UBP45_HUMAN - dbPTM
UBP45_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP45_HUMAN
UniProt AC Q70EL2
Protein Name Ubiquitin carboxyl-terminal hydrolase 45
Gene Name USP45
Organism Homo sapiens (Human).
Sequence Length 814
Subcellular Localization
Protein Description
Protein Sequence MRVKDPTKALPEKAKRSKRPTVPHDEDSSDDIAVGLTCQHVSHAISVNHVKRAIAENLWSVCSECLKERRFYDGQLVLTSDIWLCLKCGFQGCGKNSESQHSLKHFKSSRTEPHCIIINLSTWIIWCYECDEKLSTHCNKKVLAQIVDFLQKHASKTQTSAFSRIMKLCEEKCETDEIQKGGKCRNLSVRGITNLGNTCFFNAVMQNLAQTYTLTDLMNEIKESSTKLKIFPSSDSQLDPLVVELSRPGPLTSALFLFLHSMKETEKGPLSPKVLFNQLCQKAPRFKDFQQQDSQELLHYLLDAVRTEETKRIQASILKAFNNPTTKTADDETRKKVKAYGKEGVKMNFIDRIFIGELTSTVMCEECANISTVKDPFIDISLPIIEERVSKPLLWGRMNKYRSLRETDHDRYSGNVTIENIHQPRAAKKHSSSKDKSQLIHDRKCIRKLSSGETVTYQKNENLEMNGDSLMFASLMNSESRLNESPTDDSEKEASHSESNVDADSEPSESESASKQTGLFRSSSGSGVQPDGPLYPLSAGKLLYTKETDSGDKEMAEAISELRLSSTVTGDQDFDRENQPLNISNNLCFLEGKHLRSYSPQNAFQTLSQSYITTSKECSIQSCLYQFTSMELLMGNNKLLCENCTKNKQKYQEETSFAEKKVEGVYTNARKQLLISAVPAVLILHLKRFHQAGLSLRKVNRHVDFPLMLDLAPFCSATCKNASVGDKVLYGLYGIVEHSGSMREGHYTAYVKVRTPSRKLSEHNTKKKNVPGLKAADNESAGQWVHVSDTYLQVVPESRALSAQAYLLFYERVL
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
28PhosphorylationTVPHDEDSSDDIAVG
CCCCCCCCCCCEEHH
33.3529449344
29PhosphorylationVPHDEDSSDDIAVGL
CCCCCCCCCCEEHHH
52.1829449344
71 (in isoform 3)Ubiquitination-9.0321890473
141UbiquitinationLSTHCNKKVLAQIVD
HHHHCCHHHHHHHHH
28.61-
156UbiquitinationFLQKHASKTQTSAFS
HHHHHCCHHHHHHHH
45.49-
252PhosphorylationLSRPGPLTSALFLFL
CCCCCCHHHHHHHHH
18.3226074081
253PhosphorylationSRPGPLTSALFLFLH
CCCCCHHHHHHHHHH
30.5626074081
261PhosphorylationALFLFLHSMKETEKG
HHHHHHHHCHHCCCC
33.4326074081
271PhosphorylationETEKGPLSPKVLFNQ
HCCCCCCCHHHHHHH
26.3024719451
316PhosphorylationETKRIQASILKAFNN
HHHHHHHHHHHHHCC
16.4524719451
325PhosphorylationLKAFNNPTTKTADDE
HHHHCCCCCCCCCHH
42.9426546556
390PhosphorylationPIIEERVSKPLLWGR
HHHHHHCCCCCHHHC
34.4724719451
391 (in isoform 1)Ubiquitination-36.5121890473
391UbiquitinationIIEERVSKPLLWGRM
HHHHHCCCCCHHHCH
36.5121890473
403PhosphorylationGRMNKYRSLRETDHD
HCHHHCCCHHHCCCC
28.78-
432PhosphorylationRAAKKHSSSKDKSQL
CCCCCCCCCCCHHHH
40.92-
450PhosphorylationRKCIRKLSSGETVTY
HHHHHHHCCCCEEEE
39.0525159151
451PhosphorylationKCIRKLSSGETVTYQ
HHHHHHCCCCEEEEE
51.6025159151
454PhosphorylationRKLSSGETVTYQKNE
HHHCCCCEEEEECCC
22.9823403867
456PhosphorylationLSSGETVTYQKNENL
HCCCCEEEEECCCCC
27.8823403867
457PhosphorylationSSGETVTYQKNENLE
CCCCEEEEECCCCCE
17.1027642862
474PhosphorylationGDSLMFASLMNSESR
CCHHHHHHHHCCHHH
19.52-
485PhosphorylationSESRLNESPTDDSEK
CHHHCCCCCCCHHHH
31.8428985074
490PhosphorylationNESPTDDSEKEASHS
CCCCCCHHHHHHHHC
54.07-
508PhosphorylationVDADSEPSESESASK
CCCCCCCCCCHHHHH
50.10-
522PhosphorylationKQTGLFRSSSGSGVQ
HHCCCCCCCCCCCCC
22.8625262027
523PhosphorylationQTGLFRSSSGSGVQP
HCCCCCCCCCCCCCC
34.1725627689
524PhosphorylationTGLFRSSSGSGVQPD
CCCCCCCCCCCCCCC
37.9225627689
526PhosphorylationLFRSSSGSGVQPDGP
CCCCCCCCCCCCCCC
37.4325627689
560PhosphorylationKEMAEAISELRLSST
HHHHHHHHHHHHCCC
37.3124719451
597PhosphorylationLEGKHLRSYSPQNAF
ECCCCHHHCCCCHHH
36.0027732954
598PhosphorylationEGKHLRSYSPQNAFQ
CCCCHHHCCCCHHHH
20.2428555341
599PhosphorylationGKHLRSYSPQNAFQT
CCCHHHCCCCHHHHH
22.6625159151
606PhosphorylationSPQNAFQTLSQSYIT
CCCHHHHHHHHHHCC
23.1727732954
651PhosphorylationCTKNKQKYQEETSFA
CCCCHHHHHHHCCHH
20.7529978859
655PhosphorylationKQKYQEETSFAEKKV
HHHHHHHCCHHHHHH
28.5229978859
656PhosphorylationQKYQEETSFAEKKVE
HHHHHHCCHHHHHHH
26.2424719451
666PhosphorylationEKKVEGVYTNARKQL
HHHHHHHCCHHHHHH
12.7227642862
730PhosphorylationSVGDKVLYGLYGIVE
CCCHHHHHHHHHHHC
14.2030576142
733PhosphorylationDKVLYGLYGIVEHSG
HHHHHHHHHHHCCCC
10.6330576142
747PhosphorylationGSMREGHYTAYVKVR
CCCCCCEEEEEEEEE
12.1530576142
765PhosphorylationRKLSEHNTKKKNVPG
CCCCCCCCCCCCCCC
46.2624114839

