UBQL2_HUMAN - dbPTM
UBQL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBQL2_HUMAN
UniProt AC Q9UHD9
Protein Name Ubiquilin-2
Gene Name UBQLN2
Organism Homo sapiens (Human).
Sequence Length 624
Subcellular Localization Cytoplasm . Nucleus . Membrane . Cytoplasmic vesicle, autophagosome . Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells.
Protein Description Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. [PubMed: 10983987 Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome]
Protein Sequence MAENGESSGPPRPSRGPAAAQGSAAAPAEPKIIKVTVKTPKEKEEFAVPENSSVQQFKEAISKRFKSQTDQLVLIFAGKILKDQDTLIQHGIHDGLTVHLVIKSQNRPQGQSTQPSNAAGTNTTSASTPRSNSTPISTNSNPFGLGSLGGLAGLSSLGLSSTNFSELQSQMQQQLMASPEMMIQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHLLNNPDIMRQTLEIARNPAMMQEMMRNQDLALSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFASVGSSSSSGEGTQPSRTENRDPLPNPWAPPPATQSSATTSTTTSTGSGSGNSSSNATGNTVAAANYVASIFSTPGMQSLLQQITENPQLIQNMLSAPYMRSMMQSLSQNPDLAAQMMLNSPLFTANPQLQEQMRPQLPAFLQQMQNPDTLSAMSNPRAMQALMQIQQGLQTLATEAPGLIPSFTPGVGVGVLGTAIGPVGPVTPIGPIGPIVPFTPIGPIGPIGPTGPAAPPGSTGSGGPTGPTVSSAAPSETTSPTSESGPNQQFIQQMVQALAGANAPQLPNPEVRFQQQLEQLNAMGFLNREANLQALIATGGDINAAIERLLGSQPS
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
2Acetylation------MAENGESSG
------CCCCCCCCC		20.9722814378
8PhosphorylationMAENGESSGPPRPSR
CCCCCCCCCCCCCCC		51.5224719451
23PhosphorylationGPAAAQGSAAAPAEP
CCCHHCCCCCCCCCC		11.5829978859
31AcetylationAAAPAEPKIIKVTVK
CCCCCCCCEEEEEEC		48.8723236377
31UbiquitinationAAAPAEPKIIKVTVK
CCCCCCCCEEEEEEC		48.8722817900
34UbiquitinationPAEPKIIKVTVKTPK
CCCCCEEEEEECCCC		35.0122817900
36PhosphorylationEPKIIKVTVKTPKEK
CCCEEEEEECCCCHH		15.9829083192
38UbiquitinationKIIKVTVKTPKEKEE
CEEEEEECCCCHHHC		50.1423000965
39PhosphorylationIIKVTVKTPKEKEEF
EEEEEECCCCHHHCC		34.9420068231
41UbiquitinationKVTVKTPKEKEEFAV
EEEECCCCHHHCCCC		83.2523000965
43UbiquitinationTVKTPKEKEEFAVPE
EECCCCHHHCCCCCC		69.5323000965
43AcetylationTVKTPKEKEEFAVPE
EECCCCHHHCCCCCC		69.5323236377
58UbiquitinationNSSVQQFKEAISKRF
CCHHHHHHHHHHHHH		41.7323000965
62PhosphorylationQQFKEAISKRFKSQT
HHHHHHHHHHHHHHH		25.4822210691
63UbiquitinationQFKEAISKRFKSQTD
HHHHHHHHHHHHHHH		56.6023000965
66UbiquitinationEAISKRFKSQTDQLV
HHHHHHHHHHHHHEE		45.7623000965
67PhosphorylationAISKRFKSQTDQLVL
HHHHHHHHHHHHEEE		35.2821712546
69PhosphorylationSKRFKSQTDQLVLIF
HHHHHHHHHHEEEEE		32.5722210691
79UbiquitinationLVLIFAGKILKDQDT
EEEEEECHHHCCCCH		41.2423000965
82UbiquitinationIFAGKILKDQDTLIQ
EEECHHHCCCCHHHH		57.7423000965
104O-linked_GlycosylationTVHLVIKSQNRPQGQ
EEEEEEECCCCCCCC		22.8930059200
112PhosphorylationQNRPQGQSTQPSNAA
CCCCCCCCCCCCCCC		35.5227732954
112O-linked_GlycosylationQNRPQGQSTQPSNAA
CCCCCCCCCCCCCCC		35.5230059200
113PhosphorylationNRPQGQSTQPSNAAG
CCCCCCCCCCCCCCC		36.2927732954
113O-linked_GlycosylationNRPQGQSTQPSNAAG
CCCCCCCCCCCCCCC		36.2930059200
116O-linked_GlycosylationQGQSTQPSNAAGTNT
CCCCCCCCCCCCCCC		29.3230059200
116PhosphorylationQGQSTQPSNAAGTNT
CCCCCCCCCCCCCCC		29.3227732954
121O-linked_GlycosylationQPSNAAGTNTTSAST
CCCCCCCCCCCCCCC		25.3530059200
121PhosphorylationQPSNAAGTNTTSAST
CCCCCCCCCCCCCCC		25.3523186163
123O-linked_GlycosylationSNAAGTNTTSASTPR
CCCCCCCCCCCCCCC		23.2030059200
123PhosphorylationSNAAGTNTTSASTPR
CCCCCCCCCCCCCCC		23.2029116813
124O-linked_GlycosylationNAAGTNTTSASTPRS
CCCCCCCCCCCCCCC		25.1030059200
124PhosphorylationNAAGTNTTSASTPRS
CCCCCCCCCCCCCCC		25.1021955146
125O-linked_GlycosylationAAGTNTTSASTPRSN
CCCCCCCCCCCCCCC		20.4130059200
125PhosphorylationAAGTNTTSASTPRSN
CCCCCCCCCCCCCCC		20.4128985074
127O-linked_GlycosylationGTNTTSASTPRSNST
CCCCCCCCCCCCCCC		38.4230059200
127PhosphorylationGTNTTSASTPRSNST
CCCCCCCCCCCCCCC		38.4221955146
128O-linked_GlycosylationTNTTSASTPRSNSTP
CCCCCCCCCCCCCCC		23.5730059200
128PhosphorylationTNTTSASTPRSNSTP
CCCCCCCCCCCCCCC		23.5721955146
206SulfoxidationDLMRQLIMANPQMQQ
HHHHHHHHHCHHHHH		3.9228183972
211SulfoxidationLIMANPQMQQLIQRN
HHHHCHHHHHHHHHC		2.6428183972
222PhosphorylationIQRNPEISHLLNNPD
HHHCHHHHHHHCCHH		13.35-
249MethylationAMMQEMMRNQDLALS
HHHHHHHHCCCHHHH		36.03-
256PhosphorylationRNQDLALSNLESIPG
HCCCHHHHCHHCCCC		33.4927050516
260PhosphorylationLALSNLESIPGGYNA
HHHHCHHCCCCHHHH		36.9328152594
265PhosphorylationLESIPGGYNALRRMY
HHCCCCHHHHHHHHH		11.8128152594
269MethylationPGGYNALRRMYTDIQ
CCHHHHHHHHHHHCH		20.93-
272PhosphorylationYNALRRMYTDIQEPM
HHHHHHHHHHCHHHH		10.2324043423
273PhosphorylationNALRRMYTDIQEPML
HHHHHHHHHCHHHHH		19.7924043423
294PhosphorylationFGGNPFASVGSSSSS
HCCCCCCCCCCCCCC		27.6524043423
297PhosphorylationNPFASVGSSSSSGEG
CCCCCCCCCCCCCCC		25.5422210691
298PhosphorylationPFASVGSSSSSGEGT
CCCCCCCCCCCCCCC		28.4524043423
299PhosphorylationFASVGSSSSSGEGTQ
CCCCCCCCCCCCCCC		30.1624043423
300PhosphorylationASVGSSSSSGEGTQP
CCCCCCCCCCCCCCC		44.2924043423
301PhosphorylationSVGSSSSSGEGTQPS
CCCCCCCCCCCCCCC		42.6924043423
305PhosphorylationSSSSGEGTQPSRTEN
CCCCCCCCCCCCCCC		32.7622210691
308PhosphorylationSGEGTQPSRTENRDP
CCCCCCCCCCCCCCC		41.8522210691
508O-linked_GlycosylationIGPIVPFTPIGPIGP
CCCCCCCCCCCCCCC		14.1330059200
519O-linked_GlycosylationPIGPIGPTGPAAPPG
CCCCCCCCCCCCCCC		51.0530059200
527O-linked_GlycosylationGPAAPPGSTGSGGPT
CCCCCCCCCCCCCCC		35.0630059200
528O-linked_GlycosylationPAAPPGSTGSGGPTG
CCCCCCCCCCCCCCC		41.0830059200
530O-linked_GlycosylationAPPGSTGSGGPTGPT
CCCCCCCCCCCCCCC		40.4430059200
539O-linked_GlycosylationGPTGPTVSSAAPSET
CCCCCCCCCCCCCCC		19.4130059200
546O-linked_GlycosylationSSAAPSETTSPTSES
CCCCCCCCCCCCCCC		36.5930059200
550O-linked_GlycosylationPSETTSPTSESGPNQ
CCCCCCCCCCCCCCH		44.9130059200
551O-linked_GlycosylationSETTSPTSESGPNQQ
CCCCCCCCCCCCCHH		32.9030059200
553O-linked_GlycosylationTTSPTSESGPNQQFI
CCCCCCCCCCCHHHH		60.3630059200
621PhosphorylationAIERLLGSQPS----
HHHHHHCCCCC----		38.6028985074
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBQL2_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 UBQL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSA6_HUMANPSMA6physical
10983987
HERC3_HUMANHERC3physical
18535780
HERP1_HUMANHERPUD1physical
18307982
PSA2_HUMANPSMA2physical
12972570
B2L11_HUMANBCL2L11physical
21378313
UBQL1_HUMANUBQLN1physical
16813565
UBQL2_HUMANUBQLN2physical
16813565
EPS15_HUMANEPS15physical
18199683
EPN1_HUMANEPN1physical
18199683
EPN2_HUMANEPN2physical
18199683
YAP1_HUMANYAP1physical
22939629
ZRAB2_HUMANZRANB2physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
ANCHR_HUMANZFYVE19physical
22939629
UPAR_HUMANPLAURphysical
22939629
TADBP_HUMANTARDBPphysical
23541532
FAF2_HUMANFAF2physical
24215460
AASD1_HUMANAARSD1physical
22863883
PUR8_HUMANADSLphysical
22863883
CALU_HUMANCALUphysical
22863883
MARCS_HUMANMARCKSphysical
22863883
PDIA1_HUMANP4HBphysical
22863883
PDE12_HUMANPDE12physical
22863883
PFD2_HUMANPFDN2physical
22863883
WDR4_HUMANWDR4physical
22863883
ADRM1_MOUSEAdrm1physical
25666615
PRS7_HUMANPSMC2physical
25666615
PRS4_HUMANPSMC1physical
25666615
RD23A_HUMANRAD23Aphysical
26344197
RD23B_HUMANRAD23Bphysical
26344197
PSA6_HUMANPSMA6physical
26075709
PSA5_HUMANPSMA5physical
26075709
UBC_HUMANUBCphysical
26075709
ROA1_HUMANHNRNPA1physical
25616961
ROA3_HUMANHNRNPA3physical
25616961
HNRPU_HUMANHNRNPUphysical
25616961
UBQL2_HUMANUBQLN2physical
27477512
PSA6_HUMANPSMA6physical
27477512
HSP7C_HUMANHSPA8physical
27477512
UBC_HUMANUBCphysical
27477512
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300857Amyotrophic lateral sclerosis 15, with or without frontotemporal dementia (ALS15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBQL2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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