UBR1_HUMAN - dbPTM
UBR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBR1_HUMAN
UniProt AC Q8IWV7
Protein Name E3 ubiquitin-protein ligase UBR1
Gene Name UBR1
Organism Homo sapiens (Human).
Sequence Length 1749
Subcellular Localization Cytoplasm, cytosol .
Protein Description E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth..
Protein Sequence MADEEAGGTERMEISAELPQTPQRLASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSIFTPLEWYLFGEDPDICLEKLKHSGAFQLCGRVFKSGETTYSCRDCAIDPTCVLCMDCFQDSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVNHEPGRAGTIKENSRCPLNEEVIVQARKIFPSVIKYVVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGAYAACQEAKEDIKSHSENVSQHPLHVEVLHSEIMAHQKFALRLGSWMNKIMSYSSDFRQIFCQACLREEPDSENPCLISRLMLWDAKLYKGARKILHELIFSSFFMEMEYKKLFAMEFVKYYKQLQKEYISDDHDRSISITALSVQMFTVPTLARHLIEEQNVISVITETLLEVLPEYLDRNNKFNFQGYSQDKLGRVYAVICDLKYILISKPTIWTERLRMQFLEGFRSFLKILTCMQGMEEIRRQVGQHIEVDPDWEAAIAIQMQLKNILLMFQEWCACDEELLLVAYKECHKAVMRCSTSFISSSKTVVQSCGHSLETKSYRVSEDLVSIHLPLSRTLAGLHVRLSRLGAVSRLHEFVSFEDFQVEVLVEYPLRCLVLVAQVVAEMWRRNGLSLISQVFYYQDVKCREEMYDKDIIMLQIGASLMDPNKFLLLVLQRYELAEAFNKTISTKDQDLIKQYNTLIEEMLQVLIYIVGERYVPGVGNVTKEEVTMREIIHLLCIEPMPHSAIAKNLPENENNETGLENVINKVATFKKPGVSGHGVYELKDESLKDFNMYFYHYSKTQHSKAEHMQKKRRKQENKDEALPPPPPPEFCPAFSKVINLLNCDIMMYILRTVFERAIDTDSNLWTEGMLQMAFHILALGLLEEKQQLQKAPEEEVTFDFYHKASRLGSSAMNIQMLLEKLKGIPQLEGQKDMITWILQMFDTVKRLREKSCLIVATTSGSESIKNDEITHDKEKAERKRKAEAARLHRQKIMAQMSALQKNFIETHKLMYDNTSEMPGKEDSIMEEESTPAVSDYSRIALGPKRGPSVTEKEVLTCILCQEEQEVKIENNAMVLSACVQKSTALTQHRGKPIELSGEALDPLFMDPDLAYGTYTGSCGHVMHAVCWQKYFEAVQLSSQQRIHVDLFDLESGEYLCPLCKSLCNTVIPIIPLQPQKINSENADALAQLLTLARWIQTVLARISGYNIRHAKGENPIPIFFNQGMGDSTLEFHSILSFGVESSIKYSNSIKEMVILFATTIYRIGLKVPPDERDPRVPMLTWSTCAFTIQAIENLLGDEGKPLFGALQNRQHNGLKALMQFAVAQRITCPQVLIQKHLVRLLSVVLPNIKSEDTPCLLSIDLFHVLVGAVLAFPSLYWDDPVDLQPSSVSSSYNHLYLFHLITMAHMLQILLTVDTGLPLAQVQEDSEEAHSASSFFAEISQYTSGSIGCDIPGWYLWVSLKNGITPYLRCAALFFHYLLGVTPPEELHTNSAEGEYSALCSYLSLPTNLFLLFQEYWDTVRPLLQRWCADPALLNCLKQKNTVVRYPRKRNSLIELPDDYSCLLNQASHFRCPRSADDERKHPVLCLFCGAILCSQNICCQEIVNGEEVGACIFHALHCGAGVCIFLKIRECRVVLVEGKARGCAYPAPYLDEYGETDPGLKRGNPLHLSRERYRKLHLVWQQHCIIEEIARSQETNQMLFGFNWQLL
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------MADEEAGGT
------CCCCCCCCC		44.2019369195
9PhosphorylationADEEAGGTERMEISA
CCCCCCCCCCEEEEE		21.3522468782
15PhosphorylationGTERMEISAELPQTP
CCCCEEEEEECCCCH		11.4623401153
21PhosphorylationISAELPQTPQRLASW
EEEECCCCHHHHHHH		21.3229255136
91UbiquitinationDICLEKLKHSGAFQL
CCHHHHCCCCCHHHH		46.9529967540
104UbiquitinationQLCGRVFKSGETTYS
HHCCEEECCCCCEEE		55.4827667366
192UbiquitinationEVIVQARKIFPSVIK
HHHHHHHHHHHHHHH		52.2829967540
272UbiquitinationKEGRRAVKAGAYAAC
HHHHHHHHHHHHHHH		39.8722505724
283UbiquitinationYAACQEAKEDIKSHS
HHHHHHHHHHHHHHC		55.9932015554
323UbiquitinationRLGSWMNKIMSYSSD
