UBP43_HUMAN - dbPTM
UBP43_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP43_HUMAN
UniProt AC Q70EL4
Protein Name Ubiquitin carboxyl-terminal hydrolase 43
Gene Name USP43
Organism Homo sapiens (Human).
Sequence Length 1123
Subcellular Localization
Protein Description May recognize and hydrolyze 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 (By similarity)..
Protein Sequence MDLGPGDAAGGGPLAPRPRRRRSLRRLFSRFLLALGSRSRPGDSPPRPQPGHCDGDGEGGFACAPGPVPAAPGSPGEERPPGPQPQLQLPAGDGARPPGAQGLKNHGNTCFMNAVVQCLSNTDLLAEFLALGRYRAAPGRAEVTEQLAALVRALWTREYTPQLSAEFKNAVSKYGSQFQGNSQHDALEFLLWLLDRVHEDLEGSSRGPVSEKLPPEATKTSENCLSPSAQLPLGQSFVQSHFQAQYRSSLTCPHCLKQSNTFDPFLCVSLPIPLRQTRFLSVTLVFPSKSQRFLRVGLAVPILSTVAALRKMVAEEGGVPADEVILVELYPSGFQRSFFDEEDLNTIAEGDNVYAFQVPPSPSQGTLSAHPLGLSASPRLAAREGQRFSLSLHSESKVLILFCNLVGSGQQASRFGPPFLIREDRAVSWAQLQQSILSKVRHLMKSEAPVQNLGSLFSIRVVGLSVACSYLSPKDSRPLCHWAVDRVLHLRRPGGPPHVKLAVEWDSSVKERLFGSLQEERAQDADSVWQQQQAHQQHSCTLDECFQFYTKEEQLAQDDAWKCPHCQVLQQGMVKLSLWTLPDILIIHLKRFCQVGERRNKLSTLVKFPLSGLNMAPHVAQRSTSPEAGLGPWPSWKQPDCLPTSYPLDFLYDLYAVCNHHGNLQGGHYTAYCRNSLDGQWYSYDDSTVEPLREDEVNTRGAYILFYQKRNSIPPWSASSSMRGSTSSSLSDHWLLRLGSHAGSTRGSLLSWSSAPCPSLPQVPDSPIFTNSLCNQEKGGLEPRRLVRGVKGRSISMKAPTTSRAKQGPFKTMPLRWSFGSKEKPPGASVELVEYLESRRRPRSTSQSIVSLLTGTAGEDEKSASPRSNVALPANSEDGGRAIERGPAGVPCPSAQPNHCLAPGNSDGPNTARKLKENAGQDIKLPRKFDLPLTVMPSVEHEKPARPEGQKAMNWKESFQMGSKSSPPSPYMGFSGNSKDSRRGTSELDRPLQGTLTLLRSVFRKKENRRNERAEVSPQVPPVSLVSGGLSPAMDGQAPGSPPALRIPEGLARGLGSRLERDVWSAPSSLRLPRKASRAPRGSALGMSQRTVPGEQASYGTFQRVKYHTLSLGRKKTLPESSF
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
3 (in isoform 2)Phosphorylation-15.7924043423
7 (in isoform 2)Phosphorylation-36.0624043423
8 (in isoform 2)Phosphorylation-17.5824043423
9 (in isoform 2)Phosphorylation-23.1524043423
13 (in isoform 2)Phosphorylation-28.7327732954
14 (in isoform 2)Phosphorylation-13.3427732954
15 (in isoform 2)Phosphorylation-10.9427732954
23PhosphorylationPRPRRRRSLRRLFSR
CCHHHHHHHHHHHHH
25.1526074081
24 (in isoform 2)Phosphorylation-3.3327732954
25 (in isoform 2)Phosphorylation-34.2127732954
29PhosphorylationRSLRRLFSRFLLALG
HHHHHHHHHHHHHHC
27.0726074081
37PhosphorylationRFLLALGSRSRPGDS
HHHHHHCCCCCCCCC
28.1226074081
39PhosphorylationLLALGSRSRPGDSPP
HHHHCCCCCCCCCCC
44.5226074081
283PhosphorylationQTRFLSVTLVFPSKS
CCCEEEEEEECCCCC
17.52-
304PhosphorylationGLAVPILSTVAALRK
HCHHHHHHHHHHHHH
22.89-
305PhosphorylationLAVPILSTVAALRKM
CHHHHHHHHHHHHHH
15.66-
391PhosphorylationEGQRFSLSLHSESKV
CCCCEEEEEECCCCE
23.8827251275
413PhosphorylationVGSGQQASRFGPPFL
CCCCCHHHHHCCCEE
24.65-
435PhosphorylationSWAQLQQSILSKVRH
CHHHHHHHHHHHHHH
16.7324719451
469PhosphorylationVGLSVACSYLSPKDS
EEHHHHHHHCCCCCC
21.2628348404
472PhosphorylationSVACSYLSPKDSRPL
HHHHHHCCCCCCCCC
22.9824719451
507PhosphorylationKLAVEWDSSVKERLF
EEEEECCHHHHHHHH
37.80-
508PhosphorylationLAVEWDSSVKERLFG
EEEECCHHHHHHHHH
34.43-
611PhosphorylationTLVKFPLSGLNMAPH
HHCCCCCCCCCCHHH
41.28-
623PhosphorylationAPHVAQRSTSPEAGL
HHHHHCCCCCCCCCC
22.5828857561
624PhosphorylationPHVAQRSTSPEAGLG
HHHHCCCCCCCCCCC
50.9528857561
625PhosphorylationHVAQRSTSPEAGLGP
HHHCCCCCCCCCCCC
23.2224076635
635PhosphorylationAGLGPWPSWKQPDCL
CCCCCCCCCCCCCCC
42.9328102081
725PhosphorylationASSSMRGSTSSSLSD
CCHHCCCCCCCCCCC
18.1027251275
726PhosphorylationSSSMRGSTSSSLSDH
CHHCCCCCCCCCCCH
35.1428348404
727PhosphorylationSSMRGSTSSSLSDHW
HHCCCCCCCCCCCHH
21.4528348404
728PhosphorylationSMRGSTSSSLSDHWL
HCCCCCCCCCCCHHH
35.0728348404
729PhosphorylationMRGSTSSSLSDHWLL
CCCCCCCCCCCHHHH
31.4928348404
731PhosphorylationGSTSSSLSDHWLLRL
CCCCCCCCCHHHHHC
29.40-
744PhosphorylationRLGSHAGSTRGSLLS
HCCCCCCCCCCCHHC
18.7324719451
