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Protein Page:
K13 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
K13 a type I cytoskeletal keratin. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. There are two types of cytoskeletal and microfibrillar keratin: type I (acidic; 40-55 kDa) [K9 to K20] and type II (neutral to basic; 56-70 kDa) [K1 to K8]. Both a basic and an acidic keratin are required for filament assembly. Generally associates with K4 Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein
Cellular Component: intermediate filament cytoskeleton; keratin filament
Molecular Function: structural molecule activity
Biological Process: response to radiation; tongue morphogenesis
Reference #:  P13646 (UniProtKB)
Alt. Names/Synonyms: CK-13; CK13; cytokeratin 13; Cytokeratin-13; K13; K1C13; keratin 13; Keratin, type I cytoskeletal 13; Keratin-13; KRT13; MGC161462; MGC3781
Gene Symbols: KRT13
Molecular weight: 49,588 Da
Basal Isoelectric point: 4.91  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

K13

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 3 S11-p RLQSSSAsyGGGFGG
0 102 Y12-p LQSSSAsyGGGFGGG
0 6 R27-m1 SCQLGGGrGVSTCST
0 2 R35-m1 GVSTCSTrFVSGGSA
0 61 Y194-p ADDFRLKyENELALR
0 39 Y281-p LAEMREQyEAMAERN
0 2 T311-p NKEVSTNtAMIQTSK
0 2 S337-p GLEIELQsQLSMKAG
0 2 M416 LEGQDAKMIGFPssA
0 4 S421-p AKMIGFPssAGSVsP
0 2 S422-p KMIGFPssAGSVsPR
0 97 S427-p PssAGSVsPRSTSVT
0 1 S440 VTTTSSASVTTTSNA
0 1 T443 TSSASVTTTSNASGR
0 1 S445 SASVTTTSNASGRRt
0 2 T452-p SNASGRRtsDVRRP_
0 4 S453-p NASGRRtsDVRRP__
  K13 iso3  
S11 RLQSSSASYGGGFGG
Y12 LQSSSASYGGGFGGG
R27-m1 SCQLGGGrGVSTCST
R35 GVSTCSTRFVSGGSA
Y194 ADDFRLKYENELALR
Y281 LAEMREQYEAMAERN
T311 NKEVSTNTAMIQTSK
S337 GLEIELQSQLSMKAG
K416-a LEGQDAKkRQPP___
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
S11 RFQSSSMSYGGGFGA
Y12 FQSSSMSYGGGFGAG
R27 SCQLGGGRNISSCSS
R35 NISSCSSRFVTGGSA
Y186 ADDFRLKYENELTLR
Y273 LAEMREQYEALAEKN
A303 NKEVSSNAEMIQTSK
S329 GLEIELQSQLSMKAG
M408 LEGQDAKMTGFNSGG
S413 AKMTGFNSGGNNTTT
- gap
- gap
S424-p NTTTSNGsPSsNsGR
S427-p TSNGsPSsNsGRPDF
S429-p NGsPSsNsGRPDFRK
- gap
- gap
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