EVI5_HUMAN - dbPTM
EVI5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EVI5_HUMAN
UniProt AC O60447
Protein Name Ecotropic viral integration site 5 protein homolog
Gene Name EVI5
Organism Homo sapiens (Human).
Sequence Length 810
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Associates with the mitotic spindle through anaphase and remains within the midzone and midbody until completion of cytokinesis.
Protein Description Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis..
Protein Sequence MVTNKMTAAFRNPSGKQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSTSLHTTSSSTTLSTPALSPSSPSQLSPDDLELLAKLEEQNRLLETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSMPIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQHFQKVIPHQFDGVPDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELRCLKGQRGFSGQPPFDGIHIVNHLIGDDESFHSSDEDFIDNSLQETGVGFPLHGKSGSMSLDPAVADGSESETEDSVLETRESNQVVQKERPPRRRESYSTTV
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
14PhosphorylationTAAFRNPSGKQVATD
CHHHCCCCCCCCCHH		63.27-
32PhosphorylationEKLSSTLSWVKNTVS
HHHHHHHHHHHHHHH		29.88-
37PhosphorylationTLSWVKNTVSHTVSQ
HHHHHHHHHHHHHHH		20.05-
43PhosphorylationNTVSHTVSQMASQVA
HHHHHHHHHHHHHHC		18.52-
47PhosphorylationHTVSQMASQVASPST
HHHHHHHHHHCCCCC		21.61-
98PhosphorylationEQNRLLETDSKSLRS
HHHHHHHCCCCHHHH		45.6128961369
100PhosphorylationNRLLETDSKSLRSVN
HHHHHCCCCHHHHCC		31.4023186163
102PhosphorylationLLETDSKSLRSVNGS
HHHCCCCHHHHCCCC		32.7329116813
105PhosphorylationTDSKSLRSVNGSRRN
CCCCHHHHCCCCCCC		25.8127251275
113PhosphorylationVNGSRRNSGSSLVSS
CCCCCCCCCCCCCCC		37.9422617229
115PhosphorylationGSRRNSGSSLVSSSS
CCCCCCCCCCCCCCC		21.9623090842
116PhosphorylationSRRNSGSSLVSSSSA
CCCCCCCCCCCCCCC		35.9923090842
119PhosphorylationNSGSSLVSSSSASSN
CCCCCCCCCCCCCCC		29.7823090842
120PhosphorylationSGSSLVSSSSASSNL
CCCCCCCCCCCCCCC		22.3423090842
121PhosphorylationGSSLVSSSSASSNLS
CCCCCCCCCCCCCCC		23.5523090842
122PhosphorylationSSLVSSSSASSNLSH
CCCCCCCCCCCCCCC		33.8323090842
124PhosphorylationLVSSSSASSNLSHLE
CCCCCCCCCCCCCCC		23.0023090842
125PhosphorylationVSSSSASSNLSHLEE
CCCCCCCCCCCCCCC		41.3223090842
128PhosphorylationSSASSNLSHLEEDSW
CCCCCCCCCCCCCCC		30.2123090842
134PhosphorylationLSHLEEDSWILWGRI
CCCCCCCCCHHHHHH		21.2123090842
415PhosphorylationMKKLEKEYTTIKTKE
HHHHHHHHHHHCHHH		21.9129083192
416PhosphorylationKKLEKEYTTIKTKEM
HHHHHHHHHHCHHHH		24.1229083192
417PhosphorylationKLEKEYTTIKTKEME
HHHHHHHHHCHHHHH		21.4129083192
420PhosphorylationKEYTTIKTKEMEEQV
HHHHHHCHHHHHHHH		28.5229083192
450 (in isoform 2)Phosphorylation-47.0528787133
477PhosphorylationARLSEAESQCALKEM
HHHHHHHHHHHHHHH		37.2922817900
493UbiquitinationDKVLDIEKRNNSLPD
HHHHCHHHHCCCCCC		61.84-
497PhosphorylationDIEKRNNSLPDENNI
CHHHHCCCCCCCCHH		44.8420873877
546PhosphorylationWQRHLARTTGRWKDP
HHHHHHHHHCCCCCC		28.17-
687PhosphorylationLQGQLNKSDSNQYIG
CCCCCCCCCCHHHHH		45.2425159151
689PhosphorylationGQLNKSDSNQYIGEL
CCCCCCCCHHHHHHH		32.6825159151
692PhosphorylationNKSDSNQYIGELKDQ
CCCCCHHHHHHHHHH		18.3622985185
763PhosphorylationGFPLHGKSGSMSLDP
CCCCCCCCCCCCCCH		40.4728450419
765PhosphorylationPLHGKSGSMSLDPAV
CCCCCCCCCCCCHHH		16.5828450419
767PhosphorylationHGKSGSMSLDPAVAD
CCCCCCCCCCHHHCC		31.1728450419
776PhosphorylationDPAVADGSESETEDS
CHHHCCCCCCCCCCC		38.2025159151
778PhosphorylationAVADGSESETEDSVL
HHCCCCCCCCCCCHH		52.0623927012
780PhosphorylationADGSESETEDSVLET
CCCCCCCCCCCHHCC		55.1423927012
783PhosphorylationSESETEDSVLETRES
CCCCCCCCHHCCHHH		23.5223927012
787PhosphorylationTEDSVLETRESNQVV
CCCCHHCCHHHCCCC		35.2623927012
790PhosphorylationSVLETRESNQVVQKE
CHHCCHHHCCCCCCC		29.3126699800
805PhosphorylationRPPRRRESYSTTV--
CCCCCCCCCCCCC--		23.6725884760
806PhosphorylationPPRRRESYSTTV---
CCCCCCCCCCCC---		12.7929449344
807PhosphorylationPRRRESYSTTV----
CCCCCCCCCCC----		27.2129449344
808PhosphorylationRRRESYSTTV-----
CCCCCCCCCC-----		24.2823312004
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 EVI5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EVI5_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 EVI5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBX5_HUMANFBXO5physical
16439210
INCE_HUMANINCENPphysical
16764853
AURKB_HUMANAURKBphysical
16764853
BIRC5_HUMANBIRC5physical
16764853
STX3_HUMANSTX3physical
26553929
MYO5B_HUMANMYO5Bphysical
26553929
SYTL4_HUMANSYTL4physical
26553929
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 EVI5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 AND SER-778, ANDMASS SPECTROMETRY.
"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-776 AND SER-778, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND MASSSPECTROMETRY.

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