UBP11_HUMAN - dbPTM
UBP11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP11_HUMAN
UniProt AC P51784
Protein Name Ubiquitin carboxyl-terminal hydrolase 11
Gene Name USP11
Organism Homo sapiens (Human).
Sequence Length 963
Subcellular Localization Nucleus . Cytoplasm . Chromosome . Predominantly nuclear (PubMed:12084015, PubMed:15314155). Associates with chromatin (PubMed:20601937, PubMed:20233726).
Protein Description Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. [PubMed: 12084015]
Protein Sequence MAVAPRLFGGLCFRFRDQNPEVAVEGRLPISHSCVGCRRERTAMATVAANPAAAAAAVAAAAAVTEDREPQHEELPGLDSQWRQIENGESGRERPLRAGESWFLVEKHWYKQWEAYVQGGDQDSSTFPGCINNATLFQDEINWRLKEGLVEGEDYVLLPAAAWHYLVSWYGLEHGQPPIERKVIELPNIQKVEVYPVELLLVRHNDLGKSHTVQFSHTDSIGLVLRTARERFLVEPQEDTRLWAKNSEGSLDRLYDTHITVLDAALETGQLIIMETRKKDGTWPSAQLHVMNNNMSEEDEDFKGQPGICGLTNLGNTCFMNSALQCLSNVPQLTEYFLNNCYLEELNFRNPLGMKGEIAEAYADLVKQAWSGHHRSIVPHVFKNKVGHFASQFLGYQQHDSQELLSFLLDGLHEDLNRVKKKEYVELCDAAGRPDQEVAQEAWQNHKRRNDSVIVDTFHGLFKSTLVCPDCGNVSVTFDPFCYLSVPLPISHKRVLEVFFIPMDPRRKPEQHRLVVPKKGKISDLCVALSKHTGISPERMMVADVFSHRFYKLYQLEEPLSSILDRDDIFVYEVSGRIEAIEGSREDIVVPVYLRERTPARDYNNSYYGLMLFGHPLLVSVPRDRFTWEGLYNVLMYRLSRYVTKPNSDDEDDGDEKEDDEEDKDDVPGPSTGGSLRDPEPEQAGPSSGVTNRCPFLLDNCLGTSQWPPRRRRKQLFTLQTVNSNGTSDRTTSPEEVHAQPYIAIDWEPEMKKRYYDEVEAEGYVKHDCVGYVMKKAPVRLQECIELFTTVETLEKENPWYCPSCKQHQLATKKLDLWMLPEILIIHLKRFSYTKFSREKLDTLVEFPIRDLDFSEFVIQPQNESNPELYKYDLIAVSNHYGGMRDGHYTTFACNKDSGQWHYFDDNSVSPVNENQIESKAAYVLFYQRQDVARRLLSPAGSSGAPASPACSSPPSSEFMDVN
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
31PhosphorylationVEGRLPISHSCVGCR
EEEECCCCCCCCCCC		13.86-
33PhosphorylationGRLPISHSCVGCRRE
EECCCCCCCCCCCCC		12.05-
107UbiquitinationESWFLVEKHWYKQWE
CCEEEEEHHHHHHHH		31.7721890473
182UbiquitinationGQPPIERKVIELPNI
CCCCCEEEEEECCCC		34.47-
191UbiquitinationIELPNIQKVEVYPVE
EECCCCEEEEEEEEE		36.24-
195PhosphorylationNIQKVEVYPVELLLV
CCEEEEEEEEEEEEE		6.5120068231
241MethylationVEPQEDTRLWAKNSE
CCCCCCCCCEECCCC		40.32115919581
245AcetylationEDTRLWAKNSEGSLD
CCCCCEECCCCCCHH		49.8019608861
245UbiquitinationEDTRLWAKNSEGSLD
CCCCCEECCCCCCHH		49.8021890473
268PhosphorylationVLDAALETGQLIIME
HHHHHHHHCCEEEEE		30.95-
276PhosphorylationGQLIIMETRKKDGTW
CCEEEEEECCCCCCC		30.34-
303SumoylationSEEDEDFKGQPGICG
CCCCCCCCCCCCCCC		69.80-
355UbiquitinationFRNPLGMKGEIAEAY
CCCCCCCCHHHHHHH		52.1521890473
362PhosphorylationKGEIAEAYADLVKQA
CHHHHHHHHHHHHHH		7.6728796482
367UbiquitinationEAYADLVKQAWSGHH
HHHHHHHHHHHCCCC		41.4121890473
383UbiquitinationSIVPHVFKNKVGHFA
CHHCHHHHCCHHHHH		55.56-
383MethylationSIVPHVFKNKVGHFA
CHHCHHHHCCHHHHH		55.56115978921
385UbiquitinationVPHVFKNKVGHFASQ
HCHHHHCCHHHHHHH		50.62-
396PhosphorylationFASQFLGYQQHDSQE
HHHHHHCCCCCCHHH		13.72-
422UbiquitinationDLNRVKKKEYVELCD
HHHHHCHHHHHHHHH		48.86-
447UbiquitinationQEAWQNHKRRNDSVI
HHHHHHHHHHCCCEE		61.68-
452PhosphorylationNHKRRNDSVIVDTFH
HHHHHCCCEEEECCC		19.7928464451
493UbiquitinationVPLPISHKRVLEVFF
CCCCCCCCCEEEEEE		37.09-
503SulfoxidationLEVFFIPMDPRRKPE
EEEEEEECCCCCCHH		10.6721406390
519UbiquitinationHRLVVPKKGKISDLC
CCEECCCCCCHHHHH		60.41-
521UbiquitinationLVVPKKGKISDLCVA
EECCCCCCHHHHHHH		48.17-
531AcetylationDLCVALSKHTGISPE
HHHHHHHHCCCCCHH		46.1425953088
531UbiquitinationDLCVALSKHTGISPE
HHHHHHHHCCCCCHH		46.1421890473
584PhosphorylationRIEAIEGSREDIVVP
CEEEEECCHHHEEEE		21.5121406692
593PhosphorylationEDIVVPVYLRERTPA
HHEEEEEEEECCCCC		8.25-
603PhosphorylationERTPARDYNNSYYGL
CCCCCCCCCCCEEEH		15.6428450419
606PhosphorylationPARDYNNSYYGLMLF
CCCCCCCCEEEHHCC		18.9828450419
607PhosphorylationARDYNNSYYGLMLFG
CCCCCCCEEEHHCCC		12.0428450419
608PhosphorylationRDYNNSYYGLMLFGH
CCCCCCEEEHHCCCC		12.0128450419
640PhosphorylationNVLMYRLSRYVTKPN
HHHHHHHHHHCCCCC		16.7421406692
642PhosphorylationLMYRLSRYVTKPNSD
HHHHHHHHCCCCCCC		14.7530576142
644PhosphorylationYRLSRYVTKPNSDDE
HHHHHHCCCCCCCCC		31.6728787133
648PhosphorylationRYVTKPNSDDEDDGD
HHCCCCCCCCCCCCC		55.7728355574
664UbiquitinationKEDDEEDKDDVPGPS
CCCCCCCCCCCCCCC		60.14-
671PhosphorylationKDDVPGPSTGGSLRD
CCCCCCCCCCCCCCC		45.6721659604
672PhosphorylationDDVPGPSTGGSLRDP
CCCCCCCCCCCCCCC		49.0121659604
675PhosphorylationPGPSTGGSLRDPEPE
CCCCCCCCCCCCCHH		22.9021659604
677MethylationPSTGGSLRDPEPEQA
CCCCCCCCCCCHHHC		60.17115919585
714UbiquitinationWPPRRRRKQLFTLQT
CCCCHHHHCCEEEEE		49.9321890473
718PhosphorylationRRRKQLFTLQTVNSN
HHHHCCEEEEEECCC		26.9229083192
721PhosphorylationKQLFTLQTVNSNGTS
HCCEEEEEECCCCCC		25.4329083192
724PhosphorylationFTLQTVNSNGTSDRT
EEEEEECCCCCCCCC		32.0929083192
727PhosphorylationQTVNSNGTSDRTTSP
EEECCCCCCCCCCCH		31.5329083192
728PhosphorylationTVNSNGTSDRTTSPE
EECCCCCCCCCCCHH		26.8829083192
731PhosphorylationSNGTSDRTTSPEEVH
CCCCCCCCCCHHHHC		36.2926074081
732PhosphorylationNGTSDRTTSPEEVHA
CCCCCCCCCHHHHCC		43.0826074081
733PhosphorylationGTSDRTTSPEEVHAQ
CCCCCCCCHHHHCCC		29.6925159151
742PhosphorylationEEVHAQPYIAIDWEP
HHHCCCCCEEECCCH		7.3029523821
752UbiquitinationIDWEPEMKKRYYDEV
ECCCHHHHHHHCCHH		32.22-
753UbiquitinationDWEPEMKKRYYDEVE
CCCHHHHHHHCCHHC		44.30-
756PhosphorylationPEMKKRYYDEVEAEG
HHHHHHHCCHHCCCC		15.0627642862
766UbiquitinationVEAEGYVKHDCVGYV
HCCCCEECCCHHHHH		25.83-
772PhosphorylationVKHDCVGYVMKKAPV
ECCCHHHHHHHHCCC		4.1327642862
775UbiquitinationDCVGYVMKKAPVRLQ
