NAA35_HUMAN - dbPTM
NAA35_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAA35_HUMAN
UniProt AC Q5VZE5
Protein Name N-alpha-acetyltransferase 35, NatC auxiliary subunit
Gene Name NAA35
Organism Homo sapiens (Human).
Sequence Length 725
Subcellular Localization Cytoplasm .
Protein Description Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Involved in regulation of apoptosis and proliferation of smooth muscle cells..
Protein Sequence MVMKASVDDDDSGWELSMPEKMEKSNTNWVDITQDFEEACRELKLGELLHDKLFGLFEAMSAIEMMDPKMDAGMIGNQVNRKVLNFEQAIKDGTIKIKDLTLPELIGIMDTCFCCLITWLEGHSLAQTVFTCLYIHNPDFIEDPAMKAFALGILKICDIAREKVNKAAVFEEEDFQSMTYGFKMANSVTDLRVTGMLKDVEDDMQRRVKSTRSRQGEERDPEVELEHQQCLAVFSRVKFTRVLLTVLIAFTKKETSAVAEAQKLMVQAADLLSAIHNSLHHGIQAQNDTTKGDHPIMMGFEPLVNQRLLPPTFPRYAKIIKREEMVNYFARLIDRIKTVCEVVNLTNLHCILDFFCEFSEQSPCVLSRSLLQTTFLVDNKKVFGTHLMQDMVKDALRSFVSPPVLSPKCYLYNNHQAKDCIDSFVTHCVRPFCSLIQIHGHNRARQRDKLGHILEEFATLQDEAEKVDAALHTMLLKQEPQRQHLACLGTWVLYHNLRIMIQYLLSGFELELYSMHEYYYIYWYLSEFLYAWLMSTLSRADGSQMAEERIMEEQQKGRSSKKTKKKKKVRPLSREITMSQAYQNMCAGMFKTMVAFDMDGKVRKPKFELDSEQVRYEHRFAPFNSVMTPPPVHYLQFKEMSDLNKYSPPPQSPELYVAASKHFQQAKMILENIPNPDHEVNRILKVAKPNFVVMKLLAGGHKKESKVPPEFDFSAHKYFPVVKLV
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
6Phosphorylation--MVMKASVDDDDSG
--CCCCCCCCCCCCC
22.1425159151
12PhosphorylationASVDDDDSGWELSMP
CCCCCCCCCCEECCC
53.4523403867
17PhosphorylationDDSGWELSMPEKMEK
CCCCCEECCCHHHCC
22.3023403867
21UbiquitinationWELSMPEKMEKSNTN
CEECCCHHHCCCCCC
46.63-
44AcetylationEEACRELKLGELLHD
HHHHHHCCHHHHHHH
50.0923236377
44UbiquitinationEEACRELKLGELLHD
HHHHHHCCHHHHHHH
50.09-
91UbiquitinationLNFEQAIKDGTIKIK
CCHHHHHCCCCEEEE
53.79-
184SulfoxidationSMTYGFKMANSVTDL
HHHHHHHHCCCCCCC
3.8921406390
187PhosphorylationYGFKMANSVTDLRVT
HHHHHCCCCCCCCCC
19.4914702039
189PhosphorylationFKMANSVTDLRVTGM
HHHCCCCCCCCCCCC
29.1823186163
210O-linked_GlycosylationDMQRRVKSTRSRQGE
HHHHHHHHHHHCCCC
26.6230379171
213O-linked_GlycosylationRRVKSTRSRQGEERD
HHHHHHHHCCCCCCC
29.1030379171
240PhosphorylationVFSRVKFTRVLLTVL
HHHHHHHHHHHHHHH
17.72-
255PhosphorylationIAFTKKETSAVAEAQ
HHHHCHHCHHHHHHH
30.76-
256PhosphorylationAFTKKETSAVAEAQK
HHHCHHCHHHHHHHH
23.10-
380UbiquitinationTTFLVDNKKVFGTHL
EEEEECCCEECCHHH
45.94-
381UbiquitinationTFLVDNKKVFGTHLM
EEEECCCEECCHHHH
49.39-
393UbiquitinationHLMQDMVKDALRSFV
HHHHHHHHHHHHHCC
30.55-
408UbiquitinationSPPVLSPKCYLYNNH
CCCCCCCCEEEECCC
31.94-
638UbiquitinationPVHYLQFKEMSDLNK
CCEEEEEECHHHHCC
39.28-
647PhosphorylationMSDLNKYSPPPQSPE
HHHHCCCCCCCCCHH
32.3225159151
652PhosphorylationKYSPPPQSPELYVAA
CCCCCCCCHHHHHHH
26.5628985074
661UbiquitinationELYVAASKHFQQAKM
HHHHHHHHHHHHHHH
43.65-
706UbiquitinationGGHKKESKVPPEFDF
CCCCCCCCCCCCCCC
60.91-

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 NAA35_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAA35_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 NAA35_HUMAN !!

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

Oops, there are no PPI records of NAA35_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAA35_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP