OGFR_HUMAN - dbPTM
OGFR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OGFR_HUMAN
UniProt AC Q9NZT2
Protein Name Opioid growth factor receptor
Gene Name OGFR
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Cytoplasm. Nucleus. The OGF/OGFR complex is probably translocated to the nucleus.
Protein Description Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation..
Protein Sequence MDDPDCDSTWEEDEEDAEDAEDEDCEDGEAAGARDADAGDEDEESEEPRAARPSSFQSRMTGSRNWRATRDMCRYRHNYPDLVERDCNGDTPNLSFYRNEIRFLPNGCFIEDILQNWTDNYDLLEDNHSYIQWLFPLREPGVNWHAKPLTLREVEVFKSSQEIQERLVRAYELMLGFYGIRLEDRGTGTVGRAQNYQKRFQNLNWRSHNNLRITRILKSLGELGLEHFQAPLVRFFLEETLVRRELPGVRQSALDYFMFAVRCRHQRRQLVHFAWEHFRPRCKFVWGPQDKLRRFKPSSLPHPLEGSRKVEEEGSPGDPDHEASTQGRTCGPEHSKGGGRVDEGPQPRSVEPQDAGPLERSQGDEAGGHGEDRPEPLSPKESKKRKLELSRREQPPTEPGPQSASEVEKIALNLEGCALSQGSLRTGTQEVGGQDPGEAVQPCRQPLGARVADKVRKRRKVDEGAGDSAAVASGGAQTLALAGSPAPSGHPKAGHSENGVEEDTEGRTGPKEGTPGSPSETPGPSPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPSPAGPTRDEPAESPSETPGPRPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPSPAGPTRDEPAKAGEAAELQDAEVESSAKSGKP
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
1Acetylation-------MDDPDCDS
-------CCCCCCCC		13.7219413330
8PhosphorylationMDDPDCDSTWEEDEE
CCCCCCCCCCCCCHH		41.5726552605
9PhosphorylationDDPDCDSTWEEDEED
CCCCCCCCCCCCHHH		24.5226552605
45PhosphorylationAGDEDEESEEPRAAR
CCCCCCCCCCCCCCC		45.2520873877
54PhosphorylationEPRAARPSSFQSRMT
CCCCCCCCHHHHHHH		37.9326434776
55PhosphorylationPRAARPSSFQSRMTG
CCCCCCCHHHHHHHC		29.9525106551
58PhosphorylationARPSSFQSRMTGSRN
CCCCHHHHHHHCCCC		23.2426434776
158 (in isoform 2)Ubiquitination-55.1421890473
158 (in isoform 1)Ubiquitination-55.1421890473
158UbiquitinationLREVEVFKSSQEIQE
EEEEEEHHCCHHHHH		55.1421906983
171PhosphorylationQERLVRAYELMLGFY
HHHHHHHHHHHHHHH		10.0722817900
178PhosphorylationYELMLGFYGIRLEDR
HHHHHHHHCEEEECC		15.1622817900
187PhosphorylationIRLEDRGTGTVGRAQ
EEEECCCCCCHHCHH		30.49-
189PhosphorylationLEDRGTGTVGRAQNY
EECCCCCCHHCHHHH		21.45-
196PhosphorylationTVGRAQNYQKRFQNL
CHHCHHHHHHHHHHC		11.8822817900
198UbiquitinationGRAQNYQKRFQNLNW
HCHHHHHHHHHHCCC		44.8327667366
218 (in isoform 2)Ubiquitination-41.0621890473
218UbiquitinationLRITRILKSLGELGL
HHHHHHHHHHHHHCH		41.0623000965
218 (in isoform 1)Ubiquitination-41.0621890473
240PhosphorylationVRFFLEETLVRRELP
HHHHHHHHHHHHCCC		22.6025599653
252PhosphorylationELPGVRQSALDYFMF
CCCCCHHHHHHHHHH		21.8924043423
256PhosphorylationVRQSALDYFMFAVRC
CHHHHHHHHHHHHHC		9.5924043423
283UbiquitinationEHFRPRCKFVWGPQD
HHHHCCCEEEECCHH		44.20-
283AcetylationEHFRPRCKFVWGPQD
HHHHCCCEEEECCHH		44.2025953088
291UbiquitinationFVWGPQDKLRRFKPS
EEECCHHHHHCCCCC		38.3521963094
291 (in isoform 1)Ubiquitination-38.3521890473
291 (in isoform 2)Ubiquitination-38.3521890473
