GPC5C_HUMAN - dbPTM
GPC5C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPC5C_HUMAN
UniProt AC Q9NQ84
Protein Name G-protein coupled receptor family C group 5 member C
Gene Name GPRC5C
Organism Homo sapiens (Human).
Sequence Length 441
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cytoplasmic vesicle membrane
Multi-pass membrane protein. Localized in the plasma membrane and perinuclear vesicles.
Protein Description This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways..
Protein Sequence MAIHKALVMCLGLPLFLFPGAWAQGHVPPGCSQGLNPLYYNLCDRSGAWGIVLEAVAGAGIVTTFVLTIILVASLPFVQDTKKRSLLGTQVFFLLGTLGLFCLVFACVVKPDFSTCASRRFLFGVLFAICFSCLAAHVFALNFLARKNHGPRGWVIFTVALLLTLVEVIINTEWLIITLVRGSGEGGPQGNSSAGWAVASPCAIANMDFVMALIYVMLLLLGAFLGAWPALCGRYKRWRKHGVFVLLTTATSVAIWVVWIVMYTYGNKQHNSPTWDDPTLAIALAANAWAFVLFYVIPEVSQVTKSSPEQSYQGDMYPTRGVGYETILKEQKGQSMFVENKAFSMDEPVAAKRPVSPYSGYNGQLLTSVYQPTEMALMHKVPSEGAYDIILPRATANSQVMGSANSTLRAEDMYSAQSHQAATPPKDGKNSQVFRNPYVWD
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
85PhosphorylationVQDTKKRSLLGTQVF
CCCHHHHHHHHHHHH		36.5022210691
89PhosphorylationKKRSLLGTQVFFLLG
HHHHHHHHHHHHHHH		22.8722210691
191N-linked_GlycosylationGEGGPQGNSSAGWAV
CCCCCCCCCCCCCCC		27.78UniProtKB CARBOHYD
263PhosphorylationWVVWIVMYTYGNKQH
HHHHHHHHHHCCCCC		5.9626074081
264PhosphorylationVVWIVMYTYGNKQHN
HHHHHHHHHCCCCCC		13.5726074081
265PhosphorylationVWIVMYTYGNKQHNS
HHHHHHHHCCCCCCC		10.9526074081
272PhosphorylationYGNKQHNSPTWDDPT
HCCCCCCCCCCCCHH		22.9126074081
274PhosphorylationNKQHNSPTWDDPTLA
CCCCCCCCCCCHHHH		41.1526074081
279PhosphorylationSPTWDDPTLAIALAA
CCCCCCHHHHHHHHH		35.5026074081
306PhosphorylationEVSQVTKSSPEQSYQ
HHHHHCCCCCCHHCC		41.5821945579
307PhosphorylationVSQVTKSSPEQSYQG
HHHHCCCCCCHHCCC		33.7321945579
311PhosphorylationTKSSPEQSYQGDMYP
CCCCCCHHCCCCCCC		20.1221945579
312PhosphorylationKSSPEQSYQGDMYPT
CCCCCHHCCCCCCCC		19.0621945579
317PhosphorylationQSYQGDMYPTRGVGY
HHCCCCCCCCCCCCH		13.2421945579
319PhosphorylationYQGDMYPTRGVGYET
CCCCCCCCCCCCHHH		23.6721945579
324PhosphorylationYPTRGVGYETILKEQ
CCCCCCCHHHHHHHH		13.9021082442
326PhosphorylationTRGVGYETILKEQKG
CCCCCHHHHHHHHCC		24.1130266825
329UbiquitinationVGYETILKEQKGQSM
CCHHHHHHHHCCCCC		55.00-
332UbiquitinationETILKEQKGQSMFVE
HHHHHHHCCCCCEEE		61.07-
335PhosphorylationLKEQKGQSMFVENKA
HHHHCCCCCEEECCC		23.9028355574
336PhosphorylationKEQKGQSMFVENKAF
HHHCCCCCEEECCCC		3.1627642862
338PhosphorylationQKGQSMFVENKAFSM
HCCCCCEEECCCCCC		6.2427642862
341UbiquitinationQSMFVENKAFSMDEP
CCCEEECCCCCCCCC		36.9821906983
344PhosphorylationFVENKAFSMDEPVAA
EEECCCCCCCCCCCC		30.1328355574
353 (in isoform 2)Ubiquitination-31.93-
356PhosphorylationVAAKRPVSPYSGYNG
CCCCCCCCCCCCCCC		22.3225849741
357PhosphorylationAAKRPVSPYSGYNGQ
CCCCCCCCCCCCCCE		27.78-
358PhosphorylationAKRPVSPYSGYNGQL
CCCCCCCCCCCCCEE		13.7626356563
359PhosphorylationKRPVSPYSGYNGQLL
CCCCCCCCCCCCEEE		37.8826356563
361PhosphorylationPVSPYSGYNGQLLTS
CCCCCCCCCCEEEEE		15.3526356563
362PhosphorylationVSPYSGYNGQLLTSV
CCCCCCCCCEEEEEE		34.95-
367PhosphorylationGYNGQLLTSVYQPTE
CCCCEEEEEEECCCH		25.4126356563
368PhosphorylationYNGQLLTSVYQPTEM
CCCEEEEEEECCCHH		20.8526356563
369PhosphorylationNGQLLTSVYQPTEMA
CCEEEEEEECCCHHH		4.3018083107
370PhosphorylationGQLLTSVYQPTEMAL
CEEEEEEECCCHHHH		14.4527259358
371PhosphorylationQLLTSVYQPTEMALM
EEEEEEECCCHHHHC		35.9624719451
373PhosphorylationLTSVYQPTEMALMHK
