CETN3_HUMAN - dbPTM
CETN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CETN3_HUMAN
UniProt AC O15182
Protein Name Centrin-3
Gene Name CETN3
Organism Homo sapiens (Human).
Sequence Length 167
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus, nucleolus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Centrosome of interphase and mitotic cells (PubMed:9256449). Localizes to centri
Protein Description Plays a fundamental role in microtubule-organizing center structure and function.; Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. [PubMed: 22307388 The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery]
Protein Sequence MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI
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
13AcetylationRSELVVDKTKRKKRR
HHHHHHCHHHHHHHH
44.3225953088
18UbiquitinationVDKTKRKKRRELSEE
HCHHHHHHHHHCCHH
61.80-
23PhosphorylationRKKRRELSEEQKQEI
HHHHHHCCHHHHHHH
34.04-
39PhosphorylationDAFELFDTDKDEAID
HHHHHHCCCHHHCCC
37.30-
47PhosphorylationDKDEAIDYHELKVAM
CHHHCCCHHHHHHHH
7.35-
51UbiquitinationAIDYHELKVAMRALG
CCCHHHHHHHHHHCC
25.59-
62UbiquitinationRALGFDVKKADVLKI
HHCCCCCCHHHHHHH
44.05-
68UbiquitinationVKKADVLKILKDYDR
CCHHHHHHHHHCCCC
45.93-
71UbiquitinationADVLKILKDYDREAT
HHHHHHHHCCCCCCC
58.68-
105UbiquitinationDPHEEILKAFKLFDD
CCHHHHHHHHCCCCC
58.39-
108UbiquitinationEEILKAFKLFDDDDS
HHHHHHHCCCCCCCC
53.7721890473
117UbiquitinationFDDDDSGKISLRNLR
CCCCCCCCCCHHHHH
32.8321890473
125DimethylationISLRNLRRVARELGE
CCHHHHHHHHHHHHC
29.61-
134SulfoxidationARELGENMSDEELRA
HHHHHCCCCHHHHHH
4.6821406390
135PhosphorylationRELGENMSDEELRAM
HHHHCCCCHHHHHHH
54.1528985074

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 CETN3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CETN3_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 CETN3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE6D_HUMANPDE6Dphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
U119A_HUMANUNC119physical
16169070
SGSM1_HUMANSGSM1physical
25416956
POC5_HUMANPOC5physical
25416956
TELT_HUMANTCAPphysical
28514442

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CETN3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP