RAP1B_HUMAN - dbPTM
RAP1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAP1B_HUMAN
UniProt AC P61224
Protein Name Ras-related protein Rap-1b
Gene Name RAP1B
Organism Homo sapiens (Human).
Sequence Length 184
Subcellular Localization Cell membrane. Cytoplasm, cytosol. Cell junction. May shuttle between plasma membrane and cytosol. Presence of KRIT1 and CDH5 is required for its localization to the cell junction.
Protein Description GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function..
Protein Sequence MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
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
5Ubiquitination---MREYKLVVLGSG
---CCEEEEEEECCC
30.0121890473
5Ubiquitination---MREYKLVVLGSG
---CCEEEEEEECCC
30.0121890473
5Acetylation---MREYKLVVLGSG
---CCEEEEEEECCC
30.0125953088
5Ubiquitination---MREYKLVVLGSG
---CCEEEEEEECCC
30.0121906983
11PhosphorylationYKLVVLGSGGVGKSA
EEEEEECCCCCCCHH
28.3625159151
17PhosphorylationGSGGVGKSALTVQFV
CCCCCCCHHHHHHEE
23.6820068231
31UbiquitinationVQGIFVEKYDPTIED
EEEEEEEECCCCCCH
50.0421906983
32PhosphorylationQGIFVEKYDPTIEDS
EEEEEEECCCCCCHH
17.4120860994
35PhosphorylationFVEKYDPTIEDSYRK
EEEECCCCCCHHHHH
33.8223403867
39PhosphorylationYDPTIEDSYRKQVEV
CCCCCCHHHHHHHEE
17.6623401153
39ADP-ribosylationYDPTIEDSYRKQVEV
CCCCCCHHHHHHHEE
17.663141412
39ADP-ribosylationYDPTIEDSYRKQVEV
CCCCCCHHHHHHHEE
17.66-
40PhosphorylationDPTIEDSYRKQVEVD
CCCCCHHHHHHHEEC
33.8623403867
42UbiquitinationTIEDSYRKQVEVDAQ
CCCHHHHHHHEECHH
50.92-
58PhosphorylationCMLEILDTAGTEQFT
HHHHHHHHCCCHHHH
24.4427732954
61PhosphorylationEILDTAGTEQFTAMR
HHHHHCCCHHHHHHH
24.9327732954
65PhosphorylationTAGTEQFTAMRDLYM
HCCCHHHHHHHHHHH
21.1627732954
88PhosphorylationVYSITAQSTFNDLQD
EEEEEECCCCCCHHH
32.2826657352
117UbiquitinationPMILVGNKCDLEDER
CEEEECCCCCCCCCE
24.17-
128UbiquitinationEDERVVGKEQGQNLA
CCCEECCHHHHHHHH
34.94-
134MethylationGKEQGQNLARQWNNC
CHHHHHHHHHHHHCC
2.982123345
139MethylationQNLARQWNNCAFLES
HHHHHHHHCCHHHHH
25.932123345
149UbiquitinationAFLESSAKSKINVNE
HHHHHHCCCCCCHHH
54.98-
151UbiquitinationLESSAKSKINVNEIF
HHHHCCCCCCHHHHH
37.28-
159PhosphorylationINVNEIFYDLVRQIN
CCHHHHHHHHHHHHC
17.6523917254
162MethylationNEIFYDLVRQINRKT
HHHHHHHHHHHCCCC
3.752123345
169PhosphorylationVRQINRKTPVPGKAR
HHHHCCCCCCCCCCC
26.7028060719
174UbiquitinationRKTPVPGKARKKSSC
CCCCCCCCCCCCCCC
38.66-
179PhosphorylationPGKARKKSSCQLL--
CCCCCCCCCCCCC--
39.1112089143
180PhosphorylationGKARKKSSCQLL---
CCCCCCCCCCCC---
18.118463283
181GeranylgeranylationKARKKSSCQLL----
CCCCCCCCCCC----
4.222123345
181MethylationKARKKSSCQLL----
CCCCCCCCCCC----
4.222123345
181GeranylgeranylationKARKKSSCQLL----
CCCCCCCCCCC----
4.222123345

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
179SPhosphorylationKinasePRKACAP17612
GPS
179SPhosphorylationKinasePRKG1Q13976
GPS
179SPhosphorylationKinasePKA-FAMILY-GPS
179SPhosphorylationKinasePKG-FAMILY-GPS
179SPhosphorylationKinasePKA-Uniprot
179SPhosphorylationKinasePKA_GROUP-PhosphoELM
180SPhosphorylationKinasePKACAP17612
PSP
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:17318188

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAP1B_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 RAP1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCG1_HUMANCHGBphysical
21900206
A2MG_HUMANA2Mphysical
21900206
P53_HUMANTP53physical
21900206
CSAD_HUMANCSADphysical
21900206
KPYM_HUMANPKMphysical
21900206
ODPB_HUMANPDHBphysical
21900206
CAB45_HUMANSDF4physical
21900206
DDAH2_HUMANDDAH2physical
21900206
APLP1_HUMANAPLP1physical
21900206
U119A_HUMANUNC119physical
21900206
HEM1_HUMANALAS1physical
21900206
ZN135_HUMANZNF135physical
21900206
KMT2B_HUMANKMT2Bphysical
21900206
TLE1_HUMANTLE1physical
21900206
TCPH_HUMANCCT7physical
21900206
LRIF1_HUMANLRIF1physical
21900206
FAF1_HUMANFAF1physical
21900206
A4_HUMANAPPphysical
21832049
RGS2_HUMANRGS2physical
21988832
RGL2_HUMANRGL2physical
21988832
RPTOR_HUMANRPTORphysical
24337580
RASF5_HUMANRASSF5physical
25416956
CDC42_HUMANCDC42physical
26344197
RAB5A_HUMANRAB5Aphysical
26344197
RAB5B_HUMANRAB5Bphysical
26344197
RAB5C_HUMANRAB5Cphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
RAB8A_HUMANRAB8Aphysical
26344197
RAB8B_HUMANRAB8Bphysical
26344197
STX12_HUMANSTX12physical
26344197
STX7_HUMANSTX7physical
26344197
QCR2_HUMANUQCRC2physical
26344197
DMXL1_HUMANDMXL1physical
26496610
KLC1_HUMANKLC1physical
26496610
M3K4_HUMANMAP3K4physical
26496610
UBR4_HUMANUBR4physical
26496610
DICER_HUMANDICER1physical
26496610
AP3M1_HUMANAP3M1physical
26496610
GAR1_HUMANGAR1physical
26496610
WAP53_HUMANWRAP53physical
26496610
P33MX_HUMANKIAA1191physical
26496610
SYAM_HUMANAARS2physical
26496610
NCK5L_HUMANNCKAP5Lphysical
26496610
RT35_HUMANMRPS35physical
26496610
SEN2_HUMANTSEN2physical
26496610
UBP32_HUMANUSP32physical
26496610
NRBP2_HUMANNRBP2physical
26496610

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 RAP1B_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Posttranslationally processed structure of the human platelet proteinsmg p21B: evidence for geranylgeranylation and carboxyl methylation ofthe C-terminal cysteine.";
Kawata M., Farnsworth C.C., Yoshida Y., Gelb M.H., Glomset J.A.,Takai Y.;
Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990).
Cited for: ISOPRENYLATION AT CYS-181.

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