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Protein Page:
K7 (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
K7 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. Phosphorylation of keratins at specific sites affects their organization, assembly dynamics, and their interaction with signaling molecules. Specifically expressed in the simple epithelia lining the cavities of the internal organs and in the gland ducts and blood vessels. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein
Cellular Component: cytoplasm; keratin filament; intermediate filament; nucleus
Molecular Function: protein binding; structural molecule activity
Biological Process: viral reproduction
Reference #:  P08729 (UniProtKB)
Alt. Names/Synonyms: CK-7; CK7; cytokeratin 7; Cytokeratin-7; K2C7; K7; keratin 7; keratin, 55K type II cytoskeletal; keratin, simple epithelial type I, K7; Keratin, type II cytoskeletal 7; Keratin-7; KRT7; MGC129731; MGC3625; Sarcolectin; SCL; type II mesothelial keratin K7; Type-II keratin Kb7
Gene Symbols: KRT7
Molecular weight: 51,386 Da
Basal Isoelectric point: 5.4  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

K7

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 ______MsIHFssPV
0 1 S6-p __MsIHFssPVFTSR
0 2 S7-p _MsIHFssPVFTSRS
0 1 S14 sPVFTSRSAAFSGrG
0 17 R20-m1 RSAAFSGrGAQVrLS
0 5 R20-m2 RSAAFSGrGAQVrLS
0 7 R25-m1 SGrGAQVrLSSARPG
0 16 S36-p ARPGGLGsssLyGLG
0 36 S37-p RPGGLGsssLyGLGA
0 119 S38-p PGGLGsssLyGLGAs
0 596 Y40-p GLGsssLyGLGAsrP
0 4 S45-p sLyGLGAsrPrVAVR
0 1 R46-m1 LyGLGAsrPrVAVRs
0 1 R48-m1 GLGAsrPrVAVRsAy
0 2 S53-p rPrVAVRsAyGGPVG
0 88 Y55-p rVAVRsAyGGPVGAG
0 3 T67-p GAGIREVtINQsLLA
0 1 S71-p REVtINQsLLAPLRL
0 1 S83-p LRLDADPsLQRVRQE
0 5 K96-u QEESEQIktLNNkFA
0 1 T97-p EESEQIktLNNkFAs
1 29 K101-a QIktLNNkFAsFIDk
0 9 K101-u QIktLNNkFAsFIDk
0 17 S104-p tLNNkFAsFIDkVRF
0 6 K108-a kFAsFIDkVRFLEQQ
0 10 K108-u kFAsFIDkVRFLEQQ
0 3 K117-u RFLEQQNkLLETkWT
0 4 K122-u QNkLLETkWTLLQEQ
0 4 K130-u WTLLQEQkSAKSSRL
0 1 K179-a VVEDFKNkYEDEINH
0 1 K199-a NEFVVLKkDVDAAyM
0 4 K199-u NEFVVLKkDVDAAyM
0 125 Y205-p KkDVDAAyMSKVELE
0 2 K214-u SKVELEAkVDALNDE
0 1 A217 ELEAkVDALNDEINF
0 1 T227-p DEINFLRtLNETELt
0 1 T234-p tLNETELtELQsQIS
0 3 S238-p TELtELQsQISDTSV
0 4 S254-p LSMDNSRsLDLDGII
0 2 K265-u DGIIAEVkAQyEEMA
0 2 Y268-p IAEVkAQyEEMAkCS
0 3 K273-u AQyEEMAkCSRAEAE
0 10 Y283-p RAEAEAWyQTkFEtL
0 3 K286-u AEAWyQTkFEtLQAQ
0 1 T289-p WyQTkFEtLQAQAGk
0 2 K296-a tLQAQAGkHGDDLRN
0 2 K296-u tLQAQAGkHGDDLRN
0 5 K326-u QAEIDNIkNQRAKLE
0 10 K348-u ERGELALkDARAKQE
0 2 Y375-p MARQLREyQELMsVK
0 1 S380-p REyQELMsVKLALDI
0 59 K394-u IEIATYRkLLEGEES
0 2 S456-p PGLLKAYsIRtASAS
0 1 T459-p LKAYsIRtASASRRS
  mouse

