TOIP2_HUMAN - dbPTM
TOIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOIP2_HUMAN
UniProt AC Q8NFQ8
Protein Name Torsin-1A-interacting protein 2
Gene Name TOR1AIP2
Organism Homo sapiens (Human).
Sequence Length 470
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein. Nucleus membrane.
Protein Description Required for endoplasmic reticulum integrity. Regulates the distribution of TOR1A between the endoplasmic reticulum and the nuclear envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity..
Protein Sequence MADSGLREPQEDSQKDLENDPSVNSQAQETTIIASNAEEAEILHSACGLSKDHQEVETEGPESADTGDKSESPDEANVGKHPKDKTEDENKQSFLDGGKGHHLPSENLGKEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEASDGTGASQEPPTTDSQEAQSPGHSSAGQEGEDTLRRRLLAPEAGSHPQQTQKLEEIKENAQDTMRQINKKGFWSYGPVILVVLVVAVVASSVNSYYSSPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVADAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCLF
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------MADSGLREP
------CCCCCCCCC		21.4821406692
4Phosphorylation----MADSGLREPQE
----CCCCCCCCCCH		30.1325159151
7Methylation-MADSGLREPQEDSQ
-CCCCCCCCCCHHHH		58.01115918749
13PhosphorylationLREPQEDSQKDLEND
CCCCCHHHHHHHHCC		38.0828355574
22PhosphorylationKDLENDPSVNSQAQE
HHHHCCCCCCHHHHH		36.4726471730
25PhosphorylationENDPSVNSQAQETTI
HCCCCCCHHHHHEEE		25.4128348404
30PhosphorylationVNSQAQETTIIASNA
CCHHHHHEEEEECCH		15.9428348404
31PhosphorylationNSQAQETTIIASNAE
CHHHHHEEEEECCHH		15.0528348404
58PhosphorylationKDHQEVETEGPESAD
CCCCCCCCCCCCCCC		51.9629978859
63PhosphorylationVETEGPESADTGDKS
CCCCCCCCCCCCCCC		34.2829978859
66PhosphorylationEGPESADTGDKSESP
CCCCCCCCCCCCCCC		47.1723663014
70PhosphorylationSADTGDKSESPDEAN
CCCCCCCCCCCCCCC		48.3130278072
72PhosphorylationDTGDKSESPDEANVG
CCCCCCCCCCCCCCC		44.7530278072
80AcetylationPDEANVGKHPKDKTE
CCCCCCCCCCCCCCC		53.0726051181
86PhosphorylationGKHPKDKTEDENKQS
CCCCCCCCCCCCCCC		59.82-
93PhosphorylationTEDENKQSFLDGGKG
CCCCCCCCCCCCCCC		29.4125159151
105PhosphorylationGKGHHLPSENLGKEP
CCCCCCCCCCCCCCC		45.5430576142
118PhosphorylationEPLDPDPSHSPSDKV
CCCCCCCCCCCCCCC		43.9330266825
120PhosphorylationLDPDPSHSPSDKVGR
CCCCCCCCCCCCCCC		30.3629255136
122PhosphorylationPDPSHSPSDKVGRAD
CCCCCCCCCCCCCCC		53.7530266825
134PhosphorylationRADAHLGSSSVALPK
CCCCCCCCCCEECCC		26.2925159151
135PhosphorylationADAHLGSSSVALPKE
CCCCCCCCCEECCCC		27.3425159151
136PhosphorylationDAHLGSSSVALPKEA
CCCCCCCCEECCCCC		17.0725159151
144PhosphorylationVALPKEASDGTGASQ
EECCCCCCCCCCCCC		37.3529978859
147PhosphorylationPKEASDGTGASQEPP
CCCCCCCCCCCCCCC		34.2729978859
150PhosphorylationASDGTGASQEPPTTD
CCCCCCCCCCCCCCC		36.1029978859
155PhosphorylationGASQEPPTTDSQEAQ
CCCCCCCCCCCHHHC		54.6828450419
156PhosphorylationASQEPPTTDSQEAQS
CCCCCCCCCCHHHCC		39.1528450419
158PhosphorylationQEPPTTDSQEAQSPG
CCCCCCCCHHHCCCC		28.0321712546
163PhosphorylationTDSQEAQSPGHSSAG
CCCHHHCCCCCCCCC		39.6425159151
167PhosphorylationEAQSPGHSSAGQEGE
HHCCCCCCCCCCCCH		28.0028450419
168PhosphorylationAQSPGHSSAGQEGED
HCCCCCCCCCCCCHH		30.6428450419
176PhosphorylationAGQEGEDTLRRRLLA
CCCCCHHHHHHHHCC		20.1928450419
