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Protein Page:
K86 (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
K86 Defects in KRT86 are a cause of monilethrix (MLTRX). Monilethrix is an autosomal dominant hair disorder characterized clinically by alopecia and follicular papules. Affected hairs have uniform elliptical nodes of normal thickness and intermittent constrictions, internodes at which the hair easily breaks. Usually only the scalp is involved, but in severe forms, the secondary sexual hair, eyebrows, eyelashes, and nails may also be affected. Belongs to the intermediate filament family. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Motility/polarity/chemotaxis
Cellular Component: extracellular space; keratin filament
Molecular Function: structural molecule activity
Reference #:  O43790 (UniProtKB)
Alt. Names/Synonyms: FLJ25176; Hair keratin K2.11; hard keratin, type II, 6; Hb1; HB6; hHb6; K86; keratin 86; keratin protein HB6; keratin, hair, basic, 6 (monilethrix); Keratin, type II cuticular Hb6; Keratin-86; KRT86; KRTHB1; KRTHB6; MNX; Type II hair keratin Hb6; Type-II keratin Kb26
Gene Symbols: KRT86
Molecular weight: 53,501 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
Select Structure to View Below

K86

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 4 S49-p TGGFGSHsVCGGFRA
0 4 K132-ub RFLEQQNkLLETKLQ
0 1 K193-m2 VLEGYKKkYEEEVSL
0 1 K222-m2 VDCAYLRkSDLEANV
0 27 Y282-p IAEIKAQyDDIVTRS
0 6 K300-ub AESWYRSkCEEMkAT
0 7 K305-ub RSkCEEMkATVIRHG
0 7 K319-ub GETLRRTkEEINELN
0 6 K340-ub TAEVENAkCQNSkLE
0 3 K345-ub NAkCQNSkLEAAVAQ
0 7 K367-ub ALSDARCkLAELEGA
0 1 K377-m2 ELEGALQkAkQDMAC
0 7 K377-ub ELEGALQkAkQDMAC
0 7 K379-ub EGALQkAkQDMACLI
0 1 S455-p VVSTRVSsVPSNsNV
0 1 S460-p VSsVPSNsNVVVGtT
0 1 T466-p NsNVVVGtTNACAPS
  mouse

 
S49-p SGGFGSQsVCGAFRS
K132-ub RFLEQQNkLLETKWQ
R193 SMEGYKKRYEEEVSL
K222 VDCAYLRKSDLEANA
Y282 VAEIKAQYDDIASRS
K300 AESWYRTKCEEIKAT
K305 RTKCEEIKATVIRHG
R319 GETLRRTREEINELN
K340 TAEIENAKCQNTKLE
K345 NAKCQNTKLEAAVTQ
K367 ALADARCKLAELEGA
K377 ELEGALQKAKQDMAC
K377 ELEGALQKAKQDMAC
K379 EGALQKAKQDMACLL
S455 AVNTRVCSAPCSGNV
G460 VCSAPCSGNVVVGTP
T466 SGNVVVGTPNACAPC
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