ABCB9_HUMAN - dbPTM
ABCB9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCB9_HUMAN
UniProt AC Q9NP78
Protein Name ATP-binding cassette sub-family B member 9
Gene Name ABCB9
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization Lysosome membrane
Multi-pass membrane protein . May be located in membrane rafts.
Protein Description ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored..
Protein Sequence MRLWKAVVVTLAFMSVDICVTTAIYVFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCLLLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMVKLLLFSEVRRPIRDPWFWALFVWTYISLGASFLLWWLLSTVRPGTQALEPGAATEAEGFPGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLQPAADFTAGHNEPVANGSHKA
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
105PhosphorylationMVKLLLFSEVRRPIR
HHHHHHHHHCCCCCC
34.8424719451
227PhosphorylationKSMDQFSTAVVIVCL
CCHHHHHHHHHHHHH
25.4324719451
240PhosphorylationCLLAIGSSFAAGIRG
HHHHHHHHHHHHHHH
17.4324719451
325PhosphorylationVVFMFSLSWQLSLVT
EEEEEEHHHHHHHHH
16.1622210691
355MethylationKYYKRLSKEVQNALA
HHHHHHHHHHHHHHH
67.50-
376UbiquitinationEETISAMKTVRSFAN
HHHHHHHHHHHHHCC
43.512190698
376 (in isoform 1)Ubiquitination-43.5121906983
376 (in isoform 2)Ubiquitination-43.5121906983
376 (in isoform 3)Ubiquitination-43.5121906983
394UbiquitinationEAEVYLRKLQQVYKL
HHHHHHHHHHHHHHC
48.31-
418 (in isoform 2)Phosphorylation-3.0622210691
528PhosphorylationVLQNVSFSLSPGKVT
EEEEEEEEECCCEEE
22.0426437602
530PhosphorylationQNVSFSLSPGKVTAL
EEEEEEECCCEEEEE
30.3421406692
648UbiquitinationAQLSGGQKQRVAMAR
CCCCCHHHHHHHHHH
43.26-

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 ABCB9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCB9_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 ABCB9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX6L_HUMANDDX60Lphysical
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 ABCB9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND MASSSPECTROMETRY.

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