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Protein Page:
K17 (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
K17 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 K6. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein
Cellular Component: cytoplasm; intermediate filament
Molecular Function: MHC class II receptor activity; protein binding; structural constituent of cytoskeleton; MHC class II protein binding
Biological Process: positive regulation of hair follicle development; epidermis development; positive regulation of translation; keratinization; morphogenesis of an epithelium; intermediate filament organization; signal transduction; positive regulation of cell growth
Reference #:  Q04695 (UniProtKB)
Alt. Names/Synonyms: 39.1; CK-17; Cytokeratin-17; K17; K1C17; keratin 17; Keratin, type I cytoskeletal 17; Keratin-17; KRT17; PC; PC2; PCHC1
Gene Symbols: KRT17
Molecular weight: 48,106 Da
Basal Isoelectric point: 4.97  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

K17

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

 
1 0 T9 TTSIRQFTsSssIkG
0 1 S10-p TSIRQFTsSssIkGs
0 2 S12-p IRQFTsSssIkGssG
0 6 S13-p RQFTsSssIkGssGL
0 2 K15-ub FTsSssIkGssGLGG
0 2 S17-p sSssIkGssGLGGGs
0 2 S18-p SssIkGssGLGGGss
0 3 S24-p ssGLGGGssRtsCRL
0 2 S25-p sGLGGGssRtsCRLs
0 1 T27-p LGGGssRtsCRLsGG
0 1 S28-p GGGssRtsCRLsGGL
0 13 S32-p sRtsCRLsGGLGAGs
0 2 G34 tsCRLsGGLGAGsCR
0 6 S39-p sGGLGAGsCRLGSAG
2 0 S44 AGsCRLGSAGGLGST
0 1 Y69-p SFGSGGGyGSSFGGV
0 77 Y98-p LNDRLASyLDkVRAL
0 6 K101-ub RLASyLDkVRALEEA
0 2 T110-p RALEEANtELEVKIR
0 3 Y134-p PARDYSQyyRTIEEL
0 2 Y135-p ARDYSQyyRTIEELQ
0 1 Q142 yRTIEELQNKILTAT
0 7 K172-ub AADDFRTkFETEQAL
0 2 K269-ub KMAEKNRkDAEDWFF
0 1 S277-p DAEDWFFskTEELNR
0 2 K278-ub AEDWFFskTEELNRE
0 2 T288-p ELNREVAtNSELVQs
0 2 S295-p tNSELVQsGkSEIsE
0 2 K297-ub SELVQsGkSEIsELR
0 2 S301-p QsGkSEIsELRRTMQ
0 1 S319 IELQSQLSMKAsLEG
0 2 S323-p SQLSMKAsLEGNLAE
0 1 K368-ub EQQNQEYkILLDVKT
0 8 Y398-p EDAHLTQykkEPVTT
0 2 K399-ub DAHLTQykkEPVTTR
0 3 K400-ub AHLTQykkEPVTTRQ
0 1 T410-p VTTRQVRtIVEEVQD
0 2 K419-ub VEEVQDGkVISSREQ
3519 : Phospho-Keratin 17 (Ser44) Antibody
  mouse

 
T9-p TTTIRQFtSSssIKG
S10 TTIRQFtSSssIKGS
S12-p IRQFtSSssIKGSSG
S13-p RQFtSSssIKGSSGL
K15 FtSSssIKGSSGLGG
S17 SSssIKGSSGLGGGs
S18 SssIKGSSGLGGGss
S24-p SSGLGGGssRTSCRL
S25-p SGLGGGssRTSCRLs
T27 LGGGssRTSCRLsGs
S28 GGGssRTSCRLsGsL
S32-p sRTSCRLsGsLGAGs
S34-p TSCRLsGsLGAGsCR
S39-p sGsLGAGsCRLGsAS
S44-p AGsCRLGsASGLGSA
Y69 SFGTGSGYGGNFGGV
Y98 LNDRLASYLDKVRAL
K101 RLASYLDKVRALEEA
T110 RALEEANTELEVKIR
Y134 PARDYSAYYHTIEDL
Y135 ARDYSAYYHTIEDLk
K142-ub YHTIEDLkNKILVAT
K172-ub AADDFRTkFETEQAL
K269 KMAEKNRKDAEDWFF
S277 DAEDWFFSKTEELNR
K278 AEDWFFSKTEELNRE
T288 ELNREVATNSELVQS
S295 TNSELVQSGKSEISE
K297 SELVQSGKSEISELR
S301 QSGKSEISELRRTMQ
S319-p IELQSQLsMKASLEG
S323 SQLsMKASLEGSLAE
K368 EQQNQEYKILLDVKT
Y398 EDAHLTQYKPkEPVT
K399 DAHLTQYKPkEPVTT
K401-ub HLTQYKPkEPVTTRQ
T411 VTTRQVRTIVEEVQD
K420 VEEVQDGKVISSREQ
  rat

 
T9 TTTIRQFTSSSSIKG
S10 TTIRQFTSSSSIKGS
S12 IRQFTSSSSIKGSSG
S13 RQFTSSSSIKGSSGL
K15 FTSSSSIKGSSGLGG
S17 SSSSIKGSSGLGGGS
S18 SSSIKGSSGLGGGSS
S24 SSGLGGGSSRTSCRL
S25 SGLGGGSSRTSCRLS
T27 LGGGSSRTSCRLSGS
S28 GGGSSRTSCRLSGSL
S32 SRTSCRLSGSLGAGS
S34 TSCRLSGSLGAGSCR
S39 SGSLGAGSCRLGSAS
S44 AGSCRLGSASGLGSA
Y69 SFGTGSGYGGNFGGV
Y98 LNDRLASYLDKVRAL
K101 RLASYLDKVRALEEA
T110 RALEEANTELEVKIR
Y134 PARDYSAYYQTIEDL
Y135 ARDYSAYYQTIEDLK
K142 YQTIEDLKNKILVAT
K172 AADDFRTKFETEQAL
K269 KMAEKNRKDAEDWFF
S277 DAEDWFFSKTEELNR
K278 AEDWFFSKTEELNRE
T288-p ELNREVAtNSELVQs
S295-p tNSELVQsGKSEIsE
K297 SELVQsGKSEIsELR
S301-p QsGKSEIsELRRTMQ
S319 IELQSQLSMKASLEG
S323 SQLSMKASLEGSLAE
K368 EQQNQEYKILLDVKT
Y398 EDAHLTQYKPKEPVT
K399 DAHLTQYKPKEPVTT
K401 HLTQYKPKEPVTTRQ
T411 VTTRQVRTIVEEVQD
K420 VEEVQDGKVISSREQ
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