GTPBA_HUMAN - dbPTM
GTPBA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GTPBA_HUMAN
UniProt AC A4D1E9
Protein Name GTP-binding protein 10
Gene Name GTPBP10
Organism Homo sapiens (Human).
Sequence Length 387
Subcellular Localization Nucleus, nucleolus . Chromosome . Found in the dense fibrillar compartment region of the nucleolus. At the onset of mitosis moves to the chromosome surface and remains there until anaphase. Gradually re-assembles into the nucleolus at late anaphase t
Protein Description May be involved in the ribosome maturation process. Complements an ObgE(CgtA) function in E.coli ribosome maturation. Plays a role of GTPase in vitro. When missing, disorganization of the nucleolar architecture is observed..
Protein Sequence MVHCSCVLFRKYGNFIDKLRLFTRGGSGGMGYPRLGGEGGKGGDVWVVAQNRMTLKQLKDRYPRKRFVAGVGANSKISALKGSKGKDCEIPVPVGISVTDENGKIIGELNKENDRILVAQGGLGGKLLTNFLPLKGQKRIIHLDLKLIADVGLVGFPNAGKSSLLSCVSHAKPAIADYAFTTLKPELGKIMYSDFKQISVADLPGLIEGAHMNKGMGHKFLKHIERTRQLLFVVDISGFQLSSHTQYRTAFETIILLTKELELYKEELQTKPALLAVNKMDLPDAQDKFHELMSQLQNPKDFLHLFEKNMIPERTVEFQHIIPISAVTGEGIEELKNCIRKSLDEQANQENDALHKKQLLNLWISDTMSSTEPPSKHAVTTSKMDII
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
12PhosphorylationSCVLFRKYGNFIDKL
EEEEEEHHCCHHHHE
17.0320068231
27PhosphorylationRLFTRGGSGGMGYPR
EECCCCCCCCCCCCC
34.6920363803
32PhosphorylationGGSGGMGYPRLGGEG
CCCCCCCCCCCCCCC
4.0120363803
75PhosphorylationVAGVGANSKISALKG
EEECCCCHHHHHHCC
30.7220068231
78PhosphorylationVGANSKISALKGSKG
CCCCHHHHHHCCCCC
31.1420068231
81UbiquitinationNSKISALKGSKGKDC
CHHHHHHCCCCCCCC
61.9429967540
111UbiquitinationKIIGELNKENDRILV
CEEEEECCCCCEEEE
71.2029967540
184SuccinylationDYAFTTLKPELGKIM
HHHHHCCCHHHHHHC
34.0623954790
184AcetylationDYAFTTLKPELGKIM
HHHHHCCCHHHHHHC
34.0623236377
229 (in isoform 2)Ubiquitination-41.7421906983
229UbiquitinationKHIERTRQLLFVVDI
HHHHHHHEEEEEEEC
41.7422817900
270PhosphorylationLYKEELQTKPALLAV
HHHHHHCCCCEEEHH
52.17-
308 (in isoform 1)Ubiquitination-44.4721906983
308UbiquitinationDFLHLFEKNMIPERT
HHHHHHHHHCCCCCE
44.4722817900
365PhosphorylationQLLNLWISDTMSSTE
HHHHHHHCCCCCCCC
18.5629052541
367PhosphorylationLNLWISDTMSSTEPP
HHHHHCCCCCCCCCC
16.5029052541
369PhosphorylationLWISDTMSSTEPPSK
HHHCCCCCCCCCCCC
35.8829052541
370PhosphorylationWISDTMSSTEPPSKH
HHCCCCCCCCCCCCC
26.4329052541
371PhosphorylationISDTMSSTEPPSKHA
HCCCCCCCCCCCCCC
45.2529052541
375PhosphorylationMSSTEPPSKHAVTTS
CCCCCCCCCCCCCCC
48.0329052541

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 GTPBA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GTPBA_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 GTPBA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCBP4_HUMANPCBP4physical
26186194
PCBP4_HUMANPCBP4physical
28514442

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 GTPBA_HUMAN

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Related Literatures of Post-Translational Modification

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