SIG12_MOUSE - dbPTM
SIG12_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIG12_MOUSE
UniProt AC Q91Y57
Protein Name Sialic acid-binding Ig-like lectin 12
Gene Name Siglec12
Organism Mus musculus (Mouse).
Sequence Length 467
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Putative adhesion molecule that mediates sialic-acid dependent binding to cells. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules..
Protein Sequence MLLLLLLLLLWGIKGVEGQNPQEVFTLNVERKVVVQEGLCVLVPCNFSYLKKRLTDWTDSDPVHGFWYREGTDRRKDSIVATNNPIRKAVKETRNRFFLLGDPWRNDCSLNIREIRKKDAGLYFFRLERGKTKYNYMWDKMTLVVTALTNTPQILLPETLEAGHPSNLTCSVPWDCGWTAPPIFSWTGTSVSFLSTNTTGSSVLTITPQPQDHGTNLTCQVTLPGTNVSTRMTIRLNVSYAPKNLTVTIYQGADSVSTILKNGSSLPISEGQSLRLICSTDSYPPANLSWSWDNLTLCPSKLSKPGLLELFPVHLKHGGVYTCQAQHALGSQHISLSLSPQSSATLSEMMMGTFVGSGVTALLFLSVCILLLAVRSYRRKPARPAVVAPHPDALKVSVSQNPLVESQADDSSEPLPSILEAAPSSTEEEIHYATLSFHEMKPMNLWGQQDTTTEYSEIKFPQRTAWP
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
46N-linked_GlycosylationLCVLVPCNFSYLKKR
EEEEEECCHHHHHHH
23.87-
167N-linked_GlycosylationLEAGHPSNLTCSVPW
HHCCCCCCCEEECCC
43.77-
197N-linked_GlycosylationSVSFLSTNTTGSSVL
EEEEEECCCCCCCEE
32.06-
216N-linked_GlycosylationQPQDHGTNLTCQVTL
CCCCCCCCEEEEEEC
37.63-
227N-linked_GlycosylationQVTLPGTNVSTRMTI
EEECCCCCCCCCEEE
31.49-
237N-linked_GlycosylationTRMTIRLNVSYAPKN
CCEEEEEEEEECCCC
15.73-
244N-linked_GlycosylationNVSYAPKNLTVTIYQ
EEEECCCCEEEEEEE
39.63-
262N-linked_GlycosylationSVSTILKNGSSLPIS
CHHHHHHCCCCCCCC
52.73-
287N-linked_GlycosylationTDSYPPANLSWSWDN
CCCCCCCCCEECCCC
40.14-
294N-linked_GlycosylationNLSWSWDNLTLCPSK
CCEECCCCCEECHHH
28.77-
339PhosphorylationQHISLSLSPQSSATL
CEEEEEECCCCCCCH
19.95-
432PhosphorylationSTEEEIHYATLSFHE
CCHHHHEEEEEECCC
13.6211171044
451PhosphorylationNLWGQQDTTTEYSEI
CCCCCCCCCCCHHHC
31.1429472430
452PhosphorylationLWGQQDTTTEYSEIK
CCCCCCCCCCHHHCC
26.3929472430
453PhosphorylationWGQQDTTTEYSEIKF
CCCCCCCCCHHHCCC
34.7129472430
455PhosphorylationQQDTTTEYSEIKFPQ
CCCCCCCHHHCCCCC
14.9811171044
456PhosphorylationQDTTTEYSEIKFPQR
CCCCCCHHHCCCCCC
26.9829472430

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 SIG12_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIG12_MOUSE !!

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 SIG12_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIG12_MOUSESiglecephysical
11171044
LG3BP_MOUSELgals3bpphysical
25320078

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIG12_MOUSE

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Related Literatures of Post-Translational Modification

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