TOIP1_MOUSE - dbPTM
TOIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOIP1_MOUSE
UniProt AC Q921T2
Protein Name Torsin-1A-interacting protein 1
Gene Name Tor1aip1
Organism Mus musculus (Mouse).
Sequence Length 595
Subcellular Localization Nucleus inner membrane
Single-pass membrane protein.
Protein Description Required for nuclear membrane integrity. Induces TOR1A and TOR1B ATPase activity and is required for their location on the nuclear membrane. Binds to A- and B-type lamins. Possible role in membrane attachment and assembly of the nuclear lamina..
Protein Sequence MAGERWQAEGPGEGWAIYVTPRAPIREGRRRLDPRNGDSSDAPAYGAHPSRRGRREVRFSEEPAEVYGDFEPRAAKERSPGGRRTPPEKFRPASAGEEVRESAYNLRSRPRRQRRAQEAEEMKTRRSARLEQHSQQPQLSPATSGRGLRDSPSSSEDREEDEPSSRPVTSQTASKKTLRTPEASVMNEDPISNLCRPPLRSPRLDSTYQTNGNTKTNEREATIVQQVNFFEEGETEDDLESSYSDITIRARSSDSLESRDEATPAAGNHPDSLRGLPHNQDFPAHENQPLLLTSGCQENPQEWVDRAVRMRSRMAYNNIQKSNFGNQSPSTSRPQSAIHHPNEPSVKIKWWLLGLVAILAVGLFWFFHTPAVETTAVQEFQNQMKQLQSKYQSQNEKLWKRGTTFLEKHLNSSLPRPQPAILLLTAAQDAAEVLKCLSEQIADAYSSFRSVRAIRIDGAGKAAQDSDLVKHEVDQELTDGFKNGQNAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVLTVLLEEKTLEASLGLKEIEEKVRDFLKVKFTSSSTASSYNHMDPDKLNGLWSRISHLVLPVQPENTLKAGSCL
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
60PhosphorylationGRREVRFSEEPAEVY
CCCEEECCCCCHHHH		30.4125521595
67PhosphorylationSEEPAEVYGDFEPRA
CCCCHHHHCCCCCHH		11.5030635358
79PhosphorylationPRAAKERSPGGRRTP
CHHHHHCCCCCCCCC		29.0523684622
85PhosphorylationRSPGGRRTPPEKFRP
CCCCCCCCCCHHHCC		41.6622324799
89MalonylationGRRTPPEKFRPASAG
CCCCCCHHHCCCCCC		53.0726320211
94PhosphorylationPEKFRPASAGEEVRE
CHHHCCCCCCHHHHH		39.2227149854
127PhosphorylationEEMKTRRSARLEQHS
HHHHHHHHHHHHHHC		17.9129109428
134PhosphorylationSARLEQHSQQPQLSP
HHHHHHHCCCCCCCC		30.1525619855
140PhosphorylationHSQQPQLSPATSGRG
HCCCCCCCCCCCCCC		13.7719144319
140PhosphorylationHSQQPQLSPATSGRG
HCCCCCCCCCCCCCC		13.7727087446
143PhosphorylationQPQLSPATSGRGLRD
CCCCCCCCCCCCCCC		34.7921082442
144PhosphorylationPQLSPATSGRGLRDS
CCCCCCCCCCCCCCC		28.7122942356
151PhosphorylationSGRGLRDSPSSSEDR
CCCCCCCCCCCCCCC		21.9025521595
153PhosphorylationRGLRDSPSSSEDREE
CCCCCCCCCCCCCCC		50.9123684622
154PhosphorylationGLRDSPSSSEDREED
CCCCCCCCCCCCCCC		40.9223684622
155PhosphorylationLRDSPSSSEDREEDE
CCCCCCCCCCCCCCC		48.1023684622
164PhosphorylationDREEDEPSSRPVTSQ
CCCCCCCCCCCCCCC		36.6121149613
165PhosphorylationREEDEPSSRPVTSQT
CCCCCCCCCCCCCCC		51.8521149613
169PhosphorylationEPSSRPVTSQTASKK
CCCCCCCCCCCCCCC		20.1425159016
170PhosphorylationPSSRPVTSQTASKKT
CCCCCCCCCCCCCCC		26.2620531401
172PhosphorylationSRPVTSQTASKKTLR
CCCCCCCCCCCCCCC		32.4425159016
174PhosphorylationPVTSQTASKKTLRTP
CCCCCCCCCCCCCCC		37.7625159016
177PhosphorylationSQTASKKTLRTPEAS
CCCCCCCCCCCCCHH		25.8025159016
180PhosphorylationASKKTLRTPEASVMN
CCCCCCCCCCHHHCC		28.7025159016
184PhosphorylationTLRTPEASVMNEDPI
CCCCCCHHHCCCCCH		21.9025159016
192PhosphorylationVMNEDPISNLCRPPL
HCCCCCHHHCCCCCC		29.1925266776
195GlutathionylationEDPISNLCRPPLRSP
CCCHHHCCCCCCCCC		7.7924333276
201PhosphorylationLCRPPLRSPRLDSTY
CCCCCCCCCCCCCCE		23.2718779572
206PhosphorylationLRSPRLDSTYQTNGN
CCCCCCCCCEECCCC		33.3418779572
214PhosphorylationTYQTNGNTKTNEREA
CEECCCCCCCCHHHE		40.4118779572
215UbiquitinationYQTNGNTKTNEREAT
EECCCCCCCCHHHEE		54.0422790023
215UbiquitinationYQTNGNTKTNEREAT
EECCCCCCCCHHHEE		54.0422790023
235PhosphorylationNFFEEGETEDDLESS
ECCCCCCCHHHHHHH		56.42-
241PhosphorylationETEDDLESSYSDITI
CCHHHHHHHCCCEEE		41.70-
244PhosphorylationDDLESSYSDITIRAR
