UBP21_HUMAN - dbPTM
UBP21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP21_HUMAN
UniProt AC Q9UK80
Protein Name Ubiquitin carboxyl-terminal hydrolase 21
Gene Name USP21
Organism Homo sapiens (Human).
Sequence Length 565
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates. [PubMed: 10799498 Deubiquitinates BAZ2A/TIP5 leading to its stabilization]
Protein Sequence MPQASEHRLGRTREPPVNIQPRVGSKLPFAPRARSKERRNPASGPNPMLRPLPPRPGLPDERLKKLELGRGRTSGPRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLFSIRTEPPASHGSFHMISARSSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILANGPVPSPPRRGGALLEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPPRCL
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
25PhosphorylationNIQPRVGSKLPFAPR
CCCCCCCCCCCCCCC
28.3228674151
93PhosphorylationHGVPLPGSPPPTVAL
CCCCCCCCCCCCEEE
32.0927794612
97PhosphorylationLPGSPPPTVALPLPS
CCCCCCCCEEECCCC
24.9628450419
97UbiquitinationLPGSPPPTVALPLPS
CCCCCCCCEEECCCC
24.9622817900
98UbiquitinationPGSPPPTVALPLPSR
CCCCCCCEEECCCCC
6.7622817900
104UbiquitinationTVALPLPSRTNLARS
CEEECCCCCCCHHHC
60.4622817900
104PhosphorylationTVALPLPSRTNLARS
CEEECCCCCCCHHHC
60.4624117733
106PhosphorylationALPLPSRTNLARSKS
EECCCCCCCHHHCCC
38.63-
111PhosphorylationSRTNLARSKSVSSGD
CCCCHHHCCCCCCCC
24.5529083192
113AcetylationTNLARSKSVSSGDLR
CCHHHCCCCCCCCCC
28.6019413330
113PhosphorylationTNLARSKSVSSGDLR
CCHHHCCCCCCCCCC
28.6030576142
115PhosphorylationLARSKSVSSGDLRPM
HHHCCCCCCCCCCCC
35.3828450419
116PhosphorylationARSKSVSSGDLRPMG
HHCCCCCCCCCCCCE
33.8828450419
132PhosphorylationALGGHRGTGELGAAL
EECCCCCCHHHHHHH
27.6919413330
140PhosphorylationGELGAALSRLALRPE
HHHHHHHHHHHHCCC
22.1119413330
174PhosphorylationPTLFSIRTEPPASHG
CCEEEEECCCCCCCC
51.6927251275
179PhosphorylationIRTEPPASHGSFHMI
EECCCCCCCCCEEEE
33.8727251275
182PhosphorylationEPPASHGSFHMISAR
CCCCCCCCEEEEECC
13.4227251275
204PhosphorylationDDKMAHHTLLLGSGH
CCCHHCEEEEECCCC
14.8322210691
222UbiquitinationRNLGNTCFLNAVLQC
HHCCCCHHHHHHHHH
5.7722817900
223UbiquitinationNLGNTCFLNAVLQCL
HCCCCHHHHHHHHHH
4.3522817900
229UbiquitinationFLNAVLQCLSSTRPL
HHHHHHHHHHCCCCH
3.3022817900
289UbiquitinationRFRAVFQKYVPSFSG
HHHHHHHHHCCCCCC
36.43-
290PhosphorylationFRAVFQKYVPSFSGY
HHHHHHHHCCCCCCC
13.55-
297PhosphorylationYVPSFSGYSQQDAQE
HCCCCCCCCHHHHHH
11.34-
335PhosphorylationLANGPVPSPPRRGGA
CCCCCCCCCCCCCCC
48.0126091039
362PhosphorylationANLMWKRYLEREDSK
HHHHHHHHHHHCCCH
14.8026074081
368PhosphorylationRYLEREDSKIVDLFV
HHHHHCCCHHHHHHH
21.3826074081
379UbiquitinationDLFVGQLKSCLKCQA
HHHHHHHHHHHHCCC
31.10-
389PhosphorylationLKCQACGYRSTTFEV
HHCCCCCCCCCEEEE
10.9830576142
392PhosphorylationQACGYRSTTFEVFCD
CCCCCCCCEEEEEEE
26.8930576142
393PhosphorylationACGYRSTTFEVFCDL
CCCCCCCEEEEEEEE
