POMT2_HUMAN - dbPTM
POMT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POMT2_HUMAN
UniProt AC Q9UKY4
Protein Name Protein O-mannosyl-transferase 2
Gene Name POMT2
Organism Homo sapiens (Human).
Sequence Length 750
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient..
Protein Sequence MPPATGGGLAESELRPRRGRCGPQAARAAGRDVAAEAVARSPKRPAWGSRRFEAVGWWALLALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYLSGYDGTFLFQKPGDKYEHHSYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALLTFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNSCADRPFSAPWWFWLSLTGVSLAGALGVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAVHFMVLSKSGPGDGFFSSAFQARLSGNNLHNASIPEHLAYGSVITVKNLRMAIGYLHSHRHLYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPSFPVEFVRHGDIIRLEHKETSRNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLVTGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDHINPKLPNISLDVLQPSFPEILLESHMVMIRGNSGLKPKDNEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWLNLLSIALYLLSGSIIAVAMQRGARLPAEVAGLSQVLLRGGGQVLLGWTLHYFPFFLMGRVLYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPLARGIHVAGILSLLLGTAYSFYLFHPLAYGMVGPLAQDPQSPMAGLRWLDSWDF
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
41PhosphorylationAAEAVARSPKRPAWG
HHHHHHCCCCCCCCC
25.6528355574
94PhosphorylationTHFGKMGSYYINRTF
CCCCCCCCEEECCEE
15.97-
95PhosphorylationHFGKMGSYYINRTFF
CCCCCCCEEECCEEE
11.57-
96PhosphorylationFGKMGSYYINRTFFF
CCCCCCEEECCEEEE
8.07-
98N-linked_GlycosylationKMGSYYINRTFFFDV
CCCCEEECCEEEEEE
22.33UniProtKB CARBOHYD
330N-linked_GlycosylationLSGNNLHNASIPEHL
HCCCCCCCCCCCHHH
38.25UniProtKB CARBOHYD
376PhosphorylationRQQQVTTYLHKDYNN
CHHHHHEEECCCCCC
9.4625627689
419PhosphorylationIRLEHKETSRNLHSH
EEEEEHHHHCCCHHH
37.48-
420PhosphorylationRLEHKETSRNLHSHY
EEEEHHHHCCCHHHC
21.91-
425PhosphorylationETSRNLHSHYHEAPM
HHHCCCHHHCCCCCC
28.98-
445N-linked_GlycosylationQVTGYGINGTGDSND
EEEEEECCCCCCCCC
37.30UniProtKB CARBOHYD
528N-linked_GlycosylationHINPKLPNISLDVLQ
CCCCCCCCCCEEHHC
47.09UniProtKB CARBOHYD
583N-linked_GlycosylationGLRFSGVNDTDFRVY
CEEEECCCCCCEEEE
50.41UniProtKB 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

Oops, there are no upstream regulatory protein records of POMT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POMT2_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 POMT2_HUMAN !!

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

Oops, there are no PPI records of POMT2_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POMT2_HUMAN

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Related Literatures of Post-Translational Modification

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