Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Keratin, type I cytoskeletal 13

Gene

KRT13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 13
Alternative name(s):
Cytokeratin-13
Short name:
CK-13
Keratin-13
Short name:
K13
Gene namesi
Name:KRT13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6415. KRT13.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • intermediate filament cytoskeleton Source: UniProtKB
  • keratin filament Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

Pathology & Biotechi

Involvement in diseasei

White sponge nevus 2 (WSN2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615785
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti108 – 1081M → T in WSN2. 1 Publication
VAR_016035
Natural varianti111 – 1111L → P in WSN2. 1 Publication
VAR_023924
Natural varianti112 – 1121N → S in WSN2. 1 Publication
VAR_016036
Natural varianti115 – 1151L → P in WSN2. 1 Publication
VAR_016037
Natural varianti119 – 1191L → P in WSN2. 1 Publication
VAR_003836

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiKRT13.
MIMi615785. phenotype.
Orphaneti171723. White sponge nevus.
PharmGKBiPA30202.

Polymorphism and mutation databases

BioMutaiKRT13.
DMDMi269849755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Keratin, type I cytoskeletal 13PRO_0000063647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei427 – 4271PhosphoserineCombined sources1 Publication

Post-translational modificationi

O-glycosylated; glycans consist of single N-acetylglucosamine residues.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP13646.
MaxQBiP13646.
PaxDbiP13646.
PRIDEiP13646.

PTM databases

iPTMnetiP13646.
PhosphoSiteiP13646.
UniCarbKBiP13646.

Expressioni

Tissue specificityi

Expressed in some epidermal sweat gland ducts (at protein level) and in exocervix, esophagus and placenta.1 Publication

Gene expression databases

BgeeiP13646.
CleanExiHS_KRT13.
ExpressionAtlasiP13646. baseline and differential.
GenevisibleiP13646. HS.

Organism-specific databases

HPAiCAB000133.
HPA030877.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. keratin-13 is generally associated with keratin-4.

Protein-protein interaction databases

BioGridi110058. 57 interactions.
IntActiP13646. 8 interactions.
STRINGi9606.ENSP00000246635.

Structurei

3D structure databases

ProteinModelPortaliP13646.
SMRiP13646. Positions 155-253, 269-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 103103HeadAdd
BLAST
Regioni104 – 412309RodAdd
BLAST
Regioni104 – 13936Coil 1AAdd
BLAST
Regioni140 – 15819Linker 1Add
BLAST
Regioni159 – 25092Coil 1BAdd
BLAST
Regioni251 – 27323Linker 12Add
BLAST
Regioni274 – 412139Coil 2Add
BLAST
Regioni413 – 45846TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 10290Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP13646.
KOiK07604.
OMAiTCSTRFV.
PhylomeDBiP13646.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13646-1) [UniParc]FASTAAdd to basket

Also known as: A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLRLQSSSA SYGGGFGGGS CQLGGGRGVS TCSTRFVSGG SAGGYGGGVS
60 70 80 90 100
CGFGGGAGSG FGGGYGGGLG GGYGGGLGGG FGGGFAGGFV DFGACDGGLL
110 120 130 140 150
TGNEKITMQN LNDRLASYLE KVRALEEANA DLEVKIRDWH LKQSPASPER
160 170 180 190 200
DYSPYYKTIE ELRDKILTAT IENNRVILEI DNARLAADDF RLKYENELAL
210 220 230 240 250
RQSVEADING LRRVLDELTL SKTDLEMQIE SLNEELAYMK KNHEEEMKEF
260 270 280 290 300
SNQVVGQVNV EMDATPGIDL TRVLAEMREQ YEAMAERNRR DAEEWFHTKS
310 320 330 340 350
AELNKEVSTN TAMIQTSKTE ITELRRTLQG LEIELQSQLS MKAGLENTVA
360 370 380 390 400
ETECRYALQL QQIQGLISSI EAQLSELRSE MECQNQEYKM LLDIKTRLEQ
410 420 430 440 450
EIATYRSLLE GQDAKMIGFP SSAGSVSPRS TSVTTTSSAS VTTTSNASGR

RTSDVRRP
Length:458
Mass (Da):49,588
Last modified:November 24, 2009 - v4
Checksum:iA51AECFD6195ACB4
GO
Isoform 2 (identifier: P13646-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     62-73: Missing.
     351-458: ETECRYALQL...GRRTSDVRRP → DPGTHQQHRGPAERAPQ

