PGTB2_HUMAN - dbPTM
PGTB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGTB2_HUMAN
UniProt AC P53611
Protein Name Geranylgeranyl transferase type-2 subunit beta
Gene Name RABGGTB
Organism Homo sapiens (Human).
Sequence Length 331
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 MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVLQRVNVQPELVS
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------MGTPQKDVI
------CCCCCCCEE
46.2119413330
3Phosphorylation-----MGTPQKDVII
-----CCCCCCCEEE
22.6523401153
6Acetylation--MGTPQKDVIIKSD
--CCCCCCCEEECCC
55.9823749302
6Ubiquitination--MGTPQKDVIIKSD
--CCCCCCCEEECCC
55.98-
11SumoylationPQKDVIIKSDAPDTL
CCCCEEECCCCCCEE
31.03-
11UbiquitinationPQKDVIIKSDAPDTL
CCCCEEECCCCCCEE
31.0321906983
11SumoylationPQKDVIIKSDAPDTL
CCCCEEECCCCCCEE
31.03-
12PhosphorylationQKDVIIKSDAPDTLL
CCCEEECCCCCCEEH
28.7025850435
17PhosphorylationIKSDAPDTLLLEKHA
ECCCCCCEEHHHHHH
20.4627251275
22UbiquitinationPDTLLLEKHADYIAS
CCEEHHHHHHHHHHH
44.0221906983
22AcetylationPDTLLLEKHADYIAS
CCEEHHHHHHHHHHH
44.0227452117
29PhosphorylationKHADYIASYGSKKDD
HHHHHHHHCCCCCCH
22.0728152594
30PhosphorylationHADYIASYGSKKDDY
HHHHHHHCCCCCCHH
19.1828152594
32PhosphorylationDYIASYGSKKDDYEY
HHHHHCCCCCCHHHH
28.4428152594
33UbiquitinationYIASYGSKKDDYEYC
HHHHCCCCCCHHHHH
56.7221906983
34UbiquitinationIASYGSKKDDYEYCM
HHHCCCCCCHHHHHH
58.49-
37PhosphorylationYGSKKDDYEYCMSEY
CCCCCCHHHHHHHHH
20.9428674419
39PhosphorylationSKKDDYEYCMSEYLR
CCCCHHHHHHHHHHH
6.2927642862
124AcetylationNKVVEYVKGLQKEDG
HHHHHHHHCCCCCCC
53.6627452117
124UbiquitinationNKVVEYVKGLQKEDG
HHHHHHHHCCCCCCC
53.6621906983
241PhosphorylationEKLPDVCYSWWVLAS
HHCCCHHHHHHHHHH
13.7424719451
248PhosphorylationYSWWVLASLKIIGRL
HHHHHHHHHHHHHHC
26.4924719451
307SumoylationLLGEEQIKPVNPVFC
HCCCHHCCCCCCCEE
42.48-
331PhosphorylationNVQPELVS-------
CCCHHHCC-------
47.3228102081

