dbPTM

NUA_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NUA_ARATH
UniProt AC	A4GSN8
Protein Name	Nuclear-pore anchor {ECO:0000303\|PubMed:17513499, ECO:0000303\|PubMed:21189294}
Gene Name	NUA {ECO:0000303\|PubMed:17513499, ECO:0000303\|PubMed:21189294}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	2093
Subcellular Localization	Nucleus envelope . Nucleus membrane Peripheral membrane protein Nucleoplasmic side . Nucleus, nuclear pore complex . Located at the inner surface of the nuclear envelope during interphase and in the vicinity of the spindle during prometaphase.
Protein Description	Component of the nuclear pore complex. Acts as a docking site for activities required for desumoylation and mRNA export. Required for the proper expression or localization of a subset of miRNAs. Plays a role in meristematic cell division by interacting with spindle assembly checkpoint proteins..
Protein Sequence	MPLFMPDEELARLSSDAASVVAERADEYIRKIYAELDSVRAKADAASITAEQTCSLLEQKYLSLSQDFSSLESQNAKLQSDFDDRLAELAQSQAQKHQLHLQSIEKDGEVERMSTEMSELHKSKRQLMELLEQKDAEISEKNSTIKSYLDKIVKLTDTSSEKEARLAEATAELARSQAMCSRLSQEKELTERHAKWLDEELTAKVDSYAELRRRHSDLESEMSAKLVDVEKNYIECSSSLNWHKERLRELETKIGSLQEDLSSCKDAATTTEEQYTAELFTANKLVDLYKESSEEWSRKAGELEGVIKALEARLSQVESSYKERLDKEVSTKQLLEKENGDLKQKLEKCEAEIEKTRKTDELNLIPFSNFTRRVDNSGTSNMIEESQAVISKVPAGVSGTALAASLLRDGWSLAKIYEKYQEAVDAMRHEQLGRKEAEMILQRVLSELEEKAGFIQEERGEYERVVEAYCLVNQKLQDSVSEQSNMEKFIMELKADLRRRERENTLLQKDISDLQKQVTILLKECRDVQLRCGAARDDDEDDYPLLSDVEMEMESEADKIISEHLLKFKDINGLVEQNVKLRNLVRSLSEQIESRETELKETFEVDLKNKTDEASAKVATVLKRAEEQGQMIESLHTSVAMYKRLYEEEQKLHSSDSRSSDLSPAVVPGRKNFLHLLEDSEEATKRAQEKAFERIRILEEDFAKARSEVIAIRSERDKLAMEANFAREKLEGIMKESERKREEMNSVLARNIEFSQLIIDHQRKLRESSESLHAAEEISRKLSMEVSVLKQEKELLSNAEKRASDEVSALSQRVYRLQATLDTVQSTEEVREETRAAERRKQEEHIKQLQREWAEAKKELQEERSNARDFTSDRNQTLNNAVMQVEEMGKELANALKAVSVAESRASVAEARLSDLEKKIRSSDPKTLDMDSGGIVSLSDKEMSIELRTAKEEIEKLRGEVESSKSHMLQYKSIAQVNETALKQMESAHENFRLEAEKRQRSLEAELVSLRERVSELENDCIQKSEQLATAAAGKEDALLSASAEIASLREENLVKKSQIEAMNIQMSTLKNDLETEHEKWRVAQRNYERQVILLSETIQELTKTSQALAALQEEASELRKLADARGIENSELNAKWSEEKLMLEQQKNLAEKKYHELNEQNKLLHSRLEAKHLNSAEKNSRSGTISSGSTDSDHLEDSGLQRVVHYLRRTKEIAETEISLMRQEKLRLQSQLESALKMAESARGSLTAERASTRASLLTDDGIKSLQLQVSEMNLLRESNMQLREENKHNFEKCQEMREVAQKARMESENFENLLKTKQTELDLCMKEMEKLRMETDLHKKRVDELRETYRNIDIADYNRLKDEVRQLEEKLKAKDAHAEDCKKVLLEKQNKISLLEKELTNCKKDLSEREKRLDDAQQAQATMQSEFNKQKQELEKNKKIHYTLNMTKRKYEKEKDELSKQNQSLAKQLEEAKEEAGKRTTTDAVVEQSVKEREEKEKRIQILDKYVHQLKDEVRKKTEDLKKKDEELTKERSERKSVEKEVGDSLTKIKKEKTKVDEELAKLERYQTALTHLSEELEKLKHADGNLPEGTSAVQVLSGSILNDQAAAYVSAVEYFERVARSIASNSQVSTKPTDMVTEPSSGIPAAEPSTMTRVPSSTPLIKSPVATTQQLPKVASDNKEKRLISQKPSTEFRRPSGRRIVRPQLVKPEESPKVDVDMPEAEGTGDEGKQPAAHEPESQVTTSVRPVQTLVRKRQADSLVSEPQQDSLTQGETSSEIAPPASKKAKGSESHPDTSEGENLAKEPAIDELMDATTTTDGDNEETEAENAEEKTEEYVEAQQDNEADEPVEESPTETETIPTEEESRDQTEEENQEPLTDMESDKEEGELDLDTLEDLEEGTDVASMMRSPEKEEVQPETLATPTQSPSRMETAMEEAETTIETPVEDDKTDEGGDAAEEAADIPNNANDQQEAPETDIKPETSAATTSPVSTAPTTSSTLASAITSSGAPETEDPKRAPSPGGGSSTIVTLADRAQMKRRERIANIVVSRAPNPATRGARGRTVNLRGGGRLLPRGGRAPRGGRGQSPSPP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	DEELARLSSDAASVV HHHHHHHCCCHHHHH	22.18	30407730
15	Phosphorylation	EELARLSSDAASVVA HHHHHHCCCHHHHHH	35.54	30407730
19	Phosphorylation	RLSSDAASVVAERAD HHCCCHHHHHHHHHH	20.88	30407730
319	Phosphorylation	ARLSQVESSYKERLD HHHHHHHHHHHHHHC	39.86	23572148
543	Phosphorylation	RDDDEDDYPLLSDVE CCCCCCCCCCHHHHH	14.22	23776212
547	Phosphorylation	EDDYPLLSDVEMEME CCCCCCHHHHHHHHH	47.49	23776212
555	Phosphorylation	DVEMEMESEADKIIS HHHHHHHHHHHHHHH	36.45	23776212
562	Phosphorylation	SEADKIISEHLLKFK HHHHHHHHHHHHHHH	23.57	23776212
589	Phosphorylation	RNLVRSLSEQIESRE HHHHHHHHHHHHCCC	28.80	29654922
611	Phosphorylation	EVDLKNKTDEASAKV ECCCCCCCCHHHHHH	48.76	24894044
620	Phosphorylation	EASAKVATVLKRAEE HHHHHHHHHHHHHHH	29.38	24894044
659	Phosphorylation	LHSSDSRSSDLSPAV HCCCCCCCCCCCCCC	31.96	30407730
660	Phosphorylation	HSSDSRSSDLSPAVV CCCCCCCCCCCCCCC	41.27	29654922
663	Phosphorylation	DSRSSDLSPAVVPGR CCCCCCCCCCCCCCC	18.79	30291188
932	Phosphorylation	PKTLDMDSGGIVSLS CCCCCCCCCCEEECC	32.08	23572148
937 (in isoform 2)	Phosphorylation	-	21.89	23572148
937	Phosphorylation	MDSGGIVSLSDKEMS CCCCCEEECCHHHHE	21.89	23572148
1466	Phosphorylation	ELSKQNQSLAKQLEE HHHHHHHHHHHHHHH	37.53	19880383
1659	Phosphorylation	STMTRVPSSTPLIKS CCCCCCCCCCCCCCC	43.94	25561503
1666	Phosphorylation	SSTPLIKSPVATTQQ CCCCCCCCCCCCCCC	20.01	30291188
1670	Phosphorylation	LIKSPVATTQQLPKV CCCCCCCCCCCCCCC	25.93	25561503
1671	Phosphorylation	IKSPVATTQQLPKVA CCCCCCCCCCCCCCC	12.46	25561503
1791	Phosphorylation	ASKKAKGSESHPDTS CCCCCCCCCCCCCCH	34.91	30407730
1793	Phosphorylation	KKAKGSESHPDTSEG CCCCCCCCCCCCHHC	41.85	30407730
1797	Phosphorylation	GSESHPDTSEGENLA CCCCCCCCHHCCCCC	32.88	30407730
1798	Phosphorylation	SESHPDTSEGENLAK CCCCCCCHHCCCCCC	51.49	30407730
1854	Phosphorylation	ADEPVEESPTETETI CCCCCCCCCCCCCCC	24.50	30407730
1856	Phosphorylation	EPVEESPTETETIPT CCCCCCCCCCCCCCC	65.89	30407730
1858	Phosphorylation	VEESPTETETIPTEE CCCCCCCCCCCCCHH	40.69	30407730
1871	Phosphorylation	EEESRDQTEEENQEP HHHCCCCCHHHHCCC	50.05	23776212
1880	Phosphorylation	EENQEPLTDMESDKE HHHCCCCCCCHHHHC	43.97	23776212
1884	Phosphorylation	EPLTDMESDKEEGEL CCCCCCHHHHCCCCC	47.55	23776212
1895	Phosphorylation	EGELDLDTLEDLEEG CCCCCHHHHHHHHCC	39.07	23776212
1903	Phosphorylation	LEDLEEGTDVASMMR HHHHHCCCCHHHHCC	30.49	23776212
1907	Phosphorylation	EEGTDVASMMRSPEK HCCCCHHHHCCCCCC	16.98	23776212
1911	Phosphorylation	DVASMMRSPEKEEVQ CHHHHCCCCCCCCCC	21.37	30291188
1921	Phosphorylation	KEEVQPETLATPTQS CCCCCCCCCCCCCCC	28.51	23776212
1924	Phosphorylation	VQPETLATPTQSPSR CCCCCCCCCCCCCHH	29.95	19880383
1926	Phosphorylation	PETLATPTQSPSRME CCCCCCCCCCCHHHH	37.01	23776212
1928	Phosphorylation	TLATPTQSPSRMETA CCCCCCCCCHHHHHH	27.59	19880383
1930	Phosphorylation	ATPTQSPSRMETAME CCCCCCCHHHHHHHH	49.89	23776212
2022	Phosphorylation	EDPKRAPSPGGGSST CCCCCCCCCCCCCCC	34.88	30291188
2027	Phosphorylation	APSPGGGSSTIVTLA CCCCCCCCCCEEHHH	27.81	23776212
2028	Phosphorylation	PSPGGGSSTIVTLAD CCCCCCCCCEEHHHH	25.98	23776212
2029	Phosphorylation	SPGGGSSTIVTLADR CCCCCCCCEEHHHHH	22.59	23776212
2032	Phosphorylation	GGSSTIVTLADRAQM CCCCCEEHHHHHHHH	16.63	24243849
2065	Phosphorylation	TRGARGRTVNLRGGG CCCCCCCEEECCCCC	19.30	19880383

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 NUA_ARATH !!

Functions of PTM Sites

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

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 NUA_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MAD1_ARATH	AT5G49880	physical	22457071

Drug and Disease Associations

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

Regulatory Network of NUA_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1928 AND SER-2022, ANDMASS SPECTROMETRY.	19376835 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2022, AND MASSSPECTROMETRY.	18433157 [Abstract]