21.0330576142
406UbiquitinationDLSLPIPKKGFAGGK
EECCCCCCCCCCCCC
67.2722817900
407 (in isoform 3)Ubiquitination-54.6421906983
407 (in isoform 1)Ubiquitination-54.6421906983
407UbiquitinationLSLPIPKKGFAGGKV
ECCCCCCCCCCCCCE
54.6421906983
413 (in isoform 3)Ubiquitination-27.9421906983
413 (in isoform 1)Ubiquitination-27.9421906983
413UbiquitinationKKGFAGGKVSLRDCF
CCCCCCCCEEHHHHH
27.9422817900
435UbiquitinationELESENAPVCDRCRQ
HHHCCCCCCCHHHHH
38.5622817900
436UbiquitinationLESENAPVCDRCRQK
HHCCCCCCCHHHHHH
5.0122817900
442UbiquitinationPVCDRCRQKTRSTKK
CCCHHHHHHCCCCCC
55.9122817900
451PhosphorylationTRSTKKLTVQRFPRI
CCCCCCCHHHHCCCE
24.3824719451
475UbiquitinationASRGSIKKSSVGVDF
CCCCCCCHHCCCCCC
46.4229967540
499PhosphorylationFASDKAGSPVYQLYA
HCCCCCCCCHHHHHH
18.9524043423
502PhosphorylationDKAGSPVYQLYALCN
CCCCCCHHHHHHHHC
9.0024043423
504UbiquitinationAGSPVYQLYALCNHS
CCCCHHHHHHHHCCC
1.1629967540
505PhosphorylationGSPVYQLYALCNHSG
CCCHHHHHHHHCCCC
5.0824043423
511PhosphorylationLYALCNHSGSVHYGH
HHHHHCCCCCCEEEE
20.8324043423
513PhosphorylationALCNHSGSVHYGHYT
HHHCCCCCCEEEEEE
14.5624043423
516PhosphorylationNHSGSVHYGHYTALC
CCCCCCEEEEEEEEE
11.9324043423
519PhosphorylationGSVHYGHYTALCRCQ
CCCEEEEEEEEEECC
6.8524043423
520PhosphorylationSVHYGHYTALCRCQT
CCEEEEEEEEEECCC
13.8924043423
538PhosphorylationVYNDSRVSPVSENQV
EECCCCCCCCCHHHC
20.62-

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
538SPhosphorylationKinaseMAPK14Q16539
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP21_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 UBP21_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MARK2_HUMANMARK2physical
19615732
FUCO_HUMANFUCA1physical
19615732
MARK1_HUMANMARK1physical
19615732
MARK3_HUMANMARK3physical
19615732
PPIB_HUMANPPIBphysical
19615732
KPCI_HUMANPRKCIphysical
19615732
UCHL1_HUMANUCHL1physical
19615732
UTRO_HUMANUTRNphysical
19615732
RBM8A_HUMANRBM8Aphysical
19615732
UBP20_HUMANUSP20physical
19615732
ANR28_HUMANANKRD28physical
19615732
PP6R3_HUMANPPP6R3physical
19615732
BEND3_HUMANBEND3physical
19615732
MARK4_HUMANMARK4physical
19615732
REN3B_HUMANUPF3Bphysical
19615732
UBP48_HUMANUSP48physical
19615732
RBM45_HUMANRBM45physical
19615732
RIPK1_HUMANRIPK1physical
19910467
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
TRAF6_HUMANTRAF6physical
20622874
XPO1_HUMANXPO1physical
21888622
UBC_HUMANUBCphysical
22195557
ISG15_HUMANISG15physical
21399617
UBC_HUMANUBCphysical
21399617
MARK2_HUMANMARK2physical
22298430
MAP4_HUMANMAP4physical
22298430
ARHG2_HUMANARHGEF2physical
22298430
CKAP5_HUMANCKAP5physical
22298430
MARK3_HUMANMARK3physical
22298430
UBC_HUMANUBCphysical
22298430
MARK1_HUMANMARK1physical
22298430
UBP20_HUMANUSP20physical
