UBP34_MOUSE - dbPTM
UBP34_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP34_MOUSE
UniProt AC Q6ZQ93
Protein Name Ubiquitin carboxyl-terminal hydrolase 34
Gene Name Usp34
Organism Mus musculus (Mouse).
Sequence Length 3582
Subcellular Localization
Protein Description Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins..
Protein Sequence MCENCADLVEVLNEISDIEGGDGLQLRKEHTLKIFAYINSWTQRQCLCCFKEYKHLEIFNQVVCALINLVIAQVQVLRDQLCKHCTTINIDSTWQDESNQAEEPLSIDRECNEGNTERQKSIEKKSNSTRTCNLTEEESSKSSDPFSLWNTDEKEKLLLCVAKIFQIQFPLYTAYKHNTHPTIEDISTQESNILGAFCDMNDVEVPLHLLRYVCLFCGKNGLSLMKDCFEYGTPETLPFLIAHAFITVVSNIRIWLHIPAVMQHIIPFRTYVIRYLCKLSDQELRQSAARNMADLMWSTVKEPLDTTLCFDKESLDLAFKYFMSPTLTMRLAGLSQITNQLHTFNDVCNNESLVSDTETSIAKELADWLISNNVVEHIFGPNLHIEIIKQCQVILNFLAAEGRLSTQHIDCIWAAAQLKHCSRYIHDLFPSLIKNLDPVPLRHLLNLVSALEPGVHTEQTLYLASMLIKALWNNALAAKAQLSKQSSFASLLNTNMPIGNKKEEEELRRAAPSPWSPAASPQSSDNSDTHQSGASDIEMDEQLINRNKHVQQRLSDTEESMQGSSDETANSGEDGSSGPGSSSGHSDGSSNEVNSSHASQSAGSPGSEVQSEDIADIEALKEEEEEEEEEEEEEEEEDDEEEEDEEEDDDDDDDHGHNPAKNTCGTELRNRKLENPAGICLGESQGTSERNGTNSGTGKDLVFNTEPLPSVDNRIRMLDACAHSEDPEHGISGEVSSAHLAQGSQEACITRSGDFLGETIGNELFNCRQFIGPQHHHHHHHHHHHHHHHHHHHHHHHDGHMVDDMLSADDVSCSSSQVSAKSEKNMADFDGEESGCEEELVQINSHAELTSHLQQHLPNLASIYHEHLSQGPAVHKHQFSSNAVTDINLDNVCKKGNTLLWDIVQDDDAINLSEGLINEAEKLLCSLVCWFTDRQIRMRFIEGCLENLGNNRSVVISLRLLPKLFGTFQQFGSSYDTHWITMWAEKELNMMKLFFDNLVYYIQGIREGRQKHALYSHSAEVQVRLQFLTCVFSTLGSPDHFRLSLEQVDILWHCLVEDSECYDDALHWFLNQVRSKDQHAMGMETYKHLFLEKMPQLKPETISMTGLNLFQHLCNLARLATSAYDGGSNSELCGMDQFWGIALRAQSGDVSRAAIQYINSYYINGKTGLEKEQEFISKCMESLMIASSSLEQESHSSLTVIERGLLMLKTHLEAFRRRFAYHLRQWQIEGTGISSHLKALSDKQSLPLRVVCQPAGLPDKMTIEMYPSDQVADLRAEVTHWYENLQKEQINQQAQLQEFGQSSRKGEFPGGLMGPVRMISSGHELTTDYDEKALHELGFKDMQMVFVSLGAPRRERKGEGVQLPASCLPPPQKDNIPMLLLLQEPHLTTLFDLLEMLASFKPPSGKVAVDDSESLKCEELHLHAENLSRRVWELLMLLPTCPNMLTAFQNVSDEQSNDGLNWKELLKIKSAHKLLYALEIIEALGKPNRRIRRESTGSYSDLYPDSDDSSEDQVENSKNSWTCKFVAAGGLQQLLEIFNSAILEPKEQESWTVWQLDCLACLLKLICQFAVDPSDLDLAYHDVFAWSGIAESHRKRTWPGKSRKAAGDHAKSLHIPRLTEVFLVLVQGTSLIQRLMSVAYTYDNLAPRVLKAQSDHRSRHEVSHYSMWLLVSWAHCCSLVKSSLADSDHLQDWLKQLTLLIPETAVRHESCNGLYKLSLSGLDGGDSIHRSFLLLAASTLLKFLPDAQALKPPRIDDYEEEPLLKPGCKEYFWLLCKLVDNIHIKDASQTTLLDLDALARHLADCIRSREILDHLDGSIEDDGLSGLLRLATSVIKHKPPFKFSREGQEFLRDIFNLLFLLPSLKDRRQPKCKSHSCRAAAYDLLVEMVKGSVENYRLIHNWVMAQHMQSHAPYKWDYWPHEDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKVEEMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLMGKSDRKEGFKDVGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRDIVNPHAYKNNKWYLFNDAEVKPFDSAQLASECFGGEMTTKTYDSVTDKFMDFSFEKTHSAYMLFYKRMEPEEENGREYKFDVSSELLEWIWHDNMQFLQDKNIFEHTYFGFMWQLCSCIPSTLPDPKAVSLMTAKLSTSFVLETFIHSKEKPTMLQWIELLTKQFNNSQAACEWFLDRMADDDWWPMQILIKCPNQIVRQMFQRLCIHVIQRLRPVHAHLYLQPGMEDGSDDMDASVEDIGGRSCVTRFVRTLLLIMEHGVKPHSKHLTEYFAFLYEFAKMGEEESQFLLSLQAISTMVHFYMGTKGPENPQVEVLSEEEGEEEEEEEDILSLAEEKYRPAALEKMIALVALLVEQSRSERHLTLSQTDMAALTGGKGFPFLFQHIRDGINIRQTCNLIFSLCRYNNRLAEHIVSMLFTSIAKLTPEAANPFFKLLTMLMEFAGGPPGMPPFASYILQRIWEVIEYNPSQCLDWLAVQTPRNKLAHSWVLQNMENWVERFLLAHNYPRVRTSAAYLLVSLIPSNSFRQMFRSTRSLHIPTRDLPLSPDTTVVLHQVYNVLLGLLSRAKLYVDAAVHGTTKLVPYLSFMTYCLISKTEKLMFSTYFMDLWNLFQPKLSEPAIATNHNKQALLSFWYNVCADCPENIRLIVQNPVVTKNIAFNYILADHDDQDVVLFNRGMLPAYYGILRLCCEQSPAFTRQLASHQNIQWAFKNLTPHASQYPGAVEELFNLMQLFIAQRPDMREEELEDIKQFKKTTISCYLRCLDGRSCWTTLISAFRILLESDEDRLLVVFNRGLILMTESFNTLHMMYHEATACHVTGDLVELLSIFLSVLKSTRPYLQRKDVKQALIQWQERIEFAHKLLTLLNSYSPPELRNACIDVLKELVLLSPHDFLHTLVPFLQHNHCTYHHSNIPMSLGPYFPCRENIKLIGGKSNIRPPRPELNMCLLPTMVETSKGKDDVYDRMLLDYFFSYHQFIHLLCRVAINCEKFTETLVKLSVLVAYEGLPLHLALFPKLWTELCQTQSAMSKNCIKLLCEDPVFAEYIKCILMDERTFLNNNIVYTFMTHFLLKVQSQVFSEANCASLISTLITNLINQYQNLQSDFTNRVEISKASAALNGDLRALALLLSVHTPKQLNPALIPTLQELLNKCRTCLQQRNSLQEQEAKERKTKDDEGATPVKRRRVSSDEEHTVDSCIGDIKTETREVLTPTSTSDNETRDSSIIDPGTEQDLPSPENSSVKEYRMEGPSSFSEDGSHIRSQHAEEQSNNGRFDDCKEFKDHCSKDTTLAEDESEFPSTSISAVLSDLADLRSCDGQALSSQDPEAAVSLSCGHSRGLISHMQQHDILDTLCRTIESTIHVVTRISGKGNQAAS
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
271PhosphorylationHIIPFRTYVIRYLCK
HHHHHHHHHHHHHHH		6.9322802335
312AcetylationDTTLCFDKESLDLAF
CCEECCCHHHHHHHH		29.027970961
352PhosphorylationNDVCNNESLVSDTET
CHHCCCCCCCCCCCH		35.87-
483PhosphorylationLAAKAQLSKQSSFAS
HHHHHHHHCHHHHHH		19.3021743459
486PhosphorylationKAQLSKQSSFASLLN
HHHHHCHHHHHHHHC		31.0325521595
487PhosphorylationAQLSKQSSFASLLNT
HHHHCHHHHHHHHCC		23.4926643407
490PhosphorylationSKQSSFASLLNTNMP
HCHHHHHHHHCCCCC		31.2329233185
494PhosphorylationSFASLLNTNMPIGNK
HHHHHHCCCCCCCCH		32.6328285833
699AcetylationGTNSGTGKDLVFNTE
CCCCCCCCCCEECCC		47.9623236377
1076UbiquitinationFLNQVRSKDQHAMGM
HHHHHHCCCCCCCCH		51.33-
1182PhosphorylationFISKCMESLMIASSS
HHHHHHHHHHHHCCC		9.0629899451
1243UbiquitinationHLKALSDKQSLPLRV
HHHHHCCCCCCCEEE		38.11-
1262PhosphorylationAGLPDKMTIEMYPSD
CCCCCCEEEEEECCH		21.3722802335
1266PhosphorylationDKMTIEMYPSDQVAD
CCEEEEEECCHHHHH		6.1822802335
1414PhosphorylationVAVDDSESLKCEELH
EECCCHHHCCCHHHH		36.7623140645
1495PhosphorylationNRRIRRESTGSYSDL
CCCCCCCCCCCCCCC		35.9419060867
1496PhosphorylationRRIRRESTGSYSDLY
CCCCCCCCCCCCCCC		25.9525293948
1498PhosphorylationIRRESTGSYSDLYPD
CCCCCCCCCCCCCCC		22.8819060867
1499PhosphorylationRRESTGSYSDLYPDS
CCCCCCCCCCCCCCC		13.9325293948
1500PhosphorylationRESTGSYSDLYPDSD
CCCCCCCCCCCCCCC		23.8825293948
1503PhosphorylationTGSYSDLYPDSDDSS
CCCCCCCCCCCCCCC		15.2425293948
1506PhosphorylationYSDLYPDSDDSSEDQ
CCCCCCCCCCCCHHH		38.5225521595
1509PhosphorylationLYPDSDDSSEDQVEN
CCCCCCCCCHHHHHH		40.3925521595
1510PhosphorylationYPDSDDSSEDQVENS
CCCCCCCCHHHHHHC		52.7927087446
1517PhosphorylationSEDQVENSKNSWTCK
CHHHHHHCCCCEEHH		21.5125293948
1731PhosphorylationGGDSIHRSFLLLAAS
CCCCHHHHHHHHHHH		13.1922942356
1807UbiquitinationRHLADCIRSREILDH
HHHHHHHHHHHHHHH		35.6727667366
1994UbiquitinationSECKAYNPRPFCKTY
HHHHHCCCCCCCCEE		32.4227667366
2005UbiquitinationCKTYTMDKQPLNTGE
CCEEECCCCCCCCCC		42.8927667366
2006UbiquitinationKTYTMDKQPLNTGEQ
CEEECCCCCCCCCCC		43.3727667366
2137UbiquitinationFNMVTMMKEKVNTHF
EEHHHHCHHHCCCCC		43.49-
2139UbiquitinationMVTMMKEKVNTHFSF
HHHHCHHHCCCCCCC		34.95-
2233PhosphorylationAEVKPFDSAQLASEC
CCCCCCCHHHHHHHH		20.4920469934
2256UbiquitinationTYDSVTDKFMDFSFE
CCCHHHHHCCCCCCC		32.97-
2286NitrationEEENGREYKFDVSSE
CHHCCCEEECCCCHH		18.65-
2336PhosphorylationSTLPDPKAVSLMTAK
CCCCCHHHHHHHHHH		11.0815345747
2393PhosphorylationRMADDDWWPMQILIK
HHCCCCCCCHHHHHH		5.8617203969
2438PhosphorylationQPGMEDGSDDMDASV
CCCCCCCCCCCCCCH		42.6425338131
2525PhosphorylationNPQVEVLSEEEGEEE
CCCEEEECHHCCCCH		48.4127087446
2540PhosphorylationEEEEDILSLAEEKYR
HHHHHHHHHHHHHHC		26.3525338131
2582PhosphorylationQTDMAALTGGKGFPF
HHHHHHHHCCCCCHH		38.8817203969
3137UbiquitinationFPCRENIKLIGGKSN
CCCCCCCEECCCCCC		45.71-
3271PhosphorylationFLNNNIVYTFMTHFL
CCCCCHHHHHHHHHH		7.1722807455
3323PhosphorylationRVEISKASAALNGDL
CHHHHHHHHHHCCCH		20.1522942356
3387PhosphorylationTKDDEGATPVKRRRV
CCCCCCCCCCCCCCC		39.2025266776
3395PhosphorylationPVKRRRVSSDEEHTV
CCCCCCCCCCCCCCH		30.2025521595
3396PhosphorylationVKRRRVSSDEEHTVD
CCCCCCCCCCCCCHH		46.3025521595
3401PhosphorylationVSSDEEHTVDSCIGD
CCCCCCCCHHHHHCC		29.3221082442
3404PhosphorylationDEEHTVDSCIGDIKT
CCCCCHHHHHCCCCC		11.8725619855
3418PhosphorylationTETREVLTPTSTSDN
CCCEEECCCCCCCCC		29.6925521595
3420PhosphorylationTREVLTPTSTSDNET
CEEECCCCCCCCCCC		39.1324899341
3421PhosphorylationREVLTPTSTSDNETR
EEECCCCCCCCCCCC		27.4120469934
3422PhosphorylationEVLTPTSTSDNETRD
EECCCCCCCCCCCCC		42.4521082442
3423PhosphorylationVLTPTSTSDNETRDS
ECCCCCCCCCCCCCC		37.9025521595
3427PhosphorylationTSTSDNETRDSSIID
CCCCCCCCCCCCCCC		46.1321743459
3431PhosphorylationDNETRDSSIIDPGTE
CCCCCCCCCCCCCCC		28.0525619855
3437PhosphorylationSSIIDPGTEQDLPSP
CCCCCCCCCCCCCCC		35.5425619855
3443PhosphorylationGTEQDLPSPENSSVK
CCCCCCCCCCCCCCC		52.7425521595
3447PhosphorylationDLPSPENSSVKEYRM
CCCCCCCCCCCEECC		34.5428973931
3448PhosphorylationLPSPENSSVKEYRME
CCCCCCCCCCEECCC		49.1125521595
3452PhosphorylationENSSVKEYRMEGPSS
CCCCCCEECCCCCCC		15.0025293948
3458PhosphorylationEYRMEGPSSFSEDGS
EECCCCCCCCCCCCC		55.6717203969
3459PhosphorylationYRMEGPSSFSEDGSH
ECCCCCCCCCCCCCC		35.6117203969
3465PhosphorylationSSFSEDGSHIRSQHA
CCCCCCCCCCHHHHH		28.2317203969
3539PhosphorylationPEAAVSLSCGHSRGL
HHHHHHHHCCCHHHH		15.56-
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 UBP34_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP34_MOUSE !!
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 UBP34_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBP34_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP34_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2525, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2582, AND MASSSPECTROMETRY.

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