GT253_HUMAN - dbPTM
GT253_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GT253_HUMAN
UniProt AC Q5T4B2
Protein Name Inactive glycosyltransferase 25 family member 3
Gene Name CERCAM
Organism Homo sapiens (Human).
Sequence Length 595
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Probable cell adhesion protein involved in leukocyte transmigration across the blood-brain barrier. Does not express any beta-galactosyltransferase activity in vitro..
Protein Sequence MRAARAAPLLQLLLLLGPWLEAAGVAESPLPAVVLAILARNAEHSLPHYLGALERLDYPRARMALWCATDHNVDNTTEMLQEWLAAVGDDYAAVVWRPEGEPRFYPDEEGPKHWTKERHQFLMELKQEALTFARNWGADYILFADTDNILTNNQTLRLLMGQGLPVVAPMLDSQTYYSNFWCGITPQGYYRRTAEYFPTKNRQRRGCFRVPMVHSTFLASLRAEGADQLAFYPPHPNYTWPFDDIIVFAYACQAAGVSVHVCNEHRYGYMNVPVKSHQGLEDERVNFIHLILEALVDGPRMQASAHVTRPSKRPSKIGFDEVFVISLARRPDRRERMLASLWEMEISGRVVDAVDGWMLNSSAIRNLGVDLLPGYQDPYSGRTLTKGEVGCFLSHYSIWEEVVARGLARVLVFEDDVRFESNFRGRLERLMEDVEAEKLSWDLIYLGRKQVNPEKETAVEGLPGLVVAGYSYWTLAYALRLAGARKLLASQPLRRMLPVDEFLPIMFDQHPNEQYKAHFWPRDLVAFSAQPLLAAPTHYAGDAEWLSDTETSSPWDDDSGRLISWSGSQKTLRSPRLDLTGSSGHSLQPQPRDEL
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
34UbiquitinationESPLPAVVLAILARN
CCCHHHHHHHHHHHC
3.0429967540
48UbiquitinationNAEHSLPHYLGALER
CCHHCHHHHHHHHHH
35.4221963094
49PhosphorylationAEHSLPHYLGALERL
CHHCHHHHHHHHHHC
12.6120363803
75N-linked_GlycosylationATDHNVDNTTEMLQE
HCCCCCCCHHHHHHH
44.62UniProtKB CARBOHYD
112UbiquitinationYPDEEGPKHWTKERH
CCCCCCCCCCCHHHH
63.7329967540
122UbiquitinationTKERHQFLMELKQEA
CHHHHHHHHHHHHHH
1.7821963094
126UbiquitinationHQFLMELKQEALTFA
HHHHHHHHHHHHHHH
32.5521963094
153N-linked_GlycosylationTDNILTNNQTLRLLM
CCCCCCCHHHHHHHH
30.86UniProtKB CARBOHYD
200UbiquitinationTAEYFPTKNRQRRGC
CHHHCCCCCCCCCCC
50.8221963094
215PhosphorylationFRVPMVHSTFLASLR
EECCCCHHHHHHHHH
14.9426074081
216PhosphorylationRVPMVHSTFLASLRA
ECCCCHHHHHHHHHH
14.0626074081
220PhosphorylationVHSTFLASLRAEGAD
CHHHHHHHHHHCCCC
22.1224719451
237N-linked_GlycosylationAFYPPHPNYTWPFDD
EECCCCCCCCCCHHH
43.78UniProtKB CARBOHYD
275UbiquitinationGYMNVPVKSHQGLED
CEECCCCCCCCCCCC
35.83-
360N-linked_GlycosylationAVDGWMLNSSAIRNL
CCCCEECCHHHHHHC
20.15UniProtKB CARBOHYD
438UbiquitinationMEDVEAEKLSWDLIY
HHHHHHHHHCCHHEE
55.67-
492UbiquitinationRKLLASQPLRRMLPV
HHHHHCCCHHHCCCH
25.9121890473
492 (in isoform 2)Ubiquitination-25.9121890473
570UbiquitinationISWSGSQKTLRSPRL
EEECCCCCCCCCCCE
51.7522817900
570 (in isoform 1)Ubiquitination-51.7521890473
574PhosphorylationGSQKTLRSPRLDLTG
CCCCCCCCCCEECCC
19.9317081983
582PhosphorylationPRLDLTGSSGHSLQP
CCEECCCCCCCCCCC
28.10-
583PhosphorylationRLDLTGSSGHSLQPQ
CEECCCCCCCCCCCC
41.70-

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 GT253_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GT253_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 GT253_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOPC_HUMANGOPCphysical
25416956

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 GT253_HUMAN

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Related Literatures of Post-Translational Modification

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