UBXN6_HUMAN - dbPTM
UBXN6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBXN6_HUMAN
UniProt AC Q9BZV1
Protein Name UBX domain-containing protein 6 {ECO:0000305}
Gene Name UBXN6 {ECO:0000312|HGNC:HGNC:14928}
Organism Homo sapiens (Human).
Sequence Length 441
Subcellular Localization Cytoplasm . Cytoplasm, cytosol . Membrane
Peripheral membrane protein . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Early endosome membrane
Peripheral membrane protein . Late endosome membrane
Peripheral membrane p
Protein Description May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes. [PubMed: 26475856 As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation]
Protein Sequence MKKFFQEFKADIKFKSAGPGQKLKESVGEKAHKEKPNQPAPRPPRQGPTNEAQMAAAAALARLEQKQSRAWGPTSQDTIRNQVRKELQAEATVSGSPEAPGTNVVSEPREEGSAHLAVPGVYFTCPLTGATLRKDQRDACIKEAILLHFSTDPVAASIMKIYTFNKDQDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKLQNKVFQERINCLEGTHEFFEAIGFQKVLLPAQDQEDPEEFYVLSETTLAQPQSLERHKEQLLAAEPVRAKLDRQRRVFQPSPLASQFELPGDFFNLTAEEIKREQRLRSEAVERLSVLRTKAMREKEEQRGLRKYNYTLLRVRLPDGCLLQGTFYARERLGAVYGFVREALQSDWLPFELLASGGQKLSEDENLALNECGLVPSALLTFSWDMAVLEDIKAAGAEPDSILKPELLSAIEKLL
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
2Ubiquitination------MKKFFQEFK
------CHHHHHHHH
59.2823000965
3Ubiquitination-----MKKFFQEFKA
-----CHHHHHHHHH
50.5423000965
9UbiquitinationKKFFQEFKADIKFKS
HHHHHHHHHCCCEEC
44.3823000965
13UbiquitinationQEFKADIKFKSAGPG
HHHHHCCCEECCCCC
47.4927667366
15UbiquitinationFKADIKFKSAGPGQK
HHHCCCEECCCCCHH
34.1027667366
22UbiquitinationKSAGPGQKLKESVGE
ECCCCCHHHHHHHHH
68.4027667366
24SumoylationAGPGQKLKESVGEKA
CCCCHHHHHHHHHHH
55.78-
24UbiquitinationAGPGQKLKESVGEKA
CCCCHHHHHHHHHHH
55.7829967540
24SumoylationAGPGQKLKESVGEKA
CCCCHHHHHHHHHHH
55.78-
26PhosphorylationPGQKLKESVGEKAHK
CCHHHHHHHHHHHHH
33.5628857561
30UbiquitinationLKESVGEKAHKEKPN
HHHHHHHHHHHCCCC
50.2733845483
32 (in isoform 2)Ubiquitination-50.2921906983
32UbiquitinationESVGEKAHKEKPNQP
HHHHHHHHHCCCCCC
50.2921963094
35UbiquitinationGEKAHKEKPNQPAPR
HHHHHHCCCCCCCCC
54.8127667366
66UbiquitinationALARLEQKQSRAWGP
HHHHHHHHHHHHCCC
40.6527667366
68PhosphorylationARLEQKQSRAWGPTS
HHHHHHHHHHCCCCC
30.88-
69UbiquitinationRLEQKQSRAWGPTSQ
HHHHHHHHHCCCCCH
31.6827667366
75PhosphorylationSRAWGPTSQDTIRNQ
HHHCCCCCHHHHHHH
29.2328857561
78PhosphorylationWGPTSQDTIRNQVRK
CCCCCHHHHHHHHHH
17.7528857561
85 (in isoform 1)Ubiquitination-65.0121906983
85UbiquitinationTIRNQVRKELQAEAT
HHHHHHHHHHHHHEE
65.0121906983
92PhosphorylationKELQAEATVSGSPEA
HHHHHHEEECCCCCC
13.5030266825
94PhosphorylationLQAEATVSGSPEAPG
HHHHEEECCCCCCCC
29.2430266825
96PhosphorylationAEATVSGSPEAPGTN
HHEEECCCCCCCCCC
16.4430266825
100UbiquitinationVSGSPEAPGTNVVSE
ECCCCCCCCCCCCCC
48.7827667366
102PhosphorylationGSPEAPGTNVVSEPR
CCCCCCCCCCCCCCC
24.6330266825
106PhosphorylationAPGTNVVSEPREEGS
CCCCCCCCCCCCCCC
37.2926699800
113PhosphorylationSEPREEGSAHLAVPG
CCCCCCCCCCEECCC
18.7826657352
113UbiquitinationSEPREEGSAHLAVPG
CCCCCCCCCCEECCC
18.7827667366
119UbiquitinationGSAHLAVPGVYFTCP
CCCCEECCCEEEECC
22.4121963094
119 (in isoform 2)Ubiquitination-22.4121906983
122PhosphorylationHLAVPGVYFTCPLTG
