KLK5_HUMAN - dbPTM
KLK5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLK5_HUMAN
UniProt AC Q9Y337
Protein Name Kallikrein-5 {ECO:0000312|HGNC:HGNC:6366}
Gene Name KLK5 {ECO:0000312|HGNC:HGNC:6366}
Organism Homo sapiens (Human).
Sequence Length 293
Subcellular Localization Secreted.
Protein Description May be involved in desquamation..
Protein Sequence MATARPPWMWVLCALITALLLGVTEHVLANNDVSCDHPSNTVPSGSNQDLGAGAGEDARSDDSSSRIINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
46PhosphorylationSNTVPSGSNQDLGAG
CCCCCCCCCCCCCCC
35.3424505115
69N-linked_GlycosylationDSSSRIINGSDCDMH
CCCCCEECCCCCCCC
41.36UniProtKB CARBOHYD
173N-linked_GlycosylationTKDVRPINVSSHCPS
CCCCCCCCCCCCCCC
30.24UniProtKB CARBOHYD
188PhosphorylationAGTKCLVSGWGTTKS
CCCEEEEECCCCCCC
18.8420639409
192PhosphorylationCLVSGWGTTKSPQVH
EEEECCCCCCCCCCC
25.2520639409
193PhosphorylationLVSGWGTTKSPQVHF
EEECCCCCCCCCCCH
26.1120639409
195PhosphorylationSGWGTTKSPQVHFPK
ECCCCCCCCCCCHHH
20.6220639409
208N-linked_GlycosylationPKVLQCLNISVLSQK
HHHHHHHCHHHHCCC
31.9217881000
213PhosphorylationCLNISVLSQKRCEDA
HHCHHHHCCCCCCCC
31.34-
252N-linked_GlycosylationSGGPVVCNGSLQGLV
CCCCEEECCCEECEE
31.32UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KLK5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLK5_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KLK5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBB4A_HUMANTUBB4Aphysical
26186194
TBB3_HUMANTUBB3physical
26186194
TBB8_HUMANTUBB8physical
26186194
INT14_HUMANVWA9physical
26186194
FREM2_HUMANFREM2physical
26186194
MET13_HUMANMETTL13physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
ITB5_HUMANITGB5physical
26186194
NEUR3_HUMANNEU3physical
26186194
OS9_HUMANOS9physical
26186194
CBWD1_HUMANCBWD1physical
26186194
FRAS1_HUMANFRAS1physical
26186194
PASK_HUMANPASKphysical
26186194
EME1_HUMANEME1physical
26186194
LOXL2_HUMANLOXL2physical
26186194
DPOE2_HUMANPOLE2physical
26186194
PCDH7_HUMANPCDH7physical
26186194
AP3S1_HUMANAP3S1physical
26186194
NU1M_HUMANND1physical
26186194
LCHN_HUMANKIAA1147physical
26186194
TTC5_HUMANTTC5physical
26186194
PYC_HUMANPCphysical
26186194
CHD1L_HUMANCHD1Lphysical
26186194
BBS7_HUMANBBS7physical
26186194
GT253_HUMANCERCAMphysical
26186194
COX11_HUMANCOX11physical
26186194
CPNE1_HUMANCPNE1physical
26186194
TRM44_HUMANTRMT44physical
26186194
CELR2_HUMANCELSR2physical
26186194
MKS1_HUMANMKS1physical
26186194
MCM8_HUMANMCM8physical
26186194
FUK_HUMANFUKphysical
26186194
FUK_HUMANFUKphysical
28514442
DPOE2_HUMANPOLE2physical
28514442
LOXL2_HUMANLOXL2physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
CBWD1_HUMANCBWD1physical
28514442
LCHN_HUMANKIAA1147physical
28514442
AP3S1_HUMANAP3S1physical
28514442
ITB5_HUMANITGB5physical
28514442
TBB3_HUMANTUBB3physical
28514442
MET13_HUMANMETTL13physical
28514442
MKS1_HUMANMKS1physical
28514442
CPNE1_HUMANCPNE1physical
28514442
EME1_HUMANEME1physical
28514442
FRAS1_HUMANFRAS1physical
28514442
TBA1A_HUMANTUBA1Aphysical
28514442
PCDH7_HUMANPCDH7physical
28514442
LRP6_HUMANLRP6physical
28514442
NU1M_HUMANND1physical
28514442
COX11_HUMANCOX11physical
28514442
ARSA_HUMANARSAphysical
28514442
TBB8_HUMANTUBB8physical
28514442
OS9_HUMANOS9physical
28514442
PASK_HUMANPASKphysical
28514442
MCM8_HUMANMCM8physical
28514442
GT253_HUMANCERCAMphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KLK5_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis of the zinc inhibition of human tissue kallikrein5.";
Debela M., Goettig P., Magdolen V., Huber R., Schechter N.M., Bode W.;
J. Mol. Biol. 373:1017-1031(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 67-293 ALONE AND IN COMPLEXWITH ZINC, ENZYME REGULATION, ACTIVE SITE, GLYCOSYLATION AT ASN-208,AND DISULFIDE BONDS.

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