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 PGTB2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGTB2_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 PGTB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB3A_HUMANRAB3Aphysical
8706741
TP4A2_HUMANPTP4A2physical
11447212
FBXL2_HUMANFBXL2physical
24035498
WDR4_HUMANWDR4physical
25416956
B4GT7_HUMANB4GALT7physical
25416956
TMM25_HUMANTMEM25physical
25416956
RAB37_HUMANRAB37physical
25416956
F19A1_HUMANFAM19A1physical
25416956
I5P1_HUMANINPP5Aphysical
26186194
PRC2C_HUMANPRRC2Cphysical
26186194
PI51C_HUMANPIP5K1Cphysical
26186194
PI51A_HUMANPIP5K1Aphysical
26186194
AKA11_HUMANAKAP11physical
26186194
PALM_HUMANPALMphysical
26186194
NOTC3_HUMANNOTCH3physical
26186194
NOTC2_HUMANNOTCH2physical
26186194
MAGD4_HUMANMAGED4Bphysical
26186194
MCMBP_HUMANMCMBPphysical
26186194
BORA_HUMANBORAphysical
26186194
ABRX1_HUMANFAM175Aphysical
26186194
CACO1_HUMANCALCOCO1physical
26186194
TRI33_HUMANTRIM33physical
26186194
PTAR1_HUMANPTAR1physical
26186194
RHBT3_HUMANRHOBTB3physical
26186194
RRAS2_HUMANRRAS2physical
26186194
RASH_HUMANHRASphysical
26186194
RASN_HUMANNRASphysical
26186194
PAXI_HUMANPXNphysical
26186194
RB40C_HUMANRAB40Cphysical
26186194
RAP2A_HUMANRAP2Aphysical
26186194
PGTA_HUMANRABGGTAphysical
26186194
ARHG6_HUMANARHGEF6physical
26186194
ACOT9_HUMANACOT9physical
26186194
TP4A1_HUMANPTP4A1physical
26186194
TP4A2_HUMANPTP4A2physical
26186194
KAPCB_HUMANPRKACBphysical
26186194
MCM5_HUMANMCM5physical
26186194
F219A_HUMANFAM219Aphysical
26186194
KAP1_HUMANPRKAR1Bphysical
26186194
FOXK1_HUMANFOXK1physical
26186194
NCOA1_HUMANNCOA1physical
26186194
GNB1L_HUMANGNB1Lphysical
26186194
HOOK1_HUMANHOOK1physical
26186194
GIT1_HUMANGIT1physical
26186194
GIT2_HUMANGIT2physical
26186194
PP16A_HUMANPPP1R16Aphysical
26186194
ZCCHL_HUMANZC3HAV1Lphysical
26186194
PGBD5_HUMANPGBD5physical
26186194
TRM2_HUMANTRMT2Bphysical
26186194
YKT6_HUMANYKT6physical
26186194
PGTA_HUMANRABGGTAphysical
26344197
PTAR1_HUMANPTAR1physical
28514442
PGTA_HUMANRABGGTAphysical
28514442
PGBD5_HUMANPGBD5physical
28514442
PAXI_HUMANPXNphysical
28514442
NCOA1_HUMANNCOA1physical
28514442
PI51C_HUMANPIP5K1Cphysical
28514442
PI51A_HUMANPIP5K1Aphysical
28514442
PP16A_HUMANPPP1R16Aphysical
28514442
I5P1_HUMANINPP5Aphysical
28514442
TRI33_HUMANTRIM33physical
28514442
RB40C_HUMANRAB40Cphysical
28514442
CACO1_HUMANCALCOCO1physical
28514442
ARHG6_HUMANARHGEF6physical
28514442
PALM_HUMANPALMphysical
28514442
NOTC2_HUMANNOTCH2physical
28514442
TP4A2_HUMANPTP4A2physical
28514442
ACOT9_HUMANACOT9physical
28514442
BORA_HUMANBORAphysical
28514442
F219A_HUMANFAM219Aphysical
28514442
ABRX1_HUMANFAM175Aphysical
28514442
RHBT3_HUMANRHOBTB3physical
28514442
FXL20_HUMANFBXL20physical
28514442
AKA11_HUMANAKAP11physical
28514442
RASH_HUMANHRASphysical
28514442
TRM2_HUMANTRMT2Bphysical
28514442
RAP2A_HUMANRAP2Aphysical
28514442
YKT6_HUMANYKT6physical
28514442
GIT1_HUMANGIT1physical
28514442
GNB1L_HUMANGNB1Lphysical
28514442
HOOK1_HUMANHOOK1physical
28514442
FOXK1_HUMANFOXK1physical
28514442
PRC2C_HUMANPRRC2Cphysical
28514442
TP4A1_HUMANPTP4A1physical
28514442
RASN_HUMANNRASphysical
28514442
MCMBP_HUMANMCMBPphysical
28514442
NOTC3_HUMANNOTCH3physical
28514442
GIT2_HUMANGIT2physical
28514442
KAPCB_HUMANPRKACBphysical
28514442
RAP2C_HUMANRAP2Cphysical
28514442
ZCCHL_HUMANZC3HAV1Lphysical
28514442
MCM3_HUMANMCM3physical
28514442
XRCC3_HUMANXRCC3genetic
27453043
ATAD5_HUMANATAD5genetic
27453043
BLM_HUMANBLMgenetic
27453043
MTOR_HUMANMTORgenetic
27453043
RS19_HUMANRPS19genetic
27453043

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 PGTB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.

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