USPL1_HUMAN - dbPTM
USPL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USPL1_HUMAN
UniProt AC Q5W0Q7
Protein Name SUMO-specific isopeptidase USPL1
Gene Name USPL1
Organism Homo sapiens (Human).
Sequence Length 1092
Subcellular Localization Nucleus, Cajal body .
Protein Description SUMO-specific isopeptidase involved in protein desumoylation. Specifically binds SUMO proteins with a higher affinity for SUMO2 and SUMO3 which it cleaves more efficiently. Also able to process full-length SUMO proteins to their mature forms. [PubMed: 22878415 Plays a key role in RNA polymerase-II-mediated snRNA transcription in the Cajal bodies]
Protein Sequence MMDSPKIGNGLPVIGPGTDIGISSLHMVGYLGKNFDSAKVPSDEYCPACREKGKLKALKTYRISFQESIFLCEDLQCIYPLGSKSLNNLISPDLEECHTPHKPQKRKSLESSYKDSLLLANSKKTRNYIAIDGGKVLNSKHNGEVYDETSSNLPDSSGQQNPIRTADSLERNEILEADTVDMATTKDPATVDVSGTGRPSPQNEGCTSKLEMPLESKCTSFPQALCVQWKNAYALCWLDCILSALVHSEELKNTVTGLCSKEESIFWRLLTKYNQANTLLYTSQLSGVKDGDCKKLTSEIFAEIETCLNEVRDEIFISLQPQLRCTLGDMESPVFAFPLLLKLETHIEKLFLYSFSWDFECSQCGHQYQNRHMKSLVTFTNVIPEWHPLNAAHFGPCNNCNSKSQIRKMVLEKVSPIFMLHFVEGLPQNDLQHYAFHFEGCLYQITSVIQYRANNHFITWILDADGSWLECDDLKGPCSERHKKFEVPASEIHIVIWERKISQVTDKEAACLPLKKTNDQHALSNEKPVSLTSCSVGDAASAETASVTHPKDISVAPRTLSQDTAVTHGDHLLSGPKGLVDNILPLTLEETIQKTASVSQLNSEAFLLENKPVAENTGILKTNTLLSQESLMASSVSAPCNEKLIQDQFVDISFPSQVVNTNMQSVQLNTEDTVNTKSVNNTDATGLIQGVKSVEIEKDAQLKQFLTPKTEQLKPERVTSQVSNLKKKETTADSQTTTSKSLQNQSLKENQKKPFVGSWVKGLISRGASFMPLCVSAHNRNTITDLQPSVKGVNNFGGFKTKGINQKASHVSKKARKSASKPPPISKPPAGPPSSNGTAAHPHAHAASEVLEKSGSTSCGAQLNHSSYGNGISSANHEDLVEGQIHKLRLKLRKKLKAEKKKLAALMSSPQSRTVRSENLEQVPQDGSPNDCESIEDLLNELPYPIDIASESACTTVPGVSLYSSQTHEEILAELLSPTPVSTELSENGEGDFRYLGMGDSHIPPPVPSEFNDVSQNTHLRQDHNYCSPTKKNPCEVQPDSLTNNACVRTLNLESPMKTDIFDEFFSSSALNALANDTLDLPHFDEYLFENY
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
39UbiquitinationGKNFDSAKVPSDEYC
CCCCCCCCCCCCCCC
59.64-
85PhosphorylationIYPLGSKSLNNLISP
EEECCCHHHHCCCCC
37.7229083192
91PhosphorylationKSLNNLISPDLEECH
HHHHCCCCCCHHHCC
18.6128985074
99PhosphorylationPDLEECHTPHKPQKR
CCHHHCCCCCCCHHC
38.4523898821
108PhosphorylationHKPQKRKSLESSYKD
CCCHHCCCHHHHHHH
41.2128985074
114UbiquitinationKSLESSYKDSLLLAN
CCHHHHHHHHEEECC
42.67-
116PhosphorylationLESSYKDSLLLANSK
HHHHHHHHEEECCCC
19.4329214152
135AcetylationYIAIDGGKVLNSKHN
EEEECCCCEECCCCC
49.4223236377
184PhosphorylationADTVDMATTKDPATV
ECEEEECCCCCCCEE
27.95-
185PhosphorylationDTVDMATTKDPATVD
CEEEECCCCCCCEEE
24.74-
190PhosphorylationATTKDPATVDVSGTG
CCCCCCCEEECCCCC
23.7223312004
194PhosphorylationDPATVDVSGTGRPSP
CCCEEECCCCCCCCC
26.6123312004
196PhosphorylationATVDVSGTGRPSPQN
CEEECCCCCCCCCCC
23.6325850435
200PhosphorylationVSGTGRPSPQNEGCT
CCCCCCCCCCCCCCC
37.4425849741
207PhosphorylationSPQNEGCTSKLEMPL
CCCCCCCCCCCCCCC
39.4923663014
208PhosphorylationPQNEGCTSKLEMPLE
CCCCCCCCCCCCCCC
39.0423663014
415PhosphorylationKMVLEKVSPIFMLHF
HHHHHHHCHHHHHHE
24.28-
479PhosphorylationDDLKGPCSERHKKFE
CCCCCCCCHHHHCCC
40.58-
559PhosphorylationDISVAPRTLSQDTAV
CCEECCCCCCCCCCC
29.6929978859
561PhosphorylationSVAPRTLSQDTAVTH
EECCCCCCCCCCCCC
25.9529978859
564PhosphorylationPRTLSQDTAVTHGDH
CCCCCCCCCCCCCHH
18.5229978859
567PhosphorylationLSQDTAVTHGDHLLS
CCCCCCCCCCHHHCC
20.0623186163
574PhosphorylationTHGDHLLSGPKGLVD
CCCHHHCCCCCCHHH
60.4523186163
597PhosphorylationETIQKTASVSQLNSE
HHHHHHCCHHHHHHH
27.77-
720PhosphorylationLKPERVTSQVSNLKK
CCHHHHHHHHHHCCC
26.2328555341
731PhosphorylationNLKKKETTADSQTTT
HCCCCCCCCCCCCCC
29.5624719451
737PhosphorylationTTADSQTTTSKSLQN
CCCCCCCCCCHHHHC
22.80-
738PhosphorylationTADSQTTTSKSLQNQ
CCCCCCCCCHHHHCH
37.2324719451
739PhosphorylationADSQTTTSKSLQNQS
CCCCCCCCHHHHCHH
20.3929759185
741PhosphorylationSQTTTSKSLQNQSLK
CCCCCCHHHHCHHHH
34.6524719451
908PhosphorylationKKLAALMSSPQSRTV
HHHHHHHCCCCCCCC
39.4527050516
909PhosphorylationKLAALMSSPQSRTVR
HHHHHHCCCCCCCCC
17.0030631047
912PhosphorylationALMSSPQSRTVRSEN
HHHCCCCCCCCCCCC
33.0527732954
995PhosphorylationNGEGDFRYLGMGDSH
CCCCCEEECCCCCCC
13.9630257219
1009PhosphorylationHIPPPVPSEFNDVSQ
CCCCCCCCCCCCCCC
55.8730257219
1026PhosphorylationHLRQDHNYCSPTKKN
CCCCCCCCCCCCCCC
7.2923312004
1028PhosphorylationRQDHNYCSPTKKNPC
CCCCCCCCCCCCCCC
25.8328985074
1030PhosphorylationDHNYCSPTKKNPCEV
CCCCCCCCCCCCCCC
38.0523312004
1041PhosphorylationPCEVQPDSLTNNACV
CCCCCCCCCCCCCEE
43.7223312004
1043PhosphorylationEVQPDSLTNNACVRT
CCCCCCCCCCCEEEE
30.3123312004
1055PhosphorylationVRTLNLESPMKTDIF
EEECCCCCCCCCCHH
33.2021815630

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 USPL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USPL1_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 USPL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANXA1_HUMANANXA1physical
19615732
KCRB_HUMANCKBphysical
19615732
KINH_HUMANKIF5Bphysical
19615732
KRT85_HUMANKRT85physical
19615732
6PGD_HUMANPGDphysical
19615732
PIP_HUMANPIPphysical
19615732
KPYR_HUMANPKLRphysical
19615732
ELL_HUMANELLphysical
19615732
ICE1_HUMANICE1physical
19615732
ANFY1_HUMANANKFY1physical
19615732
RAGP1_HUMANRANGAP1physical
22878415
COIL_HUMANCOILphysical
22878415
SUMO1_HUMANSUMO1physical
22878415
SUMO2_HUMANSUMO2physical
22878415
SUMO3_HUMANSUMO3physical
22878415
SP100_HUMANSP100physical
22878415
ELL_HUMANELLphysical
24413172
COIL_HUMANCOILphysical
24413172
ICE1_HUMANICE1physical
24413172
RPB1_HUMANPOLR2Aphysical
24413172

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USPL1_HUMAN

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Related Literatures of Post-Translational Modification

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