UBQL1_HUMAN - dbPTM
UBQL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBQL1_HUMAN
UniProt AC Q9UMX0
Protein Name Ubiquilin-1
Gene Name UBQLN1
Organism Homo sapiens (Human).
Sequence Length 589
Subcellular Localization Cytoplasm . Nucleus . Endoplasmic reticulum . Cytoplasmic vesicle, autophagosome . Cell membrane . Detected in neuronal processes and at synapses (By similarity). Recruited to the ER during ER-associated protein degradation (ERAD) (PubMed:19822669).
Protein Description Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and 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: 15147878 Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome]
Protein Sequence MAESGESGGPPGSQDSAAGAEGAGAPAAAASAEPKIMKVTVKTPKEKEEFAVPENSSVQQFKEEISKRFKSHTDQLVLIFAGKILKDQDTLSQHGIHDGLTVHLVIKTQNRPQDHSAQQTNTAGSNVTTSSTPNSNSTSGSATSNPFGLGGLGGLAGLSSLGLNTTNFSELQSQMQRQLLSNPEMMVQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHMLNNPDIMRQTLELARNPAMMQEMMRNQDRALSNLESIPGGYNALRRMYTDIQEPMLSAAQEQFGGNPFASLVSNTSSGEGSQPSRTENRDPLPNPWAPQTSQSSSASSGTASTVGGTTGSTASGTSGQSTTAPNLVPGVGASMFNTPGMQSLLQQITENPQLMQNMLSAPYMRSMMQSLSQNPDLAAQMMLNNPLFAGNPQLQEQMRQQLPTFLQQMQNPDTLSAMSNPRAMQALLQIQQGLQTLATEAPGLIPGFTPGLGALGSTGGSSGTNGSNATPSENTSPTAGTTEPGHQQFIQQMLQALAGVNPQLQNPEVRFQQQLEQLSAMGFLNREANLQALIATGGDINAAIERLLGSQPS
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------MAESGESGG
------CCCCCCCCC
21.4720068231
4Phosphorylation----MAESGESGGPP
----CCCCCCCCCCC
38.0228355574
7Phosphorylation-MAESGESGGPPGSQ
-CCCCCCCCCCCCCC
53.2025159151
13PhosphorylationESGGPPGSQDSAAGA
CCCCCCCCCCCHHCC
36.2725159151
13 (in isoform 2)Phosphorylation-36.27-
16PhosphorylationGPPGSQDSAAGAEGA
CCCCCCCCHHCCCCC
16.6325159151
16 (in isoform 2)Phosphorylation-16.6321406692
31PhosphorylationGAPAAAASAEPKIMK
CCCHHHHHCCCCEEE
28.5625850435
35 (in isoform 2)Ubiquitination-47.1121890473
35 (in isoform 1)Ubiquitination-47.1121890473
35UbiquitinationAAASAEPKIMKVTVK
HHHHCCCCEEEEEEC
47.1121890473
38UbiquitinationSAEPKIMKVTVKTPK
HCCCCEEEEEECCCH
37.92-
42UbiquitinationKIMKVTVKTPKEKEE
CEEEEEECCCHHHHC
50.14-
43PhosphorylationIMKVTVKTPKEKEEF
EEEEEECCCHHHHCC
34.9420068231
43 (in isoform 2)Phosphorylation-34.94-
45UbiquitinationKVTVKTPKEKEEFAV
EEEECCCHHHHCCCC
83.2521906983
45 (in isoform 1)Ubiquitination-83.2521890473
45 (in isoform 2)Ubiquitination-83.2521890473
47 (in isoform 1)Ubiquitination-69.5321890473
47 (in isoform 2)Ubiquitination-69.5321890473
47UbiquitinationTVKTPKEKEEFAVPE
EECCCHHHHCCCCCC
69.5322053931
62 (in isoform 1)Ubiquitination-50.5321890473
62 (in isoform 2)Ubiquitination-50.5321890473
62UbiquitinationNSSVQQFKEEISKRF
CCHHHHHHHHHHHHH
50.5321890473
67 (in isoform 2)Ubiquitination-68.4621890473