291AcetylationFVWGPQDKLRRFKPS
EEECCHHHHHCCCCC		38.3521339330
296UbiquitinationQDKLRRFKPSSLPHP
HHHHHCCCCCCCCCC		42.0222817900
298PhosphorylationKLRRFKPSSLPHPLE
HHHCCCCCCCCCCCC		45.1323401153
299PhosphorylationLRRFKPSSLPHPLEG
HHCCCCCCCCCCCCC		55.2220873877
307PhosphorylationLPHPLEGSRKVEEEG
CCCCCCCCCCCCCCC		21.3923186163
309SumoylationHPLEGSRKVEEEGSP
CCCCCCCCCCCCCCC		56.55-
309SumoylationHPLEGSRKVEEEGSP
CCCCCCCCCCCCCCC		56.55-
309UbiquitinationHPLEGSRKVEEEGSP
CCCCCCCCCCCCCCC		56.5524816145
315PhosphorylationRKVEEEGSPGDPDHE
CCCCCCCCCCCCCCC		29.0529255136
324PhosphorylationGDPDHEASTQGRTCG
CCCCCCHHCCCCCCC		20.4823927012
325PhosphorylationDPDHEASTQGRTCGP
CCCCCHHCCCCCCCC		41.9323927012
329PhosphorylationEASTQGRTCGPEHSK
CHHCCCCCCCCCCCC		28.74-
335PhosphorylationRTCGPEHSKGGGRVD
CCCCCCCCCCCCCCC		31.1920860994
349PhosphorylationDEGPQPRSVEPQDAG
CCCCCCCCCCCCCCC		37.2029255136
361PhosphorylationDAGPLERSQGDEAGG
CCCCCCHHCCCCCCC		29.1930266825
378PhosphorylationEDRPEPLSPKESKKR
CCCCCCCCHHHHHHH		44.6429255136
382PhosphorylationEPLSPKESKKRKLEL
CCCCHHHHHHHHHHH		49.9923401153
384UbiquitinationLSPKESKKRKLELSR
CCHHHHHHHHHHHHH		65.1324816145
386UbiquitinationPKESKKRKLELSRRE
HHHHHHHHHHHHHCC		56.0127667366
390PhosphorylationKKRKLELSRREQPPT
HHHHHHHHHCCCCCC		21.6624117733
397PhosphorylationSRREQPPTEPGPQSA
HHCCCCCCCCCCCCH		62.5929978859
403PhosphorylationPTEPGPQSASEVEKI
CCCCCCCCHHHHHHH		36.5725159151
405PhosphorylationEPGPQSASEVEKIAL
CCCCCCHHHHHHHHH		47.6325262027
420PhosphorylationNLEGCALSQGSLRTG
CCCCHHHCCCCCCCC		17.6117525332
423PhosphorylationGCALSQGSLRTGTQE
CHHHCCCCCCCCCCC		13.6728450419
426PhosphorylationLSQGSLRTGTQEVGG
HCCCCCCCCCCCCCC		50.2922817900
428PhosphorylationQGSLRTGTQEVGGQD
CCCCCCCCCCCCCCC		22.4222817900
454AcetylationLGARVADKVRKRRKV
CCHHHHHHHHHHCCC		33.9130591015
468PhosphorylationVDEGAGDSAAVASGG
CCCCCCCCHHHHCCC		19.7423927012
473PhosphorylationGDSAAVASGGAQTLA
CCCHHHHCCCCCEEE		31.0330278072
478PhosphorylationVASGGAQTLALAGSP
HHCCCCCEEEECCCC		17.2923927012
484PhosphorylationQTLALAGSPAPSGHP
CEEEECCCCCCCCCC		16.5729255136
488PhosphorylationLAGSPAPSGHPKAGH
ECCCCCCCCCCCCCC		52.4123401153
496PhosphorylationGHPKAGHSENGVEED
CCCCCCCCCCCCCCC		31.6628985074
508PhosphorylationEEDTEGRTGPKEGTP
CCCCCCCCCCCCCCC		69.5626074081
514PhosphorylationRTGPKEGTPGSPSET
CCCCCCCCCCCCCCC		26.1030266825
517 (in isoform 2)Phosphorylation-26.8425137130
517PhosphorylationPKEGTPGSPSETPGP
CCCCCCCCCCCCCCC		26.8419664994
519 (in isoform 2)Phosphorylation-56.6625137130
519PhosphorylationEGTPGSPSETPGPSP
CCCCCCCCCCCCCCC		56.6630266825
521 (in isoform 2)Phosphorylation-37.5725137130
521PhosphorylationTPGSPSETPGPSPAG
CCCCCCCCCCCCCCC		37.5730266825
525PhosphorylationPSETPGPSPAGPAGD
CCCCCCCCCCCCCCC		33.0430266825
