UBR2_HUMAN - dbPTM
UBR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBR2_HUMAN
UniProt AC Q8IWV8
Protein Name E3 ubiquitin-protein ligase UBR2
Gene Name UBR2
Organism Homo sapiens (Human).
Sequence Length 1755
Subcellular Localization Nucleus. Associated with chromatin during meiosis.
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. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (By similarity). Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retranstoposon mobilization (By similarity)..
Protein Sequence MASELEPEVQAIDRSLLECSAEEIAGKWLQATDLTREVYQHLAHYVPKIYCRGPNPFPQKEDMLAQHVLLGPMEWYLCGEDPAFGFPKLEQANKPSHLCGRVFKVGEPTYSCRDCAVDPTCVLCMECFLGSIHRDHRYRMTTSGGGGFCDCGDTEAWKEGPYCQKHELNTSEIEEEEDPLVHLSEDVIARTYNIFAITFRYAVEILTWEKESELPADLEMVEKSDTYYCMLFNDEVHTYEQVIYTLQKAVNCTQKEAIGFATTVDRDGRRSVRYGDFQYCEQAKSVIVRNTSRQTKPLKVQVMHSSIVAHQNFGLKLLSWLGSIIGYSDGLRRILCQVGLQEGPDGENSSLVDRLMLSDSKLWKGARSVYHQLFMSSLLMDLKYKKLFAVRFAKNYQQLQRDFMEDDHERAVSVTALSVQFFTAPTLARMLITEENLMSIIIKTFMDHLRHRDAQGRFQFERYTALQAFKFRRVQSLILDLKYVLISKPTEWSDELRQKFLEGFDAFLELLKCMQGMDPITRQVGQHIEMEPEWEAAFTLQMKLTHVISMMQDWCASDEKVLIEAYKKCLAVLMQCHGGYTDGEQPITLSICGHSVETIRYCVSQEKVSIHLPVSRLLAGLHVLLSKSEVAYKFPELLPLSELSPPMLIEHPLRCLVLCAQVHAGMWRRNGFSLVNQIYYYHNVKCRREMFDKDVVMLQTGVSMMDPNHFLMIMLSRFELYQIFSTPDYGKRFSSEITHKDVVQQNNTLIEEMLYLIIMLVGERFSPGVGQVNATDEIKREIIHQLSIKPMAHSELVKSLPEDENKETGMESVIEAVAHFKKPGLTGRGMYELKPECAKEFNLYFYHFSRAEQSKAEEAQRKLKRQNREDTALPPPVLPPFCPLFASLVNILQSDVMLCIMGTILQWAVEHNGYAWSESMLQRVLHLIGMALQEEKQHLENVTEEHVVTFTFTQKISKPGEAPKNSPSILAMLETLQNAPYLEVHKDMIRWILKTFNAVKKMRESSPTSPVAETEGTIMEESSRDKDKAERKRKAEIARLRREKIMAQMSEMQRHFIDENKELFQQTLELDASTSAVLDHSPVASDMTLTALGPAQTQVPEQRQFVTCILCQEEQEVKVESRAMVLAAFVQRSTVLSKNRSKFIQDPEKYDPLFMHPDLSCGTHTSSCGHIMHAHCWQRYFDSVQAKEQRRQQRLRLHTSYDVENGEFLCPLCECLSNTVIPLLLPPRNIFNNRLNFSDQPNLTQWIRTISQQIKALQFLRKEESTPNNASTKNSENVDELQLPEGFRPDFRPKIPYSESIKEMLTTFGTATYKVGLKVHPNEEDPRVPIMCWGSCAYTIQSIERILSDEDKPLFGPLPCRLDDCLRSLTRFAAAHWTVASVSVVQGHFCKLFASLVPNDSHEELPCILDIDMFHLLVGLVLAFPALQCQDFSGISLGTGDLHIFHLVTMAHIIQILLTSCTEENGMDQENPPCEEESAVLALYKTLHQYTGSALKEIPSGWHLWRSVRAGIMPFLKCSALFFHYLNGVPSPPDIQVPGTSHFEHLCSYLSLPNNLICLFQENSEIMNSLIESWCRNSEVKRYLEGERDAIRYPRESNKLINLPEDYSSLINQASNFSCPKSGGDKSRAPTLCLVCGSLLCSQSYCCQTELEGEDVGACTAHTYSCGSGVGIFLRVRECQVLFLAGKTKGCFYSPPYLDDYGETDQGLRRGNPLHLCKERFKKIQKLWHQHSVTEEIGHAQEANQTLVGIDWQHL
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------MASELEPEV
------CCCCCHHHH		24.0222223895
