TT39C_HUMAN - dbPTM
TT39C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TT39C_HUMAN
UniProt AC Q8N584
Protein Name Tetratricopeptide repeat protein 39C
Gene Name TTC39C
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization
Protein Description
Protein Sequence MAGSEQQRPRRRDDGDSDAAAAAAAPLQDAELALAGINMLLNNGFRESDQLFKQYRNHSPLMSFGASFVSFLNAMMTFEEEKMQLACDDLKTTEKLCESEEAGVIETIKNKIKKNVDVRKSAPSMVDRLQRQIIIADCQVYLAVLSFVKQELSAYIKGGWILRKAWKIYNKCYLDINALQELYQKKLTEESLTSDAANDNHIVAEGVSEESLNRLKGAVSFGYGLFHLCISMVPPNLLKIINLLGFPGDRLQGLSSLMYASESKDMKAPLATLALLWYHTVVRPFFALDGSDNKAGLDEAKEILLKKEAAYPNSSLFMFFKGRIQRLECQINSALTSFHTALELAVDQREIQHVCLYEIGWCSMIELNFKDAFDSFERLKNESRWSQCYYAYLTAVCQGATGDVDGAQIVFKEVQKLFKRKNNQIEQFSVKKAERFRKQTPTKALCVLASIEVLYLWKALPNCSFPNLQRMSQACHEVDDSSVVGLKYLLLGAIHKCLGNSEDAVQYFQRAVKDELCRQNNLYVQPYACYELGCLLLDKPETVGRGRALLLQAKEDFSGYDFENRLHVRIHAALASLRELVPQ
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
2 (in isoform 2)Phosphorylation-30.1629507054
6 (in isoform 2)Phosphorylation-46.4029507054
53UbiquitinationRESDQLFKQYRNHSP
HHHHHHHHHHHCCCC
55.82-
77PhosphorylationSFLNAMMTFEEEKMQ
HHHHHHHCCCHHHHH
18.1429507054
91AcetylationQLACDDLKTTEKLCE
HHHHCHHHHHHHHHH
61.4726051181
109UbiquitinationAGVIETIKNKIKKNV
CCHHHHHHHHHHHCC
60.66-
167UbiquitinationWILRKAWKIYNKCYL
HHHHHHHHHHHHHHC
39.92-
185UbiquitinationALQELYQKKLTEESL
HHHHHHHHHCCHHHC
35.87-
186UbiquitinationLQELYQKKLTEESLT
HHHHHHHHCCHHHCC
45.15-
188PhosphorylationELYQKKLTEESLTSD
HHHHHHCCHHHCCCC
46.7328555341
193PhosphorylationKLTEESLTSDAANDN
HCCHHHCCCCCCCCC
33.5628555341
301UbiquitinationKAGLDEAKEILLKKE
CCCHHHHHHHHHHHH
43.15-
355AcetylationQREIQHVCLYEIGWC
HHHHCCEEHHHCCCC
2.9219608861
358AcetylationIQHVCLYEIGWCSMI
HCCEEHHHCCCCCEE
23.2919608861
416AcetylationIVFKEVQKLFKRKNN
HHHHHHHHHHHHCCC
62.1519608861
419AcetylationKEVQKLFKRKNNQIE
HHHHHHHHHCCCCCC
73.2719608861
431UbiquitinationQIEQFSVKKAERFRK
CCCCHHHHHHHHHHC
45.10-
487AcetylationDSSVVGLKYLLLGAI
HHHHHHHHHHHHHHH
28.117409433
513UbiquitinationQYFQRAVKDELCRQN
HHHHHHHHHHHHHCC
44.49-
513AcetylationQYFQRAVKDELCRQN
HHHHHHHHHHHHHCC
44.4927452117
576PhosphorylationRIHAALASLRELVPQ
HHHHHHHHHHHHCCC
28.8924719451

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 TT39C_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TT39C_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 TT39C_HUMAN !!

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

Oops, there are no PPI records of TT39C_HUMAN !!

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 TT39C_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-416, AND MASS SPECTROMETRY.

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