67 (in isoform 1)Ubiquitination-68.4621890473
67UbiquitinationQFKEEISKRFKSHTD
HHHHHHHHHHHHHHH
68.4621906983
70UbiquitinationEEISKRFKSHTDQLV
HHHHHHHHHHHHHEE
45.4121890473
70 (in isoform 2)Ubiquitination-45.4121890473
70 (in isoform 1)Ubiquitination-45.4121890473
83UbiquitinationLVLIFAGKILKDQDT
EEEEEECCHHCCCCH
41.2421890473
83 (in isoform 1)Ubiquitination-41.2421890473
83 (in isoform 2)Ubiquitination-41.2421890473
86UbiquitinationIFAGKILKDQDTLSQ
EEECCHHCCCCHHHH
57.74-
210SulfoxidationDLMRQLIMANPQMQQ
HHHHHHHHHCHHHHH
3.9228183972
215SulfoxidationLIMANPQMQQLIQRN
HHHHCHHHHHHHHHC
2.6428183972
253MethylationAMMQEMMRNQDRALS
HHHHHHHHCHHHHHH
36.03-
257MethylationEMMRNQDRALSNLES
HHHHCHHHHHHCHHH
27.88-
260PhosphorylationRNQDRALSNLESIPG
HCHHHHHHCHHHCCC
38.0827050516
264PhosphorylationRALSNLESIPGGYNA
HHHHCHHHCCCHHHH
36.9328152594
269PhosphorylationLESIPGGYNALRRMY
HHHCCCHHHHHHHHH
11.8128796482
269 (in isoform 2)Phosphorylation-11.81-
273MethylationPGGYNALRRMYTDIQ
CCHHHHHHHHHHHCH
20.93-
276PhosphorylationYNALRRMYTDIQEPM
HHHHHHHHHHCHHHH
10.2327642862
277PhosphorylationNALRRMYTDIQEPML
HHHHHHHHHCHHHHH
19.79-
285PhosphorylationDIQEPMLSAAQEQFG
HCHHHHHHHHHHHHC
18.4625022875
298PhosphorylationFGGNPFASLVSNTSS
HCCCCCHHHHCCCCC
29.6826074081
301PhosphorylationNPFASLVSNTSSGEG
CCCHHHHCCCCCCCC
39.4226074081
303PhosphorylationFASLVSNTSSGEGSQ
CHHHHCCCCCCCCCC
19.4326074081
304PhosphorylationASLVSNTSSGEGSQP
HHHHCCCCCCCCCCC
40.3626074081
305PhosphorylationSLVSNTSSGEGSQPS
HHHCCCCCCCCCCCC
38.5326074081
309PhosphorylationNTSSGEGSQPSRTEN
CCCCCCCCCCCCCCC
34.3226074081
312PhosphorylationSGEGSQPSRTENRDP
CCCCCCCCCCCCCCC
44.1726074081
314PhosphorylationEGSQPSRTENRDPLP
CCCCCCCCCCCCCCC
41.7826074081
328O-linked_GlycosylationPNPWAPQTSQSSSAS
CCCCCCCCCCCCCCC
27.8923301498
329O-linked_GlycosylationNPWAPQTSQSSSASS
CCCCCCCCCCCCCCC
23.8723301498
335O-linked_GlycosylationTSQSSSASSGTASTV
CCCCCCCCCCCCEEC
31.1123301498
349O-linked_GlycosylationVGGTTGSTASGTSGQ
CCCCCCCCCCCCCCC
26.6223301498
402 (in isoform 2)Phosphorylation-11.3221406692
406 (in isoform 2)Phosphorylation-16.4621406692
408 (in isoform 2)Phosphorylation-32.9121406692
422 (in isoform 2)Phosphorylation-27.9921406692
424 (in isoform 2)Phosphorylation-9.6121406692
427 (in isoform 2)Phosphorylation-20.0921406692
518O-linked_GlycosylationTSPTAGTTEPGHQQF
CCCCCCCCCHHHHHH
38.9923301498
557SulfoxidationQLEQLSAMGFLNREA
HHHHHHHCCCCCHHH
3.3328183972
586PhosphorylationAIERLLGSQPS----
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 UBQL1_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 UBQL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTOR_HUMANMTORphysical
11853878
PDIA1_HUMANP4HBphysical
12095988
TMCO6_HUMANTMCO6physical
16189514
UBQL1_HUMANUBQLN1physical
16189514
RIC8A_HUMANRIC8Aphysical
16189514
FBLN4_HUMANEFEMP2physical
16189514
MID49_HUMANMIEF2physical
16189514
KLH42_HUMANKLHL42physical
16189514
PSN1_HUMANPSEN1physical
11076969
PSN2_HUMANPSEN2physical
11076969
UBE3A_HUMANUBE3Aphysical
10983987
HERC3_HUMANHERC3physical
18535780
HERP1_HUMANHERPUD1physical
18307982
PSN2_HUMANPSEN2physical
17614368
PSMD4_HUMANPSMD4physical
16862145
ATX3_HUMANATXN3physical
17082820
EPS15_HUMANEPS15physical
17082820
DNJB2_HUMANDNAJB2physical
17082820
PSMD4_HUMANPSMD4physical
15147878
UBC_HUMANUBCphysical
15147878
PSMD4_HUMANPSMD4physical
11827521
B2L10_HUMANBCL2L10physical
22233804
SCG1_HUMANCHGBphysical
21852239
A4_HUMANAPPphysical
21852239
SPRC_HUMANSPARCphysical
21852239
STMN3_HUMANSTMN3physical
21852239
TCAM1_HUMANTICAM1physical
21695056
MLP3A_HUMANMAP1LC3Aphysical
20529957
UBXN4_HUMANUBXN4physical
19822669
TERA_HUMANVCPphysical
19822669
TADBP_HUMANTARDBPphysical
19112176
A4_HUMANAPPphysical
16945923
UBQL1_HUMANUBQLN1physical
16813565
UBQL2_HUMANUBQLN2physical
16813565
PSN1_HUMANPSEN1physical
16813565
PSN2_HUMANPSEN2physical
16813565
GBRA1_HUMANGABRA1physical
11528422
GBRB2_HUMANGABRB2physical
11528422
GBRB3_HUMANGABRB3physical
11528422
GBRA2_HUMANGABRA2physical
11528422
GBRA3_HUMANGABRA3physical
11528422
GBRA6_HUMANGABRA6physical
11528422
GBRB1_HUMANGABRB1physical
11528422
HGS_HUMANHGSphysical
16159959
STAM2_HUMANSTAM2physical
16159959
GBB1_HUMANGNB1physical
14662753
EPS15_HUMANEPS15physical
18199683
PSMD4_HUMANPSMD4physical
20059542
ADRM1_HUMANADRM1physical
20059542
PSMD4_ARATHRPN10physical
20059542
RPN10_YEASTRPN10physical
20059542
RPN13_ARATHRPN13physical
20059542
ADRM1_HUMANADRM1physical
16713569
RTL8C_HUMANFAM127Aphysical
16713569
FBLN4_HUMANEFEMP2physical
16713569
GKAP1_HUMANGKAP1physical
16713569
RASF5_HUMANRASSF5physical
16713569
RIC8A_HUMANRIC8Aphysical
16713569
SPI2_HUMANSERPINI2physical
16713569
UBQL1_HUMANUBQLN1physical
16713569
ZG16_HUMANZG16physical
16713569
UBC_HUMANUBCphysical
16007098
UBC_HUMANUBCphysical
15004330
PRS7_YEASTRPT1physical
16712842
PRS8_YEASTRPT6physical
16712842
PSB4_YEASTPRE1physical
16712842
UBQL4_HUMANUBQLN4physical
22939629
VP26A_HUMANVPS26Aphysical
22939629
VPS4B_HUMANVPS4Bphysical
22939629
VATB2_HUMANATP6V1B2physical
22939629
ZRAB2_HUMANZRANB2physical
22939629
UCHL3_HUMANUCHL3physical
22939629
USP9X_HUMANUSP9Xphysical
22939629
UBXN1_HUMANUBXN1physical
22939629
VATH_HUMANATP6V1Hphysical
22939629
UNK_HUMANUNKphysical
22939629
WDFY1_HUMANWDFY1physical
22939629
CRCM1_HUMANORAI1physical
23307288
UBQL4_HUMANUBQLN4physical
23459205
MLP3A_HUMANMAP1LC3Aphysical
23459205
DCTP1_HUMANDCTPP1physical
22863883
G3P_HUMANGAPDHphysical