525 (in isoform 2)Phosphorylation-33.0425137130
537 (in isoform 2)Phosphorylation-35.5125137130
537PhosphorylationAGDEPAESPSETPGP
CCCCCCCCCCCCCCC		35.5119664994
539 (in isoform 2)Phosphorylation-64.4825137130
539PhosphorylationDEPAESPSETPGPRP
CCCCCCCCCCCCCCC		64.4823401153
541 (in isoform 2)Phosphorylation-37.5725137130
541PhosphorylationPAESPSETPGPRPAG
CCCCCCCCCCCCCCC		37.5730266825
557PhosphorylationAGDEPAESPSETPGP
CCCCCCCCCCCCCCC		35.5119664994
557 (in isoform 2)Phosphorylation-35.5125137130
559PhosphorylationDEPAESPSETPGPRP
CCCCCCCCCCCCCCC		64.4830266825
561PhosphorylationPAESPSETPGPRPAG
CCCCCCCCCCCCCCC		37.5730266825
577PhosphorylationAGDEPAESPSETPGP
CCCCCCCCCCCCCCC		35.5130266825
579PhosphorylationDEPAESPSETPGPSP
CCCCCCCCCCCCCCC		64.4830266825
581PhosphorylationPAESPSETPGPSPAG
CCCCCCCCCCCCCCC		37.5730266825
585PhosphorylationPSETPGPSPAGPTRD
CCCCCCCCCCCCCCC		33.0430266825
590PhosphorylationGPSPAGPTRDEPAES
CCCCCCCCCCCCCCC		50.2423663014
597PhosphorylationTRDEPAESPSETPGP
CCCCCCCCCCCCCCC		35.5123401153
599PhosphorylationDEPAESPSETPGPRP
CCCCCCCCCCCCCCC		64.4823401153
601PhosphorylationPAESPSETPGPRPAG
CCCCCCCCCCCCCCC		37.5723663014
617PhosphorylationAGDEPAESPSETPGP
CCCCCCCCCCCCCCC		35.5119664994
619PhosphorylationDEPAESPSETPGPRP
CCCCCCCCCCCCCCC		64.4830266825
621PhosphorylationPAESPSETPGPRPAG
CCCCCCCCCCCCCCC		37.5730266825
636 (in isoform 2)Ubiquitination-74.11-
637PhosphorylationAGDEPAESPSETPGP
CCCCCCCCCCCCCCC		35.5130266825
639PhosphorylationDEPAESPSETPGPSP
CCCCCCCCCCCCCCC		64.4830266825
641PhosphorylationPAESPSETPGPSPAG
CCCCCCCCCCCCCCC		37.5730266825
645PhosphorylationPSETPGPSPAGPTRD
CCCCCCCCCCCCCCC		33.0430266825
650PhosphorylationGPSPAGPTRDEPAKA
CCCCCCCCCCCCCCC		50.2429255136
656UbiquitinationPTRDEPAKAGEAAEL
CCCCCCCCCCCHHHH		68.5823503661
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
378SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OGFR_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 OGFR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC37_HUMANCDC37physical
22863883
FKBP5_HUMANFKBP5physical
22863883
SHOT1_HUMANKIAA1598physical
22863883
MAGD2_HUMANMAGED2physical
22863883
TRAP1_HUMANTRAP1physical
22863883
UBP7_HUMANUSP7physical
22863883
CDK4_HUMANCDK4physical
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 OGFR_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-349 ANDSER-378, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-361; SER-378AND SER-484, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASSSPECTROMETRY.
"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-420, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY.
"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-315 AND SER-378, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory