UBX2B_HUMAN - dbPTM
UBX2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBX2B_HUMAN
UniProt AC Q14CS0
Protein Name UBX domain-containing protein 2B
Gene Name UBXN2B
Organism Homo sapiens (Human).
Sequence Length 331
Subcellular Localization Nucleus . Cytoplasm, cytosol . Endoplasmic reticulum . Golgi apparatus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to centrosome during mitotic prophase and metaphase.
Protein Description Adapter protein required for Golgi and endoplasmic reticulum biogenesis. [PubMed: 17141156 Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis]
Protein Sequence MAEGGGPEPGEQERRSSGPRPPSARDLQLALAELYEDEVKCKSSKSNRPKATVFKSPRTPPQRFYSSEHEYSGLNIVRPSTGKIVNELFKEAREHGAVPLNEATRASGDDKSKSFTGGGYRLGSSFCKRSEYIYGENQLQDVQILLKLWSNGFSLDDGELRPYNEPTNAQFLESVKRGEIPLELQRLVHGGQVNLDMEDHQDQEYIKPRLRFKAFSGEGQKLGSLTPEIVSTPSSPEEEDKSILNAVVLIDDSVPTTKIQIRLADGSRLIQRFNSTHRILDVRNFIVQSRPEFAALDFILVTSFPNKELTDESLTLLEADILNTVLLQQLK
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------MAEGGGPEP
------CCCCCCCCC
24.9222814378
16PhosphorylationPGEQERRSSGPRPPS
CCHHCCCCCCCCCCC
45.9620873877
17PhosphorylationGEQERRSSGPRPPSA
CHHCCCCCCCCCCCH
51.5125159151
23PhosphorylationSSGPRPPSARDLQLA
CCCCCCCCHHHHHHH
38.3224670416
35PhosphorylationQLALAELYEDEVKCK
HHHHHHHHHCHHHCC
16.9128796482
40UbiquitinationELYEDEVKCKSSKSN
HHHHCHHHCCCCCCC
33.62-
46PhosphorylationVKCKSSKSNRPKATV
HHCCCCCCCCCCCEE
39.76-
50UbiquitinationSSKSNRPKATVFKSP
CCCCCCCCCEEECCC
54.15-
52PhosphorylationKSNRPKATVFKSPRT
CCCCCCCEEECCCCC
32.3829449344
55UbiquitinationRPKATVFKSPRTPPQ
CCCCEEECCCCCCCH
56.04-
55MethylationRPKATVFKSPRTPPQ
CCCCEEECCCCCCCH
56.04115978971
56PhosphorylationPKATVFKSPRTPPQR
CCCEEECCCCCCCHH
14.2425159151
59PhosphorylationTVFKSPRTPPQRFYS
EEECCCCCCCHHCCC
42.5825159151
65PhosphorylationRTPPQRFYSSEHEYS
CCCCHHCCCCCCCCC
17.3028450419
66PhosphorylationTPPQRFYSSEHEYSG
CCCHHCCCCCCCCCC
26.9127273156
67PhosphorylationPPQRFYSSEHEYSGL
CCHHCCCCCCCCCCC
31.4326657352
71PhosphorylationFYSSEHEYSGLNIVR
CCCCCCCCCCCCEEC
15.2223927012
72PhosphorylationYSSEHEYSGLNIVRP
CCCCCCCCCCCEECC
33.5428450419
80PhosphorylationGLNIVRPSTGKIVNE
CCCEECCCCHHHHHH
38.9527251275
81PhosphorylationLNIVRPSTGKIVNEL
CCEECCCCHHHHHHH
45.2227251275
83UbiquitinationIVRPSTGKIVNELFK
EECCCCHHHHHHHHH
43.50-
90UbiquitinationKIVNELFKEAREHGA
HHHHHHHHHHHHHCC
64.19-
104PhosphorylationAVPLNEATRASGDDK
CEECCHHHHHCCCCC
22.1628555341
107PhosphorylationLNEATRASGDDKSKS
CCHHHHHCCCCCCCC
39.19-
112PhosphorylationRASGDDKSKSFTGGG
HHCCCCCCCCCCCCC
40.29-
113UbiquitinationASGDDKSKSFTGGGY
HCCCCCCCCCCCCCC
56.16-
114PhosphorylationSGDDKSKSFTGGGYR
CCCCCCCCCCCCCCC
34.82-
125PhosphorylationGGYRLGSSFCKRSEY
CCCCCCCCHHCCHHC
32.6327251275
128UbiquitinationRLGSSFCKRSEYIYG
CCCCCHHCCHHCCCC
57.88-
132PhosphorylationSFCKRSEYIYGENQL
CHHCCHHCCCCCCHH
10.7329978859
134PhosphorylationCKRSEYIYGENQLQD
HCCHHCCCCCCHHHH
19.9329978859
154PhosphorylationKLWSNGFSLDDGELR
HHHHCCCCCCCCCCC
32.0828348404
163PhosphorylationDDGELRPYNEPTNAQ
CCCCCCCCCCCCCHH
26.2328348404
167PhosphorylationLRPYNEPTNAQFLES
CCCCCCCCCHHHHHH
36.6928348404
176UbiquitinationAQFLESVKRGEIPLE
HHHHHHHHCCCCCHH
65.0621906983
205PhosphorylationEDHQDQEYIKPRLRF
CCCCCHHHCCCCEEE
14.4929978859
207UbiquitinationHQDQEYIKPRLRFKA
CCCHHHCCCCEEEEE
24.15-
213UbiquitinationIKPRLRFKAFSGEGQ
CCCCEEEEEECCCCC
41.93-
216PhosphorylationRLRFKAFSGEGQKLG
CEEEEEECCCCCCCC
40.5729978859
221UbiquitinationAFSGEGQKLGSLTPE
EECCCCCCCCCCCCC
66.72-
224PhosphorylationGEGQKLGSLTPEIVS
CCCCCCCCCCCCHHC
39.2330278072
226PhosphorylationGQKLGSLTPEIVSTP
CCCCCCCCCCHHCCC
22.1430278072
231PhosphorylationSLTPEIVSTPSSPEE
CCCCCHHCCCCCHHH
40.0230278072
232PhosphorylationLTPEIVSTPSSPEEE
CCCCHHCCCCCHHHH
19.1230278072
234PhosphorylationPEIVSTPSSPEEEDK
CCHHCCCCCHHHHCC
59.6229255136
235PhosphorylationEIVSTPSSPEEEDKS
CHHCCCCCHHHHCCH
37.2229255136
242PhosphorylationSPEEEDKSILNAVVL
CHHHHCCHHHEEEEE
44.6326657352
276PhosphorylationLIQRFNSTHRILDVR
HHHHHHCCCCEEHHH
19.1124719451
302PhosphorylationALDFILVTSFPNKEL
CCCEEEEECCCCCCC
22.6228450419
303PhosphorylationLDFILVTSFPNKELT
CCEEEEECCCCCCCC
31.0928450419

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
56SPhosphorylationKinaseCDK1P06493
PSP
59TPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBX2B_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 UBX2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INCA1_HUMANINCA1physical
25416956
TERA_HUMANVCPphysical
26186194
MRCKB_HUMANCDC42BPBphysical
26186194
NIF3L_HUMANNIF3L1physical
26186194
PP1R7_HUMANPPP1R7physical
26186194
PP1RB_HUMANPPP1R11physical
26186194
ASPC1_HUMANASPSCR1physical
26186194
ARP6_HUMANACTR6physical
26186194
F104A_HUMANFAM104Aphysical
26186194
ASPC1_HUMANASPSCR1physical
26389662
PP1R7_HUMANPPP1R7physical
26389662
VCIP1_HUMANVCPIP1physical
26389662
PP1RB_HUMANPPP1R11physical
26389662
TERA_HUMANVCPphysical
26389662
LACTB_HUMANLACTBphysical
26389662
PP1A_HUMANPPP1CAphysical
26389662
PP1B_HUMANPPP1CBphysical
26389662
MRCKB_HUMANCDC42BPBphysical
26389662
SC24A_HUMANSEC24Aphysical
26389662
F104A_HUMANFAM104Aphysical
26389662
GSK3B_HUMANGSK3Bphysical
26389662
HPBP1_HUMANHSPBP1physical
26389662
KLH36_HUMANKLHL36physical
26389662
PP1G_HUMANPPP1CCphysical
26389662
TRAF2_HUMANTRAF2physical
26389662
UBR2_HUMANUBR2physical
26389662
FAF1_HUMANFAF1physical
26389662
F104A_HUMANFAM104Aphysical
28514442
MRCKB_HUMANCDC42BPBphysical
28514442
ASPC1_HUMANASPSCR1physical
28514442
TERA_HUMANVCPphysical
28514442
ARP6_HUMANACTR6physical
28514442
PP1R7_HUMANPPP1R7physical
28514442
FA89A_HUMANFAM89Aphysical
28514442
PP1RB_HUMANPPP1R11physical
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 UBX2B_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-231 AND SER-235, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232; SER-234 ANDSER-235, AND MASS SPECTROMETRY.
"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-56 AND THR-59, AND MASSSPECTROMETRY.

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