22863883
GNPI1_HUMANGNPDA1physical
22863883
HS71L_HUMANHSPA1Lphysical
22863883
C1TC_HUMANMTHFD1physical
22863883
GDS1_HUMANRAP1GDS1physical
22863883
PYM1_HUMANWIBGphysical
22863883
PSMD3_HUMANPSMD3physical
15147878
UBQL1_HUMANUBQLN1physical
25416956
FBLN4_HUMANEFEMP2physical
25416956
CTAG2_HUMANCTAG2physical
25416956
UBXN1_HUMANUBXN1physical
25416956
TXD12_HUMANTXNDC12physical
25416956
DHB12_HUMANHSD17B12physical
25416956
BPIA1_HUMANBPIFA1physical
25416956
NB5R1_HUMANCYB5R1physical
25416956
GHRL_HUMANGHRLphysical
25416956
MID51_HUMANMIEF1physical
25416956
PLCE_HUMANAGPAT5physical
25416956
TMCO6_HUMANTMCO6physical
25416956
EKI1_HUMANETNK1physical
25416956
NNRD_HUMANCARKDphysical
25416956
NGLY1_HUMANNGLY1physical
25416956
PBIP1_HUMANPBXIP1physical
25416956
KLH42_HUMANKLHL42physical
25416956
RIC8A_HUMANRIC8Aphysical
25416956
MANBL_HUMANMANBALphysical
25416956
XPO4_HUMANXPO4physical
25416956
SIL1_HUMANSIL1physical
25416956
RSRC2_HUMANRSRC2physical
25416956
SMIM2_HUMANSMIM2physical
25416956
TMUB2_HUMANTMUB2physical
25416956
ZN343_HUMANZNF343physical
25416956
RASF5_HUMANRASSF5physical
25416956
C99L2_HUMANCD99L2physical
25416956
P3IP1_HUMANPIK3IP1physical
25416956
C1QT2_HUMANC1QTNF2physical
25416956
PRAP1_HUMANPRAP1physical
25416956
CMTD1_HUMANCOMTD1physical
25416956
ERP27_HUMANERP27physical
25416956
ZG16B_HUMANZG16Bphysical
25416956
MID49_HUMANMIEF2physical
25416956
ZFN2B_HUMANZFAND2Bphysical
25416956
IPIL1_HUMANITPRIPL1physical
25416956
AGR3_HUMANAGR3physical
25416956
TMM31_HUMANTMEM31physical
25416956
RTL8B_HUMANFAM127Cphysical
25416956
ZG16_HUMANZG16physical
25416956
RN208_HUMANRNF208physical
25416956
UBC_HUMANUBCphysical
23823328
UBC_HUMANUBCphysical
23649778
PSA6_HUMANPSMA6physical
19822669
PSA7_HUMANPSMA7physical
19822669
CD3D_HUMANCD3Dphysical
19822669
UBC_HUMANUBCphysical
25752573
ASNS_HUMANASNSphysical
26344197
PDCD6_HUMANPDCD6physical
26344197
RD23A_HUMANRAD23Aphysical
26344197
RD23B_HUMANRAD23Bphysical
26344197
TRIA1_HUMANTRIAP1physical
26344197
ZMYM3_HUMANZMYM3physical
26344197
ZMYM4_HUMANZMYM4physical
26344197
SPI2_HUMANSERPINI2physical
21516116
PARVA_HUMANPARVAphysical
21516116
RIC8A_HUMANRIC8Aphysical
21516116
SCG2_HUMANSCG2physical
21516116
PNMA1_HUMANPNMA1physical
21516116
HERC3_HUMANHERC3physical
26476452
TF65_HUMANRELAphysical
26476452
PRS7_HUMANPSMC2physical
26476452
UBC_HUMANUBCphysical
28075048
B2L10_HUMANBCL2L10physical
28075048
IGF1R_HUMANIGF1Rphysical
28075048
ESYT2_HUMANESYT2physical
28075048
PSMD4_HUMANPSMD4physical
28075048
BAG6_HUMANBAG6physical
28075048
UBQL1_HUMANUBQLN1physical
28075048

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 UBQL1_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