UBL7_HUMAN - dbPTM
UBL7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBL7_HUMAN
UniProt AC Q96S82
Protein Name Ubiquitin-like protein 7
Gene Name UBL7
Organism Homo sapiens (Human).
Sequence Length 380
Subcellular Localization
Protein Description
Protein Sequence MSLSDWHLAVKLADQPLTPKSILRLPETELGEYSLGGYSISFLKQLIAGKLQESVPDPELIDLIYCGRKLKDDQTLDFYGIQPGSTVHVLRKSWPEPDQKPEPVDKVAAMREFRVLHTALHSSSSYREAVFKMLSNKESLDQIIVATPGLSSDPIALGVLQDKDLFSVFADPNMLDTLVPAHPALVNAIVLVLHSVAGSAPMPGTDSSSRSMPSSSYRDMPGGFLFEGLSDDEDDFHPNTRSTPSSSTPSSRPASLGYSGAAGPRPITQSELATALALASTPESSSHTPTPGTQGHSSGTSPMSSGVQSGTPITNDLFSQALQHALQASGQPSLQSQWQPQLQQLRDMGIQDDELSLRALQATGGDIQAALELIFAGGAP
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
2Phosphorylation------MSLSDWHLA
------CCHHHHHHH		36.2628348404
4Phosphorylation----MSLSDWHLAVK
----CCHHHHHHHHH		31.2025159151
11UbiquitinationSDWHLAVKLADQPLT
HHHHHHHHHCCCCCC		32.1421890473
18PhosphorylationKLADQPLTPKSILRL
HHCCCCCCHHHHHCC		35.0428674419
20UbiquitinationADQPLTPKSILRLPE
CCCCCCHHHHHCCCC		44.9121890473
21PhosphorylationDQPLTPKSILRLPET
CCCCCHHHHHCCCCC		28.2324719451
33PhosphorylationPETELGEYSLGGYSI
CCCCCCCCCCCCCHH		13.85-
34PhosphorylationETELGEYSLGGYSIS
CCCCCCCCCCCCHHH		19.08-
41PhosphorylationSLGGYSISFLKQLIA
CCCCCHHHHHHHHHH		20.7024719451
44UbiquitinationGYSISFLKQLIAGKL
CCHHHHHHHHHHHCH		40.8421906983
51UbiquitinationKQLIAGKLQESVPDP
HHHHHHCHHHCCCCH		7.17-
54PhosphorylationIAGKLQESVPDPELI
HHHCHHHCCCCHHHH		26.45-
58PhosphorylationLQESVPDPELIDLIY
HHHCCCCHHHHHHEE		32.02-
60UbiquitinationESVPDPELIDLIYCG
HCCCCHHHHHHEEEC		4.49-
69UbiquitinationDLIYCGRKLKDDQTL
HHEEECCCCCCCCCC		45.21-
71UbiquitinationIYCGRKLKDDQTLDF
EEECCCCCCCCCCCE		63.3921890473
84UbiquitinationDFYGIQPGSTVHVLR
CEECCCCCCEEEEEE		21.41-
90UbiquitinationPGSTVHVLRKSWPEP
CCCEEEEEECCCCCC		3.26-
92UbiquitinationSTVHVLRKSWPEPDQ
CEEEEEECCCCCCCC		53.3521906983
93PhosphorylationTVHVLRKSWPEPDQK
EEEEEECCCCCCCCC		41.2425159151
100UbiquitinationSWPEPDQKPEPVDKV
CCCCCCCCCCCCHHH		59.7421890473
106UbiquitinationQKPEPVDKVAAMREF
CCCCCCHHHHHHHHH		33.7321890473
109UbiquitinationEPVDKVAAMREFRVL
CCCHHHHHHHHHHHH		10.68-
111UbiquitinationVDKVAAMREFRVLHT
CHHHHHHHHHHHHHH		34.86-
118PhosphorylationREFRVLHTALHSSSS
HHHHHHHHHHHCCCH		27.1023312004
122PhosphorylationVLHTALHSSSSYREA
HHHHHHHCCCHHHHH		32.5323312004
123PhosphorylationLHTALHSSSSYREAV
HHHHHHCCCHHHHHH		16.7423312004
124PhosphorylationHTALHSSSSYREAVF
HHHHHCCCHHHHHHH		34.1124719451
125PhosphorylationTALHSSSSYREAVFK
HHHHCCCHHHHHHHH		30.1123312004
126PhosphorylationALHSSSSYREAVFKM
HHHCCCHHHHHHHHH		17.8923312004
132UbiquitinationSYREAVFKMLSNKES
HHHHHHHHHHCCCHH		32.1221890473
133PhosphorylationYREAVFKMLSNKESL
HHHHHHHHHCCCHHH		3.18-
137UbiquitinationVFKMLSNKESLDQII
HHHHHCCCHHHCEEE		45.352190698
140UbiquitinationMLSNKESLDQIIVAT
HHCCCHHHCEEEEEC		6.19-
146UbiquitinationSLDQIIVATPGLSSD
HHCEEEEECCCCCCC		9.54-
147PhosphorylationLDQIIVATPGLSSDP
