Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Torsin-1A-interacting protein 2  

UniProtKB / Swiss-Prot ID :  TOIP2_HUMAN

Gene Name (Synonyms) : 
TOR1AIP2, LULL1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane. 

Protein Function :  Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope. 

Transmembrane Topology (topPTM) : TOIP2_HUMAN 

Protein Sequence MADSGLREPQEDSQKDLENDPSVNSQAQETTIIASNAEEAEILHSACGLSKDHQEVETEGPESADTGDKS...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCC...
Protein Variant -
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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
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADSGL
---CCCCCC
21.48UniProtKB
Link-
13PhosphoserinePQEDSQKDL
CCCCCCCCC
38.08Phosphositeplus
Link-
118PhosphoserineDPDPSHSPS
CCCCCCCCC
43.93HPRD
Link-
118PhosphoserineDPDPSHSPS
CCCCCCCCC
43.93PhosphoELM
Link-
120PhosphoserineDPSHSPSDK
CCCCCCCCC
30.36HPRD
Link-
120PhosphoserineDPSHSPSDK
CCCCCCCCC
30.36PhosphoELM
Link-
120PhosphoserineDPSHSPSDK
CCCCCCCCC
30.36Phosphositeplus
Link-
120PhosphoserineDPSHSPSDK
CCCCCCCCC
30.36SysPTM
Link-
120Phosphoserine.DPSHSPSDK
CCCCCCCCC
30.36UniProtKB
Link-
122PhosphoserineSHSPSDKVG
CCCCCCCCC
53.75HPRD
Link-
150PhosphoserineGTGASQEPP
CCCCCCCCC
36.10HPRD
Link-
150PhosphoserineGTGASQEPP
CCCCCCCCC
36.10Phosphositeplus
Link-
155PhosphothreonineQEPPTTDSQ
CCCCCCCCH
54.68Phosphositeplus
Link-
158PhosphoserinePTTDSQEAQ
CCCCCHHCC
28.03HPRD
Link-
158PhosphoserinePTTDSQEAQ
CCCCCHHCC
28.03Phosphositeplus
Link-
163PhosphoserineQEAQSPGHS
HHCCCCCCC
39.64HPRD
Link-
163PhosphoserineQEAQSPGHS
HHCCCCCCC
39.64PhosphoELM
Link-
163PhosphoserineQEAQSPGHS
HHCCCCCCC
39.64Phosphositeplus
Link-
163PhosphoserineQEAQSPGHS
HHCCCCCCC
39.64SysPTM
Link-
163Phosphoserine.QEAQSPGHS
HHCCCCCCC
39.64UniProtKB
Link-
167PhosphoserineSPGHSSAGQ
CCCCCCCCC
28.00HPRD
Link-
167PhosphoserineSPGHSSAGQ
CCCCCCCCC
28.00PhosphoELM
Link-
195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QQTQKLEEI
HHHCCCCHH
62.34Phosphositeplus
Link-
200Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEEIKENAQ
CCHHHHHHH
48.47Phosphositeplus
Link-
326PhosphoserineSQKVSPIQI
HHCCCEEEE
24.26HPRD
Link-
326PhosphoserineSQKVSPIQI
HHCCCEEEE
24.26Phosphositeplus
Link-
425Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLWAKFTNS
HHEEEECCC
40.93Phosphositeplus
Link-
442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MDSDKLSGL
CCHHHHHHH
48.80Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TOR1A_HUMANin vivoHPRD:10048HPRD15767459
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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.
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-120 AND SER-163, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures