GCP60_HUMAN - dbPTM
GCP60_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCP60_HUMAN
UniProt AC Q9H3P7
Protein Name Golgi resident protein GCP60
Gene Name ACBD3
Organism Homo sapiens (Human).
Sequence Length 528
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side. Mitochondrion. Also mitochondrial (via its interaction with PBR)..
Protein Description Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. [PubMed: 11590181 Involved in hormone-induced steroid biosynthesis in testicular Leydig cells (By similarity Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase]
Protein Sequence MAAVLNAERLEVSVDGLTLSPDPEERPGAEGAPLLPPPLPPPSPPGSGRGPGASGEQPEPGEAAAGGAAEEARRLEQRWGFGLEELYGLALRFFKEKDGKAFHPTYEEKLKLVALHKQVLMGPYNPDTCPEVGFFDVLGNDRRREWAALGNMSKEDAMVEFVKLLNRCCHLFSTYVASHKIEKEEQEKKRKEEEERRRREEEERERLQKEEEKRRREEEERLRREEEERRRIEEERLRLEQQKQQIMAALNSQTAVQFQQYAAQQYPGNYEQQQILIRQLQEQHYQQYMQQLYQVQLAQQQAALQKQQEVVVAGSSLPTSSKVNATVPSNMMSVNGQAKTHTDSSEKELEPEAAEEALENGPKESLPVIAAPSMWTRPQIKDFKEKIQQDADSVITVGRGEVVTVRVPTHEEGSYLFWEFATDNYDIGFGVYFEWTDSPNTAVSVHVSESSDDDEEEEENIGCEEKAKKNANKPLLDEIVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKSVYYRVYYTR
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
2Acetylation------MAAVLNAER
------CCCCCCCCE		13.2822223895
13PhosphorylationNAERLEVSVDGLTLS
CCCEEEEEEECEEEC		12.7123401153
18PhosphorylationEVSVDGLTLSPDPEE
EEEEECEEECCCCCC		30.6230278072
20PhosphorylationSVDGLTLSPDPEERP
EEECEEECCCCCCCC		23.2530278072
43PhosphorylationPPPLPPPSPPGSGRG
CCCCCCCCCCCCCCC		49.8829255136
47PhosphorylationPPPSPPGSGRGPGAS
CCCCCCCCCCCCCCC		30.9629255136
54PhosphorylationSGRGPGASGEQPEPG
CCCCCCCCCCCCCCC		49.1025850435
105PhosphorylationDGKAFHPTYEEKLKL
CCCCCCCCHHHHHHH		34.6928152594
106PhosphorylationGKAFHPTYEEKLKLV
CCCCCCCHHHHHHHH		26.9228152594
109AcetylationFHPTYEEKLKLVALH
CCCCHHHHHHHHHHH		38.6926051181
1092-HydroxyisobutyrylationFHPTYEEKLKLVALH
CCCCHHHHHHHHHHH		38.69-
121SulfoxidationALHKQVLMGPYNPDT
HHHHHHHCCCCCCCC		5.5130846556
129GlutathionylationGPYNPDTCPEVGFFD
CCCCCCCCCCCCCEE		3.3622555962
163UbiquitinationDAMVEFVKLLNRCCH
HHHHHHHHHHHHHHH		53.2121906983
293PhosphorylationQQYMQQLYQVQLAQQ
HHHHHHHHHHHHHHH		11.4222817900
315PhosphorylationQEVVVAGSSLPTSSK
CCEEECCCCCCCCCC		20.9726657352
316PhosphorylationEVVVAGSSLPTSSKV
CEEECCCCCCCCCCC		37.1326657352
319PhosphorylationVAGSSLPTSSKVNAT
ECCCCCCCCCCCCEE		51.4220068231
320PhosphorylationAGSSLPTSSKVNATV
CCCCCCCCCCCCEEC		26.6520068231
321PhosphorylationGSSLPTSSKVNATVP
CCCCCCCCCCCEECC		43.0020068231
326PhosphorylationTSSKVNATVPSNMMS
CCCCCCEECCCCCCC		27.9611771105
333PhosphorylationTVPSNMMSVNGQAKT
ECCCCCCCCCCEEEE		11.1562177581
