PGTA_HUMAN - dbPTM
PGTA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGTA_HUMAN
UniProt AC Q92696
Protein Name Geranylgeranyl transferase type-2 subunit alpha
Gene Name RABGGTA
Organism Homo sapiens (Human).
Sequence Length 567
Subcellular Localization
Protein Description Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A..
Protein Sequence MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVPPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPEDVLLKELELVQNAFFTDPNDQSAWFYHRWLLGRADPQDALRCLHVSRDEACLTVSFSRPLLVGSRMEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTAGDVQKECVLLKGRQEGWCRDSTTDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFQTLKAVDPMRATYLDDLRSKFLLENSVLKMEYAEVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLQQPAVLQPLASCPRLVLLNLQGNPLCQAVGILEQLAELLPSVSSVLT
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
8UbiquitinationMHGRLKVKTSEEQAE
CCCCCCCCCHHHHHH
44.75-
9PhosphorylationHGRLKVKTSEEQAEA
CCCCCCCCHHHHHHH
44.3429514088
10PhosphorylationGRLKVKTSEEQAEAK
CCCCCCCHHHHHHHH
33.1629514088
17UbiquitinationSEEQAEAKRLEREQK
HHHHHHHHHHHHHHH
49.3624816145
30PhosphorylationQKLKLYQSATQAVFQ
HHHHHHHHHHHHHHH
21.5228857561
38UbiquitinationATQAVFQKRQAGELD
HHHHHHHHHHCCCCC
34.7121906983
47PhosphorylationQAGELDESVLELTSQ
HCCCCCHHHHHHHHH
31.5024043423
52PhosphorylationDESVLELTSQILGAN
CHHHHHHHHHHHCCC
14.8124043423
53PhosphorylationESVLELTSQILGANP
HHHHHHHHHHHCCCC
28.0424043423
64PhosphorylationGANPDFATLWNCRRE
CCCCCHHHHHHHHHH
32.0924043423
80UbiquitinationLQQLETQKSPEELAA
HHHHHHCCCHHHHHH
75.3329967540
98PhosphorylationAELGFLESCLRVNPK
HHHCHHHHHHCCCCC
22.16-
105UbiquitinationSCLRVNPKSYGTWHH
HHHCCCCCHHCCHHH
51.62-
169PhosphorylationEELAFTDSLITRNFS
HHHHCCCCHHHCCCC
20.7224719451
329UbiquitinationWTAGDVQKECVLLKG
EEECCHHHHEEEEEC
53.59-
329AcetylationWTAGDVQKECVLLKG
EEECCHHHHEEEEEC
53.5925038526
335UbiquitinationQKECVLLKGRQEGWC
HHHEEEEECCCCCCC
48.1329967540
335AcetylationQKECVLLKGRQEGWC
HHHEEEEECCCCCCC
48.1325953088
360UbiquitinationRCELSVEKSTVLQSE
EEEEECCCHHHHHHH
49.6329967540
362PhosphorylationELSVEKSTVLQSELE
EEECCCHHHHHHHHH
35.98-
366PhosphorylationEKSTVLQSELESCKE
CCHHHHHHHHHHHHH
39.73-
370PhosphorylationVLQSELESCKELQEL
HHHHHHHHHHHHHHH
43.01-
372UbiquitinationQSELESCKELQELEP
HHHHHHHHHHHHHCC
71.4029967540
402UbiquitinationLDPLLYEKETLQYFQ
HHHHHCCHHHHHHHH
42.30-
404PhosphorylationPLLYEKETLQYFQTL
HHHCCHHHHHHHHHH
30.1721406692
407PhosphorylationYEKETLQYFQTLKAV
CCHHHHHHHHHHHHC
10.7721406692
410PhosphorylationETLQYFQTLKAVDPM
HHHHHHHHHHHCCCC
21.9621406692
412UbiquitinationLQYFQTLKAVDPMRA
HHHHHHHHHCCCCCC
50.1521906983
428UbiquitinationYLDDLRSKFLLENSV
HHHHHHHHHHHHCCC
33.3321906983

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 PGTA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGTA_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 PGTA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PFD2_HUMANPFDN2physical
22863883
LA_HUMANSSBphysical
22863883
SAE2_HUMANUBA2physical
22863883
PFD3_HUMANVBP1physical
22863883
ETFB_HUMANETFBphysical
26344197
DPCD_HUMANDPCDphysical
28514442
RAE2_HUMANCHMLphysical
28514442
RAE1_HUMANCHMphysical
28514442
G3P_HUMANGAPDHphysical
28514442
YKT6_HUMANYKT6physical
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 PGTA_HUMAN

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Related Literatures of Post-Translational Modification

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