TTC38_HUMAN - dbPTM
TTC38_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTC38_HUMAN
UniProt AC Q5R3I4
Protein Name Tetratricopeptide repeat protein 38
Gene Name TTC38
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization
Protein Description
Protein Sequence MAAASPLRDCQAWKDARLPLSTTSNEACKLFDATLTQYVKWTNDKSLGGIEGCLSKLKAADPTFVMGHAMATGLVLIGTGSSVKLDKELDLAVKTMVEISRTQPLTRREQLHVSAVETFANGNFPKACELWEQILQDHPTDMLALKFSHDAYFYLGYQEQMRDSVARIYPFWTPDIPLSSYVKGIYSFGLMETNFYDQAEKLAKEALSINPTDAWSVHTVAHIHEMKAEIKDGLEFMQHSETFWKDSDMLACHNYWHWALYLIEKGEYEAALTIYDTHILPSLQANDAMLDVVDSCSMLYRLQMEGVSVGQRWQDVLPVARKHSRDHILLFNDAHFLMASLGAHDPQTTQELLTTLRDASESPGENCQHLLARDVGLPLCQALVEAEDGNPDRVLELLLPIRYRIVQLGGSNAQRDVFNQLLIHAALNCTSSVHKNVARSLLMERDALKPNSPLTERLIRKAATVHLMQ
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
2Acetylation------MAAASPLRD
------CCCCCCCCC
16.2520068231
5Phosphorylation---MAAASPLRDCQA
---CCCCCCCCCCHH
21.5323401153
14UbiquitinationLRDCQAWKDARLPLS
CCCCHHHCCCCCCCC
44.5229967540
29UbiquitinationTTSNEACKLFDATLT
CCCHHHHHHHHCHHH
60.2721963094
40UbiquitinationATLTQYVKWTNDKSL
CHHHHHEECCCCCCC
43.2821963094
45UbiquitinationYVKWTNDKSLGGIEG
HEECCCCCCCCCHHH
50.0421963094
56UbiquitinationGIEGCLSKLKAADPT
CHHHHHHHHHHCCCC
40.8521963094
58UbiquitinationEGCLSKLKAADPTFV
HHHHHHHHHCCCCCH
45.3122817900
63PhosphorylationKLKAADPTFVMGHAM
HHHHCCCCCHHCCCC
29.4322210691
87UbiquitinationGSSVKLDKELDLAVK
CCCCCCHHHHHHHHH
71.2929967540
136UbiquitinationELWEQILQDHPTDML
HHHHHHHHHCCCCEE
48.9021963094
139UbiquitinationEQILQDHPTDMLALK
HHHHHHCCCCEEEHH
38.0822817900
201UbiquitinationNFYDQAEKLAKEALS
CCHHHHHHHHHHHHC
57.6821963094
204UbiquitinationDQAEKLAKEALSINP
HHHHHHHHHHHCCCC
54.6922817900
208PhosphorylationKLAKEALSINPTDAW
HHHHHHHCCCCCCCC
27.63-
227UbiquitinationVAHIHEMKAEIKDGL
HHHHHHHHHHHHHHH
39.6229967540
362PhosphorylationTLRDASESPGENCQH
HHHHHHCCCCCCHHH
35.3929214152
384UbiquitinationLPLCQALVEAEDGNP
HHHHHHHHHCCCCCH
8.0022817900
449UbiquitinationLMERDALKPNSPLTE
HHHCCCCCCCCHHHH
43.8221906983
452PhosphorylationRDALKPNSPLTERLI
CCCCCCCCHHHHHHH
29.7925159151

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 TTC38_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTC38_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 TTC38_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR4_HUMANPFASphysical
26344197

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 TTC38_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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