CEECCCEEEECCCCC
10.0927642862
127UbiquitinationGVYFTCPLTGATLRK
CEEEECCCCCCCCCH
8.2021963094
127 (in isoform 2)Ubiquitination-8.2021906983
128PhosphorylationVYFTCPLTGATLRKD
EEEECCCCCCCCCHH
15.2024076635
131PhosphorylationTCPLTGATLRKDQRD
ECCCCCCCCCHHHHH
28.5728857561
140UbiquitinationRKDQRDACIKEAILL
CHHHHHHHHHHHHHH
5.5230230243
145UbiquitinationDACIKEAILLHFSTD
HHHHHHHHHHHCCCC
4.3922817900
149UbiquitinationKEAILLHFSTDPVAA
HHHHHHHCCCCHHHH
9.4330230243
149 (in isoform 2)Ubiquitination-9.4321906983
166MalonylationMKIYTFNKDQDRVKL
HHHEECCCCHHHHEC
53.2026320211
166UbiquitinationMKIYTFNKDQDRVKL
HHHEECCCCHHHHEC
53.2027667366
172UbiquitinationNKDQDRVKLGVDTIA
CCCHHHHECCHHHHH
40.1821906983
172 (in isoform 1)Ubiquitination-40.1821906983
177PhosphorylationRVKLGVDTIAKYLDN
HHECCHHHHHHHHHH
22.0428857561
180UbiquitinationLGVDTIAKYLDNIHL
CCHHHHHHHHHHCCC
42.3621906983
180 (in isoform 1)Ubiquitination-42.3621906983
181PhosphorylationGVDTIAKYLDNIHLH
CHHHHHHHHHHCCCC
15.4029496907
193UbiquitinationHLHPEEEKYRKIKLQ
CCCHHHHHHHHHHHH
54.3530230243
194PhosphorylationLHPEEEKYRKIKLQN
CCHHHHHHHHHHHHH
22.0327642862
196UbiquitinationPEEEKYRKIKLQNKV
HHHHHHHHHHHHHHH
40.89-
198UbiquitinationEEKYRKIKLQNKVFQ
HHHHHHHHHHHHHHH
47.2422817900
200UbiquitinationKYRKIKLQNKVFQER
HHHHHHHHHHHHHHH
42.5722505724
202 (in isoform 1)Ubiquitination-31.3121906983
202UbiquitinationRKIKLQNKVFQERIN
HHHHHHHHHHHHHHH
31.3121906983
204UbiquitinationIKLQNKVFQERINCL
HHHHHHHHHHHHHCH
7.1522505724
206UbiquitinationLQNKVFQERINCLEG
HHHHHHHHHHHCHHC
44.0221963094
214UbiquitinationRINCLEGTHEFFEAI
HHHCHHCHHHHHHHH
14.6221963094
216UbiquitinationNCLEGTHEFFEAIGF
HCHHCHHHHHHHHCC
52.4429967540
232UbiquitinationKVLLPAQDQEDPEEF
EEEEECCCCCCHHHE
56.8122817900
236UbiquitinationPAQDQEDPEEFYVLS
ECCCCCCHHHEEEEE
42.1122817900
240PhosphorylationQEDPEEFYVLSETTL
CCCHHHEEEEEECCC
12.0825693802
243PhosphorylationPEEFYVLSETTLAQP
HHHEEEEEECCCCCC
23.8930622161
245PhosphorylationEFYVLSETTLAQPQS
HEEEEEECCCCCCCC
24.5930622161
246PhosphorylationFYVLSETTLAQPQSL
EEEEEECCCCCCCCH
18.9530622161
248UbiquitinationVLSETTLAQPQSLER
EEEECCCCCCCCHHH
19.5422817900
248 (in isoform 2)Ubiquitination-19.5421906983
252PhosphorylationTTLAQPQSLERHKEQ
CCCCCCCCHHHHHHH
38.5927470641
257UbiquitinationPQSLERHKEQLLAAE
CCCHHHHHHHHHHHH
54.0722505724
269UbiquitinationAAEPVRAKLDRQRRV
HHHHHHHHHHHCCCC
40.1129967540
272UbiquitinationPVRAKLDRQRRVFQP
HHHHHHHHCCCCCCC
42.2029967540
280PhosphorylationQRRVFQPSPLASQFE
CCCCCCCCCCHHHCC
23.0530622161
284PhosphorylationFQPSPLASQFELPGD
CCCCCCHHHCCCCCC
42.9830622161
291UbiquitinationSQFELPGDFFNLTAE
HHCCCCCCHHCCCHH
42.9222505724
301 (in isoform 1)Ubiquitination-53.8421906983
301UbiquitinationNLTAEEIKREQRLRS
CCCHHHHHHHHHHHH
53.8421906983
308PhosphorylationKREQRLRSEAVERLS
HHHHHHHHHHHHHHH
34.2028555341
315PhosphorylationSEAVERLSVLRTKAM
HHHHHHHHHHHHHHH
25.9028555341
325UbiquitinationRTKAMREKEEQRGLR
HHHHHHHHHHHHCHH
57.0729967540
333MalonylationEEQRGLRKYNYTLLR
HHHHCHHHCCEEEEE
42.7826320211
333UbiquitinationEEQRGLRKYNYTLLR
HHHHCHHHCCEEEEE
42.78-
335UbiquitinationQRGLRKYNYTLLRVR
HHCHHHCCEEEEEEE
26.7522817900
336PhosphorylationRGLRKYNYTLLRVRL
HCHHHCCEEEEEEEC
8.8220090780
337PhosphorylationGLRKYNYTLLRVRLP
CHHHCCEEEEEEECC
18.7128152594
352PhosphorylationDGCLLQGTFYARERL
CCCEEEEEEEHHHHH
10.6628152594
354PhosphorylationCLLQGTFYARERLGA
CEEEEEEEHHHHHHH
12.4628152594
363PhosphorylationRERLGAVYGFVREAL
HHHHHHHHHHHHHHH
12.3328152594
377UbiquitinationLQSDWLPFELLASGG
HHCCCCCHHHHHCCC
10.9422817900
377 (in isoform 2)Ubiquitination-10.9421906983
386UbiquitinationLLASGGQKLSEDENL
HHHCCCCCCCCCCCC
58.2029967540
427PhosphorylationAAGAEPDSILKPELL
HCCCCCCCCCCHHHH
40.3024719451
430 (in isoform 1)Ubiquitination-34.4721906983
430UbiquitinationAEPDSILKPELLSAI
CCCCCCCCHHHHHHH
34.4722817900
439UbiquitinationELLSAIEKLL-----
HHHHHHHHHC-----
49.3129967540
464Ubiquitination------------------------------
------------------------------
22817900

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 UBXN6_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 UBXN6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
19174149
TERA_HUMANVCPphysical
21896481
TERA_HUMANVCPphysical
18775313
PPB1_HUMANALPPphysical
18775313
VCIP1_HUMANVCPIP1physical
18775313
TERA_HUMANVCPphysical
16807242
TERA_HUMANVCPphysical
19275885
DERL1_HUMANDERL1physical
19275885
PSMD2_HUMANPSMD2physical
18656546
TERA_HUMANVCPphysical
22350894
LMAN1_HUMANLMAN1physical
22337587
TERA_HUMANVCPphysical
22337587
LIMA1_HUMANLIMA1physical
22337587
SEPT9_HUMANSEPT9physical
22337587
DYST_HUMANDSTphysical
22337587
TBA1C_HUMANTUBA1Cphysical
22337587
RUVB2_HUMANRUVBL2physical
22337587
ASPC1_HUMANASPSCR1physical
22337587
FAF2_HUMANFAF2physical
22337587
UGGG1_HUMANUGGT1physical
22337587
EF1A2_HUMANEEF1A2physical
22337587
TBB6_HUMANTUBB6physical
22337587
RUVB1_HUMANRUVBL1physical
22337587
RS3_HUMANRPS3physical
22337587
PRKDC_HUMANPRKDCphysical
22337587
TCPQ_HUMANCCT8physical
22337587
IRS4_HUMANIRS4physical
22337587
NPL4_HUMANNPLOC4physical
22337587
CALX_HUMANCANXphysical
22337587
FLOT1_HUMANFLOT1physical
22337587
HNRPU_HUMANHNRNPUphysical
22337587
MCFD2_HUMANMCFD2physical
22337587
COPA_HUMANCOPAphysical
22337587
A4_HUMANAPPphysical
21832049
VPS39_HUMANVPS39physical
22939629
Z3H7B_HUMANZC3H7Bphysical
22939629
XPO6_HUMANXPO6physical
22939629
TERA_HUMANVCPphysical
26186194
NCPR_HUMANPORphysical
26186194
MT21D_HUMANVCPKMTphysical
26186194
UBX2A_HUMANUBXN2Aphysical
26186194
ASPC1_HUMANASPSCR1physical
26186194
F104A_HUMANFAM104Aphysical
26186194
TERA_HUMANVCPphysical
26475856
TERA_HUMANVCPphysical
26389662
NSF1C_HUMANNSFL1Cphysical
26389662
ARAF_HUMANARAFphysical
26389662
ACTBL_HUMANACTBL2physical
26389662
NCPR_HUMANPORphysical
26389662
ASPC1_HUMANASPSCR1physical
26389662
TERA_HUMANVCPphysical
27913212
MT21D_HUMANVCPKMTphysical
28514442
TERA_HUMANVCPphysical
28514442
F104A_HUMANFAM104Aphysical
28514442
UBX2A_HUMANUBXN2Aphysical
28514442
NCPR_HUMANPORphysical
28514442
ASPC1_HUMANASPSCR1physical
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 UBXN6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-96, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-336, AND MASSSPECTROMETRY.

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