Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  UBX domain-containing protein 2B  

UniProtKB / Swiss-Prot ID :  UBX2B_HUMAN

Gene Name (Synonyms) : 
UBXN2B  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Cytoplasm, cytosol (By similarity). Endoplasmic reticulum (By similarity). Golgi apparatus (By similarity). 

Protein Function :  Adapter protein required for Golgi and endoplasmic reticulum biogenesis. Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis. The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L. VCPIP1 is also required, but not its deubiquitinating activity. 

Protein Sequence MAEGGGPEPGEQERRSSGPRPPSARDLQLALAELYEDEVKCKSSKSNRPKATVFKSPRTPPQRFYSSEHE...
Predicted Secondary Structure  -
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
56PhosphoserineTVFKSPRTP
14.24HPRD
Link-
56PhosphoserineTVFKSPRTP
14.24Phosphositeplus
Link-
56PhosphoserineTVFKSPRTP
14.24SysPTM
Link-
56Phosphoserine.TVFKSPRTP
14.24UniProtKB
Link-
59PhosphothreonineKSPRTPPQR
42.58HPRD
Link-
59PhosphothreonineKSPRTPPQR
42.58Phosphositeplus
Link-
59PhosphothreonineKSPRTPPQR
42.58SysPTM
Link-
59Phosphothreonine.KSPRTPPQR
42.58UniProtKB
Link-
66PhosphoserineQRFYSSEHE
26.91Phosphositeplus
Link-
176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LESVKRGEI
65.06Phosphositeplus
Link-
226PhosphothreonineLGSLTPEIV
22.14Phosphositeplus
Link-
231PhosphoserinePEIVSTPSS
40.02HPRD
Link-
231PhosphoserinePEIVSTPSS
40.02Phosphositeplus
Link-
231Phosphoserine.PEIVSTPSS
40.02UniProtKB
Link-
232PhosphothreonineEIVSTPSSP
19.12HPRD
Link-
232Phosphothreonine.EIVSTPSSP
19.12UniProtKB
Link-
234PhosphoserineVSTPSSPEE
59.62HPRD
Link-
234PhosphoserineVSTPSSPEE
59.62Phosphositeplus
Link-
234Phosphoserine.VSTPSSPEE
59.62UniProtKB
Link-
235PhosphoserineSTPSSPEEE
37.22HPRD
Link-
235PhosphoserineSTPSSPEEE
37.22Phosphositeplus
Link-
235Phosphoserine.STPSSPEEE
37.22UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
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-56 AND THR-59, AND MASSSPECTROMETRY.
"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.
"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.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures