AP5B1_HUMAN - dbPTM
AP5B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP5B1_HUMAN
UniProt AC Q2VPB7
Protein Name AP-5 complex subunit beta-1
Gene Name AP5B1
Organism Homo sapiens (Human).
Sequence Length 878
Subcellular Localization
Protein Description As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport..
Protein Sequence MGPLSRDAWAQRLGAFRASPSAFMAGPEGEDLGRDLLSDLRSEKLSEQTKVSLLALSMEYPAQLWPDASAAEVAATSLLDTLVLLPPRPSALRRPLLLAATTALAAGGALGPTSGASCRLLPLLLGLAAGSDLGRGFVPASEQRPLQATACECLRELESCKPGLLGGSLGLLRGLLGQEGPVQPLSLLLALALRNTLVLQSRVGAGLGGLLTDKVSPTGGGPWDWTLVEEGDGRLQPQAPSWPAAEEGEGERSLTAREHSPEEARELRAAVIQLLDTSYLLTPVAQAQLLWLLGWALRGLQGQPPALFKPQLVRLLGTAQLTLLHAMLALKAAFGEALFTAQDEALLLRRLTLAAQHPALPPPTHLFYLHCVLSFPENWPLGPEGEEAAPLLLGPQLCRGLLPSLLHDPMALLARLHLLCLLCAEEEEEEKGQLPSPRHYLEELLAGLRQRAALDGGPRALATLCFQASYLVACCLAGQPTVLTPLIHGLAQLYQARPMLAPHFVDLLDQVDSELREPLKVVLRQVVVSRPGRDEALCWHLQMLAKVADGDAQSATLNFLQAAAAHCTNWDLQQGLLRVCRALLRAGVRGGLVDLLQVLARQLEDPDGRDHARLYYILLAHLAAPKLGVALGPSLAAPALASSLVAENQGFVAALMVQEAPALVRLSLGSHRVKGPLPVLKLQPEALEPIYSLELRFRVEGQLYAPLEAVHVPCLCPGRPARPLLLPLQPRCPAPARLDVHALYTTSTGLTCHAHLPPLFVNFADLFLPFPQPPEGAGLGFFEELWDSCLPEGAESRVWCPLGPQGLEGLVSRHLEPFVVVAQPPTSYCVAIHLPPDSKLLLRLEAALADGVPVALRTDDWAVLPLAGDYLRGLAAAV
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
38PhosphorylationDLGRDLLSDLRSEKL
HHCHHHHHHHHHHHC
41.7324719451
44UbiquitinationLSDLRSEKLSEQTKV
HHHHHHHHCCHHHHH
59.5727667366
117PhosphorylationLGPTSGASCRLLPLL
CCCCCHHHHHHHHHH
11.86-
161UbiquitinationLRELESCKPGLLGGS
HHHHHCCCCCCHHHH
51.9421963094
214UbiquitinationLGGLLTDKVSPTGGG
CCCHHCCCCCCCCCC
39.1021906983
218PhosphorylationLTDKVSPTGGGPWDW
HCCCCCCCCCCCCCC
40.7428464451
241PhosphorylationRLQPQAPSWPAAEEG
CCCCCCCCCCCCCCC
49.0227251275
252UbiquitinationAEEGEGERSLTAREH
CCCCCCCCCCCCCCC
48.0721890473
252UbiquitinationAEEGEGERSLTAREH
CCCCCCCCCCCCCCC
48.0721890473
253PhosphorylationEEGEGERSLTAREHS
CCCCCCCCCCCCCCC
26.2727251275
255PhosphorylationGEGERSLTAREHSPE
CCCCCCCCCCCCCHH
25.5627251275
309UbiquitinationGQPPALFKPQLVRLL
CCCCHHHHHHHHHHH
32.4827667366
431UbiquitinationAEEEEEEKGQLPSPR
HCHHHHHCCCCCCHH
56.0621890473
436PhosphorylationEEKGQLPSPRHYLEE
HHCCCCCCHHHHHHH
43.0623403867
617UbiquitinationDHARLYYILLAHLAA
CHHHHHHHHHHHHHH
1.2821890473
617UbiquitinationDHARLYYILLAHLAA
CHHHHHHHHHHHHHH
1.2821890473
624UbiquitinationILLAHLAAPKLGVAL
HHHHHHHHCCCCCCC
14.2321890473
624UbiquitinationILLAHLAAPKLGVAL
HHHHHHHHCCCCCCC
14.2321890473
674UbiquitinationSLGSHRVKGPLPVLK
CCCCCCCCCCCCEEE
55.5621906983
681UbiquitinationKGPLPVLKLQPEALE
CCCCCEEECCHHHHC
45.3621906983
692PhosphorylationEALEPIYSLELRFRV
HHHCCEEEEEEEEEE
18.9824719451

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 AP5B1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP5B1_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 AP5B1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCNRG_HUMANKCNRGphysical
16189514

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 AP5B1_HUMAN

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Related Literatures of Post-Translational Modification

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