ARP3B_HUMAN - dbPTM
ARP3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARP3B_HUMAN
UniProt AC Q9P1U1
Protein Name Actin-related protein 3B
Gene Name ACTR3B
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Cytoplasm, cytoskeleton. Cell projection.
Protein Description Plays a role in the organization of the actin cytoskeleton. May function as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. May decrease the metastatic potential of tumors..
Protein Sequence MAGSLPPCVVDCGTGYTKLGYAGNTEPQFIIPSCIAIRESAKVVDQAQRRVLRGVDDLDFFIGDEAIDKPTYATKWPIRHGIIEDWDLMERFMEQVVFKYLRAEPEDHYFLMTEPPLNTPENREYLAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKYDVDPRKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDFMESISDVVDEVIQNCPIDVRRPLYKNVVLSGGSTMFRDFGRRLQRDLKRVVDARLRLSEELSGGRIKPKPVEVQVVTHHMQRYAVWFGGSMLASTPEFFQVCHTKKDYEEYGPSICRHNPVFGVMS
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
2Acetylation------MAGSLPPCV
------CCCCCCCEE
19.11-
16PhosphorylationVVDCGTGYTKLGYAG
EEECCCCCEECCCCC
10.6718083107
69UbiquitinationIGDEAIDKPTYATKW
ECCCCCCCCCCCCCC
32.90-
133PhosphorylationLAEIMFESFNVPGLY
HHHHHHHHCCCCHHH
15.74-
140PhosphorylationSFNVPGLYIAVQAVL
HCCCCHHHHHHHHHH
7.86-
152PhosphorylationAVLALAASWTSRQVG
HHHHHHHHHHCCCCC
25.86-
184PhosphorylationVIPVAEGYVIGSCIK
EEEECCCEEEHHHHH
4.7620090780
188PhosphorylationAEGYVIGSCIKHIPI
CCCEEEHHHHHCCCC
11.09-
201PhosphorylationPIAGRDITYFIQQLL
CCCCCHHHHHHHHHH
19.3728450419
202PhosphorylationIAGRDITYFIQQLLR
CCCCHHHHHHHHHHH
10.0622115753
230UbiquitinationTAKAIKEKYCYICPD
HHHHHHHHHEEECHH
35.30-
231PhosphorylationAKAIKEKYCYICPDI
HHHHHHHHEEECHHH
7.5021082442
240AcetylationYICPDIVKEFAKYDV
EECHHHHHHHHHCCC
47.66-
244AcetylationDIVKEFAKYDVDPRK
HHHHHHHHCCCCHHH
47.51-
244UbiquitinationDIVKEFAKYDVDPRK
HHHHHHHHCCCCHHH
47.51-
251AcetylationKYDVDPRKWIKQYTG
HCCCCHHHHHHHHHC
59.67-
254AcetylationVDPRKWIKQYTGINA
CCHHHHHHHHHCCCC
35.82-
254UbiquitinationVDPRKWIKQYTGINA
CCHHHHHHHHHCCCC
35.82-
256PhosphorylationPRKWIKQYTGINAIN
HHHHHHHHHCCCCCC
11.2611172439
265UbiquitinationGINAINQKKFVIDVG
CCCCCCCCEEEEEEC
43.63-
266UbiquitinationINAINQKKFVIDVGY
CCCCCCCEEEEEECH
34.79-
293SulfoxidationEFANPDFMESISDVV
HHCCHHHHHHHHHHH
5.2810
354PhosphorylationLRLSEELSGGRIKPK
HHCCHHHCCCCCCCC
42.3463650335
398UbiquitinationFQVCHTKKDYEEYGP
HHHHCCCCCHHHHCC
67.70-
403PhosphorylationTKKDYEEYGPSICRH
CCCCHHHHCCCCCCC
23.54153589
418PhosphorylationNPVFGVMS-------
CCCCCCCC-------
34.3625159151

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 ARP3B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARP3B_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 ARP3B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARPC2_HUMANARPC2physical
17353931
ARC1A_HUMANARPC1Aphysical
17353931
ARP2_HUMANACTR2physical
17353931
ARPC4_HUMANARPC4physical
17353931
ARC1B_HUMANARPC1Bphysical
17353931
CDK4_HUMANCDK4physical
17353931
ARP5L_HUMANARPC5Lphysical
17353931
ARPC3_HUMANARPC3physical
17353931
ARPC5_HUMANARPC5physical
17353931
TWF2_HUMANTWF2physical
17353931
CCAR2_HUMANCCAR2physical
17353931
EXOC5_HUMANEXOC5physical
21988832
ARP2_HUMANACTR2physical
28514442
ARPC2_HUMANARPC2physical
28514442
CHUR_HUMANCHURC1physical
28514442
OSBL3_HUMANOSBPL3physical
28514442
ARP3_HUMANACTR3physical
28514442
ARP5L_HUMANARPC5Lphysical
28514442
ARPC4_HUMANARPC4physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPH_HUMANCCT7physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPA_HUMANTCP1physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPQ_HUMANCCT8physical
28514442
PHLP_HUMANPDCLphysical
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 ARP3B_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP