dbPTM

NBN_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NBN_MOUSE
UniProt AC	Q9R207
Protein Name	Nibrin
Gene Name	Nbn
Organism	Mus musculus (Mouse).
Sequence Length	751
Subcellular Localization	Nucleus . Nucleus, PML body. Chromosome, telomere. Localizes to discrete nuclear foci after treatment with genotoxic agents.
Protein Description	Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (By similarity)..
Protein Sequence	MWKLLPAAGAAPGEPYRLLAGVEYVVGRKNCGILIENDQSISRNHAVLTVNFPVTSLSQTDEIPTLTIKDNSKYGTFVNEEKMQTGLSCTLKTGDRVTFGVFESKFRVEYEPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKAVESKKQPPDIESFYPPIDEPAIGSKSVDLSGRHERKQIFKGKTFVFLNAKQHKKLSSAVAFGGGEARLMAEDDEEEQSFFSAPGTCVVDVGITNTQLIISHSQKKWIHLIMDTLQRNGLRPIPEAEIGLAVIFMTTENYCNPQGQPCTELKTTTPGPSLSQVLSANGKIIPSAPVNMTTYVADTESEPADTCMPLSERPEEVKIPGLEQSSRKLSQETFNIKEAPKPSSKANNVASDTLVRGKTPSYQLSPMKFPVANKNKDWTSQQQQNSIKNYFQPCTRKRERDEDNPELSSCKSSRMELSCSLLEQTQPAGPSLWKSKEHQSQNATLDREADTSSVGGMDIELNRKSPDRKPLPTETLRPRKRKDVDLATEEEVLEELLRSTKPELAVQVKVEKQEADDTIRKKPRMDAERNRPLNGGSEPESNSALQEDEREKKDELQTESWSTKHEIANSDGLQDSSEELPRKLLLTEFRSLVVSNHNSTSRNLCVNECGPLKNFKKFKKATFPGAGKLPHIIGGSDLVGHHARKNTELEEWLKQEMEVQKQQAKEESLADDLFRYNPNVKRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
49	Phosphorylation	SRNHAVLTVNFPVTS CCCCEEEEEECCCCC	13.55	25293948
55	Phosphorylation	LTVNFPVTSLSQTDE EEEECCCCCCCCCCC	24.96	26239621
56	Phosphorylation	TVNFPVTSLSQTDEI EEECCCCCCCCCCCC	26.68	26239621
58	Phosphorylation	NFPVTSLSQTDEIPT ECCCCCCCCCCCCCE	30.70	26239621
60	Phosphorylation	PVTSLSQTDEIPTLT CCCCCCCCCCCCEEE	32.02	26239621
65	Phosphorylation	SQTDEIPTLTIKDNS CCCCCCCEEEECCCC	42.04	26643407
67	Phosphorylation	TDEIPTLTIKDNSKY CCCCCEEEECCCCCC	28.58	26643407
72	Phosphorylation	TLTIKDNSKYGTFVN EEEECCCCCCCEECC	37.07	-
269	S-palmitoylation	FFSAPGTCVVDVGIT HHCCCCEEEEEECCC	3.30	26165157
278	Phosphorylation	VDVGITNTQLIISHS EEECCCCCEEEEECC	18.99	21664921
337	Phosphorylation	CTELKTTTPGPSLSQ CCCCCCCCCCCCHHH	31.32	-
341	Phosphorylation	KTTTPGPSLSQVLSA CCCCCCCCHHHHHHC	46.71	26239621
343	Phosphorylation	TTPGPSLSQVLSANG CCCCCCHHHHHHCCC	23.68	26239621
347	Phosphorylation	PSLSQVLSANGKIIP CCHHHHHHCCCEECC	22.34	26239621
398	Phosphorylation	EQSSRKLSQETFNIK HHHCHHHHHHCCCCC	29.07	17525332
401	Phosphorylation	SRKLSQETFNIKEAP CHHHHHHCCCCCCCC	17.85	28833060
419	Phosphorylation	SKANNVASDTLVRGK CCCCCCCCCCCCCCC	27.18	29176673
421	Phosphorylation	ANNVASDTLVRGKTP CCCCCCCCCCCCCCC	25.34	29176673
427	Phosphorylation	DTLVRGKTPSYQLSP CCCCCCCCCCCCCCC	21.94	24453211
429	Phosphorylation	LVRGKTPSYQLSPMK CCCCCCCCCCCCCCC	30.64	25266776
430	Phosphorylation	VRGKTPSYQLSPMKF CCCCCCCCCCCCCCC	18.06	26643407
433	Phosphorylation	KTPSYQLSPMKFPVA CCCCCCCCCCCCCCC	13.86	22942356
480	Phosphorylation	PELSSCKSSRMELSC CCHHHHHHHHHHHHH	27.74	26643407
481	Phosphorylation	ELSSCKSSRMELSCS CHHHHHHHHHHHHHH	22.57	26643407
486	Phosphorylation	KSSRMELSCSLLEQT HHHHHHHHHHHHHHC	6.59	23984901
488	Phosphorylation	SRMELSCSLLEQTQP HHHHHHHHHHHHCCC	32.39	23984901
493	Phosphorylation	SCSLLEQTQPAGPSL HHHHHHHCCCCCCCH	27.43	30635358
499	Phosphorylation	QTQPAGPSLWKSKEH HCCCCCCCHHCCCCH	46.04	30635358
503	Phosphorylation	AGPSLWKSKEHQSQN CCCCHHCCCCHHCCC	31.52	30635358
508	Phosphorylation	WKSKEHQSQNATLDR HCCCCHHCCCCCCCC	27.58	27841257
512	Phosphorylation	EHQSQNATLDREADT CHHCCCCCCCCCCCC	36.42	30635358
521	Phosphorylation	DREADTSSVGGMDIE CCCCCCCCCCCEEEE	27.20	25338131
533	Phosphorylation	DIELNRKSPDRKPLP EEEECCCCCCCCCCC	28.88	22942356
543	Phosphorylation	RKPLPTETLRPRKRK CCCCCCCCCCCCCCC	30.46	20531401
605	Phosphorylation	NRPLNGGSEPESNSA CCCCCCCCCCCCCCC	51.91	25266776
638	Phosphorylation	TKHEIANSDGLQDSS CHHHHHCCCCCCCCC	24.84	26643407
644	Phosphorylation	NSDGLQDSSEELPRK CCCCCCCCCHHHHHH	27.04	21149613
645	Phosphorylation	SDGLQDSSEELPRKL CCCCCCCCHHHHHHH	43.30	21149613
736	Phosphorylation	KQQAKEESLADDLFR HHHHHHHHHHHHHHH	29.92	25338131

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
278	T	Phosphorylation	Kinase	ATM	Q13315	PSP
343	S	Phosphorylation	Kinase	ATM	Q62388	Uniprot
433	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NBN_MOUSE !!

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 NBN_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NBN_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NBN_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.	17525332 [Abstract]