GRAA_HUMAN - dbPTM
GRAA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRAA_HUMAN
UniProt AC P12544
Protein Name Granzyme A
Gene Name GZMA
Organism Homo sapiens (Human).
Sequence Length 262
Subcellular Localization Isoform alpha: Secreted. Cytoplasmic granule.
Protein Description Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA..
Protein Sequence MRNSYRFLASSLSVVVSLLLIPEDVCEKIIGGNEVTPHSRPYMVLLSLDRKTICAGALIAKDWVLTAAHCNLNKRSQVILGAHSITREEPTKQIMLVKKEFPYPCYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDRNHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCEGVFRGVTSFGLENKCGDPRGPGVYILLSKKHLNWIIMTIKGAV
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
47PhosphorylationRPYMVLLSLDRKTIC
CCEEEEEECCCCCCC
24.8624719451
99UbiquitinationKQIMLVKKEFPYPCY
CEEEEEEECCCCCCC
58.0429967540
170N-linked_GlycosylationSDTLREVNITIIDRK
HHHCCEEEEEEECCC
22.4119159218
200PhosphorylationMNMVCAGSLRGGRDS
EEEEECCCCCCCCCC
9.0727080861
226PhosphorylationEGVFRGVTSFGLENK
CCEECCCCCCCCCCC
22.5929396449
227PhosphorylationGVFRGVTSFGLENKC
CEECCCCCCCCCCCC
18.2129396449
257PhosphorylationHLNWIIMTIKGAV--
HCCEEEEEECCCC--
14.77-

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 GRAA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRAA_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 GRAA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMGB2_HUMANHMGB2physical
11909973
NDUS3_HUMANNDUFS3physical
18485875
NDUS3_MOUSENdufs3physical
18485875
LMNA_HUMANLMNAphysical
11331782
H11_HUMANHIST1H1Aphysical
11060286
H2B2E_HUMANHIST2H2BEphysical
11060286
SET_HUMANSETphysical
19059912
GRAA_HUMANGZMAphysical
19059912
ACTG_HUMANACTG1physical
19059912
HNRPK_HUMANHNRNPKphysical
19059912
DCHS_HUMANHDCphysical
19059912
GOGA2_HUMANGOLGA2physical
19059912
XRCC6_HUMANXRCC6physical
16440001
APEX1_HUMANAPEX1physical
17008916
HMGB2_HUMANHMGB2physical
17008916
HSP74_HUMANHSPA4physical
18485875
HS90A_HUMANHSP90AA1physical
18485875

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 GRAA_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-170, AND MASSSPECTROMETRY.

TOP