ACKR3_HUMAN - dbPTM
ACKR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACKR3_HUMAN
UniProt AC P25106
Protein Name Atypical chemokine receptor 3
Gene Name ACKR3
Organism Homo sapiens (Human).
Sequence Length 362
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cytoplasm, perinuclear region. Early endosome. Recycling endosome. Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrest
Protein Description Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates..
Protein Sequence MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQSTK
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
13N-linked_GlycosylationFDYSEPGNFSDISWP
CCCCCCCCCCCCCCC
UniProtKB CARBOHYD
22N-linked_GlycosylationSDISWPCNSSDCIVV
CCCCCCCCCCCEEEE
UniProtKB CARBOHYD
39N-linked_GlycosylationVMCPNMPNKSVLLYT
EECCCCCCCHHHHHH
UniProtKB CARBOHYD
143PhosphorylationTCMSVDRYLSITYFT
HHHCCCCCHHEEEEC
23663014
145PhosphorylationMSVDRYLSITYFTNT
HCCCCCHHEEEECCC
23663014
147PhosphorylationVDRYLSITYFTNTPS
CCCCHHEEEECCCHH
23663014
148PhosphorylationDRYLSITYFTNTPSS
CCCHHEEEECCCHHH
23663014
150PhosphorylationYLSITYFTNTPSSRK
CHHEEEECCCHHHHH
23663014
152PhosphorylationSITYFTNTPSSRKKM
HEEEECCCHHHHHHH
23663014
154PhosphorylationTYFTNTPSSRKKMVR
EEECCCHHHHHHHHH
23663014
155PhosphorylationYFTNTPSSRKKMVRR
EECCCHHHHHHHHHH
23663014
328UbiquitinationNYRYELMKAFIFKYS
HHHHHHHHHHHHHHH
23000965
333UbiquitinationLMKAFIFKYSAKTGL
HHHHHHHHHHHCCCC
23000965
334PhosphorylationMKAFIFKYSAKTGLT
HHHHHHHHHHCCCCC
19835603
335PhosphorylationKAFIFKYSAKTGLTK
HHHHHHHHHCCCCCH
19835603
337UbiquitinationFIFKYSAKTGLTKLI
HHHHHHHCCCCCHHH
25015289
338PhosphorylationIFKYSAKTGLTKLID
HHHHHHCCCCCHHHC
19835603
342UbiquitinationSAKTGLTKLIDASRV
HHCCCCCHHHCHHHC
23503661
347PhosphorylationLTKLIDASRVSETEY
CCHHHCHHHCCHHHH
30266825
350PhosphorylationLIDASRVSETEYSAL
HHCHHHCCHHHHHHH
19664994
352PhosphorylationDASRVSETEYSALEQ
CHHHCCHHHHHHHHH
30266825
354PhosphorylationSRVSETEYSALEQST
HHCCHHHHHHHHHHC
21955146
355PhosphorylationRVSETEYSALEQSTK
HCCHHHHHHHHHHCC
30266825
360PhosphorylationEYSALEQSTK-----
HHHHHHHHCC-----
23403867
361PhosphorylationYSALEQSTK------
HHHHHHHCC------
21955146
362UbiquitinationSALEQSTK-------
HHHHHHCC-------
-

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 ACKR3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACKR3_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 ACKR3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATPB_HUMANATP5Bphysical
26186194
ATPA_HUMANATP5A1physical
26186194
ATPD_HUMANATP5Dphysical
26186194
ATPO_HUMANATP5Ophysical
26186194
ATPA_HUMANATP5A1physical
26496610
ATPB_HUMANATP5Bphysical
26496610
ATPO_HUMANATP5Ophysical
26496610
ESPL1_HUMANESPL1physical
26496610
ATP5H_HUMANATP5Hphysical
26496610
RM04_HUMANMRPL4physical
26496610
UBR7_HUMANUBR7physical
26496610
HECD2_HUMANHECTD2physical
26496610
ATPB_HUMANATP5Bphysical
28514442
ATPA_HUMANATP5A1physical
28514442
ATPO_HUMANATP5Ophysical
28514442

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 ACKR3_HUMAN

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Related Literatures of Post-Translational Modification

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