Note: No experimental confirmation available.
Show »
Length:355
Mass (Da):38,581
Checksum:i4961456B245B173B
GO
Isoform 3 (identifier: P13646-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-458: MIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVRRP → KRQPP

Show »
Length:420
Mass (Da):45,867
Checksum:i2C1A7FAF2BD62DCD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461G → R in BAD96771 (Ref. 6) Curated
Sequence conflicti46 – 461G → R in BAD96797 (Ref. 6) Curated
Sequence conflicti58 – 581G → D in CAA32786 (PubMed:2475110).Curated
Sequence conflicti58 – 581G → D (PubMed:2477803).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti81 – 811F → Y.
Corresponds to variant rs12150581 [ dbSNP | Ensembl ].
VAR_059376
Natural varianti108 – 1081M → T in WSN2. 1 Publication
VAR_016035
Natural varianti111 – 1111L → P in WSN2. 1 Publication
VAR_023924
Natural varianti112 – 1121N → S in WSN2. 1 Publication
VAR_016036
Natural varianti115 – 1151L → P in WSN2. 1 Publication
VAR_016037
Natural varianti119 – 1191L → P in WSN2. 1 Publication
VAR_003836
Natural varianti146 – 1461A → G.
Corresponds to variant rs760134 [ dbSNP | Ensembl ].
VAR_024488
Natural varianti187 – 1871A → V.Combined sources7 Publications
Corresponds to variant rs9891361 [ dbSNP | Ensembl ].
VAR_060724
Natural varianti298 – 2981T → A.7 Publications
Corresponds to variant rs4796697 [ dbSNP | Ensembl ].
VAR_059377

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei62 – 7312Missing in isoform 2. 1 PublicationVSP_016376Add
BLAST
Alternative sequencei351 – 458108ETECR…DVRRP → DPGTHQQHRGPAERAPQ in isoform 2. 1 PublicationVSP_016377Add
BLAST
Alternative sequencei416 – 45843MIGFP…DVRRP → KRQPP in isoform 3. 1 PublicationVSP_038433Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14640 mRNA. Translation: CAA32786.1.
X52426 mRNA. Translation: CAA36673.1.
AF049259 Genomic DNA. Translation: AAC35754.1.
AK092276 mRNA. Translation: BAC03847.1.
AK223051 mRNA. Translation: BAD96771.1.
AK223077 mRNA. Translation: BAD96797.1.
AC019349 Genomic DNA. No translation available.
BC002661 mRNA. Translation: AAH02661.3.
BC077718 mRNA. Translation: AAH77718.2.
CCDSiCCDS11396.1. [P13646-1]
CCDS11397.1. [P13646-3]
PIRiA37343.
S06088. KRHU3.
RefSeqiNP_002265.2. NM_002274.3.
NP_705694.2. NM_153490.2.
UniGeneiHs.654550.

Genome annotation databases

EnsembliENST00000246635; ENSP00000246635; ENSG00000171401. [P13646-1]
ENST00000336861; ENSP00000336604; ENSG00000171401. [P13646-3]
GeneIDi3860.
KEGGihsa:3860.
UCSCiuc002hwu.2. human. [P13646-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database
Wikipedia

Keratin-13 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14640 mRNA. Translation: CAA32786.1.
X52426 mRNA. Translation: CAA36673.1.
AF049259 Genomic DNA. Translation: AAC35754.1.
AK092276 mRNA. Translation: BAC03847.1.
AK223051 mRNA. Translation: BAD96771.1.
AK223077 mRNA. Translation: BAD96797.1.
AC019349 Genomic DNA. No translation available.
BC002661 mRNA. Translation: AAH02661.3.
BC077718 mRNA. Translation: AAH77718.2.
CCDSiCCDS11396.1. [P13646-1]
CCDS11397.1. [P13646-3]
PIRiA37343.
S06088. KRHU3.
RefSeqiNP_002265.2. NM_002274.3.
NP_705694.2. NM_153490.2.
UniGeneiHs.654550.

3D structure databases

ProteinModelPortaliP13646.
SMRiP13646. Positions 155-253, 269-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110058. 57 interactions.
IntActiP13646. 8 interactions.
STRINGi9606.ENSP00000246635.

PTM databases

iPTMnetiP13646.
PhosphoSiteiP13646.
UniCarbKBiP13646.