746MethylationGSHAGSTRGSLLSWS
CCCCCCCCCCHHCCC
34.11-
746Asymmetric dimethylarginineGSHAGSTRGSLLSWS
CCCCCCCCCCHHCCC
34.11-
754PhosphorylationGSLLSWSSAPCPSLP
CCHHCCCCCCCCCCC
29.9428102081
759PhosphorylationWSSAPCPSLPQVPDS
CCCCCCCCCCCCCCC
60.4428102081
766PhosphorylationSLPQVPDSPIFTNSL
CCCCCCCCCCCCCCC
17.5227966365
770PhosphorylationVPDSPIFTNSLCNQE
CCCCCCCCCCCCCCC
25.3128102081
772PhosphorylationDSPIFTNSLCNQEKG
CCCCCCCCCCCCCCC
31.1028102081
794PhosphorylationVRGVKGRSISMKAPT
HCCCCCCEEECCCCC
27.9030183078
796PhosphorylationGVKGRSISMKAPTTS
CCCCCEEECCCCCCC
18.5727422710
812PhosphorylationAKQGPFKTMPLRWSF
CCCCCCCCCCEEEEC
25.1324719451
818PhosphorylationKTMPLRWSFGSKEKP
CCCCEEEECCCCCCC
17.1925159151
821PhosphorylationPLRWSFGSKEKPPGA
CEEEECCCCCCCCCC
35.3122617229
835PhosphorylationASVELVEYLESRRRP
CCHHHHHHHHHCCCC
14.3228102081
838PhosphorylationELVEYLESRRRPRST
HHHHHHHHCCCCCCC
28.6128102081
844PhosphorylationESRRRPRSTSQSIVS
HHCCCCCCCCHHHHH
34.7830278072
845PhosphorylationSRRRPRSTSQSIVSL
HCCCCCCCCHHHHHH
31.8729116813
846PhosphorylationRRRPRSTSQSIVSLL
CCCCCCCCHHHHHHH
24.1530278072
847PhosphorylationRRPRSTSQSIVSLLT
CCCCCCCHHHHHHHH
36.9518669648
848PhosphorylationRPRSTSQSIVSLLTG
CCCCCCHHHHHHHHC
25.4028102081
849PhosphorylationPRSTSQSIVSLLTGT
CCCCCHHHHHHHHCC
1.5718669648
851PhosphorylationSTSQSIVSLLTGTAG
CCCHHHHHHHHCCCC
18.9118669648
852PhosphorylationTSQSIVSLLTGTAGE
CCHHHHHHHHCCCCC
3.2518669648
854PhosphorylationQSIVSLLTGTAGEDE
HHHHHHHHCCCCCCC
37.4722210691
856PhosphorylationIVSLLTGTAGEDEKS
HHHHHHCCCCCCCCC
26.6723312004
863PhosphorylationTAGEDEKSASPRSNV
CCCCCCCCCCCCCCC
31.7524719451
865PhosphorylationGEDEKSASPRSNVAL
CCCCCCCCCCCCCCC
28.1223312004
876PhosphorylationNVALPANSEDGGRAI
CCCCCCCCCCCCCCH
38.8929083192
965PhosphorylationSFQMGSKSSPPSPYM
HHCCCCCCCCCCCCC
50.1828985074
966PhosphorylationFQMGSKSSPPSPYMG
HCCCCCCCCCCCCCC
44.5622617229
969PhosphorylationGSKSSPPSPYMGFSG
CCCCCCCCCCCCCCC
31.8522617229
971PhosphorylationKSSPPSPYMGFSGNS
CCCCCCCCCCCCCCC
17.7623090842
975PhosphorylationPSPYMGFSGNSKDSR
CCCCCCCCCCCCCCC
31.1928985074
978PhosphorylationYMGFSGNSKDSRRGT
CCCCCCCCCCCCCCC
41.1723090842
985PhosphorylationSKDSRRGTSELDRPL
CCCCCCCCCCCCCHH
19.7424719451
995PhosphorylationLDRPLQGTLTLLRSV
CCCHHHHHHHHHHHH
12.0123312004
997PhosphorylationRPLQGTLTLLRSVFR
CHHHHHHHHHHHHHH
24.4723312004
1024PhosphorylationSPQVPPVSLVSGGLS
CCCCCCCEEEECCCC
28.9128102081
1027PhosphorylationVPPVSLVSGGLSPAM
CCCCEEEECCCCCCC
32.2228102081
1031PhosphorylationSLVSGGLSPAMDGQA
EEEECCCCCCCCCCC
17.5628102081
1041PhosphorylationMDGQAPGSPPALRIP
CCCCCCCCCCCHHCC
27.0128102081
1042PhosphorylationDGQAPGSPPALRIPE
CCCCCCCCCCHHCCH
24.8918669648
1053MethylationRIPEGLARGLGSRLE
HCCHHHHHCCCHHHH
46.01115919633
1065PhosphorylationRLERDVWSAPSSLRL
HHHHCCCCCCCCCCC
30.1022617229
1068PhosphorylationRDVWSAPSSLRLPRK
HCCCCCCCCCCCCCC
41.5427050516
1069PhosphorylationDVWSAPSSLRLPRKA
CCCCCCCCCCCCCCH
19.2230183078
1071MethylationWSAPSSLRLPRKASR
CCCCCCCCCCCCHHC
44.5982797551
1081MethylationRKASRAPRGSALGMS
CCHHCCCCCCCCCCC
51.19115919637
1088PhosphorylationRGSALGMSQRTVPGE
CCCCCCCCCCCCCCC
18.0824719451
1098PhosphorylationTVPGEQASYGTFQRV
CCCCCHHCCCCCHHH
24.6425106551
1099PhosphorylationVPGEQASYGTFQRVK
CCCCHHCCCCCHHHE
24.1725106551
1101PhosphorylationGEQASYGTFQRVKYH
CCHHCCCCCHHHEEE
14.3628348404
1107PhosphorylationGTFQRVKYHTLSLGR
CCCHHHEEEEECCCC
9.3620873877
1109PhosphorylationFQRVKYHTLSLGRKK
CHHHEEEEECCCCCC
18.2320873877
1111PhosphorylationRVKYHTLSLGRKKTL
HHEEEEECCCCCCCC
29.9022617229
1111O-linked_GlycosylationRVKYHTLSLGRKKTL
HHEEEEECCCCCCCC
29.9030379171
1117PhosphorylationLSLGRKKTLPESSF-
ECCCCCCCCCCCCC-
51.0524719451