EEEEECCCHHHHCCC		23.9126356563
374UbiquitinationTSVYQPTEMALMHKV
EEEECCCHHHHCCCC		29.19-
377UbiquitinationYQPTEMALMHKVPSE
ECCCHHHHCCCCCCC		3.40-
380PhosphorylationTEMALMHKVPSEGAY
CHHHHCCCCCCCCCC		41.7024719451
383PhosphorylationALMHKVPSEGAYDII
HHCCCCCCCCCCEEE		52.2121945579
386UbiquitinationHKVPSEGAYDIILPR
CCCCCCCCCEEEEEC		8.52-
387PhosphorylationKVPSEGAYDIILPRA
CCCCCCCCEEEEECC		20.6621945579
389PhosphorylationPSEGAYDIILPRATA
CCCCCCEEEEECCCC		1.9624719451
395PhosphorylationDIILPRATANSQVMG
EEEEECCCCCCCCCC		27.8723403867
397UbiquitinationILPRATANSQVMGSA
EEECCCCCCCCCCCH		28.72-
398PhosphorylationLPRATANSQVMGSAN
EECCCCCCCCCCCHH		22.9917525332
399PhosphorylationPRATANSQVMGSANS
ECCCCCCCCCCCHHC		29.0827642862
401PhosphorylationATANSQVMGSANSTL
CCCCCCCCCCHHCCC		2.4524719451
403PhosphorylationANSQVMGSANSTLRA
CCCCCCCCHHCCCCH		13.2325159151
406PhosphorylationQVMGSANSTLRAEDM
CCCCCHHCCCCHHHH		28.6523898821
407PhosphorylationVMGSANSTLRAEDMY
CCCCHHCCCCHHHHH		21.7730206219
414PhosphorylationTLRAEDMYSAQSHQA
CCCHHHHHHCHHCCC		17.1220007894
415PhosphorylationLRAEDMYSAQSHQAA
CCHHHHHHCHHCCCC		17.1321082442
418PhosphorylationEDMYSAQSHQAATPP
HHHHHCHHCCCCCCC		19.7930266825
423PhosphorylationAQSHQAATPPKDGKN
CHHCCCCCCCCCCCC		43.0430266825
428PhosphorylationAATPPKDGKNSQVFR
CCCCCCCCCCCCCCC		36.8520166139
431PhosphorylationPPKDGKNSQVFRNPY
CCCCCCCCCCCCCCC		31.0728152594
432PhosphorylationPKDGKNSQVFRNPYV
CCCCCCCCCCCCCCC		48.0024719451
438PhosphorylationSQVFRNPYVWD----
CCCCCCCCCCC----		20.0927273156
443PhosphorylationNPYVWD---------
CCCCCC---------		24719451
448PhosphorylationD--------------
C--------------		24719451
450Phosphorylation----------------
----------------		27642862
451Phosphorylation-----------------
-----------------		-
459Phosphorylation-------------------------
-------------------------		-
460Phosphorylation--------------------------
--------------------------		27251275
468Phosphorylation----------------------------------
----------------------------------		27251275
474Ubiquitination----------------------------------------
----------------------------------------		-
476Phosphorylation------------------------------------------
------------------------------------------		27251275
483Phosphorylation-------------------------------------------------
-------------------------------------------------		-
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 GPC5C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPC5C_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 GPC5C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLP3L_HUMANGOLPH3Lphysical
28514442
NMT2_HUMANNMT2physical
28514442
PCY1A_HUMANPCYT1Aphysical
28514442
BI2L1_HUMANBAIAP2L1physical
28514442
NMT1_HUMANNMT1physical
28514442
GOLP3_HUMANGOLPH3physical
28514442
NNTM_HUMANNNTphysical
28514442
NJMU_HUMANC17orf75physical
28514442
CTGE5_HUMANCTAGE5physical
28514442
CTR1_HUMANSLC7A1physical
28514442
SNX17_HUMANSNX17physical
28514442
FA8A1_HUMANFAM8A1physical
28514442
BAG1_HUMANBAG1physical
28514442
FHL2_HUMANFHL2physical
28514442
PXK_HUMANPXKphysical
28514442
BTBD9_HUMANBTBD9physical
28514442
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 GPC5C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-387, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-324, AND MASSSPECTROMETRY.

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