CHHHHHHHHCCCCHH		35.42-
776UbiquitinationCVGYVMKKAPVRLQE
HHHHHHHHCCCCHHH		39.57-
806UbiquitinationPWYCPSCKQHQLATK
CCCCCCHHHHCCCCC		55.9721890473
813UbiquitinationKQHQLATKKLDLWML
HHHCCCCCCCCHHHC		45.81-
835UbiquitinationLKRFSYTKFSREKLD
HHCCCCCCCCHHHHH		32.8621890473
840UbiquitinationYTKFSREKLDTLVEF
CCCCCHHHHHHEEEE		51.0221890473
865PhosphorylationVIQPQNESNPELYKY
EECCCCCCCHHHEEE		66.2919845377
871UbiquitinationESNPELYKYDLIAVS
CCCHHHEEEEEEEEE		44.93-
896UbiquitinationYTTFACNKDSGQWHY
EEEEEEECCCCCEEE		53.83-
898PhosphorylationTFACNKDSGQWHYFD
EEEEECCCCCEEECC		34.2029978859
903PhosphorylationKDSGQWHYFDDNSVS
CCCCCEEECCCCCCC		13.0229978859
905PhosphorylationSGQWHYFDDNSVSPV
CCCEEECCCCCCCCC		47.1918669648
908PhosphorylationWHYFDDNSVSPVNEN
EEECCCCCCCCCCHH		30.8529978859
910PhosphorylationYFDDNSVSPVNENQI
ECCCCCCCCCCHHHH		23.9729978859
919PhosphorylationVNENQIESKAAYVLF
CCHHHHHHHHEEEEE		29.2629978859
920UbiquitinationNENQIESKAAYVLFY
CHHHHHHHHEEEEEC		25.01-
923PhosphorylationQIESKAAYVLFYQRQ
HHHHHHEEEEECCHH		11.5328152594
927PhosphorylationKAAYVLFYQRQDVAR
HHEEEEECCHHHHHH		9.9129978859
938PhosphorylationDVARRLLSPAGSSGA
HHHHHHHCCCCCCCC		19.8028674151
942PhosphorylationRLLSPAGSSGAPASP
HHHCCCCCCCCCCCC		27.9228674151
943PhosphorylationLLSPAGSSGAPASPA
HHCCCCCCCCCCCCC		37.7530177828
948PhosphorylationGSSGAPASPACSSPP
CCCCCCCCCCCCCCC		16.3927362937
952PhosphorylationAPASPACSSPPSSEF
CCCCCCCCCCCCHHH		48.2427362937
953PhosphorylationPASPACSSPPSSEFM
CCCCCCCCCCCHHHC		40.4921712546
956PhosphorylationPACSSPPSSEFMDVN
CCCCCCCCHHHCCCC		45.9828674151
957PhosphorylationACSSPPSSEFMDVN-
CCCCCCCHHHCCCC-		40.4028674151
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 UBP11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP11_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 UBP11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETB1_HUMANSETDB1physical
16169070
XIAP_HUMANXIAPphysical
19615732
CDC27_HUMANCDC27physical
19615732
CISY_HUMANCSphysical
19615732
IF4B_HUMANEIF4Bphysical
19615732
SYFA_HUMANFARSAphysical
19615732
MRE11_HUMANMRE11Aphysical
19615732
MYO6_HUMANMYO6physical
19615732
RPAB1_HUMANPOLR2Ephysical
19615732
PKN2_HUMANPKN2physical
19615732
P53_HUMANTP53physical
19615732
UBP4_HUMANUSP4physical
19615732
ZNF24_HUMANZNF24physical
19615732
UBP7_HUMANUSP7physical
19615732
RAE1L_HUMANRAE1physical
19615732
BUB3_HUMANBUB3physical
19615732
TRIPC_HUMANTRIP12physical
19615732
TCAL1_HUMANTCEAL1physical
19615732
RPAC1_HUMANPOLR1Cphysical
19615732
KEAP1_HUMANKEAP1physical
19615732
NU153_HUMANNUP153physical
19615732
RAD50_HUMANRAD50physical
19615732
