PTMS_HUMAN - dbPTM
PTMS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTMS_HUMAN
UniProt AC P20962
Protein Name Parathymosin
Gene Name PTMS
Organism Homo sapiens (Human).
Sequence Length 102
Subcellular Localization
Protein Description Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections..
Protein Sequence MSEKSVEAAAELSAKDLKEKKEKVEEKASRKERKKEVVEEEENGAEEEEEETAEDGEEEDEGEEEDEEEEEEDDEGPALKRAAEEEDEADPKRQKTENGASA
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------MSEKSVEAA
------CCHHHHHHH
54.4522814378
2Phosphorylation------MSEKSVEAA
------CCHHHHHHH
54.4529255136
4Acetylation----MSEKSVEAAAE
----CCHHHHHHHHH
53.1219608861
4Ubiquitination----MSEKSVEAAAE
----CCHHHHHHHHH
53.1221890473
5Phosphorylation---MSEKSVEAAAEL
---CCHHHHHHHHHH
22.5729255136
13PhosphorylationVEAAAELSAKDLKEK
HHHHHHHCHHHHHHH
25.4429255136
15AcetylationAAAELSAKDLKEKKE
HHHHHCHHHHHHHHH
61.2819608861
15UbiquitinationAAAELSAKDLKEKKE
HHHHHCHHHHHHHHH
61.2821890473
15SuccinylationAAAELSAKDLKEKKE
HHHHHCHHHHHHHHH
61.2823954790
27AcetylationKKEKVEEKASRKERK
HHHHHHHHHHHHHHH
37.8526051181
29PhosphorylationEKVEEKASRKERKKE
HHHHHHHHHHHHHHH
55.7621601212
52PhosphorylationAEEEEEETAEDGEEE
CHHHHHHHCCCCCCC
38.3330576142
80AcetylationDDEGPALKRAAEEED
CCCCHHHHHHHHHCC
41.9426051181
92AcetylationEEDEADPKRQKTENG
HCCCCCHHHHCCCCC
68.9219608861
92UbiquitinationEEDEADPKRQKTENG
HCCCCCHHHHCCCCC
68.9221906983
96PhosphorylationADPKRQKTENGASA-
CCHHHHCCCCCCCC-
26.7520736484

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 PTMS_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTMS_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 PTMS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCR_HUMANNR3C1physical
16150697
EP300_HUMANEP300physical
16150697
CBP_HUMANCREBBPphysical
16150697
A4_HUMANAPPphysical
21832049
CH60_HUMANHSPD1physical
22863883
CH10_HUMANHSPE1physical
22863883
RBBP7_HUMANRBBP7physical
22863883
TALDO_HUMANTALDO1physical
22863883
WDR1_HUMANWDR1physical
22863883
SDCB2_HUMANSDCBP2physical
25416956

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 PTMS_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-4; LYS-15 AND LYS-92, ANDMASS SPECTROMETRY.

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