UBA5_HUMAN - dbPTM
UBA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA5_HUMAN
UniProt AC Q9GZZ9
Protein Name Ubiquitin-like modifier-activating enzyme 5
Gene Name UBA5
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization Cytoplasm . Nucleus . Golgi apparatus . Localizes mainly in the cytoplasm, while it localizes to the nucleus in presence of SUMO2 (PubMed:18442052).
Protein Description E1-like enzyme which activates UFM1 and SUMO2..
Protein Sequence MAESVERLQQRVQELERELAQERSLQVPRSGDGGGGRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEIIHEDNEWGIELVSEVSEEELKNFSGPVPDLPEGITVAYTIPKKQEDSVTELTVEDSGESLEDLMAKMKNM
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
4Phosphorylation----MAESVERLQQR
----CHHHHHHHHHH		21.5324719451
14UbiquitinationRLQQRVQELERELAQ
HHHHHHHHHHHHHHH		50.1424816145
42UbiquitinationGGRVRIEKMSSEVVD
CCCEEEEECCCCCCC		41.5324816145
43SulfoxidationGRVRIEKMSSEVVDS
CCEEEEECCCCCCCC		3.2821406390
44PhosphorylationRVRIEKMSSEVVDSN
CEEEEECCCCCCCCC		34.1225850435
45PhosphorylationVRIEKMSSEVVDSNP
EEEEECCCCCCCCCH		30.8021082442
50PhosphorylationMSSEVVDSNPYSRLM
CCCCCCCCCHHHHHH		28.2622210691
51UbiquitinationSSEVVDSNPYSRLMA
CCCCCCCCHHHHHHH		34.7629967540
53PhosphorylationEVVDSNPYSRLMALK
CCCCCCHHHHHHHHH		15.6322461510
66PhosphorylationLKRMGIVSDYEKIRT
HHHCCCCCCHHHHHH		32.3320068231
68PhosphorylationRMGIVSDYEKIRTFA
HCCCCCCHHHHHHHE		16.1820068231
70UbiquitinationGIVSDYEKIRTFAVA
CCCCCHHHHHHHEEE		31.1224816145
99UbiquitinationLTRCGIGKLLLFDYD
HHHCCCCCEEEECCC		33.76-
107UbiquitinationLLLFDYDKVELANMN
EEEECCCHHHHCCHH		31.2329967540
127UbiquitinationPHQAGLSKVQAAEHT
HHHCCCHHHHHHHHH		43.33-
134PhosphorylationKVQAAEHTLRNINPD
HHHHHHHHHHHCCCC		20.9328857561
173AcetylationNGGLEEGKPVDLVLS
CCCCCCCCCCCEEEE		45.1826051181
173UbiquitinationNGGLEEGKPVDLVLS
CCCCCCCCCCCEEEE		45.18-
190PhosphorylationDNFEARMTINTACNE
CCCHHHHHHHHHHHH		12.9128176443
193PhosphorylationEARMTINTACNELGQ
HHHHHHHHHHHHHHH		28.8328176443
201PhosphorylationACNELGQTWMESGVS
HHHHHHHHHHHCCCC		25.6128176443
205PhosphorylationLGQTWMESGVSENAV
HHHHHHHCCCCCCCC		28.5228176443
208PhosphorylationTWMESGVSENAVSGH
HHHHCCCCCCCCCCE		28.7628176443
213PhosphorylationGVSENAVSGHIQLII
CCCCCCCCCEEEEEE		23.4228176443
224PhosphorylationQLIIPGESACFACAP
EEEECCCCCCCCCCC		35.9328176443
264UbiquitinationTMGVVAGILVQNVLK
CHHHHHHHHHHHHHH		2.1622817900
265UbiquitinationMGVVAGILVQNVLKF
HHHHHHHHHHHHHHH		2.9522817900
286UbiquitinationVSFYLGYNAMQDFFP
HHEEECHHHHHHHCC		27.4322817900
287UbiquitinationSFYLGYNAMQDFFPT
HEEECHHHHHHHCCC		6.6322817900
296PhosphorylationQDFFPTMSMKPNPQC
HHHCCCCCCCCCCCC		26.5724719451
320UbiquitinationEEYKKKVAALPKQEV
HHHHHHHHHCCHHHH		16.5022817900
321UbiquitinationEYKKKVAALPKQEVI
HHHHHHHHCCHHHHH		27.6422817900
350PhosphorylationIELVSEVSEEELKNF
EEEEEECCHHHHHCC		34.9321815630
358PhosphorylationEEELKNFSGPVPDLP
HHHHHCCCCCCCCCC		52.1321945579
369PhosphorylationPDLPEGITVAYTIPK
CCCCCCEEEEEECCC		15.2221945579
372PhosphorylationPEGITVAYTIPKKQE
CCCEEEEEECCCCCC		10.8121945579
373PhosphorylationEGITVAYTIPKKQED
CCEEEEEECCCCCCC		22.5221945579
376UbiquitinationTVAYTIPKKQEDSVT
EEEEECCCCCCCCCE		64.3422817900
377UbiquitinationVAYTIPKKQEDSVTE
EEEECCCCCCCCCEE		54.2722817900
381PhosphorylationIPKKQEDSVTELTVE
CCCCCCCCCEEEEEE		30.1321712546
383PhosphorylationKKQEDSVTELTVEDS
CCCCCCCEEEEEECC		29.2718669648
386PhosphorylationEDSVTELTVEDSGES
CCCCEEEEEECCCCC		18.6721712546
390PhosphorylationTELTVEDSGESLEDL
EEEEEECCCCCHHHH		30.8421712546
393PhosphorylationTVEDSGESLEDLMAK
EEECCCCCHHHHHHH		40.3528192239
398SulfoxidationGESLEDLMAKMKNM-
CCCHHHHHHHHHCC-		5.3621406390
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 UBA5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA5_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 UBA5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UFM1_HUMANUFM1physical
20562859
UFC1_HUMANUFC1physical
20562859
ALDH2_HUMANALDH2physical
20562859
SYSC_HUMANSARSphysical
20562859
LKHA4_HUMANLTA4Hphysical
20562859
GBRL2_HUMANGABARAPL2physical
20562859
PGK1_HUMANPGK1physical
20562859
FKBP4_HUMANFKBP4physical
20562859
SYTC_HUMANTARSphysical
20562859
PDC6I_HUMANPDCD6IPphysical
20562859
PA2G4_HUMANPA2G4physical
20562859
CBR1_HUMANCBR1physical
20562859
SND1_HUMANSND1physical
20562859
DHB4_HUMANHSD17B4physical
20562859
ENPL_HUMANHSP90B1physical
20562859
PGM1_HUMANPGM1physical
20562859
AL7A1_HUMANALDH7A1physical
20562859
GLYM_HUMANSHMT2physical
20562859
HCDH_HUMANHADHphysical
20562859
SFXN1_HUMANSFXN1physical
20562859
GSTO1_HUMANGSTO1physical
20562859
EIF3A_HUMANEIF3Aphysical
20562859
MCM2_HUMANMCM2physical
20562859
COPB2_HUMANCOPB2physical
20562859
PSMD2_HUMANPSMD2physical
20562859
ETFA_HUMANETFAphysical
20562859
GANAB_HUMANGANABphysical
20562859
SYFB_HUMANFARSBphysical
20562859
NAA15_HUMANNAA15physical
20562859
AMPL_HUMANLAP3physical
20562859
DX39A_HUMANDDX39Aphysical
20562859
ECHM_HUMANECHS1physical
20562859
UFM1_HUMANUFM1physical
15071506
UFM1_HUMANUFM1physical
21304510
UBA5_HUMANUBA5physical
20368332
UBP5_HUMANUSP5physical
22939629
NSF1C_HUMANNSFL1Cphysical
22863883
PARP6_HUMANPARP6physical
22863883
PLIN3_HUMANPLIN3physical
22863883
UFM1_HUMANUFM1physical
24966333
GOGA1_HUMANGOLGA1physical
26496610
CH10_HUMANHSPE1physical
26496610
IPP_HUMANIPPphysical
26496610
P4HA1_HUMANP4HA1physical
26496610
RS28_HUMANRPS28physical
26496610
MOGS_HUMANMOGSphysical
26496610
YBOX3_HUMANYBX3physical
26496610
CYH1_HUMANCYTH1physical
26496610
DDX17_HUMANDDX17physical
26496610
PRDX3_HUMANPRDX3physical
26496610
NCBP2_HUMANNCBP2physical
26496610
UFM1_HUMANUFM1physical
26496610
Z512B_HUMANZNF512Bphysical
26496610
RM17_HUMANMRPL17physical
26496610
AN32E_HUMANANP32Ephysical
26496610
JUPI2_HUMANHN1Lphysical
26496610
MZT2A_HUMANMZT2Aphysical
26496610
ACOX1_HUMANACOX1physical
28514442
UFC1_HUMANUFC1physical
28514442
GBRL2_HUMANGABARAPL2physical
28514442
REXO5_HUMANLOC81691physical
28514442
UFM1_HUMANUFM1physical
28514442
KLHL8_HUMANKLHL8physical
28514442
VATD_HUMANATP6V1Dphysical
28514442
PRPK_HUMANTP53RKphysical
28514442
DPYL1_HUMANCRMP1physical
28514442
G3PT_HUMANGAPDHSphysical
28514442
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 UBA5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASSSPECTROMETRY.

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