UBP44_HUMAN - dbPTM
UBP44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP44_HUMAN
UniProt AC Q9H0E7
Protein Name Ubiquitin carboxyl-terminal hydrolase 44
Gene Name USP44
Organism Homo sapiens (Human).
Sequence Length 712
Subcellular Localization Nucleus . Peaks in interphase, with relatively low levels maintained throughout mitosis..
Protein Description Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination..
Protein Sequence MLAMDTCKHVGQLQLAQDHSSLNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNTTGDLKLLRRTLSAIKSQNYHCTTRSGRFLRSMGTGDDSYFLHDGAQSLLQSEDQLYTALWHRRRILMGKIFRTWFEQSPIGRKKQEEPFQEKIVVKREVKKRRQELEYQVKAELESMPPRKSLRLQGLAQSTIIEIVSVQVPAQTPASPAKDKVLSTSENEISQKVSDSSVKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAMTASEKTRSCKHPPVTDTVVYQMNECQEKDTGFVCSRQSSLSSGLSGGASKGRKMELIQPKEPTSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQRELETTGTSLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCSGKDIASQPCLVTEMLAKFTETEALEGKIYVCDQCNSKRRRFSSKPVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRETLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLLGSQHPNEDADTSSNEILS
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
34PhosphorylationWHCVDCNTTESIWAC
EEEECCCCCCCHHHH		37.97-
35PhosphorylationHCVDCNTTESIWACL
EEECCCCCCCHHHHH		17.47-
45PhosphorylationIWACLSCSHVACGRY
HHHHHHCCHHHHHHH		20.02-
101PhosphorylationDLKLLRRTLSAIKSQ
CHHHHHHHHHHHHHC		20.7328270605
103PhosphorylationKLLRRTLSAIKSQNY
HHHHHHHHHHHHCCC		27.6028270605
106UbiquitinationRRTLSAIKSQNYHCT
HHHHHHHHHCCCEEE		45.78-
107PhosphorylationRTLSAIKSQNYHCTT
HHHHHHHHCCCEEEC		19.9728270605
110PhosphorylationSAIKSQNYHCTTRSG
HHHHHCCCEEECCCC		7.2228270605
113PhosphorylationKSQNYHCTTRSGRFL
HHCCCEEECCCCCCH		16.3628270605
114PhosphorylationSQNYHCTTRSGRFLR
HCCCEEECCCCCCHH		28.3828270605
169PhosphorylationFRTWFEQSPIGRKKQ
HHHHHHHCCCCCCCC		15.9922692537
199PhosphorylationKRRQELEYQVKAELE
HHHHHHHHHHHHHHH		31.0925072903
207PhosphorylationQVKAELESMPPRKSL
HHHHHHHHCCCCCHH		49.5725072903
239PhosphorylationVPAQTPASPAKDKVL
CCCCCCCCCCCCCCC		26.9622692537
244UbiquitinationPASPAKDKVLSTSEN
CCCCCCCCCCCCCHH		44.35-
247PhosphorylationPAKDKVLSTSENEIS
CCCCCCCCCCHHHHH		32.6429449344
248PhosphorylationAKDKVLSTSENEISQ
CCCCCCCCCHHHHHH		35.5829449344
249PhosphorylationKDKVLSTSENEISQK
CCCCCCCCHHHHHHH		34.7429449344
254PhosphorylationSTSENEISQKVSDSS
CCCHHHHHHHCCCCC		20.1229449344
256UbiquitinationSENEISQKVSDSSVK
CHHHHHHHCCCCCCC		36.59-
269PhosphorylationVKRRPIVTPGVTGLR
CCCCCCCCCCCCCHH		18.2922692537
327PhosphorylationSCKHPPVTDTVVYQM
CCCCCCCCCEEEEEC		31.5524719451
342PhosphorylationNECQEKDTGFVCSRQ
CCCCCCCCCEEEECC		43.5224719451
350PhosphorylationGFVCSRQSSLSSGLS
CEEEECCHHCCCCCC		31.9429449344
351PhosphorylationFVCSRQSSLSSGLSG
EEEECCHHCCCCCCC		24.7529449344
353PhosphorylationCSRQSSLSSGLSGGA
EECCHHCCCCCCCCC		25.0629449344
354PhosphorylationSRQSSLSSGLSGGAS
ECCHHCCCCCCCCCC		49.3929449344
357PhosphorylationSSLSSGLSGGASKGR
HHCCCCCCCCCCCCC		38.4129449344
361PhosphorylationSGLSGGASKGRKMEL
CCCCCCCCCCCCCEE		38.6319651622
401PhosphorylationSGKWALVSPFAMLHS
CCCCEEECHHHHHHH		18.3614702039
508UbiquitinationERYQCSGKDIASQPC
CHHCCCCCCHHCCCC		29.66-
512PhosphorylationCSGKDIASQPCLVTE
CCCCCHHCCCCHHHH		34.6830631047
518PhosphorylationASQPCLVTEMLAKFT
HCCCCHHHHHHHHHC		11.6130631047
523UbiquitinationLVTEMLAKFTETEAL
HHHHHHHHHCCCHHH		49.18-
527PhosphorylationMLAKFTETEALEGKI
HHHHHCCCHHHCCCE		24.41-
543UbiquitinationVCDQCNSKRRRFSSK
EECCCCCCCCCCCCC		35.61-
548PhosphorylationNSKRRRFSSKPVVLT
CCCCCCCCCCCEECC		35.32-
549PhosphorylationSKRRRFSSKPVVLTE
CCCCCCCCCCEECCH		37.96-
550UbiquitinationKRRRFSSKPVVLTEA
CCCCCCCCCEECCHH		40.40-
555PhosphorylationSSKPVVLTEAQKQLM
CCCCEECCHHHHHHH		20.05-
667AcetylationCTMDEVCKAQAYILF
CCHHHHHHHHHHHHH		49.027380801
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 UBP44_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

20402667
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 UBP44_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CETN2_HUMANCETN2physical
19615732
RPB7_HUMANPOLR2Gphysical
19615732
RM23_HUMANMRPL23physical
19615732
TCOF_HUMANTCOF1physical
19615732
KRR1_HUMANKRR1physical
19615732
TBL2_HUMANTBL2physical
19615732
RT21_HUMANMRPS21physical
19615732
SYSM_HUMANSARS2physical
19615732
RM40_HUMANMRPL40physical
19615732
RM53_HUMANMRPL53physical
19615732
CETN2_HUMANCETN2physical
28514442
CETN2_HUMANCETN2physical
27880911
TBL1R_HUMANTBL1XR1physical
27880911
TBL1X_HUMANTBL1Xphysical
27880911
PRS6B_HUMANPSMC4physical
27880911
HDAC3_HUMANHDAC3physical
27880911
PRS4_HUMANPSMC1physical
27880911
PRS7_HUMANPSMC2physical
27880911
PRS8_HUMANPSMC5physical
27880911
NCOR1_HUMANNCOR1physical
27880911
NCOR2_HUMANNCOR2physical
27880911
H2B1A_HUMANHIST1H2BAphysical
27880911
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 UBP44_HUMAN

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Related Literatures of Post-Translational Modification

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