GOLM1_HUMAN - dbPTM
GOLM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GOLM1_HUMAN
UniProt AC Q8NBJ4
Protein Name Golgi membrane protein 1
Gene Name GOLM1
Organism Homo sapiens (Human).
Sequence Length 401
Subcellular Localization Golgi apparatus, cis-Golgi network membrane
Single-pass type II membrane protein . Early Golgi. Cycles via the cell surface and endosomes upon lumenal pH disruption.
Protein Description Unknown. Cellular response protein to viral infection..
Protein Sequence MMGLGNGRRSMKSPPLVLAALVACIIVLGFNYWIASSRSVDLQTRIMELEGRVRRAAAERGAVELKKNEFQGELEKQREQLDKIQSSHNFQLESVNKLYQDEKAVLVNNITTGERLIRVLQDQLKTLQRNYGRLQQDVLQFQKNQTNLERKFSYDLSQCINQMKEVKEQCEERIEEVTKKGNEAVASRDLSENNDQRQQLQALSEPQPRLQAAGLPHTEVPQGKGNVLGNSKSQTPAPSSEVVLDSKRQVEKEETNEIQVVNEEPQRDRLPQEPGREQVVEDRPVGGRGFGGAGELGQTPQVQAALSVSQENPEMEGPERDQLVIPDGQEEEQEAAGEGRNQQKLRGEDDYNMDENEAESETDKQAALAGNDRNIDVFNVEDQKRDTINLLDQREKRNHTL
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
1Acetylation-------MMGLGNGR
-------CCCCCCCC		4.3025732826
47SulfoxidationVDLQTRIMELEGRVR
CCHHHHHHHHHHHHH		4.3021406390
76UbiquitinationEFQGELEKQREQLDK
HHHHHHHHHHHHHHH		68.24-
832-HydroxyisobutyrylationKQREQLDKIQSSHNF
HHHHHHHHHHHHCCC		51.76-
86PhosphorylationEQLDKIQSSHNFQLE
HHHHHHHHHCCCCHH		36.7223312004
87PhosphorylationQLDKIQSSHNFQLES
HHHHHHHHCCCCHHH		13.1823312004
109N-linked_GlycosylationEKAVLVNNITTGERL
CCEEEEECCCHHHHH		26.0417623646
109N-linked_GlycosylationEKAVLVNNITTGERL
CCEEEEECCCHHHHH		26.0417623646
111O-linked_GlycosylationAVLVNNITTGERLIR
EEEEECCCHHHHHHH		30.7655832711
115 (in isoform 2)Ubiquitination-36.4421890473
125UbiquitinationRVLQDQLKTLQRNYG
HHHHHHHHHHHHHHH		41.372189047
125 (in isoform 1)Ubiquitination-41.3721890473
144N-linked_GlycosylationDVLQFQKNQTNLERK
HHHHHHHCCCCHHHH		43.0312754519
144N-linked_GlycosylationDVLQFQKNQTNLERK
HHHHHHHCCCCHHHH		43.0312754519
153PhosphorylationTNLERKFSYDLSQCI
CCHHHHHHHCHHHHH		22.2926091039
154PhosphorylationNLERKFSYDLSQCIN
CHHHHHHHCHHHHHH		24.8427080861
164UbiquitinationSQCINQMKEVKEQCE
HHHHHHHHHHHHHHH		49.98-
187PhosphorylationKGNEAVASRDLSENN
HHCHHHHHCCCCCCH		21.5221955146
191PhosphorylationAVASRDLSENNDQRQ
HHHHCCCCCCHHHHH		42.4329743597
204PhosphorylationRQQLQALSEPQPRLQ
HHHHHHHHCCCHHHH		50.6924505115
218O-linked_GlycosylationQAAGLPHTEVPQGKG
HHCCCCCCCCCCCCC		36.4255823693
231PhosphorylationKGNVLGNSKSQTPAP
CCCCCCCCCCCCCCC		31.7025159151
231O-linked_GlycosylationKGNVLGNSKSQTPAP
CCCCCCCCCCCCCCC		31.7072253631
233PhosphorylationNVLGNSKSQTPAPSS
CCCCCCCCCCCCCCC		38.82-
233O-linked_GlycosylationNVLGNSKSQTPAPSS
CCCCCCCCCCCCCCC		38.8255827751
235O-linked_GlycosylationLGNSKSQTPAPSSEV
CCCCCCCCCCCCCCE		28.6355827757
235PhosphorylationLGNSKSQTPAPSSEV
CCCCCCCCCCCCCCE		28.63-
239O-linked_GlycosylationKSQTPAPSSEVVLDS
CCCCCCCCCCEEECC		41.0355827761
239PhosphorylationKSQTPAPSSEVVLDS
CCCCCCCCCCEEECC		41.0326657352
255PhosphorylationRQVEKEETNEIQVVN
CCCCHHHCCCEEECC		38.9619664994
255O-linked_GlycosylationRQVEKEETNEIQVVN
CCCCHHHCCCEEECC		38.96OGP
299PhosphorylationGAGELGQTPQVQAAL
CCCCCCCCHHHHHHH		17.5620639409
299O-linked_GlycosylationGAGELGQTPQVQAAL
CCCCCCCCHHHHHHH		17.56OGP
307PhosphorylationPQVQAALSVSQENPE
HHHHHHHHCCCCCCC		18.2630278072
307O-linked_GlycosylationPQVQAALSVSQENPE
HHHHHHHHCCCCCCC		18.26OGP
309PhosphorylationVQAALSVSQENPEME
HHHHHHCCCCCCCCC		28.5330278072
351PhosphorylationKLRGEDDYNMDENEA
HHCCCCCCCCCHHHH		25.3926657352
360PhosphorylationMDENEAESETDKQAA
CCHHHHCCHHHHHHH		53.4930266825
362O-linked_GlycosylationENEAESETDKQAALA
HHHHCCHHHHHHHHH		58.75OGP
362PhosphorylationENEAESETDKQAALA
HHHHCCHHHHHHHHH		58.7530266825
384AcetylationVFNVEDQKRDTINLL
EEECCHHCCCHHHHH		65.647666309
398N-linked_GlycosylationLDQREKRNHTL----
HHHHHHHCCCC----		43.49UniProtKB CARBOHYD
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
309SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
-KUbiquitinationE3 ubiquitin ligaseHACE1Q8IYU2
PMID:21988917
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GOLM1_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 GOLM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DCK_HUMANDCKphysical
16169070
DCTN2_HUMANDCTN2physical
16169070
EIF3J_HUMANEIF3Jphysical
16169070
GEMI7_HUMANGEMIN7physical
16169070
CA174_HUMANC1orf174physical
16169070
RL13A_HUMANRPL13Aphysical
16169070
MED22_HUMANMED22physical
16169070
SYT1_HUMANSYT1physical
16169070
RFA2_HUMANRPA2physical
16169070
FRIH_HUMANFTH1physical
16169070
RACK1_HUMANGNB2L1physical
16169070
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 GOLM1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255, AND MASSSPECTROMETRY.

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