AKIR2_HUMAN - dbPTM
AKIR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKIR2_HUMAN
UniProt AC Q53H80
Protein Name Akirin-2
Gene Name AKIRIN2
Organism Homo sapiens (Human).
Sequence Length 203
Subcellular Localization Nucleus .
Protein Description Required for the innate immune response. Downstream effector of the Toll-like receptor (TLR), TNF and IL-1 beta signaling pathways leading to the production of IL-6. Forms a complex with YWHAB that acts to repress transcription of DUSP1 (By similarity)..
Protein Sequence MACGATLKRTLDFDPLLSPASPKRRRCAPLSAPTSAAASPLSAAAATAASFSAAAASPQKYLRMEPSPFGDVSSRLTTEQILYNIKQEYKRMQKRRHLETSFQQTDPCCTSDAQPHAFLLSGPASPGTSSAASSPLKKEQPLFTLRQVGMICERLLKEREEKVREEYEEILNTKLAEQYDAFVKFTHDQIMRRYGEQPASYVS
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
8MethylationMACGATLKRTLDFDP
CCCCCCCEECCCCCC
38.69-
10PhosphorylationCGATLKRTLDFDPLL
CCCCCEECCCCCCCC
29.1423927012
18PhosphorylationLDFDPLLSPASPKRR
CCCCCCCCCCCCCCC
26.5529255136
21PhosphorylationDPLLSPASPKRRRCA
CCCCCCCCCCCCCCC
34.0519664994
31PhosphorylationRRRCAPLSAPTSAAA
CCCCCCCCCCCHHHC
31.0127080861
34PhosphorylationCAPLSAPTSAAASPL
CCCCCCCCHHHCCHH
30.6222199227
35PhosphorylationAPLSAPTSAAASPLS
CCCCCCCHHHCCHHH
18.1722199227
39PhosphorylationAPTSAAASPLSAAAA
CCCHHHCCHHHHHHH
22.9622199227
42PhosphorylationSAAASPLSAAAATAA
HHHCCHHHHHHHHHH
21.1763766285
47PhosphorylationPLSAAAATAASFSAA
HHHHHHHHHHHHHHH
20.3122210691
50PhosphorylationAAAATAASFSAAAAS
HHHHHHHHHHHHHCC
19.7829255136
52PhosphorylationAATAASFSAAAASPQ
HHHHHHHHHHHCCHH
17.9529255136
57PhosphorylationSFSAAAASPQKYLRM
HHHHHHCCHHHHCCC
24.1229255136
61PhosphorylationAAASPQKYLRMEPSP
HHCCHHHHCCCCCCC
8.3522210691
67PhosphorylationKYLRMEPSPFGDVSS
HHCCCCCCCCCCHHH
21.3921815630
78PhosphorylationDVSSRLTTEQILYNI
CHHHCCCHHHHHHHH
30.4046161617
100PhosphorylationQKRRHLETSFQQTDP
HHHHHHHHHHHHCCC
41.0023312004
101PhosphorylationKRRHLETSFQQTDPC
HHHHHHHHHHHCCCC
16.2223312004
105PhosphorylationLETSFQQTDPCCTSD
HHHHHHHCCCCCCCC
31.0023312004
110PhosphorylationQQTDPCCTSDAQPHA
HHCCCCCCCCCCCCE
36.0428450419
111PhosphorylationQTDPCCTSDAQPHAF
HCCCCCCCCCCCCEE
19.6228450419
121PhosphorylationQPHAFLLSGPASPGT
CCCEEEECCCCCCCC
44.9028450419
125PhosphorylationFLLSGPASPGTSSAA
EEECCCCCCCCCCCC
27.3125159151
128PhosphorylationSGPASPGTSSAASSP
CCCCCCCCCCCCCCC
23.9228464451
129PhosphorylationGPASPGTSSAASSPL
CCCCCCCCCCCCCCC
24.7230576142
130PhosphorylationPASPGTSSAASSPLK
CCCCCCCCCCCCCCC
27.9128450419
133PhosphorylationPGTSSAASSPLKKEQ
CCCCCCCCCCCCCCC
32.0030576142
134PhosphorylationGTSSAASSPLKKEQP
CCCCCCCCCCCCCCC
29.5328450419
144PhosphorylationKKEQPLFTLRQVGMI
CCCCCCHHHHHHHHH
28.8124719451
174UbiquitinationYEEILNTKLAEQYDA
HHHHHHHHHHHHHHH
44.63-
194PhosphorylationHDQIMRRYGEQPASY
HHHHHHHHCCCCCCC
18.0422461510
200PhosphorylationRYGEQPASYVS----
HHCCCCCCCCC----
32.5268703755
201PhosphorylationYGEQPASYVS-----
HCCCCCCCCC-----
13.5668703761
203PhosphorylationEQPASYVS-------
CCCCCCCC-------
26.6959303271

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
18SPhosphorylationKinaseCDK2P24941
PSP
21SPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKIR2_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 AKIR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LNX1_HUMANLNX1physical
16189514
RAN_HUMANRANphysical
28514442
RGPD8_HUMANRGPD8physical
28514442
SPG21_HUMANSPG21physical
28514442
AKIR1_HUMANAKIRIN1physical
28514442
RGPD5_HUMANRGPD5physical
28514442
UBAC1_HUMANUBAC1physical
28514442
IPO9_HUMANIPO9physical
28514442
RN123_HUMANRNF123physical
28514442
TOM34_HUMANTOMM34physical
28514442
BUD31_HUMANBUD31physical
28514442
RGPD3_HUMANRGPD3physical
28514442
PPID_HUMANPPIDphysical
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 AKIR2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-21, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-21, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.

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