188PhosphorylationLLAPEAGSHPQQTQK
HCCCCCCCCHHHHHH		38.7626462736
193PhosphorylationAGSHPQQTQKLEEIK
CCCCHHHHHHHHHHH		23.5630266825
195UbiquitinationSHPQQTQKLEEIKEN
CCHHHHHHHHHHHHH		62.3421890473
200UbiquitinationTQKLEEIKENAQDTM
HHHHHHHHHHHHHHH		48.4721890473
207SulfoxidationKENAQDTMRQINKKG
HHHHHHHHHHHHHCC		3.9021406390
286N-linked_GlycosylationKFLQKHLNASNPTEP
HHHHHHHCCCCCCCC		40.83-
289N-linked_GlycosylationQKHLNASNPTEPATI
HHHHCCCCCCCCCEE		45.14UniProtKB CARBOHYD
309UbiquitinationREGRETLKCLSHHVA
CCCHHHHHHHHHHHH		40.32-
310GlutathionylationEGRETLKCLSHHVAD
CCHHHHHHHHHHHHH		5.4722555962
324UbiquitinationDAYTSSQKVSPIQID
HCCCCCCCCCCEEEC		46.78-
326PhosphorylationYTSSQKVSPIQIDGA
CCCCCCCCCEEECCC		24.2620068231
425UbiquitinationVRDLLWAKFTNSDTP
HHHHHHHHCCCCCCC		40.9321890473
433PhosphorylationFTNSDTPTSFNHMDS
CCCCCCCCCCCCCCH		48.30-
440PhosphorylationTSFNHMDSDKLSGLW
CCCCCCCHHHCCHHH		29.12-
442UbiquitinationFNHMDSDKLSGLWSR
CCCCCHHHCCHHHHH		48.8021890473
468GlutathionylationSSIEEQGCLF-----
CCHHHCCCCC-----		3.3422555962
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

Oops, there are no upstream regulatory protein records of TOIP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOIP2_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 TOIP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOR1A_HUMANTOR1Aphysical
20861018
TOR1A_HUMANTOR1Aphysical
15767459
TOR1A_HUMANTOR1Aphysical
23569223
TOR1B_HUMANTOR1Bphysical
24275647
TOR1A_HUMANTOR1Aphysical
25352667
SH3B4_HUMANSH3BP4physical
28514442
MCU_HUMANMCUphysical
28514442
ACSL4_HUMANACSL4physical
28514442
MTCH1_HUMANMTCH1physical
28514442
CQ080_HUMANC17orf80physical
28514442
FOLC_HUMANFPGSphysical
28514442
MOT10_HUMANSLC16A10physical
28514442
ITPA_HUMANITPAphysical
28514442
S20A2_HUMANSLC20A2physical
28514442
GDC_HUMANSLC25A16physical
28514442
RAD21_HUMANRAD21physical
28514442
INT7_HUMANINTS7physical
28514442
GLT11_HUMANGALNT11physical
28514442
MYO1D_HUMANMYO1Dphysical
28514442
OZF_HUMANZNF146physical
28514442
RL23_HUMANRPL23physical
28514442
NSUN3_HUMANNSUN3physical
28514442
S38AA_HUMANSLC38A10physical
28514442
TM223_HUMANTMEM223physical
28514442
PMGT1_HUMANPOMGNT1physical
28514442
NTCP7_HUMANSLC10A7physical
28514442
PXYP1_HUMANPXYLP1physical
28514442
AB17B_HUMANABHD17Bphysical
28514442
GCP4_HUMANTUBGCP4physical
28514442
NDUA1_HUMANNDUFA1physical
28514442
KMCP1_HUMANSLC25A30physical
28514442
RPP29_HUMANPOP4physical
28514442
TIM29_HUMANC19orf52physical
28514442
RPP38_HUMANRPP38physical
28514442
EXT1_HUMANEXT1physical
28514442
UCP5_HUMANSLC25A14physical
28514442
GNL3L_HUMANGNL3Lphysical
28514442
XRCC3_HUMANXRCC3physical
28514442
MTFP1_HUMANMTFP1physical
28514442
MGAT2_HUMANMGAT2physical
28514442
RBM15_HUMANRBM15physical
28514442
TBB8_HUMANTUBB8physical
28514442
SAMD1_HUMANSAMD1physical
28514442
ARL6_HUMANARL6physical
27173435
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 TOIP2_HUMAN

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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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