dbPTM

NU189_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NU189_SCHPO
UniProt AC	Q9UTK4
Protein Name	Nucleoporin nup189
Gene Name	nup189
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	1807
Subcellular Localization	Nucleoporin nup98: Nucleus, nuclear pore complex . Nucleoporin nup96: Nucleus, nuclear pore complex .
Protein Description	Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. [PubMed: 15116432 Nup189 is autocatalytically cleaved in vivo in 2 polypeptides which assume different functions in the NPC]
Protein Sequence	MFGQNNSSGFGGGTGAFGQNNQQTGGLFGSNSNTPGNTLFGSQNTSTTGFGQNTTQPLFGSNTNGGLFGNRNNTTTTGGTGFGMSSGTGMFGQSNTPAFGGTNNATNPSGGGLFGSNTANNNANTGTSFSFGSNAGSTGFGNTASNTGTGGGLFGSQNNAGNTAGNTGFGSQGTGGGLFGSSTTPATTNAFGTSGFVSSNANAVNGTANPPYAVTSEKDPQTNGTSVFQSITCMPAYRSYSFEELRLQDYNQGRRFGNASSTNTTSAFGSTPAFGASTTPFGQNLSGTTNNATPFGTSNATNTTPGSGLFGGGSAFGSNTTNTGFGSGTNNASGGLFGQNNNTTSTPSTGLFGGSTFNQQKPAFSGFGSTTNTTNTGTGTGLFGSNNATNTGTGQTTGGLFGGAATGTGTGFGSSTGGFGSNTNNQPNSGTMGTGLFGFGANNNTANNNTAPTSTFGGNNSSNFSFGANNNAATKPSGFGFGSTTTTPASGGFSFGQNANNAPKPAFGSTATTAPKPAGTGLFGGLGAGANTNTATNATGTGGSLFGNANTAGSNMFGSANSSTPGTGLFGSTQTNNATSNTGTGLFGSNNANTTNTGGSLFNKPSTTTGGLFGNTTAQQPSTTTSGLFGASNTNNQAQTSNFGTGLFGGSQAGQQQQPLQASIDQNPYGNNPLFSSTTSQVAPTSIQEPIASPLTSKPTPKKAASLPQFWLSPRSHNTARLASISSFAKSAVMNSTSASGKPKSLHLFDSLNDDVLLSADAFTPRQNIKKLVITHKISKDDILQNGVKNGNDAKSDSKVQEKAPQNEADGSLKKDEHVVLSDDYWMKPSIEELSKYPKEKLCSVHQFSVGRTGYGQVAFLKPVDLSGFEKLEDIPGKVVVFERKICAVYPVEGSSPPLGEGLNVPAIITLEKTWPLSRETREPIKDPQNPRYIQHVKRLHRIKDTEFIDFNDGKWIFKVQHFSRYGLLDDEEEENDMSSTSNEAGNLKKYDQPNLKVSGKNDSFVTHHTPGAFPNDSKNKELNRHFLKVDDSAPLDDTFMSKKVKLDFSSDSNVSERGDYDDNAKKVDEVISIEKVDGYSKENNVPLSEDDLSNSSESSNESVYSLVEESDASLAADNMDIEDISEESDREELSSMRFGAQDFHGLVVTDNWRDQLNLSVQRSALIKAAFPESQSNANLKNSRGIYYNEHDLVTDIFGNQNLDTDRPWQSLDKPGAFIPSKFHFTANGSCIYVLKSSDVKIRSIYDFIPTKDPNGTKLLEYQLDQTEVYLDLSGTHAASPRSSMTVKPLSLCSSGYESIVWDLTSILFDPKNYSLPSELSSEAREVLYQKLVRESLSEWITKTLEHETTTLAKEAETSEERIYILLTGNLIGQACEEAVQSQNNRLSTLIPLVNSDVDIQQEVKQQLEEWRKHGDLPFINKFTRLIFELLSGNTDIAEGCGTKGDEDYVQSIPITKNMTWLRAFGLKLWYNTDISIGEAMQLYVESLQKFPEIMQKPIATSAVQGIEVYDIIYLLLKAYAMGTSLEELTIPESAKCSPLNYRVVWQLAIYLSKARSLCDFSDRVVDINMAEDLKPISVHSDQLTLAYASQLEASGQWLWSLFVLLHLENVETRTSTITSCLARNLRGGLGAGAVEMIEKLCIPESWLNEAKALYARYVGDHLNELYFLQEAALYEDAHKVLLDTLAPQAVISGNKTQLKKALEGFNGQTDGLASWRFGGQIYSDYLDLLEGNFDANQELKLFTLRKISVALKELNATNLLQKAALHKISRFVNALCNEESLTDAICNLPLPLADSLANLQNISVQF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
240	Phosphorylation	CMPAYRSYSFEELRL EEECCCCCCHHHHEE	30.26	25720772
483	Phosphorylation	PSGFGFGSTTTTPAS CCCCCCCCCCCCCCC	24.47	21712547
484	Phosphorylation	SGFGFGSTTTTPASG CCCCCCCCCCCCCCC	38.20	24763107
