RBP1_RAT - dbPTM
RBP1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBP1_RAT
UniProt AC Q62796
Protein Name RalA-binding protein 1
Gene Name Ralbp1
Organism Rattus norvegicus (Rat).
Sequence Length 647
Subcellular Localization Membrane
Peripheral membrane protein. Cytoplasm, cytosol. Cytoplasm, cytoskeleton, spindle pole. Cytosolic protein that transiently associates with the mitotic spindle poles in early prophase, and dissociates from them after completion of mitosis.
Protein Description Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin (By similarity). Involved in the assembly and function of the mitotic apparatus..
Protein Sequence MTECFLPPTSSPSEHRRAEHGSGLTRTPSSEEISPTKFPELYRTGEPSPPHDILHEPPDIVSDDEKDHGKKKGKFKKKEKRTEGYVAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKCKDFTAADVVKQWKEKKKKKKPTQEPEVPQTDAPSLRPIFGAPFADAVERTMMYDGIRLPAVFRECVDYMEKHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTEVEKVQEFQRLLRELPEYNHLLLSWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVLFTHVQELFGTVLLKQVTRPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDFSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEETNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQHGRSETEEYSSDSESESEDEEELQIILEDLQRQNEELEIKNNHLNQAVHEEREAIVELRVQLRLLQMLRAKSEQQLQEEEEPERRGGTGPLPCEGVLEVRAAKEQAKPSPSKDRKETPI
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------MTECFLPPT
------CCCCCCCCC
41.27-
9PhosphorylationTECFLPPTSSPSEHR
CCCCCCCCCCHHHHC
39.6427097102
10PhosphorylationECFLPPTSSPSEHRR
CCCCCCCCCHHHHCC
46.1327097102
11PhosphorylationCFLPPTSSPSEHRRA
CCCCCCCCHHHHCCH
34.6223589303
13PhosphorylationLPPTSSPSEHRRAEH
CCCCCCHHHHCCHHC
48.2427097102
22PhosphorylationHRRAEHGSGLTRTPS
HCCHHCCCCCCCCCC
32.3223984901
25PhosphorylationAEHGSGLTRTPSSEE
HHCCCCCCCCCCCCC
35.7027097102
27PhosphorylationHGSGLTRTPSSEEIS
CCCCCCCCCCCCCCC
23.4527097102
29PhosphorylationSGLTRTPSSEEISPT
CCCCCCCCCCCCCCC
50.1723712012
30PhosphorylationGLTRTPSSEEISPTK
CCCCCCCCCCCCCCC
40.2121738781
34PhosphorylationTPSSEEISPTKFPEL
CCCCCCCCCCCCCHH
29.7827097102
36PhosphorylationSSEEISPTKFPELYR
CCCCCCCCCCCHHHC
38.2328432305
44PhosphorylationKFPELYRTGEPSPPH
CCCHHHCCCCCCCCC
32.1328432305
48PhosphorylationLYRTGEPSPPHDILH
HHCCCCCCCCCCCCC
46.9230240740
62PhosphorylationHEPPDIVSDDEKDHG
CCCCCCCCCCCCCCC
39.4128432305
92PhosphorylationYVAFQEDSSGDEAES
EEEEECCCCCCCCCC
35.15-
93PhosphorylationVAFQEDSSGDEAESP
EEEECCCCCCCCCCH
63.6928689409
461PhosphorylationKIAQEIASLSKEDVS
HHHHHHHHCCHHHCC
38.5528432305
463PhosphorylationAQEIASLSKEDVSKE
HHHHHHCCHHHCCHH
31.3530411139
468PhosphorylationSLSKEDVSKEETNEN
HCCHHHCCHHHCCCC
46.8228432305
600PhosphorylationLQMLRAKSEQQLQEE
HHHHHHHHHHHHHHH
39.3928432305
637PhosphorylationAKEQAKPSPSKDRKE
HHHHCCCCCCCCCCC
40.8928432305
639PhosphorylationEQAKPSPSKDRKETP
HHCCCCCCCCCCCCC
52.0728432305

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 RBP1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBP1_RAT !!

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 RBP1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RBP1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBP1_RAT

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Related Literatures of Post-Translational Modification

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