ADA12_HUMAN - dbPTM
ADA12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA12_HUMAN
UniProt AC O43184
Protein Name Disintegrin and metalloproteinase domain-containing protein 12
Gene Name ADAM12
Organism Homo sapiens (Human).
Sequence Length 909
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Secreted.
Isoform 3: Secreted .
Isoform 4: Secreted .
Protein Description Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity)..
Protein Sequence MAARPLPVSPARALLLALAGALLAPCEARGVSLWNQGRADEVVSASVGSGDLWIPVKSFDSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTVILGHCYYHGHVRGYSDSAVSLSTCSGLRGLIVFENESYVLEPMKSATNRYKLFPAKKLKSVRGSCGSHHNTPNLAAKNVFPPPSQTWARRHKRETLKATKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLPEVRESFGGQKCGNRFVEEGEECDCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVYLHDGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSKSSFAKCEMRDAKCGKIQCQGGASRPVIGTNAVSIETNIPLQQGGRILCRGTHVYLGDDMPDPGLVLAGTKCADGKICLNRQCQNISVFGVHECAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFTNKKTTIEKLRCVRPSRPPRGFQPCQAHLGHLGKGLMRKPPDSYPPKDNPRRLLQCQNVDISRPLNGLNVPQPQSTQRVLPPLHRAPRAPSVPARPLPAKPALRQAQGTCKPNPPQKPLPADPLARTTRLTHALARTPGQWETGLRLAPLRPAPQYPHQVPRSTHTAYIK
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
111N-linked_GlycosylationTDVSLARNYTVILGH
CCCCHHHCEEEEEEE
31.08UniProtKB CARBOHYD
149N-linked_GlycosylationRGLIVFENESYVLEP
CEEEEECCCCEEECC
31.86UniProtKB CARBOHYD
381N-linked_GlycosylationEKGGCIMNASTGYPF
ECCCEEEECCCCCCC
15.72UniProtKB CARBOHYD
430MethylationGGQKCGNRFVEEGEE
CCCCCCCCCCCCCCC
23.44-
449DimethylationEPEECMNRCCNATTC
CHHHHHHHHCCCCCC
10.24-
449MethylationEPEECMNRCCNATTC
CHHHHHHHHCCCCCC
10.24-
452N-linked_GlycosylationECMNRCCNATTCTLK
HHHHHHCCCCCCCCC
43.90UniProtKB CARBOHYD
651N-linked_GlycosylationCLNRQCQNISVFGVH
EECCCCCCEEEECHH
35.81UniProtKB CARBOHYD
782PhosphorylationLMRKPPDSYPPKDNP
CCCCCCCCCCCCCCC
45.3662162251
783PhosphorylationMRKPPDSYPPKDNPR
CCCCCCCCCCCCCCC
30.8229632367
876PhosphorylationLTHALARTPGQWETG
HHHHHHCCCCCCCCC
26.6025954137
882PhosphorylationRTPGQWETGLRLAPL
CCCCCCCCCCEECCC
38.2645553629
895PhosphorylationPLRPAPQYPHQVPRS
CCCCCCCCCCCCCCC
11.1325884760
902PhosphorylationYPHQVPRSTHTAYIK
CCCCCCCCCCCEECC
20.6225954137
903PhosphorylationPHQVPRSTHTAYIK-
CCCCCCCCCCEECC-
25.2425954137
907PhosphorylationPRSTHTAYIK-----
CCCCCCEECC-----
15.48-

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
907YPhosphorylationKinaseSRCP12931
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA12_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 ADA12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IBP5_HUMANIGFBP5physical
11095942
IBP3_HUMANIGFBP3physical
11095942
P85A_HUMANPIK3R1physical
11313349

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADA12_HUMAN

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Related Literatures of Post-Translational Modification

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