XRP2_HUMAN - dbPTM
XRP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XRP2_HUMAN
UniProt AC O75695
Protein Name Protein XRP2
Gene Name RP2
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cell projection, cilium . Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus.
Protein Description Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins..
Protein Sequence MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
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
2N-myristoyl glycine------MGCFFSKRR
------CCCCCCCCC
19.55-
2Myristoylation------MGCFFSKRR
------CCCCCCCCC
19.5510942419
3S-palmitoylation-----MGCFFSKRRK
-----CCCCCCCCCC
2.7610942419
13UbiquitinationSKRRKADKESRPENE
CCCCCCCCCCCCCCH
63.55-
15PhosphorylationRRKADKESRPENEEE
CCCCCCCCCCCCHHH
59.9025159151
25UbiquitinationENEEERPKQYSWDQR
CCHHHCCCCCCCHHH
69.00-
27PhosphorylationEEERPKQYSWDQREK
HHHCCCCCCCHHHHC
20.1828796482
28PhosphorylationEERPKQYSWDQREKV
HHCCCCCCCHHHHCC
22.9828355574
34UbiquitinationYSWDQREKVDPKDYM
CCCHHHHCCCHHHHC
54.87-
38UbiquitinationQREKVDPKDYMFSGL
HHHCCCHHHHCCCCC
57.9621890473
40PhosphorylationEKVDPKDYMFSGLKD
HCCCHHHHCCCCCCC
13.24-
43PhosphorylationDPKDYMFSGLKDETV
CHHHHCCCCCCCCCC
27.04-
49PhosphorylationFSGLKDETVGRLPGT
CCCCCCCCCCCCCCC
38.0929759185
109UbiquitinationFRNCRDCKCTLACQQ
EECCCCCCCEEEEEE
34.25-
198PhosphorylationEDAVVQDYVPIPTTE
CCCEECCCCCCCCHH
7.34-
203PhosphorylationQDYVPIPTTEELKAV
CCCCCCCCHHHHEEE
47.78-
204PhosphorylationDYVPIPTTEELKAVR
CCCCCCCHHHHEEEE
23.31-
219PhosphorylationVSTEANRSIVPISRG
EECCCCCCEEECCCC
27.9523401153
224PhosphorylationNRSIVPISRGQRQKS
CCCEEECCCCCCCCC
25.0423401153
245PhosphorylationVVLFAGDYTIANARK
EEEEECCCCHHHHHH
10.10-
252UbiquitinationYTIANARKLIDEMVG
CCHHHHHHHHHHHHC
47.59-
260UbiquitinationLIDEMVGKGFFLVQT
HHHHHHCCCEEEEEE
40.9321890473
273UbiquitinationQTKEVSMKAEDAQRV
EECEECCCHHHHHHH
40.9121890473
284UbiquitinationAQRVFREKAPDFLPL
HHHHHHHHCCCCHHH
62.05-
341PhosphorylationSGDVDSFYNFADIQM
CCCCHHHEEHHHHHC
17.2127642862

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 XRP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2GMyristoylation

25255805
3CPalmitoylation

10942419

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 XRP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARL3_HUMANARL3physical
11847227
XPO7_HUMANXPO7physical
26186194
IPO7_HUMANIPO7physical
26186194
TNPO2_HUMANTNPO2physical
26186194
NMT1_HUMANNMT1physical
26186194
GLMN_HUMANGLMNphysical
26186194
XPO2_HUMANCSE1Lphysical
26186194
TSC2_HUMANTSC2physical
26186194
XPO4_HUMANXPO4physical
26186194
ECM29_HUMANKIAA0368physical
26186194
CSTF2_HUMANCSTF2physical
26186194
DMXL2_HUMANDMXL2physical
26186194
PDS5A_HUMANPDS5Aphysical
26186194
OSTF1_HUMANOSTF1physical
26186194
MTOR_HUMANMTORphysical
26186194
TBL3_HUMANTBL3physical
26186194
CND2_HUMANNCAPHphysical
26186194
SYMPK_HUMANSYMPKphysical
26186194
TARB1_HUMANTARBP1physical
26186194
STAT3_HUMANSTAT3physical
26186194
TNPO3_HUMANTNPO3physical
26186194
INT3_HUMANINTS3physical
26186194
TRXR1_HUMANTXNRD1physical
26186194
KNTC1_HUMANKNTC1physical
26186194
UBP24_HUMANUSP24physical
26186194
KC1D_HUMANCSNK1Dphysical
26186194
KC1E_HUMANCSNK1Ephysical
26186194
COG7_HUMANCOG7physical
26186194
MARC2_HUMANMARC2physical
26186194
CTL2_HUMANSLC44A2physical
26186194
TKFC_HUMANDAKphysical
26186194
PRAF2_HUMANPRAF2physical
26186194
MRRP3_HUMANKIAA0391physical
26186194
CTU1_HUMANCTU1physical
26186194
TRIPC_HUMANTRIP12physical
26186194
QSOX1_HUMANQSOX1physical
26186194
CTL2_HUMANSLC44A2physical
28514442
MARC2_HUMANMARC2physical
28514442
GLMN_HUMANGLMNphysical
28514442
MTOR_HUMANMTORphysical
28514442
KC1D_HUMANCSNK1Dphysical
28514442
KC1E_HUMANCSNK1Ephysical
28514442
DMXL2_HUMANDMXL2physical
28514442
XPO7_HUMANXPO7physical
28514442
TKFC_HUMANDAKphysical
28514442
STAT3_HUMANSTAT3physical
28514442
TNPO2_HUMANTNPO2physical
28514442
QSOX1_HUMANQSOX1physical
28514442
TRIPC_HUMANTRIP12physical
28514442
SYMPK_HUMANSYMPKphysical
28514442
UBP24_HUMANUSP24physical
28514442
TSC2_HUMANTSC2physical
28514442
PDS5A_HUMANPDS5Aphysical
28514442
COG8_HUMANCOG8physical
28514442
TRXR1_HUMANTXNRD1physical
28514442
TNPO3_HUMANTNPO3physical
28514442
ECM29_HUMANKIAA0368physical
28514442
PRAF2_HUMANPRAF2physical
28514442
CTU1_HUMANCTU1physical
28514442
XPO4_HUMANXPO4physical
28514442

Drug and Disease Associations
Kegg Disease
H00527 Retinitis pigmentosa (RP)
OMIM Disease
312600Retinitis pigmentosa 2 (RP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XRP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-28, AND MASSSPECTROMETRY.

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