485	Phosphorylation	GFGFGSTTTTPASGG CCCCCCCCCCCCCCC	13.03	24763107
487	Phosphorylation	GFGSTTTTPASGGFS CCCCCCCCCCCCCCC	45.06	21712547
684	Phosphorylation	STTSQVAPTSIQEPI CCCCCCCCCCCCCCC	14.63	22817900
695	Phosphorylation	QEPIASPLTSKPTPK CCCCCCCCCCCCCCC	27.82	22817900
713	Phosphorylation	SLPQFWLSPRSHNTA CCCCEECCCCCCCHH	46.94	28889911
724	Phosphorylation	HNTARLASISSFAKS CCHHHHHHHHHHHHH	47.60	28889911
731	Phosphorylation	SISSFAKSAVMNSTS HHHHHHHHHHHCCCC	16.48	24763107
736	Phosphorylation	AKSAVMNSTSASGKP HHHHHHCCCCCCCCC	29.43	29996109
738	Phosphorylation	SAVMNSTSASGKPKS HHHHCCCCCCCCCCC	58.15	29996109
740	Phosphorylation	VMNSTSASGKPKSLH HHCCCCCCCCCCCEE	2.93	21712547
779	Phosphorylation	LVITHKISKDDILQN HEEEEECCHHHHHHH	42.78	25720772
812	Phosphorylation	PQNEADGSLKKDEHV CCCCCCCCCCCCCCE	62.00	24763107
979	Phosphorylation	EEEENDMSSTSNEAG HHHHCCCCCCCCCCC	19.95	25720772
980	Phosphorylation	EEENDMSSTSNEAGN HHHCCCCCCCCCCCC	25.13	25720772
981	Phosphorylation	EENDMSSTSNEAGNL HHCCCCCCCCCCCCC	18.80	25720772
982	Phosphorylation	ENDMSSTSNEAGNLK HCCCCCCCCCCCCCC	27.97	25720772
999	Phosphorylation	DQPNLKVSGKNDSFV CCCCCEECCCCCCCC	4.28	21712547
1004	Phosphorylation	KVSGKNDSFVTHHTP EECCCCCCCCCCCCC	27.59	25720772
1007	Phosphorylation	GKNDSFVTHHTPGAF CCCCCCCCCCCCCCC	10.47	21712547
1010	Phosphorylation	DSFVTHHTPGAFPND CCCCCCCCCCCCCCC	22.39	24763107
1018	Phosphorylation	PGAFPNDSKNKELNR CCCCCCCCCCHHHHH	10.08	21712547
1022	Phosphorylation	PNDSKNKELNRHFLK CCCCCCHHHHHHEEC	45.08	18257517
1024	Phosphorylation	DSKNKELNRHFLKVD CCCCHHHHHHEECCC	40.87	19547744
1050	Phosphorylation	KKVKLDFSSDSNVSE CEEEEECCCCCCCCC	31.44	21712547
1051	Phosphorylation	KVKLDFSSDSNVSER EEEEECCCCCCCCCC	16.47	28889911
1053	Phosphorylation	KLDFSSDSNVSERGD EEECCCCCCCCCCCC	56.85	28889911
1056	Phosphorylation	FSSDSNVSERGDYDD CCCCCCCCCCCCCCC	37.56	21712547
1061	Phosphorylation	NVSERGDYDDNAKKV CCCCCCCCCCCCCCC	64.33	21712547
1073	Phosphorylation	KKVDEVISIEKVDGY CCCCEEEEEEEECCC	43.46	24763107
1160	Phosphorylation	WRDQLNLSVQRSALI HHHHHCHHHHHHHHH	24.13	25720772
1315	Phosphorylation	LFDPKNYSLPSELSS HCCCCCCCCCHHHCH	28.82	25720772

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 NU189_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NU189_SCHPO !!

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 NU189_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SEC13_SCHPO	sec13	physical	22955883

Drug and Disease Associations

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

Regulatory Network of NU189_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-1022, ANDMASS SPECTROMETRY.	18257517 [Abstract]