GORS1_HUMAN - dbPTM
GORS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GORS1_HUMAN
UniProt AC Q9BQQ3
Protein Name Golgi reassembly-stacking protein 1
Gene Name GORASP1
Organism Homo sapiens (Human).
Sequence Length 440
Subcellular Localization Golgi apparatus, cis-Golgi network membrane
Peripheral membrane protein
Cytoplasmic side . Undergoes rapid exchange with the cytosol.
Protein Description Stacking factor involved in the postmitotic assembly of Golgi stacks from mitotic Golgi fragments. Key structural protein required for the maintenance of the Golgi apparatus integrity: its caspase-mediated cleavage is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes. [PubMed: 16489344]
Protein Sequence MGLGVSAEQPAGGAEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSDQILQESEDFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAPGSSMEDPLPGPGSPSHSAPDPDGLPHFMETPLQPPPPVQRVMDPGFLDVSGISLLDNSNASVWPSLPSSTELTTTAVSTSGPEDICSSSSSHERGGEATWSGSEFEVSFLDSPGAQAQADHLPQLTLPDSLTSAASPEDGLSAELLEAQAEEEPASTEGLDTGTEAEGLDSQAQISTTE
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
2N-myristoyl glycine------MGLGVSAEQ
------CCCCCCCCC		31.01-
2Myristoylation------MGLGVSAEQ
------CCCCCCCCC		31.01-
50UbiquitinationIGHSRLNKENDTLKA
ECCHHHCCCCHHHHH		63.59-
56 (in isoform 2)Ubiquitination-38.8021890473
56UbiquitinationNKENDTLKALLKANV
CCCCHHHHHHHHCCC		38.8021890473
56 (in isoform 1)Ubiquitination-38.8021890473
56UbiquitinationNKENDTLKALLKANV
CCCCHHHHHHHHCCC		38.8021890473
60UbiquitinationDTLKALLKANVEKPV
HHHHHHHHCCCCCCE		38.47-
60MalonylationDTLKALLKANVEKPV
HHHHHHHHCCCCCCE		38.4726320211
65UbiquitinationLLKANVEKPVKLEVF
HHHCCCCCCEEEEEE		51.32-
104PhosphorylationGASVRFCSFRRASEQ
HCEEEECCCEECCCC		21.05-
169AcetylationKLMVYNSKSDSCREV
EEEEEECCCCCCEEE		55.4326051181
169MalonylationKLMVYNSKSDSCREV
EEEEEECCCCCCEEE		55.4326320211
169UbiquitinationKLMVYNSKSDSCREV
EEEEEECCCCCCEEE		55.43-
189PhosphorylationAAWGGEGSLGCGIGY
CCCCCCCCCCCCCCC		19.7922523075
204PhosphorylationGYLHRIPTQPPSYHK
CCCCCCCCCCCCCCC		51.8723312004
208PhosphorylationRIPTQPPSYHKKPPG
CCCCCCCCCCCCCCC		46.6923312004
209PhosphorylationIPTQPPSYHKKPPGT
CCCCCCCCCCCCCCC		24.3524275569
216PhosphorylationYHKKPPGTPPPSALP
CCCCCCCCCCCCCCC		38.0929255136
220PhosphorylationPPGTPPPSALPLGAP
CCCCCCCCCCCCCCC		48.4923401153
237PhosphorylationDALPPGPTPEDSPSL
CCCCCCCCCCCCCCC		45.2729255136
241PhosphorylationPGPTPEDSPSLETGS
CCCCCCCCCCCCCCC		18.0930278072
243PhosphorylationPTPEDSPSLETGSRQ
CCCCCCCCCCCCCCC		42.6730278072
246PhosphorylationEDSPSLETGSRQSDY
CCCCCCCCCCCCHHH		45.8330278072
248PhosphorylationSPSLETGSRQSDYME
CCCCCCCCCCHHHHH		34.2730278072
253PhosphorylationTGSRQSDYMEALLQA
CCCCCHHHHHHHHHC		11.34-
274PhosphorylationDPLPGPGSPSHSAPD
CCCCCCCCCCCCCCC		26.7720068231
276PhosphorylationLPGPGSPSHSAPDPD
CCCCCCCCCCCCCCC		31.6020068231
278PhosphorylationGPGSPSHSAPDPDGL
CCCCCCCCCCCCCCC		45.9220068231
349PhosphorylationGPEDICSSSSSHERG
CHHHHHCCCCCCCCC		29.8124275569
352PhosphorylationDICSSSSSHERGGEA
HHHCCCCCCCCCCCC		31.1724275569
362PhosphorylationRGGEATWSGSEFEVS
CCCCCEECCCEEEEE		28.2522468782
364PhosphorylationGEATWSGSEFEVSFL
CCCEECCCEEEEEEE		33.3322468782
373PhosphorylationFEVSFLDSPGAQAQA
EEEEEECCCCHHHCH		27.64-
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
189SPhosphorylationKinasePLK1P53350
PSP
274SPhosphorylationKinaseMAPK9P45984
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW8Q8N3Y1
PMID:24658274
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GORS1_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 GORS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GORS1_HUMANGORASP1physical
12839990
TMED2_HUMANTMED2physical
11739402
GOGA2_HUMANGOLGA2physical
11739402
TMED3_HUMANTMED3physical
11739402
TGFA_HUMANTGFAphysical
11739402
GOGA2_HUMANGOLGA2physical
11739401
FBXW8_HUMANFBXW8physical
21572988
LONF1_HUMANLONRF1physical
25416956
GOGA2_HUMANGOLGA2physical
28514442
CLIP1_HUMANCLIP1physical
28514442
GO45_HUMANBLZF1physical
28514442
TES_HUMANTESphysical
28514442
UBP46_HUMANUSP46physical
28514442
CCNJ_HUMANCCNJphysical
28514442
PP6R2_HUMANPPP6R2physical
28514442
SLX4I_HUMANSLX4IPphysical
28514442
CH60_HUMANHSPD1physical
28514442
AL1A3_HUMANALDH1A3physical
28514442
GUCD1_HUMANGUCD1physical
28514442
TMTC4_HUMANTMTC4physical
28514442
RTCA_HUMANRTCAphysical
28514442
TPRKB_HUMANTPRKBphysical
28514442
NIF3L_HUMANNIF3L1physical
28514442
CLAP2_HUMANCLASP2physical
28514442
STX12_HUMANSTX12physical
28514442
CENPL_HUMANCENPLphysical
28514442
CDK2_HUMANCDK2physical
28514442
DOC11_HUMANDOCK11physical
28514442
WWOX_HUMANWWOXphysical
28514442
UBP12_HUMANUSP12physical
28514442
S15A4_HUMANSLC15A4physical
28514442
F219A_HUMANFAM219Aphysical
28514442
FEM1B_HUMANFEM1Bphysical
28514442
ACSF4_HUMANAASDHphysical
28514442
INT4_HUMANINTS4physical
28514442
TYDP2_HUMANTDP2physical
28514442
MRRP3_HUMANKIAA0391physical
28514442
NXN_HUMANNXNphysical
28514442
CENPN_HUMANCENPNphysical
28514442
SYHM_HUMANHARS2physical
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 GORS1_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 THR-216 AND SER-248, 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 THR-216 AND SER-243, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND MASSSPECTROMETRY.
"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 THR-216, AND MASSSPECTROMETRY.

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