CA122_HUMAN - dbPTM
CA122_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CA122_HUMAN
UniProt AC Q6ZSJ8
Protein Name Uncharacterized protein C1orf122
Gene Name C1orf122
Organism Homo sapiens (Human).
Sequence Length 110
Subcellular Localization
Protein Description
Protein Sequence MEWGPGSDWSRGEAAGVDRGKAGLGLGGRPPPQPPREERAQQLLDAVEQRQRQLLDTIAACEEMLRQLGRRRPEPAGGGNVSAKPGAPPQPAVSARGGFPKDAGDGAAEP
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
82PhosphorylationPAGGGNVSAKPGAPP
CCCCCCCCCCCCCCC
34.2820068231
94PhosphorylationAPPQPAVSARGGFPK
CCCCCCCCCCCCCCC
17.8524719451

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 CA122_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CA122_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 CA122_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNX2_HUMANSNX2physical
21988832

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 CA122_HUMAN

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Related Literatures of Post-Translational Modification

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