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 UBP45_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP45_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 UBP45_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK1_HUMANCDK1physical
19615732
FLNA_HUMANFLNAphysical
19615732
MYH9_HUMANMYH9physical
19615732
MYH10_HUMANMYH10physical
19615732
MYL6_HUMANMYL6physical
19615732
PK3CG_HUMANPIK3CGphysical
19615732
RPB7_HUMANPOLR2Gphysical
19615732
SAFB1_HUMANSAFBphysical
19615732
SF3A2_HUMANSF3A2physical
19615732
RTCA_HUMANRTCAphysical
19615732
SYFM_HUMANFARS2physical
19615732
RALY_HUMANRALYphysical
19615732
COR1C_HUMANCORO1Cphysical
19615732
RBMX_HUMANRBMXphysical
19615732
TMOD3_HUMANTMOD3physical
19615732
NOP53_HUMANGLTSCR2physical
19615732
ZFR_HUMANZFRphysical
19615732
SRBD1_HUMANSRBD1physical
19615732
YLPM1_HUMANYLPM1physical
19615732
ML12B_HUMANMYL12Bphysical
19615732
SLX4_HUMANSLX4physical
25538220
ERCC1_HUMANERCC1physical
25538220
XPF_HUMANERCC4physical
25538220
MYH10_HUMANMYH10physical
25538220
RBMX_HUMANRBMXphysical
25538220
ML12B_HUMANMYL12Bphysical
25538220
ZFR_HUMANZFRphysical
25538220
MYH9_HUMANMYH9physical
25538220

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 UBP45_HUMAN

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Related Literatures of Post-Translational Modification

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