HHHHHHHHHHHCCHH		24.5521963094
361UbiquitinationRLMLWDAKLYKGARK
HHHHHCCHHHHHHHH		50.29-
376PhosphorylationILHELIFSSFFMEME
HHHHHHHHHHHHHHH		21.1724043423
377PhosphorylationLHELIFSSFFMEMEY
HHHHHHHHHHHHHHH		16.2624043423
384PhosphorylationSFFMEMEYKKLFAME
HHHHHHHHHHHHHHH		16.4724043423
397UbiquitinationMEFVKYYKQLQKEYI
HHHHHHHHHHHHHHC		41.2529967540
418PhosphorylationSISITALSVQMFTVP
CCEEEEEEEEEECHH		14.0822210691
423PhosphorylationALSVQMFTVPTLARH
EEEEEEECHHHHHHH		21.8922210691
426PhosphorylationVQMFTVPTLARHLIE
EEEECHHHHHHHHHH		28.8122210691
458 (in isoform 1)Ubiquitination-45.2821890473
458 (in isoform 2)Ubiquitination-45.2821906983
458UbiquitinationEYLDRNNKFNFQGYS
HHHHCCCCCCCCCCC		45.2822817900
468UbiquitinationFQGYSQDKLGRVYAV
CCCCCHHCHHHEEEE		45.2422817900
468 (in isoform 1)Ubiquitination-45.2421890473
468 (in isoform 2)Ubiquitination-45.2421906983
504PhosphorylationQFLEGFRSFLKILTC
HHHHHHHHHHHHHHH		32.4424719451
575PhosphorylationHKAVMRCSTSFISSS
HHHHHHHCHHHHHCC		19.40-
580PhosphorylationRCSTSFISSSKTVVQ
HHCHHHHHCCCCHHH		26.92-
582PhosphorylationSTSFISSSKTVVQSC
CHHHHHCCCCHHHHC		26.09-
596UbiquitinationCGHSLETKSYRVSED
CCCCCCCCCEEECCC		35.7921963094
601PhosphorylationETKSYRVSEDLVSIH
CCCCEEECCCCEEEE		19.1823909892
606PhosphorylationRVSEDLVSIHLPLSR
EECCCCEEEECCCHH		16.1623909892
614PhosphorylationIHLPLSRTLAGLHVR
EECCCHHHHCCHHHH		19.99-
688PhosphorylationVKCREEMYDKDIIML
CCCCHHHCCCCEEEE		24.11-
706UbiquitinationASLMDPNKFLLLVLQ
HHHCCCCHHHHHHHH		42.66-
728UbiquitinationFNKTISTKDQDLIKQ
HHHHCCHHHHHHHHH		46.7532015554
764UbiquitinationPGVGNVTKEEVTMRE
CCCCCCCHHHCCHHH		47.82-
788UbiquitinationMPHSAIAKNLPENEN
CCCHHHHHCCCCCCC		53.56-
806 (in isoform 1)Ubiquitination-23.3221890473
806UbiquitinationGLENVINKVATFKKP
HHHHHHHHHHCCCCC		23.3222817900
811 (in isoform 1)Ubiquitination-54.4221890473
811UbiquitinationINKVATFKKPGVSGH
HHHHHCCCCCCCCCC		54.4221890473
812UbiquitinationNKVATFKKPGVSGHG
HHHHCCCCCCCCCCC		42.6933845483
816PhosphorylationTFKKPGVSGHGVYEL
CCCCCCCCCCCEEEC		30.8728555341
824UbiquitinationGHGVYELKDESLKDF
CCCEEECCCCCCCCC		47.7329967540
849SulfoxidationQHSKAEHMQKKRRKQ
CCHHHHHHHHHHHHH		4.7430846556
855UbiquitinationHMQKKRRKQENKDEA
HHHHHHHHHHCCCCC		67.0329967540
859UbiquitinationKRRKQENKDEALPPP
HHHHHHCCCCCCCCC		57.0832015554
901PhosphorylationVFERAIDTDSNLWTE
HHHHHCCCCCCCCHH		34.90-
944UbiquitinationVTFDFYHKASRLGSS
CCHHHHHHHHHHCHH		36.3622505724
991UbiquitinationTVKRLREKSCLIVAT
HHHHHHHCCEEEEEE		39.7829967540
998PhosphorylationKSCLIVATTSGSESI
CCEEEEEECCCCHHH		15.5927251275
999PhosphorylationSCLIVATTSGSESIK
CEEEEEECCCCHHHC		22.7327251275
999O-linked_GlycosylationSCLIVATTSGSESIK
CEEEEEECCCCHHHC		22.7328657654
1000PhosphorylationCLIVATTSGSESIKN
EEEEEECCCCHHHCC		35.6528555341
1002PhosphorylationIVATTSGSESIKNDE
EEEECCCCHHHCCCC		28.1228985074
