ISOC2_HUMAN - dbPTM
ISOC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ISOC2_HUMAN
UniProt AC Q96AB3
Protein Name Isochorismatase domain-containing protein 2
Gene Name ISOC2
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization Cytoplasm . Nucleus . Localizes to the nucleus in the presence of CDKN2A.
Protein Description
Protein Sequence MAAARPSLGRVLPGSSVLFLCDMQEKFRHNIAYFPQIVSVAARMLKVARLLEVPVMLTEQYPQGLGPTVPELGTEGLRPLAKTCFSMVPALQQELDSRPQLRSVLLCGIEAQACILNTTLDLLDRGLQVHVVVDACSSRSQVDRLVALARMRQSGAFLSTSEGLILQLVGDAVHPQFKEIQKLIKEPAPDSGLLGLFQGQNSLLH
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
7Phosphorylation-MAAARPSLGRVLPG
-CCCCCCCCCCCCCC		37.5917192257
15PhosphorylationLGRVLPGSSVLFLCD
CCCCCCCCEEEEEEC		18.4820068231
16PhosphorylationGRVLPGSSVLFLCDM
CCCCCCCEEEEEECC		28.8420068231
21S-nitrosylationGSSVLFLCDMQEKFR
CCEEEEEECCHHHHH		2.9925040305
26 (in isoform 2)Ubiquitination-30.7021890473
26UbiquitinationFLCDMQEKFRHNIAY
EEECCHHHHHHHCCH		30.7021890473
26 (in isoform 1)Ubiquitination-30.7021890473
26UbiquitinationFLCDMQEKFRHNIAY
EEECCHHHHHHHCCH		30.7021890473
26AcetylationFLCDMQEKFRHNIAY
EEECCHHHHHHHCCH		30.7025825284
107S-nitrosylationQLRSVLLCGIEAQAC
HHHHHHHHHHHHHHH		4.5125040305
112AcetylationLLCGIEAQACILNTT
HHHHHHHHHHHHHHH		24.7919608861
112UbiquitinationLLCGIEAQACILNTT
HHHHHHHHHHHHHHH		24.7922817900
114S-nitrosylationCGIEAQACILNTTLD
HHHHHHHHHHHHHHH		2.1225040305
115UbiquitinationGIEAQACILNTTLDL
HHHHHHHHHHHHHHH		3.5922817900
118PhosphorylationAQACILNTTLDLLDR
HHHHHHHHHHHHHHC		25.8720860994
144MethylationSSRSQVDRLVALARM
CCHHHHHHHHHHHHH		32.00115480645
178AcetylationDAVHPQFKEIQKLIK
HHHCHHHHHHHHHHH		48.9725038526
182AcetylationPQFKEIQKLIKEPAP
HHHHHHHHHHHCCCC		58.8219608861
182UbiquitinationPQFKEIQKLIKEPAP
HHHHHHHHHHHCCCC		58.8222817900
185MalonylationKEIQKLIKEPAPDSG
HHHHHHHHCCCCCCC		68.9926320211
185 (in isoform 1)Ubiquitination-68.9921890473
185UbiquitinationKEIQKLIKEPAPDSG
HHHHHHHHCCCCCCC		68.9922817900
185AcetylationKEIQKLIKEPAPDSG
HHHHHHHHCCCCCCC		68.9923954790
191PhosphorylationIKEPAPDSGLLGLFQ
HHCCCCCCCHHHHHC		30.2230108239
198UbiquitinationSGLLGLFQGQNSLLH
CCHHHHHCCCCCCCC		58.5722817900
198AcetylationSGLLGLFQGQNSLLH
CCHHHHHCCCCCCCC		58.5719608861
201 (in isoform 2)Ubiquitination-41.2621890473
201UbiquitinationLGLFQGQNSLLH---
HHHHCCCCCCCC---		41.2622817900
202PhosphorylationGLFQGQNSLLH----
HHHCCCCCCCC----		25.1527499020
218 (in isoform 2)Phosphorylation-24719451
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 ISOC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ISOC2_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 ISOC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ISOC2_HUMANISOC2physical
25416956
FUMH_HUMANFHphysical
26344197
CALL3_HUMANCALML3physical
21516116
HEM2_HUMANALADphysical
28514442
NIT1_HUMANNIT1physical
28514442
TGFA1_HUMANTGFBRAP1physical
28514442
PUSL1_HUMANPUSL1physical
28514442
DNLZ_HUMANDNLZphysical
28514442
SELO_HUMANSELOphysical
28514442
C102A_HUMANCCDC102Aphysical
28514442
VPS11_HUMANVPS11physical
28514442
MPP2_HUMANMPP2physical
28514442
ELP3_HUMANELP3physical
28514442
HBS1L_HUMANHBS1Lphysical
28514442
MTNB_HUMANAPIPphysical
28514442
I5P1_HUMANINPP5Aphysical
28514442
IF172_HUMANIFT172physical
28514442
GTPB1_HUMANGTPBP1physical
28514442
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 ISOC2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.

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