ACTZ_HUMAN - dbPTM
ACTZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACTZ_HUMAN
UniProt AC P61163
Protein Name Alpha-centractin
Gene Name ACTR1A
Organism Homo sapiens (Human).
Sequence Length 376
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cell cortex .
Protein Description Component of a multi-subunit complex involved in microtubule based vesicle motility. It is associated with the centrosome..
Protein Sequence MESYDVIANQPVVIDNGSGVIKAGFAGDQIPKYCFPNYVGRPKHVRVMAGALEGDIFIGPKAEEHRGLLSIRYPMEHGIVKDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPRKNRERAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRIDIAGRDVSRFLRLYLRKEGYDFHSSSEFEIVKAIKERACYLSINPQKDETLETEKAQYYLPDGSTIEIGPSRFRAPELLFRPDLIGEESEGIHEVLVFAIQKSDMDLRRTLFSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGARSIHRKTF
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
1Sulfoxidation-------MESYDVIA
-------CCCCCEEC
7.5228465586
1Acetylation-------MESYDVIA
-------CCCCCEEC
7.5222223895
3Phosphorylation-----MESYDVIANQ
-----CCCCCEECCC
25.9046158779
4Phosphorylation----MESYDVIANQP
----CCCCCEECCCC
10.8326552605
18PhosphorylationPVVIDNGSGVIKAGF
CEEEECCCCEEECCC
35.8227251275
22UbiquitinationDNGSGVIKAGFAGDQ
ECCCCEEECCCCCCC
39.80-
32UbiquitinationFAGDQIPKYCFPNYV
CCCCCCCCCCCCCCC
57.17-
32AcetylationFAGDQIPKYCFPNYV
CCCCCCCCCCCCCCC
57.1730586733
33PhosphorylationAGDQIPKYCFPNYVG
CCCCCCCCCCCCCCC
8.2529496907
34S-nitrosylationGDQIPKYCFPNYVGR
CCCCCCCCCCCCCCC
5.9621278135
34S-nitrosocysteineGDQIPKYCFPNYVGR
CCCCCCCCCCCCCCC
5.96-
38PhosphorylationPKYCFPNYVGRPKHV
CCCCCCCCCCCCCCC
12.4329496907
43UbiquitinationPNYVGRPKHVRVMAG
CCCCCCCCCCCCEEC
54.06-
48SulfoxidationRPKHVRVMAGALEGD
CCCCCCCEECCEECC
1.6721406390
66MethylationGPKAEEHRGLLSIRY
CCCHHHCCCCEEEEC
40.51-
72MethylationHRGLLSIRYPMEHGI
CCCCEEEECCCCCCC
26.57-
73PhosphorylationRGLLSIRYPMEHGIV
CCCEEEECCCCCCCC
12.7828509920
75SulfoxidationLLSIRYPMEHGIVKD
CEEEECCCCCCCCCC
4.3830846556
81UbiquitinationPMEHGIVKDWNDMER
CCCCCCCCCHHHHHH
55.9221906983
96UbiquitinationIWQYVYSKDQLQTFS
HHHHHCCHHHHHCCC
31.6321890473
171PhosphorylationVTHAVPIYEGFAMPH
CEEEEEEECCCCCCC
12.1582491
200AcetylationFLRLYLRKEGYDFHS
HHHHHHHHCCCCCCC
53.5526051181
200UbiquitinationFLRLYLRKEGYDFHS
HHHHHHHHCCCCCCC
53.5521890473
230AcetylationYLSINPQKDETLETE
EEECCCCCCCCHHCE
59.8123954790
230MalonylationYLSINPQKDETLETE
EEECCCCCCCCHHCE
59.8126320211
230UbiquitinationYLSINPQKDETLETE
EEECCCCCCCCHHCE
59.81-
238UbiquitinationDETLETEKAQYYLPD
CCCHHCEECEEECCC
48.4821890473
293PhosphorylationSDMDLRRTLFSNIVL
CCHHHHHHHHHCEEE
26.2220071362
296PhosphorylationDLRRTLFSNIVLSGG
HHHHHHHHCEEECCC
28.8524719451
301PhosphorylationLFSNIVLSGGSTLFK
HHHCEEECCCCHHHC
30.1622199227
304PhosphorylationNIVLSGGSTLFKGFG
CEEECCCCHHHCCHH
26.0122199227
305PhosphorylationIVLSGGSTLFKGFGD
EEECCCCHHHCCHHH
39.2222199227
308UbiquitinationSGGSTLFKGFGDRLL
CCCCHHHCCHHHHHH
57.342190698
313MethylationLFKGFGDRLLSEVKK
HHCCHHHHHHHHHHH
37.60-
319UbiquitinationDRLLSEVKKLAPKDV
HHHHHHHHHHCCCCC
37.71-
319MalonylationDRLLSEVKKLAPKDV
HHHHHHHHHHCCCCC
37.7126320211
331PhosphorylationKDVKIRISAPQERLY
CCCEEEEECCHHHHH
24.8523312004
338PhosphorylationSAPQERLYSTWIGGS
ECCHHHHHCCCHHHH
15.4131136907
363PhosphorylationMWVSKKEYEEDGARS
HHCCHHHHCCCCCCC
33.2329496907

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 ACTZ_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACTZ_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 ACTZ_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUMA1_HUMANNUMA1physical
10504299
DCTN2_HUMANDCTN2physical
22939629
PRS6B_HUMANPSMC4physical
22939629
MYH9_HUMANMYH9physical
22939629
PSMD1_HUMANPSMD1physical
22939629
RRS1_HUMANRRS1physical
22939629
MCM7_HUMANMCM7physical
22939629
ARP10_HUMANACTR10physical
12857853
ARP10_HUMANACTR10physical
22863883
LMNB1_HUMANLMNB1physical
22863883
MYCBP_HUMANMYCBPphysical
22863883
NU133_HUMANNUP133physical
22863883
DCTN1_HUMANDCTN1physical
26344197
DCTN2_HUMANDCTN2physical
26344197
DCTN5_HUMANDCTN5physical
26344197
PACN3_HUMANPACSIN3physical
26344197
RPB4_HUMANPOLR2Dphysical
26344197
DCTN2_HUMANDCTN2physical
27173435
DCTN1_HUMANDCTN1physical
27173435

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 ACTZ_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

TOP