INF2_MOUSE - dbPTM
INF2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INF2_MOUSE
UniProt AC Q0GNC1
Protein Name Inverted formin-2
Gene Name Inf2
Organism Mus musculus (Mouse).
Sequence Length 1273
Subcellular Localization Cytoplasm, perinuclear region.
Protein Description Severs actin filaments and accelerates their polymerization and depolymerization..
Protein Sequence MSVKEGAQRKWAALKEKLGPQDSDPTEANLESAEPELCIRLLQMPSVVNYSGLRKRLESSDGGWMVQFLEQSGLDLLLEALARLSGRGVARISDALLQLTCISCVRAVMNSQQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHALTLDALDHYKMVCSQQYRFSVIMSELSDSDNVPYVVTLLSVINAIILGPEDLRSRAQLRSEFIGLQLLDILTRLRDLEDADLLIQLEAFEEAKAEDEEELQRISDGINMNSHQEVFASLFHKVSCSPASAQLLSVLQGLMHLEPAGRSGQLLWEALENLVNRAVLLASDAQACTLEEVVERLLSIKGRPRPSPLDKAHKSVQTNSVQNQGSSSQNTTTPTTKVEGQQPVVASPCQHVGSIQSSSVDIAPQPVALEQCITALPLPTPPLSSSTPVLPPTPPPLPGPGATSPLPPPPPPLPPPLPGSGTTSPPPPPPPPPPLPPPLPGSGTISPPPPPPPPPLPGTGAVSPPPPPPLPSLPDSHKTQPPPPPPPPLPGMCPVPPPPPLPRAGQIPPPPPLPGFSVPSMMGGVEEIIVAQVDHSLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVARERNSMWATLGSPCTAAVEPDFSSIEQLFSFPTAKPKEPSAAPARKEPKEVTFLDSKKSLNLNIFLKQFKCSNEEVTSMIQAGDTSKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLSNADQFYVLLLDIPCYPLRVECMMLCEGTAIVLDMVRPKAQLVLTACESLLTSQRLPVFCQLILKIGNFLNYGSHTGDADGFKISTLLKLTETKSQQSRVTLLHHVLEEVEKSHPDLLQLSRDLEPPSQAAGINVEIIHSEASANLKKLLEAERKVSASIPEVQKQYAERLQASIEASQELDKVFDAIEQKKLELADYLCEDPQQLSLEDTFSTMKTFRDLFTRALKENKDRKEQMAKAERRKQQLAEEEARRPRDEDGKPIRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTEASGRVAPTDPPKATEPATASNPTQGTNHPASEPLDTTAADEPQGWDLVDAVTPSPQPSKEEDGPPALERRSSWYVDAIDFLDPEDTPDAQPSEGVWPVTLGDGQALNPLEFSSNKPPGVKSSHQDATDPEALWGVHQTEADSTSEGPEDEAQRGQSTHLPRTGPGEDEDGEDTAPESALDTSLDRSFSEDAVTDSSGSGTLPRVQGRVSKGTSKRRKKRPSRNQEEFVPDSDDIKAKRLCVIQ
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
2Phosphorylation------MSVKEGAQR
------CCHHHHHHH		53.8824719451
2Acetylation------MSVKEGAQR
------CCHHHHHHH		53.88-
23PhosphorylationEKLGPQDSDPTEANL
HHHCCCCCCCCHHHH		40.0026824392
26PhosphorylationGPQDSDPTEANLESA
CCCCCCCCHHHHHHC		53.3630635358
100O-linked_GlycosylationSDALLQLTCISCVRA
HHHHHHHHHHHHHHH		8.5422645316
129PhosphorylationQGYVRQLSQALDTSN
HHHHHHHHHHHCCCC		12.6925338131
343PhosphorylationEVVERLLSIKGRPRP
HHHHHHHCCCCCCCC		27.1824719451
351PhosphorylationIKGRPRPSPLDKAHK
CCCCCCCCCCHHHHH		39.1026824392
362PhosphorylationKAHKSVQTNSVQNQG
HHHHHHHCCCCCCCC		27.5725619855
370PhosphorylationNSVQNQGSSSQNTTT
CCCCCCCCCCCCCCC		19.6325619855
371PhosphorylationSVQNQGSSSQNTTTP
CCCCCCCCCCCCCCC		42.6525619855
375PhosphorylationQGSSSQNTTTPTTKV
CCCCCCCCCCCCCEE		25.1425619855
376PhosphorylationGSSSQNTTTPTTKVE
CCCCCCCCCCCCEEC		38.0225619855
377PhosphorylationSSSQNTTTPTTKVEG
CCCCCCCCCCCEECC		19.3225619855
379PhosphorylationSQNTTTPTTKVEGQQ
CCCCCCCCCEECCCC		36.8425619855
380PhosphorylationQNTTTPTTKVEGQQP
CCCCCCCCEECCCCC		34.0125619855
574 (in isoform 3)Phosphorylation-3.6119144319
576 (in isoform 3)Phosphorylation-30.2219144319
596PhosphorylationHRRVNPPTLRMKKLN
CCCCCCCCHHHHHCC		28.4027149854
609PhosphorylationLNWQKLPSNVARERN
CCHHHCCHHHHHHHH		55.1427149854
617PhosphorylationNVARERNSMWATLGS
HHHHHHHCCCHHCCC		23.1723984901
621PhosphorylationERNSMWATLGSPCTA
HHHCCCHHCCCCCCC		19.0123984901
624PhosphorylationSMWATLGSPCTAAVE
CCCHHCCCCCCCCCC		21.6623984901
627PhosphorylationATLGSPCTAAVEPDF
HHCCCCCCCCCCCCC		22.4923984901
706UbiquitinationKFDVEVLKQLLKLLP
CCCHHHHHHHHHHCC		44.0422790023
896UbiquitinationASIPEVQKQYAERLQ
CCCHHHHHHHHHHHH		50.9122790023
909PhosphorylationLQASIEASQELDKVF
HHHHHHHHHHHHHHH		16.0517203969
1082PhosphorylationWDLVDAVTPSPQPSK
CCEEECCCCCCCCCC		21.5525338131
1084PhosphorylationLVDAVTPSPQPSKEE
EEECCCCCCCCCCCC		27.1429514104
1101PhosphorylationPPALERRSSWYVDAI
CCCHHHHHCEEEEEH		31.2925338131
1102PhosphorylationPALERRSSWYVDAID
CCHHHHHCEEEEEHH		22.1828059163
1104PhosphorylationLERRSSWYVDAIDFL
HHHHHCEEEEEHHCC		7.1525338131
1116PhosphorylationDFLDPEDTPDAQPSE
HCCCCCCCCCCCCCC		22.77-
1151PhosphorylationNKPPGVKSSHQDATD
CCCCCCCCCCCCCCC		30.5525777480
1152PhosphorylationKPPGVKSSHQDATDP
CCCCCCCCCCCCCCH		21.3225777480
1157PhosphorylationKSSHQDATDPEALWG
CCCCCCCCCHHHHCE		61.4525777480
1168PhosphorylationALWGVHQTEADSTSE
HHCEEEECCCCCCCC		20.4725159016
1171PhosphorylationGVHQTEADSTSEGPE
EEEECCCCCCCCCCH		46.3324719451
1172PhosphorylationVHQTEADSTSEGPED
EEECCCCCCCCCCHH		40.6627087446
1173PhosphorylationHQTEADSTSEGPEDE
EECCCCCCCCCCHHH		31.2027087446
1174PhosphorylationQTEADSTSEGPEDEA
ECCCCCCCCCCHHHH		44.5027087446
1186PhosphorylationDEAQRGQSTHLPRTG
HHHHCCCCCCCCCCC		22.1830635358
1187PhosphorylationEAQRGQSTHLPRTGP
HHHCCCCCCCCCCCC		21.3930635358
1192PhosphorylationQSTHLPRTGPGEDED
CCCCCCCCCCCCCCC		45.8727180971
1201PhosphorylationPGEDEDGEDTAPESA
CCCCCCCCCCCCHHH		65.5924719451
1203PhosphorylationEDEDGEDTAPESALD
CCCCCCCCCCHHHHH		39.5525521595
1207PhosphorylationGEDTAPESALDTSLD
CCCCCCHHHHHHCCC		32.8329472430
1211PhosphorylationAPESALDTSLDRSFS
CCHHHHHHCCCCCCC		31.8525521595
1212PhosphorylationPESALDTSLDRSFSE
CHHHHHHCCCCCCCC		28.1221149613
1216PhosphorylationLDTSLDRSFSEDAVT
HHHCCCCCCCCCCCC		32.5625521595
1218PhosphorylationTSLDRSFSEDAVTDS
HCCCCCCCCCCCCCC		35.4927742792
1223PhosphorylationSFSEDAVTDSSGSGT
CCCCCCCCCCCCCCC		31.7025619855
1225PhosphorylationSEDAVTDSSGSGTLP
CCCCCCCCCCCCCCC		27.5122942356
1226PhosphorylationEDAVTDSSGSGTLPR
CCCCCCCCCCCCCCC		39.5321082442
1228PhosphorylationAVTDSSGSGTLPRVQ
CCCCCCCCCCCCCEE		30.4722942356
1230PhosphorylationTDSSGSGTLPRVQGR
CCCCCCCCCCCEECC		34.9722942356
1251PhosphorylationKRRKKRPSRNQEEFV
CCCCCCCCCCHHHCC		48.1525619855
1261PhosphorylationQEEFVPDSDDIKAKR
HHHCCCCHHHHHHHE		30.9825619855
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 INF2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INF2_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 INF2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of INF2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INF2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1216, 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-909, AND MASSSPECTROMETRY.

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