1014AcetylationNDEITHDKEKAERKR
CCCCCCCHHHHHHHH		54.2125953088
1032UbiquitinationAARLHRQKIMAQMSA
HHHHHHHHHHHHHHH		34.1129967540
1038PhosphorylationQKIMAQMSALQKNFI
HHHHHHHHHHHHHHH		17.4728555341
1042UbiquitinationAQMSALQKNFIETHK
HHHHHHHHHHHHHHC		55.46-
1047PhosphorylationLQKNFIETHKLMYDN
HHHHHHHHHCCCCCC		21.3528348404
1049UbiquitinationKNFIETHKLMYDNTS
HHHHHHHCCCCCCCC		42.2329967540
1052PhosphorylationIETHKLMYDNTSEMP
HHHHCCCCCCCCCCC		19.2423917254
1055PhosphorylationHKLMYDNTSEMPGKE
HCCCCCCCCCCCCCC		24.1428348404
1056PhosphorylationKLMYDNTSEMPGKED
CCCCCCCCCCCCCCC		37.8528348404
1064PhosphorylationEMPGKEDSIMEEEST
CCCCCCCCCCCCCCC		25.5628348404
1070PhosphorylationDSIMEEESTPAVSDY
CCCCCCCCCCCCCCC		42.8628348404
1071PhosphorylationSIMEEESTPAVSDYS
CCCCCCCCCCCCCCC		20.6728348404
1078PhosphorylationTPAVSDYSRIALGPK
CCCCCCCCHHCCCCC		23.3827642862
1085UbiquitinationSRIALGPKRGPSVTE
CHHCCCCCCCCCCCH		69.0927667366
1093UbiquitinationRGPSVTEKEVLTCIL
CCCCCCHHHHHHHEE		43.7029967540
1122UbiquitinationVLSACVQKSTALTQH
HHHHHHHHHHHHHHC		29.40-
1179PhosphorylationFEAVQLSSQQRIHVD
HHHHHCCCCCCEEEE		38.6417525332
1231PhosphorylationDALAQLLTLARWIQT
HHHHHHHHHHHHHHH		27.2824719451
1244PhosphorylationQTVLARISGYNIRHA
HHHHHHHHCCCCCCC		29.6727966365
1302PhosphorylationILFATTIYRIGLKVP
HHHHHHHHHCCCCCC		8.2922817900
1579UbiquitinationPALLNCLKQKNTVVR
HHHHHHHHHCCCEEE		62.52-
1581UbiquitinationLLNCLKQKNTVVRYP
HHHHHHHCCCEEECC		53.66-
1593PhosphorylationRYPRKRNSLIELPDD
ECCCCCCCCCCCCCC		34.4523927012
1601PhosphorylationLIELPDDYSCLLNQA
CCCCCCCHHHHHHCH		14.5223927012
1602PhosphorylationIELPDDYSCLLNQAS
CCCCCCHHHHHHCHH		12.7927080861
1681UbiquitinationRVVLVEGKARGCAYP
EEEEEECCCCCCCCC		22.7722817900
1681 (in isoform 1)Ubiquitination-22.7721890473
1703UbiquitinationGETDPGLKRGNPLHL
CCCCCCCCCCCCCCC		65.2622505724
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 UBR1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBR1_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 UBR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOS_HUMANFOSphysical
17018293
ZN593_HUMANZNF593physical
22939629
VINC_HUMANVCLphysical
22939629
UCHL3_HUMANUCHL3physical
22939629
XPO2_HUMANCSE1Lphysical
22939629
XPO1_HUMANXPO1physical
22939629
VATA_HUMANATP6V1Aphysical
22939629
CDC6_HUMANCDC6physical
8505328
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
243800Johanson-Blizzard syndrome (JBS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBR1_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-1179, AND MASSSPECTROMETRY.
"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 THR-21, AND MASSSPECTROMETRY.
"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 THR-21, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASSSPECTROMETRY.

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