 
S2 ______MSIHFSSRs
S6 __MSIHFSSRsTAYP
S7 _MSIHFSSRsTAYPG
S9-p SIHFSSRsTAYPGrG
R15-m1 RsTAYPGrGAQVrLS
R15 RsTAYPGRGAQVrLS
R20-m1 PGrGAQVrLSSGRAS
S30 SGRASFGSRsLyGLG
R31 GRASFGSRsLyGLGS
S32-p RASFGSRsLyGLGSs
Y34-p SFGSRsLyGLGSsRP
S39-p sLyGLGSsRPRVAVR
R40 LyGLGSsRPRVAVRs
R42 GLGSsRPRVAVRsAy
S47-p RPRVAVRsAyGGPVG
Y49-p RVAVRsAyGGPVGAG
T61 GAGIREITINQSLLA
S65 REITINQSLLAPLSV
T77 LSVDIDPTIQQVRQE
K90 QEEREQIKTLNNkFA
T91 EEREQIKTLNNkFAs
K95 QIKTLNNKFAsFIDk
K95-u QIKTLNNkFAsFIDk
S98-p TLNNkFAsFIDkVRF
K102 kFAsFIDKVRFLEQQ
K102-u kFAsFIDkVRFLEQQ
K111-u RFLEQQNkMLETKWA
K116 QNkMLETKWALLQEQ
K124 WALLQEQKSAKSSQL
K173 VVEDFKNKYEEEINR
K193 NEFVLLKKDVDAAyT
K193 NEFVLLKKDVDAAyT
Y199-p KKDVDAAyTNKVELE
K208 NKVELEAKADsLQDE
S211-p ELEAKADsLQDEINF
T221 DEINFLKTLHETELA
A228 TLHETELAELQSQIS
S232 TELAELQSQISDTSV
S248-p LSMDNSRsLDLDGII
K259 DGIIADVKAQYEEMA
Y262 IADVKAQYEEMANHS
N267 AQYEEMANHSRAEAE
Y277 RAEAEAWYQTKFETL
K280 AEAWYQTKFETLQAQ
T283 WYQTKFETLQAQAGK
K290 TLQAQAGKHGDDLRN
K290 TLQAQAGKHGDDLRN
K320-u QAEIDTLkNQRAKLE
K342 EQGELAIKDAHAKQG
Y369 VARQLREYQELLNTK
N374 REYQELLNTKLALDI
K388-u IEIATYRkLLEGEES
S444 PGALRAYSIKTTSTT
T447 LRAYSIKTTSTTRRG
  rat

 
S2 ______MSIHFSSRS
S6 __MSIHFSSRSTAYP
S7 _MSIHFSSRSTAYPG
S9 SIHFSSRSTAYPGrG
R15-m1 RSTAYPGrGAQVrLS
R15 RSTAYPGRGAQVrLS
R20-m1 PGrGAQVrLSSGRAG
S30 SGRAGFGSRSLYGLG
R31 GRAGFGSRSLYGLGT
S32 RAGFGSRSLYGLGTS
Y34 GFGSRSLYGLGTSRP
S39 SLYGLGTSRPRVAVR
R40 LYGLGTSRPRVAVRS
R42 GLGTSRPRVAVRSAY
S47 RPRVAVRSAYGGPVG
Y49 RVAVRSAYGGPVGAG
T61 GAGIREITINQNLLA
N65 REITINQNLLAPLSV
T77 LSVDIDPTIQQVRQE
K90 QEEREQIKTLNNKFA
T91 EEREQIKTLNNKFAS
K95 QIKTLNNKFASFIDK
K95 QIKTLNNKFASFIDK
S98 TLNNKFASFIDKVRF
K102 KFASFIDKVRFLEQQ
K102 KFASFIDKVRFLEQQ
K111 RFLEQQNKMLETKWA
K116 QNKMLETKWALLQDQ
K124 WALLQDQKSAKSSQL
K173 VVEDFKNKYEEEINR
K193 NEFVLLKKDVDAAYT
K193 NEFVLLKKDVDAAYT
Y199 KKDVDAAYTNKVELE
K208 NKVELEAKADSLQDK
S211 ELEAKADSLQDKINF
T221 DKINFLKTLHETELA
A228 TLHETELAELQSQIS
S232 TELAELQSQISDTCV
S248 LSMDNSRSLDLDGII
K259 DGIIADVKAQYEEMA
Y262 IADVKAQYEEMANHS
N267 AQYEEMANHSQAEAE
Y277 QAEAEAWYQTKFETL
K280 AEAWYQTKFETLQAQ
T283 WYQTKFETLQAQAGK
K290 TLQAQAGKHGDDLRN
K290 TLQAQAGKHGDDLRN
K320 QAEIDTVKNQRAKLE
K342-u EQGELALkDARAKLA
Y369 LARLLREYQELMNVK
N374 REYQELMNVKLGLDI
K388 IEIATYRKLLEGEES
S444-p PGVLRTYsIKTTSTA
T447 LRTYsIKTTSTARRG
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