UBP49_HUMAN - dbPTM
UBP49_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP49_HUMAN
UniProt AC Q70CQ1
Protein Name Ubiquitin carboxyl-terminal hydrolase 49
Gene Name USP49
Organism Homo sapiens (Human).
Sequence Length 688
Subcellular Localization Nucleus .
Protein Description Specifically deubiquitinates histone H2B at 'Lys-120' (H2BK120Ub). H2BK120Ub is a specific tag for epigenetic transcriptional activation and acts as a regulator of mRNA splicing. Deubiquitination is required for efficient cotranscriptional splicing of a large set of exons..
Protein Sequence MDRCKHVGRLRLAQDHSILNPQKWCCLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDNPEGDLKLLRSSLLAVRGQKQDTPVRRGRTLRSMASGEDVVLPQRAPQGQPQMLTALWYRRQRLLARTLRLWFEKSSRGQAKLEQRRQEEALERKKEEARRRRREVKRRLLEELASTPPRKSARLLLHTPRDAGPAASRPAALPTSRRVPAATLKLRRQPAMAPGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEHLFPKATNGKTQLSGKPTNSSATELSLRNDRAEACEREGFCWNGRASISRSLELIQNKEPSSKHISLCRELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGTTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERYHCIEKGFVPLNQTECLLTEMLAKFTETEALEGRIYACDQCNSKRRKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTMEPYCCRDMLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVEEVCKTQAYILFYTQRTVQGNARISETHLQAQVQSSNNDEGRPQTFS
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
93UbiquitinationDNPEGDLKLLRSSLL
CCCCCCHHHHHHHHH		50.6529967540
109PhosphorylationVRGQKQDTPVRRGRT
HCCCCCCCCCCCCCC		22.6124719451
116PhosphorylationTPVRRGRTLRSMASG
CCCCCCCCHHHHHCC		29.37-
154PhosphorylationRQRLLARTLRLWFEK
HHHHHHHHHHHHHHH		15.60-
202PhosphorylationRLLEELASTPPRKSA
HHHHHHHCCCCCCHH		54.8130001349
203PhosphorylationLLEELASTPPRKSAR
HHHHHHCCCCCCHHH		31.5330001349
306UbiquitinationGKTQLSGKPTNSSAT
CCCCCCCCCCCCCCC		45.34-
316PhosphorylationNSSATELSLRNDRAE
CCCCCCHHHHCHHHH		21.0324719451
335MethylationEGFCWNGRASISRSL
CCCCCCCCHHHHHHH		23.1924411747
335DimethylationEGFCWNGRASISRSL
CCCCCCCCHHHHHHH		23.19-
348UbiquitinationSLELIQNKEPSSKHI
HHHHHHCCCCCHHHH		55.41-
377PhosphorylationSGKWALVSPFAMLHS
CCCCEECCHHHHHHH		18.3614702039
443PhosphorylationQVLKVVNTIFHGQLL
HHHHHHHHHHHHCHH		17.2629888752
451PhosphorylationIFHGQLLSQVTCISC
HHHHCHHCCEEEEEC		31.0629888752
497PhosphorylationNQTECLLTEMLAKFT
CHHHHHHHHHHHHHC		13.34-
522UbiquitinationACDQCNSKRRKSNPK
EEHHCCCCCCCCCCC		42.08-
529UbiquitinationKRRKSNPKPLVLSEA
CCCCCCCCCCCCCHH		56.0629967540
647PhosphorylationSVEEVCKTQAYILFY
CHHHHHCCCEEEEEE		17.1927174698
650PhosphorylationEVCKTQAYILFYTQR
HHHCCCEEEEEEEEC		6.5827174698
654PhosphorylationTQAYILFYTQRTVQG
CCEEEEEEEECCCCC		9.8727174698
655PhosphorylationQAYILFYTQRTVQGN
CEEEEEEEECCCCCC		12.3027174698
658PhosphorylationILFYTQRTVQGNARI
EEEEEECCCCCCCEE		13.8327174698
666PhosphorylationVQGNARISETHLQAQ
CCCCCEECHHHHHHH		30.7827174698
668PhosphorylationGNARISETHLQAQVQ
CCCEECHHHHHHHHH		22.5427174698
676PhosphorylationHLQAQVQSSNNDEGR
HHHHHHHCCCCCCCC		35.8627174698
677PhosphorylationLQAQVQSSNNDEGRP
HHHHHHCCCCCCCCC		23.6627174698
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 UBP49_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP49_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 UBP49_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CETN1_HUMANCETN1physical
19615732
CETN2_HUMANCETN2physical
19615732
CETN3_HUMANCETN3physical
19615732
COPA_HUMANCOPAphysical
19615732
FA7_HUMANF7physical
19615732
FKBP5_HUMANFKBP5physical
19615732
ECHA_HUMANHADHAphysical
19615732
MCM6_HUMANMCM6physical
19615732
PDCD2_HUMANPDCD2physical
19615732
PPM1G_HUMANPPM1Gphysical
19615732
PPP5_HUMANPPP5Cphysical
19615732
KAPCA_HUMANPRKACAphysical
19615732
RPN1_HUMANRPN1physical
19615732
S39A7_HUMANSLC39A7physical
19615732
PP6R2_HUMANPPP6R2physical
19615732
HUWE1_HUMANHUWE1physical
19615732
LPPRC_HUMANLRPPRCphysical
19615732
IPO7_HUMANIPO7physical
19615732
STIP1_HUMANSTIP1physical
19615732
KRR1_HUMANKRR1physical
19615732
PP6R1_HUMANPPP6R1physical
19615732
ANR28_HUMANANKRD28physical
19615732
DICER_HUMANDICER1physical
19615732
SYYM_HUMANYARS2physical
19615732
UBR5_HUMANUBR5physical
19615732
PP6R3_HUMANPPP6R3physical
19615732
IPO9_HUMANIPO9physical
19615732
SHCBP_HUMANSHCBP1physical
19615732
NUP85_HUMANNUP85physical
19615732
UBP44_HUMANUSP44physical
19615732
SHPRH_HUMANSHPRHphysical
19615732
ANR52_HUMANANKRD52physical
19615732
TRI35_HUMANTRIM35physical
23105109
HOIL1_HUMANRBCK1physical
23105109
H2B2E_HUMANHIST2H2BEphysical
23824326
RUVB1_HUMANRUVBL1physical
23824326
PRS8_HUMANPSMC5physical
23824326
STING_HUMANTMEM173physical
27801882
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP49_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory