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Protein Page:
K13 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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
Chromosomal Location of Human Ortholog: 17q21.2
Cellular Component: intermediate filament cytoskeleton; keratin filament; nucleus
Biological Process: cytoskeleton organization and biogenesis
Disease: White Sponge Nevus 2
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



 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 1 S7‑p _MSLRLQssSAsyGG
0 1 S8‑p MSLRLQssSAsyGGG
0 3 S11‑p RLQssSAsyGGGFGG
0 102 Y12‑p LQssSAsyGGGFGGG
0 6 R27‑m1 SCQLGGGrGVSTCST
0 2 R35‑m1 GVSTCSTrFVSGGSA
0 36 Y118‑p LNDRLASyLEKVRAL
0 1 S147‑p HLKQSPAsPERDysP
0 1 Y152‑p PAsPERDysPyyKTI
0 1 S153‑p AsPERDysPyyKTIE
0 1 Y155‑p PERDysPyyKTIEEL
0 2 Y156‑p ERDysPyyKTIEELR
0 2 T168‑p ELRDKILtAtIENNR
0 1 T170‑p RDKILtAtIENNRVI
0 60 Y194‑p ADDFRLKyENELALR
0 1 Y238‑p SLNEELAyMKKNHEE
0 40 Y281‑p LAEMREQyEAMAERN
0 3 T311‑p NKEVSTNtAMIQtSK
0 1 T316‑p TNtAMIQtSKTEITE
0 3 S337‑p GLEIELQsQLSMKAG
0 1 T404‑p RLEQEIAtyRSLLEG
0 8 Y405‑p LEQEIAtyRSLLEGQ
0 2 M416 LEGQDAKMIGFPssA
0 4 S421‑p AKMIGFPssAGsVsP
0 3 S422‑p KMIGFPssAGsVsPR
0 3 S425‑p GFPssAGsVsPRSTs
0 102 S427‑p PssAGsVsPRSTsVt
0 1 S432‑p sVsPRSTsVtTTSSA
0 1 T434‑p sPRSTsVtTTSSASV
0 1 S440 VtTTSSASVTTTSNA
0 1 T443 TSSASVTTTSNASGR
0 1 S445 SASVTTTSNASGRRt
0 2 T452‑p SNASGRRtsDVRRP_
0 4 S453‑p NASGRRtsDVRRP__
  K13 iso2  
S7 _MSLRLQSSSASYGG
S8 MSLRLQSSSASYGGG
S11 RLQSSSASYGGGFGG
Y12 LQSSSASYGGGFGGG
R27 SCQLGGGRGVSTCST
R35 GVSTCSTRFVSGGSA
Y106 LNDRLASYLEKVRAL
S135 HLKQSPASPERDYSP
Y140 PASPERDYSPYYKTI
S141 ASPERDYSPYYKTIE
Y143 PERDYSPYYKTIEEL
Y144 ERDYSPYYKTIEELR
T156 ELRDKILTATIENNR
T158 RDKILTATIENNRVI
Y182 ADDFRLKYENELALR
Y226 SLNEELAYMKKNHEE
Y269 LAEMREQYEAMAERN
T299 NKEVSTNTAMIQTSK
T304 TNTAMIQTSKTEITE
S325 GLEIELQSQLSMKAG
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  K13 iso3  
S7 _MSLRLQSSSASYGG
S8 MSLRLQSSSASYGGG
S11 RLQSSSASYGGGFGG
Y12 LQSSSASYGGGFGGG
R27‑m1 SCQLGGGrGVSTCST
R35 GVSTCSTRFVSGGSA
Y118 LNDRLASYLEKVRAL
S147 HLKQSPASPERDYSP
Y152 PASPERDYSPYYKTI
S153 ASPERDYSPYYKTIE
Y155 PERDYSPYYKTIEEL
Y156 ERDYSPYYKTIEELR
T168 ELRDKILTATIENNR
T170 RDKILTATIENNRVI
Y194 ADDFRLKYENELALR
Y238 SLNEELAYMKKNHEE
Y281 LAEMREQYEAMAERN
T311 NKEVSTNTAMIQTSK
T316 TNTAMIQTSKTEITE
S337 GLEIELQSQLSMKAG
T404 RLEQEIATYRSLLEG
Y405 LEQEIATYRSLLEGQ
K416‑ac LEGQDAKkRQPP___
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
S7 _MSCRFQSSSMSYGG
S8 MSCRFQSSSMSYGGG
S11 RFQSSSMSYGGGFGA
Y12 FQSSSMSYGGGFGAG
R27 SCQLGGGRNISSCSS
R35 NISSCSSRFVTGGSA
Y110 LNDRLASYLDKVRAL
S139 HLKQSPASPERDYSA
Y144 PASPERDYSAYYKTI
S145 ASPERDYSAYYKTIE
Y147 PERDYSAYYKTIEEL
Y148 ERDYSAYYKTIEELR
E160 ELRIKILEATTDNNR
T162 RIKILEATTDNNRII
Y186 ADDFRLKYENELTLR
Y230 SLNEELAYLKKNHEE
Y273 LAEMREQYEALAEKN
A303 NKEVSSNAEMIQTSK
T308 SNAEMIQTSKTEITE
S329 GLEIELQSQLSMKAG
T396 RLEQEIATYRSLLEG
Y397 LEQEIATYRSLLEGQ
M408 LEGQDAKMTGFNSGG
S413 AKMTGFNSGGNNTTT
- gap
- gap
- gap
- gap
T418 FNSGGNNTTTSNGsP
S424‑p NTTTSNGsPSsNsGR
S427‑p TSNGsPSsNsGRPDF
S429‑p NGsPSsNsGRPDFRK
- gap
- gap
  rat

 
S7 _MSCRFQSSSMSYGG
S8 MSCRFQSSSMSYGGG
S11 RFQSSSMSYGGGFGA
Y12 FQSSSMSYGGGFGAG
R27 SCQLGGGRNISTCSS
R35 NISTCSSRFVTGGSS
Y110 LNDRLASYLEKVRAL
S139 HLKQSPTSPERDYSA
Y144 PTSPERDYSAYYKTI
S145 TSPERDYSAYYKTIE
Y147 PERDYSAYYKTIEEL
Y148 ERDYSAYYKTIEELR
E160 ELRIKILEATTDNNR
T162 RIKILEATTDNNRIV
Y186 ADDFRLKYENELALR
Y230 SLNEELAYLKKNHEE
Y273 LAEMREQYEALAEKN
A303 NKEVSSNAAMIQTSK
T308 SNAAMIQTSKTEITE
S329 GLEIELQSQLSMKAG
T396 RLEQEIATYRSLLEG
Y397 LEQEIATYRSLLEGQ
M408 LEGQDAKMTGFNTGG
T413 AKMTGFNTGGNSTTT
- gap
- gap
- gap
- gap
T418 FNTGGNSTTTSNTST
S424 STTTSNTSTSPSTSG
S428 SNTSTSPSTSGRPDF
S430 TSTSPSTSGRPDFRK
- gap
- gap
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