CYTT_HUMAN - dbPTM
CYTT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYTT_HUMAN
UniProt AC P09228
Protein Name Cystatin-SA
Gene Name CST2
Organism Homo sapiens (Human).
Sequence Length 141
Subcellular Localization Secreted .
Protein Description Thiol protease inhibitor..
Protein Sequence MAWPLCTLLLLLATQAVALAWSPQEEDRIIEGGIYDADLNDERVQRALHFVISEYNKATEDEYYRRLLRVLRAREQIVGGVNYFFDIEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFQIYEVPWEDRMSLVNSRCQEA
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
132PhosphorylationVPWEDRMSLVNSRCQ
CCHHHHHHHHHHHHH
30.021898055
136PhosphorylationDRMSLVNSRCQEA--
HHHHHHHHHHHCC--
27.271898055

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 CYTT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYTT_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 CYTT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PSA3_HUMANPSMA3physical
25416956
ATL4_HUMANADAMTSL4physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956

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

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Related Literatures of Post-Translational Modification

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