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 UBP43_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP43_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 UBP43_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDCD2_HUMANPDCD2physical
19615732
1433B_HUMANYWHABphysical
19615732
1433E_HUMANYWHAEphysical
19615732
1433F_HUMANYWHAHphysical
19615732
PSME3_HUMANPSME3physical
19615732
WDR3_HUMANWDR3physical
19615732
VPS35_HUMANVPS35physical
19615732
KT3K_HUMANFN3KRPphysical
19615732
MAGI3_HUMANMAGI3physical
19615732
CSK2B_HUMANCSNK2Bphysical
26496610
DDX11_HUMANDDX11physical
26496610
TAU_HUMANMAPTphysical
26496610
NHS_HUMANNHSphysical
26496610
DPOD1_HUMANPOLD1physical
26496610
PSA2_HUMANPSMA2physical
26496610
RT12_HUMANMRPS12physical
26496610
SSRG_HUMANSSR3physical
26496610
UBP1_HUMANUSP1physical
26496610
NCOA4_HUMANNCOA4physical
26496610
STX10_HUMANSTX10physical
26496610
CEP57_HUMANCEP57physical
26496610
TXN4A_HUMANTXNL4Aphysical
26496610
HAUS5_HUMANHAUS5physical
26496610
TRM7_HUMANFTSJ1physical
26496610
TRM6_HUMANTRMT6physical
26496610
CK5P2_HUMANCDK5RAP2physical
26496610
TM165_HUMANTMEM165physical
26496610
TRI56_HUMANTRIM56physical
26496610
ATG4A_HUMANATG4Aphysical
26496610
INT1_HUMANINTS1physical
26496610

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 UBP43_HUMAN

loading...

Related Literatures of Post-Translational Modification
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-1041, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-835, AND MASSSPECTROMETRY.

TOP