Polymorphism and mutation databases

BioMutaiKRT13.
DMDMi269849755.

Proteomic databases

EPDiP13646.
MaxQBiP13646.
PaxDbiP13646.
PRIDEiP13646.

Protocols and materials databases

DNASUi3860.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246635; ENSP00000246635; ENSG00000171401. [P13646-1]
ENST00000336861; ENSP00000336604; ENSG00000171401. [P13646-3]
GeneIDi3860.
KEGGihsa:3860.
UCSCiuc002hwu.2. human. [P13646-1]

Organism-specific databases

CTDi3860.
GeneCardsiKRT13.
HGNCiHGNC:6415. KRT13.
HPAiCAB000133.
HPA030877.
MalaCardsiKRT13.
MIMi148065. gene.
615785. phenotype.
neXtProtiNX_P13646.
Orphaneti171723. White sponge nevus.
PharmGKBiPA30202.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP13646.
KOiK07604.
OMAiTCSTRFV.
PhylomeDBiP13646.
TreeFamiTF332742.

Miscellaneous databases

ChiTaRSiKRT13. human.
GeneWikiiKeratin_13.
GenomeRNAii3860.
NextBioi15189.
PROiP13646.
SOURCEiSearch...

Gene expression databases

BgeeiP13646.
CleanExiHS_KRT13.
ExpressionAtlasiP13646. baseline and differential.
GenevisibleiP13646. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a human keratin 13 specific cDNA encompassing coil 1B through the 3' end."
    Schulz P., Wachter E., Hochstrasser K., Wild A.G., Mischke D.
    Biochem. Biophys. Res. Commun. 162:1522-1527(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-187 AND ALA-298.
  2. "The N-, but not the C-terminal domains of human keratins 13 and 15 are closely related."
    Mischke D., Schulz P., Wild A.G.
    Nucleic Acids Res. 17:7984-7984(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, PROTEIN SEQUENCE OF 291-299, VARIANTS VAL-187 AND ALA-298.
  3. "Synthesis of cytokeratin 13, a component characteristic of internal stratified epithelia, is not induced in human epidermal tumors."
    Kuruc N., Leube R.E., Moll I., Bader B.L., Franke W.W.
    Differentiation 42:111-123(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, VARIANTS VAL-187 AND ALA-298.
  4. "Isolation, sequence and expression of the gene encoding human keratin 13."
    Waseem A., Alam Y., Dogan B., White K.N., Leigh I.M., Waseem N.H.
    Gene 215:269-279(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), VARIANTS VAL-187 AND ALA-298.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS VAL-187 AND ALA-298.
    Tissue: Tongue.
  6. 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
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-187 AND ALA-298.
  7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    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.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-187 AND ALA-298.
    Tissue: Brain and Pancreas.
  9. Bienvenut W.V., von Kriegsheim A.F., Kolch W.
    Submitted (OCT-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 124-135; 176-222; 291-318 AND 416-429, PHOSPHORYLATION AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  10. "Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues."
    King I.A., Hounsell E.F.
    J. Biol. Chem. 264:14022-14028(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Keratin 13 point mutation underlies the hereditary mucosal epithelial disorder white sponge nevus."
    Richard G., de Laurenzi V., Didona B., Bale S.J., Compton J.G.
    Nat. Genet. 11:453-455(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WSN2 PRO-119.
  17. "Identification of two novel mutations in keratin 13 as the cause of white sponge naevus."
    Rugg E.L., Magee G., Wilson N., Brandrup F., Hamburger J., Lane E.B.
    Oral Dis. 5:321-324(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS WSN2 THR-108 AND PRO-115.
  18. "A novel mutation in the keratin 13 gene causing oral white sponge nevus."
    Terrinoni A., Rugg E.L., Lane E.B., Melino G., Felix D.H., Munro C.S., McLean W.H.I.
    J. Dent. Res. 80:919-923(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WSN2 SER-112.
  19. "Constitutional mutation of keratin 13 gene in familial white sponge nevus."
    Shibuya Y., Zhang J., Yokoo S., Umeda M., Komori T.
    Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod. 96:561-565(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WSN2 PRO-111.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiK1C13_HUMAN
AccessioniPrimary (citable) accession number: P13646
Secondary accession number(s): Q53G54, Q6AZK5, Q8N240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 24, 2009
Last modified: May 11, 2016
This is version 172 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.