MPP9_HUMANMPHOSPH9physical
19615732
ARHG8_HUMANNET1physical
19615732
NS1BP_HUMANIVNS1ABPphysical
19615732
MYCB2_HUMANMYCBP2physical
19615732
K0930_HUMANKIAA0930physical
19615732
RPA1_HUMANPOLR1Aphysical
19615732
SI1L1_HUMANSIPA1L1physical
19615732
GGYF2_HUMANGIGYF2physical
19615732
S61A1_HUMANSEC61A1physical
19615732
GTSE1_HUMANGTSE1physical
19615732
TCAL4_HUMANTCEAL4physical
19615732
ATD3B_HUMANATAD3Bphysical
19615732
RPA2_HUMANPOLR1Bphysical
19615732
PRC2B_HUMANPRRC2Bphysical
19615732
SPRY3_HUMANSPRYD3physical
19615732
OSBL9_HUMANOSBPL9physical
19615732
OSB10_HUMANOSBPL10physical
19615732
ADIP_HUMANSSX2IPphysical
19615732
TCAL2_HUMANTCEAL2physical
19615732
AMOT_HUMANAMOTphysical
19615732
PGAM5_HUMANPGAM5physical
19615732
KCTD6_HUMANKCTD6physical
19615732
FBSP1_HUMANFBXO45physical
19615732
OTUD1_HUMANOTUD1physical
19615732
BRCA2_HUMANBRCA2physical
15314155
PCGF2_HUMANPCGF2physical
20601937
BMI1_HUMANBMI1physical
20601937
RING1_HUMANRING1physical
20601937
RING2_HUMANRNF2physical
20601937
CBX8_HUMANCBX8physical
20601937
UBP7_HUMANUSP7physical
20601937
UBP11_HUMANUSP11physical
22001210
UBP7_HUMANUSP7physical
22411829
UHRF1_HUMANUHRF1physical
22411829
UBC_HUMANUBCphysical
22195557
WAP53_HUMANWRAP53physical
22939629
XPC_HUMANXPCphysical
22939629
CTNA1_HUMANCTNNA1physical
22863883
IF4B_HUMANEIF4Bphysical
22863883
GARS_HUMANGARSphysical
22863883
HS105_HUMANHSPH1physical
22863883
ANM3_HUMANPRMT3physical
22863883
SC23A_HUMANSEC23Aphysical
22863883
XPO7_HUMANXPO7physical
22863883
P53_HUMANTP53physical
25471832
TRI27_HUMANTRIM27physical
26496610
ELOB_HUMANTCEB2physical
26496610
UBA1_HUMANUBA1physical
26496610
MOGS_HUMANMOGSphysical
26496610
SEM3B_HUMANSEMA3Bphysical
26496610
UBP7_HUMANUSP7physical
26496610
CNOT8_HUMANCNOT8physical
26496610
TCAL1_HUMANTCEAL1physical
26496610
ESPL1_HUMANESPL1physical
26496610
DD19B_HUMANDDX19Bphysical
26496610
URFB1_HUMANUHRF1BP1physical
26496610
UB2Q1_HUMANUBE2Q1physical
26496610
PCNP_HUMANPCNPphysical
26496610
TCAL4_HUMANTCEAL4physical
26496610
ZN598_HUMANZNF598physical
26496610
EMSA1_HUMANELMSAN1physical
26496610
H2AX_HUMANH2AFXphysical
26507658
SUMO2_HUMANSUMO2physical
25969536
PALB2_HUMANPALB2physical
26649820
PML_HUMANPMLphysical
24487962
VGLL4_HUMANVGLL4physical
28042509
SPTA1_HUMANSPTA1physical
28040451
XRCC5_HUMANXRCC5physical
28040451
XIAP_HUMANXIAPphysical
28040451
EFHD2_HUMANEFHD2physical
28040451
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 UBP11_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-948 AND SER-953, ANDMASS SPECTROMETRY.

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