SIVA_HUMAN - dbPTM
SIVA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIVA_HUMAN
UniProt AC O15304
Protein Name Apoptosis regulatory protein Siva
Gene Name SIVA1
Organism Homo sapiens (Human).
Sequence Length 175
Subcellular Localization Cytoplasm . Nucleus . In the nucleus, accumulates in dot-like structures.
Protein Description Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis..
Protein Sequence MPKRSCPFADVAPLQLKVRVSQRELSRGVCAERYSQEVFEKTKRLLFLGAQAYLDHVWDEGCAVVHLPESPKPGPTGAPRAARGQMLIGPDGRLIRSLGQASEADPSGVASIACSSCVRAVDGKAVCGQCERALCGQCVRTCWGCGSVACTLCGLVDCSDMYEKVLCTSCAMFET
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
5Phosphorylation---MPKRSCPFADVA
---CCCCCCCCCCCC
32.0625159151
17UbiquitinationDVAPLQLKVRVSQRE
CCCCCEEEEEEHHHH
18.2921963094
17 (in isoform 1)Ubiquitination-18.2921890473
31 (in isoform 2)Ubiquitination-11.2521890473
34PhosphorylationRGVCAERYSQEVFEK
CCCCHHHHCHHHHHH
13.2511278261
41UbiquitinationYSQEVFEKTKRLLFL
HCHHHHHHHHHHHHH
48.1322817900
41 (in isoform 1)Ubiquitination-48.1321890473
43UbiquitinationQEVFEKTKRLLFLGA
HHHHHHHHHHHHHHH
52.7122817900
53PhosphorylationLFLGAQAYLDHVWDE
HHHHHHHHHHHHCCC
10.6920727854
59UbiquitinationAYLDHVWDEGCAVVH
HHHHHHCCCCEEEEE
41.1233845483
70PhosphorylationAVVHLPESPKPGPTG
EEEECCCCCCCCCCC
35.9622617229
76PhosphorylationESPKPGPTGAPRAAR
CCCCCCCCCCCCCCC
52.4727251275
124UbiquitinationCVRAVDGKAVCGQCE
CEEECCCCEECCCCH
32.9333845483
162PhosphorylationLVDCSDMYEKVLCTS
CCCCHHHHHHHHCHH
20.0020727854

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
34YPhosphorylationKinaseARGP42684
PSP
53YPhosphorylationKinaseTYK2P29597
PSP
162YPhosphorylationKinaseTYK2P29597
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIVA_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 SIVA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LPAR2_HUMANLPAR2physical
19293149
PXMP2_HUMANPXMP2physical
16683188
P53_HUMANTP53physical
19590512
MDM2_HUMANMDM2physical
19590512
XIAP_HUMANXIAPphysical
19584092
A4_HUMANAPPphysical
21832049
CDN2A_HUMANCDKN2Aphysical
23462994
ARF_HUMANCDKN2Aphysical
23462994
UB2D1_HUMANUBE2D1physical
23462994
TA2R_HUMANTBXA2Rphysical
22343716
PCNA_HUMANPCNAphysical
24958773
RAD18_HUMANRAD18physical
24958773
TYK2_HUMANTYK2physical
20727854
CD4_HUMANCD4physical
17653867
TELT_HUMANTCAPphysical
18849585
STMN1_HUMANSTMN1physical
21768358
KCC2G_HUMANCAMK2Gphysical
21768358
P53_HUMANTP53physical
25431847

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 SIVA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The ARG tyrosine kinase interacts with Siva-1 in the apoptoticresponse to oxidative stress.";
Cao C., Ren X., Kharbanda S., Koleske A., Prasad K.V.S., Kufe D.;
J. Biol. Chem. 276:11465-11468(2001).
Cited for: PHOSPHORYLATION AT TYR-34, AND MUTAGENESIS OF TYR-34 AND TYR-53.

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