GT251_HUMAN - dbPTM
GT251_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GT251_HUMAN
UniProt AC Q8NBJ5
Protein Name Procollagen galactosyltransferase 1
Gene Name COLGALT1
Organism Homo sapiens (Human).
Sequence Length 622
Subcellular Localization Endoplasmic reticulum lumen . Colocalized with PLOD3 and mannose binding lectin/MBL2.
Protein Description Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. [PubMed: 19075007]
Protein Sequence MAAAPRAGRRRGQPLLALLLLLLAPLPPGAPPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMINLRRRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGARKLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWDRAKSQKMREQQALSREAKNSDVLQSPLDSAARDEL
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
59UbiquitinationPRVLIALLARNAAHA
HHHHHHHHHHHHHHH		2.8824816145
61MethylationVLIALLARNAAHALP
HHHHHHHHHHHHHHC		33.03-
69UbiquitinationNAAHALPTTLGALER
HHHHHHCHHHHHHHH		35.1924816145
96N-linked_GlycosylationATDHNMDNTSTVLRE
EECCCCCCHHHHHHH		25.7619159218
99PhosphorylationHNMDNTSTVLREWLV
CCCCCHHHHHHHHHH		22.8624719451
112PhosphorylationLVAVKSLYHSVEWRP
HHHHHHHHHCCCCCC		10.1128152594
114PhosphorylationAVKSLYHSVEWRPAE
HHHHHHHCCCCCCCC		14.2628152594
133UbiquitinationYPDEEGPKHWSDSRY
CCCCCCCCCCCCHHH		69.4429967540
145UbiquitinationSRYEHVMKLRQAALK
HHHHHHHHHHHHHHH		39.15-
152UbiquitinationKLRQAALKSARDMWA
HHHHHHHHHHHHHHC		37.0224816145
184N-linked_GlycosylationLSLLIAENKTVVAPM
HHHHHCCCCEEEEEC		35.95UniProtKB CARBOHYD
198PhosphorylationMLDSRAAYSNFWCGM
CCCCHHHHCCCCCCC		11.8020068231
199PhosphorylationLDSRAAYSNFWCGMT
CCCHHHHCCCCCCCC		22.3320068231
200UbiquitinationDSRAAYSNFWCGMTS
CCHHHHCCCCCCCCC		23.0524816145
206PhosphorylationSNFWCGMTSQGYYKR
CCCCCCCCCCCCCCC		11.8120068231
207PhosphorylationNFWCGMTSQGYYKRT
CCCCCCCCCCCCCCC		16.8320068231
210PhosphorylationCGMTSQGYYKRTPAY
CCCCCCCCCCCCCCC		9.7420068231
211PhosphorylationGMTSQGYYKRTPAYI
CCCCCCCCCCCCCCC		10.7920068231
217PhosphorylationYYKRTPAYIPIRKRD
CCCCCCCCCCCCCCC		14.40-
236PhosphorylationFAVPMVHSTFLIDLR
EEEEECCEEHHHHHH		14.9420071362
288PhosphorylationYVCNKEEYGFLPVPL
EEECHHHCCCCCCCC		17.80-
325PhosphorylationKHPPAEPSRFISAPT
CCCCCCCHHCCCCCC		31.18-
326UbiquitinationHPPAEPSRFISAPTK
CCCCCCHHCCCCCCC		43.5724816145
332PhosphorylationSRFISAPTKTPDKMG
HHCCCCCCCCCCCCC		47.47-
333UbiquitinationRFISAPTKTPDKMGF
HCCCCCCCCCCCCCC		57.9329967540
334PhosphorylationFISAPTKTPDKMGFD
CCCCCCCCCCCCCCC		38.9229083192
369GlutathionylationLQAQEIECRLVEAVD
HHHHHHHHEEEEECC		5.1122555962
381N-linked_GlycosylationAVDGKAMNTSQVEAL
ECCCCCCCHHHHHHH		41.2519159218
386UbiquitinationAMNTSQVEALGIQML
CCCHHHHHHHCCEEC		30.4624816145
396UbiquitinationGIQMLPGYRDPYHGR
CCEECCCCCCCCCCC		15.2024816145
4302-HydroxyisobutyrylationVVDRGLQKSLVFEDD
HHHHHHHHEECCCCC		51.29-
479UbiquitinationMQVEHPEKAVPRVRN
CCCCCHHHHCHHHHH		60.1724816145
508UbiquitinationISLQGARKLLAAEPL
HHHHHHHHHHCCCCH		47.52-
512UbiquitinationGARKLLAAEPLSKML
HHHHHHCCCCHHHCC		20.9324816145
522UbiquitinationLSKMLPVDEFLPVMF
HHHCCCHHHHHHHCC		38.7024816145
605UbiquitinationQALSREAKNSDVLQS
HHHHHHHHCCHHHCC		52.8324816145
612PhosphorylationKNSDVLQSPLDSAAR
HCCHHHCCHHHHHHH		24.2225262027
616PhosphorylationVLQSPLDSAARDEL-
HHCCHHHHHHHHCC-		31.3529255136
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 GT251_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GT251_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 GT251_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLOD1_HUMANPLOD1physical
26344197
PLOD2_HUMANPLOD2physical
26344197
PLOD3_HUMANPLOD3physical
26344197
PR40A_HUMANPRPF40Aphysical
26344197
PYGL_HUMANPYGLphysical
26344197
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 GT251_HUMAN

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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-96 AND ASN-381, AND MASSSPECTROMETRY.

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