3Phosphorylation-----MASELEPEVQ
-----CCCCCHHHHH		55.3528985074
27UbiquitinationSAEEIAGKWLQATDL
CHHHHHHHHHHHHHH		35.39-
48UbiquitinationHLAHYVPKIYCRGPN
HHHHHCCCCEECCCC		35.94-
94UbiquitinationPKLEQANKPSHLCGR
CCHHHCCCCCHHCCC		51.41-
104UbiquitinationHLCGRVFKVGEPTYS
HHCCCEEECCCCCCC		46.61-
110PhosphorylationFKVGEPTYSCRDCAV
EECCCCCCCHHHCCC		19.25-
141PhosphorylationRDHRYRMTTSGGGGF
CCCCCEEEECCCCCC		14.60-
142PhosphorylationDHRYRMTTSGGGGFC
CCCCEEEECCCCCCC		18.94-
143PhosphorylationHRYRMTTSGGGGFCD
CCCEEEECCCCCCCC		26.69-
154PhosphorylationGFCDCGDTEAWKEGP
CCCCCCCCHHHHCCC		16.94-
170PhosphorylationCQKHELNTSEIEEEE
CCCCCCCHHHCCCCC		40.1221712546
171PhosphorylationQKHELNTSEIEEEED
CCCCCCHHHCCCCCC		35.1921712546
224PhosphorylationDLEMVEKSDTYYCML
CHHHHHCCCCEEEEE		22.98-
255UbiquitinationKAVNCTQKEAIGFAT
HHHCCCHHHHHCEEE		30.84-
263PhosphorylationEAIGFATTVDRDGRR
HHHCEEEEECCCCCC		19.5817081983
274PhosphorylationDGRRSVRYGDFQYCE
CCCCEEECCCHHHHH		20.92-
283 (in isoform 3)Ubiquitination-5.4721890473
284UbiquitinationFQYCEQAKSVIVRNT
HHHHHHCCEEEEECC		44.97-
325 (in isoform 3)Ubiquitination-4.5421890473
326 (in isoform 3)Ubiquitination-17.7721890473
328PhosphorylationLGSIIGYSDGLRRIL
HHHHHCCCHHHHHHH		21.71-
413 (in isoform 4)Phosphorylation-16.8622210691
418 (in isoform 4)Phosphorylation-16.0622210691
439 (in isoform 4)Phosphorylation-17.5022210691
443UbiquitinationNLMSIIIKTFMDHLR
HHHHHHHHHHHHHHH		25.8721906983
443 (in isoform 1)Ubiquitination-25.8721890473
443 (in isoform 4)Ubiquitination-25.8721890473
498 (in isoform 3)Ubiquitination-54.1821890473
581PhosphorylationMQCHGGYTDGEQPIT
HHHCCCCCCCCCCEE		40.58-
716PhosphorylationHFLMIMLSRFELYQI
HHHHHHHHHHHHHHH		19.9723401153
734PhosphorylationPDYGKRFSSEITHKD
CCCCCCCCCCCCHHH		30.9730108239
735PhosphorylationDYGKRFSSEITHKDV
CCCCCCCCCCCHHHH		30.2430108239
738PhosphorylationKRFSSEITHKDVVQQ
CCCCCCCCHHHHHHH		20.8728176443
748PhosphorylationDVVQQNNTLIEEMLY
HHHHHCCCHHHHHHH		36.3424043423
755PhosphorylationTLIEEMLYLIIMLVG
CHHHHHHHHHHHHHC		8.4424043423
779UbiquitinationVNATDEIKREIIHQL
CCCCHHHHHHHHHHH		41.7621906983
779 (in isoform 1)Ubiquitination-41.7621890473
779 (in isoform 4)Ubiquitination-41.7621890473
789UbiquitinationIIHQLSIKPMAHSEL
HHHHHCCCCCCCHHH		25.93-
798UbiquitinationMAHSELVKSLPEDEN
CCCHHHHHCCCCCCC		59.92-
821UbiquitinationIEAVAHFKKPGLTGR
HHHHHHCCCCCCCCC		48.46-
821 (in isoform 1)Ubiquitination-48.4621890473
