Krt18 Krt1-18] Keratin, type I cytoskeletal 18 (Cytokeratin-18) (CK-18) (Keratin-18) (K18)
[KRT17] Keratin, type I cytoskeletal 17 (39.1) (Cytokeratin-17) (CK-17) (Keratin-17) (K17)
[KRT19] Keratin, type I cytoskeletal 19 (Cytokeratin-19) (CK-19) (Keratin-19) (K19)
[KRT5] Keratin, type II cytoskeletal 5 (58 kDa cytokeratin) (Cytokeratin-5) (CK-5) (Keratin-5) (K5) (Type-II keratin Kb5)
[KRT3] Keratin, type II cytoskeletal 3 (65 kDa cytokeratin) (Cytokeratin-3) (CK-3) (Keratin-3) (K3) (Type-II keratin Kb3)
[KRT74 K6IRS4 KB37 KRT5C KRT6IRS4] Keratin, type II cytoskeletal 74 (Cytokeratin-74) (CK-74) (Keratin-5c) (K5C) (Keratin-74) (K74) (Type II inner root sheath-specific keratin-K6irs4) (Type-II keratin Kb37)
[KRT14] Keratin, type I cytoskeletal 14 (Cytokeratin-14) (CK-14) (Keratin-14) (K14)
[KRT79 K6L KB38 KRT6L] Keratin, type II cytoskeletal 79 (Cytokeratin-79) (CK-79) (Keratin-6-like) (Keratin-6L) (Keratin-79) (K79) (Type-II keratin Kb38)
[KRT9] Keratin, type I cytoskeletal 9 (Cytokeratin-9) (CK-9) (Keratin-9) (K9)
[KRT73 K6IRS3 KB36 KRT6IRS3] Keratin, type II cytoskeletal 73 (Cytokeratin-73) (CK-73) (Keratin-73) (K73) (Type II inner root sheath-specific keratin-K6irs3) (Type-II keratin Kb36)
[KRT6B K6B KRTL1] Keratin, type II cytoskeletal 6B (Cytokeratin-6B) (CK-6B) (Keratin-6B) (K6B) (Type-II keratin Kb10)
[Krt4 Krt2-4] Keratin, type II cytoskeletal 4 (Cytokeratin-4) (CK-4) (Cytoskeletal 57 kDa keratin) (Keratin-4) (K4) (Type-II keratin Kb4)
[KRT72 K6IRS2 KB35 KRT6 KRT6IRS2] Keratin, type II cytoskeletal 72 (Cytokeratin-72) (CK-72) (Keratin-72) (K72) (Type II inner root sheath-specific keratin-K6irs2) (Type-II keratin Kb35)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Krt17 Krt1-17] Keratin, type I cytoskeletal 17 (Cytokeratin-17) (CK-17) (Keratin-17) (K17)
[KRT80 KB20] Keratin, type II cytoskeletal 80 (Cytokeratin-80) (CK-80) (Keratin-80) (K80) (Type-II keratin Kb20)
[Krt6a Ker2 Krt2-6 Krt2-6a Krt6] Keratin, type II cytoskeletal 6A (Cytokeratin-6A) (CK-6A) (Keratin-6-alpha) (mK6-alpha) (Keratin-6A) (K6A)
[KRT16 KRT16A] Keratin, type I cytoskeletal 16 (Cytokeratin-16) (CK-16) (Keratin-16) (K16)
[KRT12] Keratin, type I cytoskeletal 12 (Cytokeratin-12) (CK-12) (Keratin-12) (K12)
[Krt16 Krt1-16] Keratin, type I cytoskeletal 16 (Cytokeratin-16) (CK-16) (Keratin-16) (K16)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :
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