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Protein Page:
K10 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
K10 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 K1. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein
Cellular Component: keratin filament; cytoplasm; intermediate filament
Molecular Function: structural constituent of epidermis; structural molecule activity
Biological Process: keratinocyte differentiation; epidermis development
Reference #:  P13645 (UniProtKB)
Alt. Names/Synonyms: CK-10; CK10; cytokeratin 10; Cytokeratin-10; K10; K1C10; keratin 10; Keratin, type I cytoskeletal 10; Keratin-10; KPP; KRT10
Gene Symbols: KRT10
Molecular weight: 58,827 Da
Basal Isoelectric point: 5.13  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

K10

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

 
0 1 S2-p ______MsVRYSSSK
0 1 K9 sVRYSSSKHySSSRs
0 1 Y11-p RYSSSKHySSSRsGG
0 3 S16-p KHySSSRsGGGGGGG
0 3 S42-p RISSSKGsLGGGFSS
0 1 S53 GFSSGGFSGGSFSRG
0 2 S56 SGGFSGGSFSRGSSG
0 4 S159-p NLNDRLAsyLDkVRA
0 77 Y160-p LNDRLAsyLDkVRAL
0 6 K163-u RLAsyLDkVRALEES
0 5 Y172-p RALEESNyELEGKIK
0 2 Y199-p EPRDYSKyyKTIDDL
0 1 Y200-p PRDYSKyyKTIDDLK
0 8 Y238-p ADDFRLKyENEVALR
0 1 T265 VLDELTLTKADLEMQ
0 1 T277-p EMQIESLtEELAyLK
0 1 Y282-p SLtEELAyLKKNHEE
0 3 Y325-p LNNMRSQyEQLAEQN
0 1 N353 ELTTEIDNNIEQISS
0 1 S459 LLEGEGSSGGGGRGG
0 1 S535-p GGYGGGSsGGGGGGY
0 1 S546-p GGGYGGGsSGGGSSS
0 1 Y557-p GSSSGGGyGGGSSSG
0 1 S568-p SSSGGHKssSsGsVG
0 1 S569-p SSGGHKssSsGsVGE
0 1 S571-p GGHKssSsGsVGEss
0 2 S573-p HKssSsGsVGEsssK
0 1 S577-p SsGsVGEsssKGPRy
0 1 S578-p sGsVGEsssKGPRy_
0 2 S579-p GsVGEsssKGPRy__
0 3 Y584-p sssKGPRy_______
  mouse

 
S2 ______MSVLYSSSS
K10-a VLYSSSSkQFSSSRS
F12 YSSSSkQFSSSRSGG
S17 kQFSSSRSGGGGGGG
S34-p RVSSTRGsLGGGYSS
S45-p GYSSGGFsGGsFSRG
S48-p SGGFsGGsFSRGSSG
S157-p NLNDRLAsYMDKVRA
Y158 LNDRLAsYMDKVRAL
K161 RLAsYMDKVRALEES
Y170 RALEESNYELEGKIK
Y197 EPRDYSKYYKTIEDL
Y198 PRDYSKYYKTIEDLK
Y236 ADDFRLKYENEVTLR
S263-p VLDELTLsKSDLEMQ
N275 EMQIESLNEELAYLK
Y280 SLNEELAYLKKNHEE
Y323 LNNMRNQYEQLAEKN
S351-p ELTTEIDsNIEQMSS
S457-p LLEGEGSsSGGGGGR
S525 GGYGGGSSSGGAGGH
S535 GAGGHGGSSGGGYGG
Y540 GGSSGGGYGGGSSSG
G551 SSSGGQGGSGGFKSS
S552 SSGGQGGSGGFKSSG
- gap
- gap
Q563 KSSGGGDQSSKGPRY
S564 SSGGGDQSSKGPRY_
S565 SGGGDQSSKGPRY__
Y570 QSSKGPRY_______
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