MZT2A_HUMAN - dbPTM
MZT2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MZT2A_HUMAN
UniProt AC Q6P582
Protein Name Mitotic-spindle organizing protein 2A
Gene Name MZT2A
Organism Homo sapiens (Human).
Sequence Length 158
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
Protein Description
Protein Sequence MAAQGVGPGPGSAAPPGLEAARQKLALRRKKVLSTEEMELYELAQAAGGGIDPDVFKILVDLLKLNVAPLAVFQMLKSMCAGQRLASEPQDPAAVSLPTSSVPETRGRDKGSAALGGVLALAERSNHEGSSQRMPRQPSATRLPKGGGPGKSPTQGST
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------MAAQGVGPG
------CCCCCCCCC
14.43-
12PhosphorylationGVGPGPGSAAPPGLE
CCCCCCCCCCCCCHH
25.1328122231
24UbiquitinationGLEAARQKLALRRKK
CHHHHHHHHHHHHHC
30.12-
31UbiquitinationKLALRRKKVLSTEEM
HHHHHHHCCCCHHHH
46.7429967540
34PhosphorylationLRRKKVLSTEEMELY
HHHHCCCCHHHHHHH
36.4420068231
35PhosphorylationRRKKVLSTEEMELYE
HHHCCCCHHHHHHHH
31.6327251275
41PhosphorylationSTEEMELYELAQAAG
CHHHHHHHHHHHHCC
8.8027251275
77UbiquitinationLAVFQMLKSMCAGQR
HHHHHHHHHHHHHCH
30.7032015554
87PhosphorylationCAGQRLASEPQDPAA
HHHCHHHCCCCCCCC
55.1728555341
96PhosphorylationPQDPAAVSLPTSSVP
CCCCCCCCCCCCCCC
24.7320071362
99PhosphorylationPAAVSLPTSSVPETR
CCCCCCCCCCCCCCC
38.6420071362
100PhosphorylationAAVSLPTSSVPETRG
CCCCCCCCCCCCCCC
27.6520071362
101PhosphorylationAVSLPTSSVPETRGR
CCCCCCCCCCCCCCC
44.1420071362
105PhosphorylationPTSSVPETRGRDKGS
CCCCCCCCCCCCHHH
32.1420071362
110UbiquitinationPETRGRDKGSAALGG
CCCCCCCHHHHHHHH
54.10-
112PhosphorylationTRGRDKGSAALGGVL
CCCCCHHHHHHHHHH
18.9930001349
130PhosphorylationERSNHEGSSQRMPRQ
HHCCCCCCCCCCCCC
21.9526074081
131PhosphorylationRSNHEGSSQRMPRQP
HCCCCCCCCCCCCCC
32.4426074081
133MethylationNHEGSSQRMPRQPSA
CCCCCCCCCCCCCCC
38.7324388017
136MethylationGSSQRMPRQPSATRL
CCCCCCCCCCCCCCC
52.2624388023
139PhosphorylationQRMPRQPSATRLPKG
CCCCCCCCCCCCCCC
33.6530266825
141PhosphorylationMPRQPSATRLPKGGG
CCCCCCCCCCCCCCC
36.7630266825
145UbiquitinationPSATRLPKGGGPGKS
CCCCCCCCCCCCCCC
74.8324816145
152PhosphorylationKGGGPGKSPTQGST-
CCCCCCCCCCCCCC-
38.8121955146
154PhosphorylationGGPGKSPTQGST---
CCCCCCCCCCCC---
53.2927794612
157PhosphorylationGKSPTQGST------
CCCCCCCCC------
22.5622199227
158PhosphorylationKSPTQGST-------
CCCCCCCC-------
49.8322199227

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 MZT2A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MZT2A_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 MZT2A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 MZT2A_HUMAN

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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 ALA-2, AND MASS SPECTROMETRY.

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