821 (in isoform 4)Ubiquitination-48.4621890473
822UbiquitinationEAVAHFKKPGLTGRG
HHHHHCCCCCCCCCC		43.29-
822 (in isoform 1)Ubiquitination-43.2921890473
822 (in isoform 4)Ubiquitination-43.2921890473
826PhosphorylationHFKKPGLTGRGMYEL
HCCCCCCCCCCCEEC		30.65-
844PhosphorylationCAKEFNLYFYHFSRA
HHHHCCEEEEECHHH		11.82-
994UbiquitinationDMIRWILKTFNAVKK
HHHHHHHHHHHHHHH		41.7721890473
994 (in isoform 1)Ubiquitination-41.7721890473
994 (in isoform 4)Ubiquitination-41.7721890473
1005PhosphorylationAVKKMRESSPTSPVA
HHHHHHHCCCCCCCC		31.1120044836
1006PhosphorylationVKKMRESSPTSPVAE
HHHHHHCCCCCCCCC		27.6920044836
1008PhosphorylationKMRESSPTSPVAETE
HHHHCCCCCCCCCCC		47.8420044836
1009PhosphorylationMRESSPTSPVAETEG
HHHCCCCCCCCCCCC		22.2925159151
1014PhosphorylationPTSPVAETEGTIMEE
CCCCCCCCCCCCCCC		29.9430108239
1017PhosphorylationPVAETEGTIMEESSR
CCCCCCCCCCCCCCC		15.7723186163
1022PhosphorylationEGTIMEESSRDKDKA
CCCCCCCCCCCCHHH		19.8420044836
1023PhosphorylationGTIMEESSRDKDKAE
CCCCCCCCCCCHHHH		48.0225159151
1044UbiquitinationIARLRREKIMAQMSE
HHHHHHHHHHHHHHH		35.65-
1050PhosphorylationEKIMAQMSEMQRHFI
HHHHHHHHHHHHHCC		20.1728555341
1073PhosphorylationQTLELDASTSAVLDH
HHHHCCCCCCHHHCC		23.6728348404
1074PhosphorylationTLELDASTSAVLDHS
HHHCCCCCCHHHCCC		23.5628348404
1075PhosphorylationLELDASTSAVLDHSP
HHCCCCCCHHHCCCC		17.5528348404
1081PhosphorylationTSAVLDHSPVASDMT
CCHHHCCCCCCCCCE		22.2728348404
1090PhosphorylationVASDMTLTALGPAQT
CCCCCEEEECCCCCC		15.6328348404
1133PhosphorylationLAAFVQRSTVLSKNR
HHHHHHHHHHHCCCH		13.0329978859
1134PhosphorylationAAFVQRSTVLSKNRS
HHHHHHHHHHCCCHH		27.8829978859
1137PhosphorylationVQRSTVLSKNRSKFI
HHHHHHHCCCHHHHC		24.4529978859
1141PhosphorylationTVLSKNRSKFIQDPE
HHHCCCHHHHCCCHH		41.1129038488
1142UbiquitinationVLSKNRSKFIQDPEK
HHCCCHHHHCCCHHH		43.16-
1187UbiquitinationYFDSVQAKEQRRQQR
HHHHHHHHHHHHHHH		36.9722053931
1187 (in isoform 1)Ubiquitination-36.9721890473
1187 (in isoform 4)Ubiquitination-36.9721890473
1255UbiquitinationRTISQQIKALQFLRK
HHHHHHHHHHHHHHH		38.412189047
1255 (in isoform 1)Ubiquitination-38.4121890473
1255 (in isoform 4)Ubiquitination-38.4121890473
1265PhosphorylationQFLRKEESTPNNAST
HHHHHCCCCCCCCCC		50.7028985074
1266PhosphorylationFLRKEESTPNNASTK
HHHHCCCCCCCCCCC		33.06-
1273UbiquitinationTPNNASTKNSENVDE
CCCCCCCCCCCCCCC		56.85-
1294UbiquitinationFRPDFRPKIPYSESI
CCCCCCCCCCCCHHH		52.65-
1306PhosphorylationESIKEMLTTFGTATY
HHHHHHHHHHCCEEE		20.8324043423
