dbPTM

PO210_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PO210_MOUSE
UniProt AC	Q9QY81
Protein Name	Nuclear pore membrane glycoprotein 210
Gene Name	Nup210
Organism	Mus musculus (Mouse).
Sequence Length	1886
Subcellular Localization	Nucleus, nuclear pore complex. Nucleus membrane Single-pass type I membrane protein. Endoplasmic reticulum membrane Single-pass type I membrane protein.
Protein Description	Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity..
Protein Sequence	MARASLVQPALWALLLLQVVGPAAAAKLNIPKVLLPFTRATRVNFTLEASEGCYRWSSTRPEVASIEPLGSSEQQCSQKAVVQARLTQPARLTSIIFAEDITTGQVLRCDAIVDLIHGIQIVSTTRELYLEDSPLELKIQALDSEGNTFSTLAGLVFDWTIVKDTEANGFSDSHNALRILTFLESTYIPPSYISEMEKAAKQGDTILVSGMKTGSSKLKARIQEAVYKNVRPAEVRLLILENILLNPAYDVYLLVGTSIHYKVQKIRQGKITELSMPSDQYELQLQNSIPDPQGDPARPVAILTQDTSRVTAMQMGQSNLVLGHRSIRMQGASRLPNSTIYVVEAGYLGFTVYPGDRWVLETGHLYAITIEVFDRSSNKVYPSDNIRIEAVLPAEFFEVLSSSQNGSYHHIRAIQSGQTAISATLTSVVDQDGGVHVLQVPVWNQQEVDIHIPITLYPSILTFPWQPKTGAYQYTIKAHGGSGNFSWSSSSSMVATVTVKGVMTTSGDTGLSVIRAHDVQNPLHFGEMKVYVIEPSSMEFAPCQVEARVGHTLELPLTISGFMPGGGSEVVTLSDCSHFDLVVEVENQGVFQPLPGRLPPGPEHCSGVKVKADAQGSTTLLVSYTHGHVHLDAKITLAAYLPLKAVDPSSVAVVTLGSSKEMLFEGGPRPWVLEPSKFFRNVTSEDTGSISLSLLGPPASRNYQQHRVLMTCQALGEQVIALSVGNRPSLSNPFPAVEPTVVKSICAPPSRLTLMPVYALPQLDLSCPLLQQNKQVVPVSSHRNPLLDLGAYDQQGRRFDNFSSLSIQWESSRPLLASIELDQPMQLVSQDDGNGQKKLHGLQTVSVHEASGTTAISATATGYQQSHLSEARVKQPHDPLVPVSASIELILVEDVRVSPEEMTIYNHPGVQVELYITEGSGYFFLNTSTQDIIKVAYQDTRGVALVHPLLPGSSTVMVHDLCLAFPAPAKAIIHVSDIQELYVRVVDKVEIGKAVKAYVRVLDFYKKPFLAKYFTFMDLKLQAASQIITLVTLDEALDNYTATFLVHGVAIGQTSLSASVTDKSGQRVSSTPQQIEVFPPFRLIPRKVTLIIGAMMQITSEGGPQPQSNILFSINNESVAAVSSSGLVRGLMVGNGSVLGVVQAVDAETGKVIIVSQDLVEVEVLQLQAVRIRAPITRMRTGTQMPVFVTGITSNQSPFSFGNAVPGLTFHWSVTKRDVLDLRGRHHEVSIRLPPQYNFAMNVYGRVKGRTGLRVVVKALDPTAGQLHGLGKELSDEIQIQVFEKLRLLNPEIEAEQILMSPNSFIKLQTNRDGAAILSYRVLDGPEKAPIVHTDEKGFLVSGSGIGVSTLEVIAQEPFGTNQTILVAVKVSPVSYLRISMSPVLHTQHKEALTALPLGMTVTFIVHFHDSSGDIFHAHNSVLNFATNRDDFVQIGKGATNNTCIIRTVSVGLTLLHVWDVEHLGLSDFVPLPVLQAITPELSGAVVVGDILCLASVLTSLGGVSGTWSSSASHVLYVDPKTGVAIARDAGSVTVYYEIAGQLKTFKEIVVGTPQKIVARRLHSAQTSIQEATASKVTVSVGDRSSNLLGECSPAQREAIEALHPESLISCQLQFKQDVFDFPACDVFTVEPGFDAALGQYLCSVTMRRLTDKQLKHLNMKKTSLAVTASIPSSYTSVEKVGAEVPFSPGLYANQAEILLSNHYTSSEVKVFGAVESLENLEVKSGSPAVLAFVKEKSFGLPSFITYTVGVLDPTAGSQGPLSTALTFSSPATNQAITIPVTVAFVLDRRGPGPYGASLLSHFLDSYQVMFFTFFALLAGTAVTIIAYHTVCAPRELASPLALTPRASPQHSPHYLASSPAAFNTLPSGRKASPPSGLWSPAYASH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	N-linked_Glycosylation	FTRATRVNFTLEASE CCCCEEEEEEEEECC	22.39	-
181	Phosphorylation	HNALRILTFLESTYI HCHHHHHHHHHHCCC	24.65	28576409
185	Phosphorylation	RILTFLESTYIPPSY HHHHHHHHCCCCHHH	28.76	28576409
337	N-linked_Glycosylation	QGASRLPNSTIYVVE CCCCCCCCCEEEEEE	57.27	-
405	N-linked_Glycosylation	EVLSSSQNGSYHHIR HHHHCCCCCCCEEEE	43.24	-
416	Phosphorylation	HHIRAIQSGQTAISA EEEEEECCCCCEEEE	27.10	22802335
484	N-linked_Glycosylation	KAHGGSGNFSWSSSS EECCCCCCCCCCCCC	29.49	-
486	Phosphorylation	HGGSGNFSWSSSSSM CCCCCCCCCCCCCCC	30.01	22802335
488	Phosphorylation	GSGNFSWSSSSSMVA CCCCCCCCCCCCCEE	21.10	22802335
489	Phosphorylation	SGNFSWSSSSSMVAT CCCCCCCCCCCCEEE	28.16	22802335
490	Phosphorylation	GNFSWSSSSSMVATV CCCCCCCCCCCEEEE	22.40	22802335