22626734
UBP51_HUMANUSP51physical
22626734
ATX3_HUMANATXN3physical
22626734
UBP7_HUMANUSP7physical
22626734
STABP_HUMANSTAMBPphysical
22626734
OTUB1_HUMANOTUB1physical
22626734
JOS1_HUMANJOSD1physical
22626734
UCHL3_HUMANUCHL3physical
22626734
UBP8_HUMANUSP8physical
22626734
UBP21_HUMANUSP21physical
22626734
OTUB2_HUMANOTUB2physical
22626734
UBP33_HUMANUSP33physical
22626734
UBP15_HUMANUSP15physical
22626734
UBP28_HUMANUSP28physical
22626734
ESPL1_HUMANESPL1physical
22626734
SENP8_HUMANSENP8physical
22626734
UBP14_HUMANUSP14physical
22626734
UBP2_HUMANUSP2physical
22626734
BAP1_HUMANBAP1physical
22626734
OTU1_HUMANYOD1physical
22626734
UCHL1_HUMANUCHL1physical
22626734
UBC_HUMANUBCphysical
22626734
SENP3_HUMANSENP3physical
22626734
UBP4_HUMANUSP4physical
22626734
CBLC_HUMANCBLCphysical
23105109
CBL_HUMANCBLphysical
23105109
TRI23_HUMANTRIM23physical
23105109
R144A_HUMANRNF144Aphysical
23105109
LRSM1_HUMANLRSAM1physical
23105109
HOIL1_HUMANRBCK1physical
23105109
TRIM8_HUMANTRIM8physical
23105109
PCGF6_HUMANPCGF6physical
23105109
TRIM5_HUMANTRIM5physical
23105109
RN185_HUMANRNF185physical
23105109
TRIM9_HUMANTRIM9physical
23105109
DTX3_HUMANDTX3physical
23105109
UBC_HUMANUBCphysical
23287719
GATA3_HUMANGATA3physical
23395819
DDX58_HUMANDDX58physical
24493797
IFIH1_HUMANIFIH1physical
24493797
DHX58_HUMANDHX58physical
24493797
IL33_HUMANIL33physical
25197364
H2A2A_HUMANHIST2H2AA3physical
21179169
K1C40_HUMANKRT40physical
25416956
UBC_HUMANUBCphysical
25527291
AURKA_HUMANAURKAphysical
26446837
NANOG_HUMANNANOGphysical
27886188
ZN350_HUMANZNF350physical
27621083
KCTD6_HUMANKCTD6physical
27621083
WDR47_HUMANWDR47physical
27621083
SYNE1_HUMANSYNE1physical
27621083
EM55_HUMANMPP1physical
27621083
SLF1_HUMANANKRD32physical
27621083
CUL3_HUMANCUL3physical
27621083
KCD11_HUMANKCTD11physical
27621083
GLI1_HUMANGLI1physical
27621083
GLI2_HUMANGLI2physical
27621083
P53_HUMANTP53physical
27561390
NANOG_HUMANNANOGphysical
27956178
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
F110B_HUMANFAM110Bphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
TBC25_HUMANTBC1D25physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NADK_HUMANNADKphysical
27173435
AFAD_HUMANMLLT4physical
27173435
MELK_HUMANMELKphysical
27173435
NGAP_HUMANRASAL2physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
CBY1_HUMANCBY1physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
BRCA2_HUMANBRCA2physical
28743957
RAD51_HUMANRAD51physical
28743957

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 UBP21_HUMAN

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Related Literatures of Post-Translational Modification

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