HHHHHHCCCEEEEEC		25.20-
252PhosphorylationDITIRARSSDSLESR
CEEEEECCCCCCCCC		37.2019144319
252 (in isoform 2)Phosphorylation-37.2025266776
252PhosphorylationDITIRARSSDSLESR
CEEEEECCCCCCCCC		37.2019144319
253PhosphorylationITIRARSSDSLESRD
EEEEECCCCCCCCCC		26.1830635358
253 (in isoform 2)Phosphorylation-26.1825266776
255PhosphorylationIRARSSDSLESRDEA
EEECCCCCCCCCCCC		35.6628833060
255 (in isoform 2)Phosphorylation-35.6630352176
258 (in isoform 2)Phosphorylation-50.7725293948
258PhosphorylationRSSDSLESRDEATPA
CCCCCCCCCCCCCCC		50.7719144319
258PhosphorylationRSSDSLESRDEATPA
CCCCCCCCCCCCCCC		50.7719144319
263PhosphorylationLESRDEATPAAGNHP
CCCCCCCCCCCCCCC		16.0628066266
272PhosphorylationAAGNHPDSLRGLPHN
CCCCCCHHHCCCCCC		25.1528066266
321UbiquitinationMAYNNIQKSNFGNQS
HHHHCCCCCCCCCCC		43.5022790023
321UbiquitinationMAYNNIQKSNFGNQS
HHHHCCCCCCCCCCC		43.5022790023
328PhosphorylationKSNFGNQSPSTSRPQ
CCCCCCCCCCCCCCC		25.4723684622
330PhosphorylationNFGNQSPSTSRPQSA
CCCCCCCCCCCCCCC		44.2428066266
331PhosphorylationFGNQSPSTSRPQSAI
CCCCCCCCCCCCCCC		31.9428066266
332PhosphorylationGNQSPSTSRPQSAIH
CCCCCCCCCCCCCCC		46.4228066266
336PhosphorylationPSTSRPQSAIHHPNE
CCCCCCCCCCCCCCC		31.6928285833
411N-linked_GlycosylationTFLEKHLNSSLPRPQ
HHHHHHHCCCCCCCC		29.31-
549AcetylationEKVRDFLKVKFTSSS
HHHHHHHEEEECCCC		43.2924062335
553PhosphorylationDFLKVKFTSSSTASS
HHHEEEECCCCCCCC		23.2127149854
554PhosphorylationFLKVKFTSSSTASSY
HHEEEECCCCCCCCC		25.9827149854
555PhosphorylationLKVKFTSSSTASSYN
HEEEECCCCCCCCCC		28.7527149854
556PhosphorylationKVKFTSSSTASSYNH
EEEECCCCCCCCCCC		27.9727149854
557PhosphorylationVKFTSSSTASSYNHM
EEECCCCCCCCCCCC		32.2927149854
559PhosphorylationFTSSSTASSYNHMDP
ECCCCCCCCCCCCCH		33.1827149854
560PhosphorylationTSSSTASSYNHMDPD
CCCCCCCCCCCCCHH		27.7327149854
561PhosphorylationSSSTASSYNHMDPDK
CCCCCCCCCCCCHHH		13.4427149854
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 TOIP1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOIP1_MOUSE !!
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 TOIP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOIP1_HUMANTOR1AIP1physical
20360068
CALX_HUMANCANXphysical
20360068
BLMH_HUMANBLMHphysical
26496610
CO4A_HUMANC4Aphysical
26496610
CALX_HUMANCANXphysical
26496610
CPT1A_HUMANCPT1Aphysical
26496610
DYN2_HUMANDNM2physical
26496610
ERBB2_HUMANERBB2physical
26496610
GALT2_HUMANGALNT2physical
26496610
HXK2_HUMANHK2physical
26496610
PRDX1_HUMANPRDX1physical
26496610
PEX10_HUMANPEX10physical
26496610
PSD11_HUMANPSMD11physical
26496610
AAAT_HUMANSLC1A5physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
PRDX2_HUMANPRDX2physical
26496610
M2OM_HUMANSLC25A11physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
SPN1_HUMANSNUPNphysical
26496610
CEPT1_HUMANCEPT1physical
26496610
SRBS1_HUMANSORBS1physical
26496610
FND3A_HUMANFNDC3Aphysical
26496610
SI1L3_HUMANSIPA1L3physical
26496610
CYFP1_HUMANCYFIP1physical
26496610
ORC3_HUMANORC3physical
26496610
LTN1_HUMANLTN1physical
26496610
GOLI4_HUMANGOLIM4physical
26496610
DC2L1_HUMANDYNC2LI1physical
26496610
RHOF_HUMANRHOFphysical
26496610
SAMD9_HUMANSAMD9physical
26496610
MSTO1_HUMANMSTO1physical
26496610
RN123_HUMANRNF123physical
26496610
TUT7_HUMANZCCHC6physical
26496610
FAP20_HUMANC1orf86physical
26496610
TIM23_HUMANTIMM23physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOIP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-252 ANDSER-258, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.

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