340PhosphorylationSVNGQAKTHTDSSEK
CCCCEEEECCCCCCC		32.7823927012
342PhosphorylationNGQAKTHTDSSEKEL
CCEEEECCCCCCCCC		42.6930278072
344PhosphorylationQAKTHTDSSEKELEP
EEEECCCCCCCCCCH		41.3623401153
345PhosphorylationAKTHTDSSEKELEPE
EEECCCCCCCCCCHH		56.3430278072
347UbiquitinationTHTDSSEKELEPEAA
ECCCCCCCCCCHHHH		70.33-
347AcetylationTHTDSSEKELEPEAA
ECCCCCCCCCCHHHH		70.3323236377
365PhosphorylationLENGPKESLPVIAAP
HHHCCHHHCCEEECC		44.06113334089
381UbiquitinationMWTRPQIKDFKEKIQ
CCCCHHHHHHHHHHH		52.44-
386UbiquitinationQIKDFKEKIQQDADS
HHHHHHHHHHHCCCC		46.5421906983
393PhosphorylationKIQQDADSVITVGRG
HHHHCCCCEEEECCC		19.6920873877
396PhosphorylationQDADSVITVGRGEVV
HCCCCEEEECCCEEE		18.1020873877
436PhosphorylationFGVYFEWTDSPNTAV
EEEEEEECCCCCCEE		21.2825137130
438PhosphorylationVYFEWTDSPNTAVSV
EEEEECCCCCCEEEE		16.8125137130
444PhosphorylationDSPNTAVSVHVSESS
CCCCCEEEEEEECCC		12.2125137130
450PhosphorylationVSVHVSESSDDDEEE
EEEEEECCCCCCHHH		31.4026657352
451PhosphorylationSVHVSESSDDDEEEE
EEEEECCCCCCHHHH		40.7925137130
473UbiquitinationKAKKNANKPLLDEIV
HHHHHCCCCCHHHHH		34.33-
485MethylationEIVPVYRRDCHEEVY
HHHHHHHCCCCCCCC		32.97-
492PhosphorylationRDCHEEVYAGSHQYP
CCCCCCCCCCCCCCC		14.4425839225
504PhosphorylationQYPGRGVYLLKFDNS
CCCCCEEEEEEECCC		14.7826657352
507UbiquitinationGRGVYLLKFDNSYSL
CCEEEEEEECCCEEE		48.3421906983
511PhosphorylationYLLKFDNSYSLWRSK
EEEEECCCEEEEEEC		20.2426657352
512PhosphorylationLLKFDNSYSLWRSKS
EEEECCCEEEEEECE		17.657457175
513PhosphorylationLKFDNSYSLWRSKSV
EEECCCEEEEEECEE		22.6724719451
517PhosphorylationNSYSLWRSKSVYYRV
CCEEEEEECEEEEEE		20.0826657352
519PhosphorylationYSLWRSKSVYYRVYY
EEEEEECEEEEEEEE		19.3223882029
521PhosphorylationLWRSKSVYYRVYYTR
EEEECEEEEEEEECC		7.827457185
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 GCP60_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCP60_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 GCP60_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DUS3L_HUMANDUS3Lphysical
22863883
U5S1_HUMANEFTUD2physical
22863883
SYHC_HUMANHARSphysical
22863883
RUSD2_HUMANRPUSD2physical
22863883
SYSC_HUMANSARSphysical
22863883
SNF8_HUMANSNF8physical
22863883
TBCD_HUMANTBCDphysical
22863883
UN45A_HUMANUNC45Aphysical
22863883
VPS36_HUMANVPS36physical
22863883
WDR12_HUMANWDR12physical
22863883
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 GCP60_HUMAN

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Related Literatures of Post-Translational Modification
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-43, AND MASSSPECTROMETRY.

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