491	Phosphorylation	NFSWSSSSSMVATVT CCCCCCCCCCEEEEE	25.13	22802335
492	Phosphorylation	FSWSSSSSMVATVTV CCCCCCCCCEEEEEE	21.15	22802335
496	Phosphorylation	SSSSMVATVTVKGVM CCCCCEEEEEEEEEE	12.80	22802335
498	Phosphorylation	SSMVATVTVKGVMTT CCCEEEEEEEEEEEC	16.49	22802335
649	Phosphorylation	PLKAVDPSSVAVVTL CCCCCCHHHEEEEEE	32.74	25338131
650	Phosphorylation	LKAVDPSSVAVVTLG CCCCCHHHEEEEEEC	21.34	25338131
659	Phosphorylation	AVVTLGSSKEMLFEG EEEEECCCCHHCCCC	30.73	25338131
681	N-linked_Glycosylation	EPSKFFRNVTSEDTG CHHHHCCCCCCCCCC	35.94	-
801	N-linked_Glycosylation	QQGRRFDNFSSLSIQ CCCCCCCCCCCEEEE	35.67	-
926	N-linked_Glycosylation	GSGYFFLNTSTQDII CCEEEEEECCCCHHH	27.16	-
1039	N-linked_Glycosylation	TLDEALDNYTATFLV EHHHHHHHCCEEEEE	36.58	-
1099	Phosphorylation	IGAMMQITSEGGPQP EEEEEEECCCCCCCC	12.11	22802335
1100	Phosphorylation	GAMMQITSEGGPQPQ EEEEEECCCCCCCCC	35.55	22802335
1108	Phosphorylation	EGGPQPQSNILFSIN CCCCCCCCCEEEEEC	32.30	22802335
1113	Phosphorylation	PQSNILFSINNESVA CCCCEEEEECCCCEE	22.44	22802335
1116	N-linked_Glycosylation	NILFSINNESVAAVS CEEEEECCCCEEEEE	41.05	-
1118	Phosphorylation	LFSINNESVAAVSSS EEEECCCCEEEEECC	21.12	22802335
1123	Phosphorylation	NESVAAVSSSGLVRG CCCEEEEECCCCCCE	17.66	22802335
1124	Phosphorylation	ESVAAVSSSGLVRGL CCEEEEECCCCCCEE	23.09	22802335
1125	Phosphorylation	SVAAVSSSGLVRGLM CEEEEECCCCCCEEE	28.74	22802335
1135	N-linked_Glycosylation	VRGLMVGNGSVLGVV CCEEEECCCCEEEEE	28.31	-
1137	Phosphorylation	GLMVGNGSVLGVVQA EEEECCCCEEEEEEE	20.40	22802335
1319	Phosphorylation	RDGAAILSYRVLDGP CCCCEEEEEEECCCC	12.55	24759943
1320	Phosphorylation	DGAAILSYRVLDGPE CCCEEEEEEECCCCC	10.99	24759943
1362	N-linked_Glycosylation	AQEPFGTNQTILVAV EECCCCCCCEEEEEE	37.06	-
1441	N-linked_Glycosylation	QIGKGATNNTCIIRT EECCCCCCCCEEEEE	41.08	-
1839	Phosphorylation	CAPRELASPLALTPR CCCHHHCCCCCCCCC	32.83	23527152
1844	Phosphorylation	LASPLALTPRASPQH HCCCCCCCCCCCCCC	12.72	23527152
1848	Phosphorylation	LALTPRASPQHSPHY CCCCCCCCCCCCCCC	26.77	21082442
1852	Phosphorylation	PRASPQHSPHYLASS CCCCCCCCCCCCCCC	14.23	22942356
1855	Phosphorylation	SPQHSPHYLASSPAA CCCCCCCCCCCCCHH	13.83	25159016
1858	Phosphorylation	HSPHYLASSPAAFNT CCCCCCCCCCHHHHC	33.97	28066266
1859	Phosphorylation	SPHYLASSPAAFNTL CCCCCCCCCHHHHCC	16.98	25159016
1871	Ubiquitination	NTLPSGRKASPPSGL HCCCCCCCCCCCCCC	57.66	22790023
1873	Phosphorylation	LPSGRKASPPSGLWS CCCCCCCCCCCCCCC	40.14	21082442
1876	Phosphorylation	GRKASPPSGLWSPAY CCCCCCCCCCCCCCC	50.32	25266776
1880	Phosphorylation	SPPSGLWSPAYASH- CCCCCCCCCCCCCC-	12.51	8672508
1885	Phosphorylation	LWSPAYASH------ CCCCCCCCC------	19.63	-

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
1880	S	Phosphorylation	Kinase	CDK1	P11440	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1880	S	Phosphorylation		-
Phosphorylated at Ser-1880 in mitosis specifically; not phosphorylated in interphase.

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 PO210_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PO210_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PO210_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, AND MASSSPECTROMETRY.	19144319 [Abstract]

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