1307PhosphorylationSIKEMLTTFGTATYK
HHHHHHHHHCCEEEE		18.9924043423
1310PhosphorylationEMLTTFGTATYKVGL
HHHHHHCCEEEEEEC		16.1924043423
1312PhosphorylationLTTFGTATYKVGLKV
HHHHCCEEEEEECEE		24.5824043423
1313PhosphorylationTTFGTATYKVGLKVH
HHHCCEEEEEECEEC		10.9524043423
1339PhosphorylationCWGSCAYTIQSIERI
EECCHHHHHHHHHHH		8.2620068231
1352UbiquitinationRILSDEDKPLFGPLP
HHHCCCCCCCCCCCC		41.3922053931
1352 (in isoform 4)Ubiquitination-41.3921890473
1496UbiquitinationQYTGSALKEIPSGWH
HHHCHHHHCCCCCHH		54.00-
1599UbiquitinationRYPRESNKLINLPED
CCCHHHCCCCCCCHH		61.08-
1607PhosphorylationLINLPEDYSSLINQA
CCCCCHHHHHHHHHH		9.86-
1621UbiquitinationASNFSCPKSGGDKSR
HHCCCCCCCCCCCCC		67.09-
1687UbiquitinationQVLFLAGKTKGCFYS
EEEEEECCCCCCCCC		41.26-
1689UbiquitinationLFLAGKTKGCFYSPP
EEEECCCCCCCCCCC		58.11-
1693PhosphorylationGKTKGCFYSPPYLDD
CCCCCCCCCCCCCCC		25.0923532336
1697PhosphorylationGCFYSPPYLDDYGET
CCCCCCCCCCCCCCC		26.5823532336
1701PhosphorylationSPPYLDDYGETDQGL
CCCCCCCCCCCCHHH		19.2727642862
1718UbiquitinationGNPLHLCKERFKKIQ
CCHHHHHHHHHHHHH		59.28-
1732PhosphorylationQKLWHQHSVTEEIGH
HHHHHHCCCHHHCCC		24.9424719451
1734PhosphorylationLWHQHSVTEEIGHAQ
HHHHCCCHHHCCCHH		30.8028450419
1746PhosphorylationHAQEANQTLVGIDWQ
CHHHHHCEEEECCCC		24.1828450419
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 UBR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBR2_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 UBR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A2C_HUMANHIST2H2ACphysical
20080676
UBE2B_HUMANUBE2Bphysical
20080676
UBE2Z_HUMANUBE2Zphysical
21816346
H2A2C_HUMANHIST2H2ACphysical
22616001
UBE2H_HUMANUBE2Hphysical
22616001
AMD_HUMANPAMphysical
26186194
PXDC2_HUMANPLXDC2physical
26186194
CLCC1_HUMANCLCC1physical
25582440
MET15_HUMANMETTL15physical
25582440
P5CS_HUMANALDH18A1physical
25582440
EPIPL_HUMANEPPK1physical
25582440
PDP2_HUMANPDP2physical
25582440
EPHA7_HUMANEPHA7physical
25582440
SNX18_HUMANSNX18physical
25582440
NDUS3_HUMANNDUFS3physical
25582440
UBE2A_HUMANUBE2Aphysical
25582440
UBE2B_HUMANUBE2Bphysical
25582440
UBE2A_HUMANUBE2Aphysical
26344197
PXDC2_HUMANPLXDC2physical
28514442
AMD_HUMANPAMphysical
28514442
GFAP_HUMANGFAPphysical
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 UBR2_HUMAN

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Related Literatures of Post-Translational Modification

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