RAP2A_HUMAN - dbPTM
RAP2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAP2A_HUMAN
UniProt AC P10114
Protein Name Ras-related protein Rap-2a
Gene Name RAP2A
Organism Homo sapiens (Human).
Sequence Length 183
Subcellular Localization Recycling endosome membrane
Lipid-anchor
Cytoplasmic side. Midbody. May also localize to the Golgi (PubMed:7962206) and the gelatinase-containing granules of neutrophils (PubMed:8391995). Colocalizes with RASGEF1B to midbody at telophase (PubMed:23
Protein Description Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading..
Protein Sequence MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSSEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ
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
4Phosphorylation----MREYKVVVLGS
----CCEEEEEEECC		9.94-
5Ubiquitination---MREYKVVVLGSG
---CCEEEEEEECCC		24.6523000965
11PhosphorylationYKVVVLGSGGVGKSA
EEEEEECCCCCCCCC		28.3620068231
17PhosphorylationGSGGVGKSALTVQFV
CCCCCCCCCEEEEEE		23.6820068231
20PhosphorylationGVGKSALTVQFVTGT
CCCCCCEEEEEEEEC		16.3920068231
25PhosphorylationALTVQFVTGTFIEKY
CEEEEEEEECHHHHC		31.6220068231
27PhosphorylationTVQFVTGTFIEKYDP
EEEEEEECHHHHCCC		16.4520068231
31UbiquitinationVTGTFIEKYDPTIED
EEECHHHHCCCCHHH		50.5721987572
35O-linked_GlycosylationFIEKYDPTIEDFYRK
HHHHCCCCHHHHHHC		33.8222267739
40PhosphorylationDPTIEDFYRKEIEVD
CCCHHHHHHCCCCCC		32.85-
42UbiquitinationTIEDFYRKEIEVDSS
CHHHHHHCCCCCCCC		52.2229901268
48PhosphorylationRKEIEVDSSPSVLEI
HCCCCCCCCHHHHHH		49.6928060719
49PhosphorylationKEIEVDSSPSVLEIL
CCCCCCCCHHHHHHH		19.4120068231
51PhosphorylationIEVDSSPSVLEILDT
CCCCCCHHHHHHHHC		41.0820068231
58PhosphorylationSVLEILDTAGTEQFA
HHHHHHHCCCCHHHH		24.4428060719
61PhosphorylationEILDTAGTEQFASMR
HHHHCCCCHHHHHHH		24.9330108239
66PhosphorylationAGTEQFASMRDLYIK
CCCHHHHHHHHEEEE		18.6830108239
71PhosphorylationFASMRDLYIKNGQGF
HHHHHHEEEECCCEE		17.7128270605
94UbiquitinationQQSFQDIKPMRDQII
CCCCCCCCCCHHHEE		40.8420159449PubMed
108UbiquitinationIRVKRYEKVPVILVG
EEEEECCCCCEEEEC		42.7929967540
148UbiquitinationPFMETSAKSKTMVDE
CCCCCCCCCCHHHHH		52.8620159449PubMed
149PhosphorylationFMETSAKSKTMVDEL
CCCCCCCCCHHHHHH		32.8329978859
150UbiquitinationMETSAKSKTMVDELF
CCCCCCCCHHHHHHH		39.6820159449PubMed
151PhosphorylationETSAKSKTMVDELFA
CCCCCCCHHHHHHHH		29.5329978859
166PhosphorylationEIVRQMNYAAQPDKD
HHHHHCCCCCCCCCC		9.6629978859
176S-palmitoylationQPDKDDPCCSACNIQ
CCCCCCCCCCCCCCC		3.5419061864
177S-palmitoylationPDKDDPCCSACNIQ-
CCCCCCCCCCCCCC-		3.3419061864
180FarnesylationDDPCCSACNIQ----
CCCCCCCCCCC----		2.378424780
180MethylationDDPCCSACNIQ----
CCCCCCCCCCC----		2.378424780
180FarnesylationDDPCCSACNIQ----
CCCCCCCCCCC----		2.378424780
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 RAP2A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
63Kubiquitylation

20159449
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 RAP2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUN3A_HUMANRUNDC3Aphysical
9523700
GNDS_HUMANRALGDSphysical
10085114
EF1A1_HUMANEEF1A1physical
18624398
PLMN_HUMANPLGphysical
18624398
FKBP2_HUMANFKBP2physical
18624398
U3IP2_HUMANRRP9physical
18624398
ERG24_HUMANTM7SF2physical
18624398
A1AT_HUMANSERPINA1physical
18624398
FRIL_HUMANFTLphysical
18624398
ENSA_HUMANENSAphysical
18624398
TCPZ_HUMANCCT6Aphysical
26344197
DX39A_HUMANDDX39Aphysical
26344197
MTOR_HUMANMTORphysical
25446900
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 RAP2A_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Prenyl group identification of rap2 proteins: a ras superfamilymember other than ras that is farnesylated.";
Farrell F.X., Yamamoto K., Lapetina E.G.;
Biochem. J. 289:349-355(1993).
Cited for: ISOPRENYLATION AT CYS-180.

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