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Protein Page:
K6a (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
K6a a type II 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. Associates with K16 and/or -17. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein
Cellular Component: membrane; keratin filament; nucleus
Molecular Function: protein binding; structural constituent of cytoskeleton
Biological Process: positive regulation of cell proliferation; cell differentiation
Reference #:  P02538 (UniProtKB)
Alt. Names/Synonyms: 56 cytoskeletal type II keratin; CK-6A; CK-6D; CK6A; CK6C; CK6D; cytokeratin 6A; cytokeratin 6C; cytokeratin 6D; Cytokeratin-6A; Cytokeratin-6D; K2C6A; K6A; K6C; K6D; K6D keratin; keratin 6A; keratin 6C; keratin, epidermal type II, K6A; keratin, epidermal type II, K6C; Keratin, type II cytoskeletal 6A; keratin, type II cytoskeletal 6D; Keratin-6A; KRT6A; KRT6C; KRT6D; type II keratin isoform K6c; Type-II keratin Kb6
Gene Symbols: KRT6A
Molecular weight: 60,045 Da
Basal Isoelectric point: 8.09  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

K6a

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 S10 STSTTIRSHSSSRRG
0 3 R16 RSHSSSRRGFsANSA
0 2 S19-p SSSRRGFsANSARLP
0 1 R24 GFsANSARLPGVSRS
0 1 S31 RLPGVSRSGFsSVsV
0 1 S34-p GVSRSGFsSVsVSRS
0 9 S37-p RSGFsSVsVSRSrGS
0 4 R40 FsSVsVSRSrGSGGL
0 2 R42-m1 SVsVSRSrGSGGLGG
0 1 S44 sVSRSrGSGGLGGAC
0 2 G48 SrGSGGLGGACGGAG
0 4 R59 GGAGFGSRsLyGLGG
0 40 S60-p GAGFGSRsLyGLGGS
0 188 Y62-p GFGSRsLyGLGGSKR
0 13 S71-p LGGSKRIsIGGGsCA
0 3 S76-p RIsIGGGsCAISGGy
0 142 Y83-p sCAISGGyGSRAGGS
0 3 K168-ub AEEREQIkTLNNkFA
0 30 K173-ac QIkTLNNkFAsFIDk
0 9 K173-ub QIkTLNNkFAsFIDk
0 19 S176-p TLNNkFAsFIDkVRF
0 6 K180-ac kFAsFIDkVRFLEQQ
0 10 K180-ub kFAsFIDkVRFLEQQ
0 1 K189 RFLEQQNKVLETKWT
0 1 K194 QNKVLETKWTLLQEQ
0 23 S237-p GERGRLDsELRGMQD
0 1 T269 AAENEFVTLKKDVDA
0 54 Y278-p KKDVDAAyMNKVELQ
0 1 N327 LSMDNNRNLDLDSII
0 92 Y341-p IAEVKAQyEEIAQRS
0 9 Y356-p RAEAESWyQTKyEEL
0 42 Y360-p ESWyQTKyEELQVTA
0 2 K426-ac ALKDAKNkLEGLEDA
0 1 K446 QDLARLLKEYQELMN
0 11 K467 VEIATYRKLLEGEEC
0 4 Y551-p GGSSTIKyTTTSSSS
  mouse

 
S9-p STKTTIKsQTSHRGY
R14 IKsQTSHRGYsASSA
S17-p QTSHRGYsASSARVP
R22 GYsASSARVPGLNRs
S29-p RVPGLNRsGFSSVsV
S32 GLNRsGFSSVsVCRS
S35-p RsGFSSVsVCRSrGs
R38 FSSVsVCRSrGsGGS
R40-m1 SVsVCRSrGsGGSSA
S42-p sVCRSrGsGGSSAMC
S46 SrGsGGSSAMCGGAG
R57 GGAGFGSRsLYGVGS
S58-p GAGFGSRsLYGVGSS
Y60 GFGSRsLYGVGSSKR
S69-p VGSSKRIsIGGGsCG
S74-p RIsIGGGsCGIGGGY
Y81 sCGIGGGYGSRFGGS
K157 TEEREQIKTLNNkFA
K162 QIKTLNNKFAsFIDk
K162-ub QIKTLNNkFAsFIDk
S165-p TLNNkFAsFIDkVRF
K169 kFAsFIDKVRFLEQQ
K169-ub kFAsFIDkVRFLEQQ
K178-ub RFLEQQNkVLDTkWA
K183-ub QNkVLDTkWALLQEQ
S226-p GERGRLDsELRNMQD
T258-p AAENEFVtLKKDVDA
Y267 KKDVDAAYMNKVELQ
S316-p LSMDNNRsLDLDSII
Y330 IAEVKAQYEDIAQRS
Y345 RAEAESWYQTKYEEL
Y349 ESWYQTKYEELQVTA
K415-ac ALKDARGkLEGLEDA
K435-ac QDMARLLkEYQELMN
K456-ub VEIATYRkLLEGEEC
Y541 LSSSTIKYTTTSSSK
  rat

 
S9 STKTVIRSQTSHrGF
R14-m1 IRSQTSHrGFSAGSA
S17 QTSHrGFSAGSArLP
R22-m1 GFSAGSArLPGLNRS
S29 rLPGLNRSGFSSVSV
S32 GLNRSGFSSVSVCrS
S35 RSGFSSVSVCrSrGS
R38-m1 FSSVSVCrSrGSGGS
R40-m1 SVSVCrSrGSGGSrA
S42 SVCrSrGSGGSrAVC
R46-m1 SrGSGGSrAVCGGAG
R57-m1 GGAGFGSrSLCGVGS
S58 GAGFGSrSLCGVGSS
C60 GFGSrSLCGVGSSQR
S69 VGSSQRISIGGGSCG
S74 RISIGGGSCGIGGGY
Y81 SCGIGGGYGGRFGGS
K157 TEEREQIKTLNNKFA
K162 QIKTLNNKFASFIDK
K162 QIKTLNNKFASFIDK
S165 TLNNKFASFIDKVRF
K169 KFASFIDKVRFLEQQ
K169 KFASFIDKVRFLEQQ
K178 RFLEQQNKVLDTKWA
K183 QNKVLDTKWALLQEQ
S226 GQRGRLDSELRNMQG
T258 AAENEFVTLKKDVDA
Y267 KKDVDAAYMNKVELQ
S316 LSMDNNRSLDLDSII
Y330 IAEVKAQYEEIAKRS
Y345 RAEAESWYQTKYEEL
Y349 ESWYQTKYEELQITA
K415 ALKDARGKLEGLEDA
K435 QDMARLLKEYQDLMN
T456 VEIATYRTLLEGEEC
Y540 GSSSTIKYTTTSSTR
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