AUNIP_HUMAN - dbPTM
AUNIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AUNIP_HUMAN
UniProt AC Q9H7T9
Protein Name Aurora kinase A and ninein-interacting protein {ECO:0000303|PubMed:20596670}
Gene Name AUNIP {ECO:0000303|PubMed:29042561, ECO:0000312|HGNC:HGNC:28363}
Organism Homo sapiens (Human).
Sequence Length 357
Subcellular Localization Nucleus . Chromosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Accumulates at sites of DNA damage by binding to DNA substrates that mimick structures generated at stalled replicatio
Protein Description DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination. [PubMed: 29042561 Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/CtIP to DSB sites to promote DNA end resection and ensuing homologous recombination repair]
Protein Sequence MRRTGPEEEACGVWLDAAALKRRKVQTHLIKPGTKMLTLLPGERKANIYFTQRRAPSTGIHQRSIASFFTLQPGKTNGSDQKSVSSHTESQINKESKKNATQLDHLIPGLAHDCMASPLATSTTADIQEAGLSPQSLQTSGHHRMKTPFSTELSLLQPDTPDCAGDSHTPLAFSFTEDLESSCLLDRKEEKGDSARKWEWLHESKKNYQSMEKHTKLPGDKCCQPLGKTKLERKVSAKENRQAPVLLQTYRESWNGENIESVKQSRSPVSVFSWDNEKNDKDSWSQLFTEDSQGQRVIAHNTRAPFQDVTNNWNWDLGPFPNSPWAQCQEDGPTQNLKPDLLFTQDSEGNQVIRHQF
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
27PhosphorylationLKRRKVQTHLIKPGT
HHHCCCHHEEECCCC
-
34PhosphorylationTHLIKPGTKMLTLLP
HEEECCCCEEEEECC
-
38PhosphorylationKPGTKMLTLLPGERK
CCCCEEEEECCCCHH
-
49PhosphorylationGERKANIYFTQRRAP
CCHHCEEEEECCCCC
-
236PhosphorylationTKLERKVSAKENRQA
CHHHHHCCHHHHCCC
24719451
263UbiquitinationGENIESVKQSRSPVS
CCCHHHHHHCCCCCE
29967540
265PhosphorylationNIESVKQSRSPVSVF
CHHHHHHCCCCCEEE
22199227
267PhosphorylationESVKQSRSPVSVFSW
HHHHHCCCCCEEEEE
25159151
270PhosphorylationKQSRSPVSVFSWDNE
HHCCCCCEEEEECCC
22199227
273PhosphorylationRSPVSVFSWDNEKND
CCCCEEEEECCCCCC
22199227
281UbiquitinationWDNEKNDKDSWSQLF
ECCCCCCCCCHHHHH
29967540
289PhosphorylationDSWSQLFTEDSQGQR
CCHHHHHEECCCCCE
23186163
292PhosphorylationSQLFTEDSQGQRVIA
HHHHEECCCCCEEEE
17525332

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 AUNIP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AUNIP_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 AUNIP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM6_HUMANPRMT6physical
23455924
TRI68_HUMANTRIM68physical
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 AUNIP_HUMAN

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Related Literatures of Post-Translational Modification

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