HCEEEEECCCCCCCC		13.64-
172UbiquitinationLFSVFADPNMLDTLV
HHHHCCCHHHHHHCC		25.38-
177UbiquitinationADPNMLDTLVPAHPA
CCHHHHHHCCCCCHH		26.20-
187PhosphorylationPAHPALVNAIVLVLH
CCCHHHHHHHHHHHH		25.46-
211PhosphorylationGTDSSSRSMPSSSYR
CCCCCCCCCCCCCCC		36.6724719451
214PhosphorylationSSSRSMPSSSYRDMP
CCCCCCCCCCCCCCC		24.2326270265
215PhosphorylationSSRSMPSSSYRDMPG
CCCCCCCCCCCCCCC		26.0526270265
216PhosphorylationSRSMPSSSYRDMPGG
CCCCCCCCCCCCCCC		28.6426270265
217PhosphorylationRSMPSSSYRDMPGGF
CCCCCCCCCCCCCCC		16.7526270265
230PhosphorylationGFLFEGLSDDEDDFH
CCCCCCCCCCCCCCC		54.6029255136
240PhosphorylationEDDFHPNTRSTPSSS
CCCCCCCCCCCCCCC		30.3723927012
242PhosphorylationDFHPNTRSTPSSSTP
CCCCCCCCCCCCCCC		42.5026074081
243PhosphorylationFHPNTRSTPSSSTPS
CCCCCCCCCCCCCCC		24.7326074081
245PhosphorylationPNTRSTPSSSTPSSR
CCCCCCCCCCCCCCC		36.6926074081
246PhosphorylationNTRSTPSSSTPSSRP
CCCCCCCCCCCCCCC		39.1626074081
247PhosphorylationTRSTPSSSTPSSRPA
CCCCCCCCCCCCCCC		48.9926074081
248PhosphorylationRSTPSSSTPSSRPAS
CCCCCCCCCCCCCCC		29.1926074081
250PhosphorylationTPSSSTPSSRPASLG
CCCCCCCCCCCCCCC		38.7826074081
251PhosphorylationPSSSTPSSRPASLGY
CCCCCCCCCCCCCCC		43.4126425664
254PhosphorylationSTPSSRPASLGYSGA
CCCCCCCCCCCCCCC		19.10-
255PhosphorylationTPSSRPASLGYSGAA
CCCCCCCCCCCCCCC		25.6326074081
258PhosphorylationSRPASLGYSGAAGPR
CCCCCCCCCCCCCCC		14.8226074081
259PhosphorylationRPASLGYSGAAGPRP
CCCCCCCCCCCCCCC		21.8426074081
268PhosphorylationAAGPRPITQSELATA
CCCCCCCCHHHHHHH		28.8226074081
270PhosphorylationGPRPITQSELATALA
CCCCCCHHHHHHHHH		26.4020166139
348SulfoxidationQLQQLRDMGIQDDEL
HHHHHHHCCCCCCHH		4.0421406390
356PhosphorylationGIQDDELSLRALQAT
CCCCCHHHHHHHHHC		17.4824719451
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 UBL7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBL7_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 UBL7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
16731964
ZRAB2_HUMANZRANB2physical
22939629
UBP34_HUMANUSP34physical
22939629
ZPR1_HUMANZPR1physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
VPS29_HUMANVPS29physical
22939629
UBQL2_HUMANUBQLN2physical
22939629
UBQL1_HUMANUBQLN1physical
22939629
ZYX_HUMANZYXphysical
22939629
UCHL3_HUMANUCHL3physical
22939629
UBE4B_HUMANUBE4Bphysical
22863883
UBB_HUMANUBBphysical
26186194
UBE4B_HUMANUBE4Bphysical
26186194
HDAC6_HUMANHDAC6physical
26186194
DDX3X_HUMANDDX3Xphysical
26344197
HS74L_HUMANHSPA4Lphysical
26344197
SNF8_HUMANSNF8physical
26344197
TLN2_HUMANTLN2physical
26344197
UBE4B_HUMANUBE4Bphysical
28514442
RD23B_HUMANRAD23Bphysical
28514442
HDAC6_HUMANHDAC6physical
28514442
TERA_HUMANVCPphysical
28514442
UBB_HUMANUBBphysical
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 UBL7_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-230, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY.

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