NS1BP_HUMAN - dbPTM
NS1BP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NS1BP_HUMAN
UniProt AC Q9Y6Y0
Protein Name Influenza virus NS1A-binding protein
Gene Name IVNS1ABP {ECO:0000312|HGNC:HGNC:16951}
Organism Homo sapiens (Human).
Sequence Length 642
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Nucleus, nucleoplasm . Associated with actin filaments (By similarity). Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicin
Protein Description Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity). Protects cells from cell death induced by actin destabilization (By similarity). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription. [PubMed: 16582008 In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors]
Protein Sequence MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGISHVKFDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNLLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISSSSTGCLSSPNATVQSPKHEWKIVASEKTSNNTYLCLAVLDGIFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQQDELIEKPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYNPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDSNIDDWIPVPELRTNRCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKLWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLNGKLFVCGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGIATVGNTIYAVGGFDGNEFLNTVEVYNLESNEWSPYTKIFQF
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
10UbiquitinationPNGYLMFEDENFIES
CCCEEEECCCCHHHH		50.9122817900
14UbiquitinationLMFEDENFIESSVAK
EEECCCCHHHHHHHH		6.5321890473
21UbiquitinationFIESSVAKLNALRKS
HHHHHHHHHHHHHHC		39.8727667366
27UbiquitinationAKLNALRKSGQFCDV
HHHHHHHHCCCCCCE		60.84-
28PhosphorylationKLNALRKSGQFCDVR
HHHHHHHCCCCCCEE		31.2421815630
54PhosphorylationRAVLACCSPYLFEIF
HHHHHHHCHHHHHHH		19.23-
63PhosphorylationYLFEIFNSDSDPHGI
HHHHHHCCCCCCCCC		27.95-
71PhosphorylationDSDPHGISHVKFDDL
CCCCCCCCCCEECCC		27.16-
99UbiquitinationTAQLKADKELVKDVY
HHHHHCCHHHHHHHH		58.7822817900
103UbiquitinationKADKELVKDVYSAAK
HCCHHHHHHHHHHHH		54.8522817900
110UbiquitinationKDVYSAAKKLKMDRV
HHHHHHHHHCCHHHH		59.3527667366
118UbiquitinationKLKMDRVKQVCGDYL
HCCHHHHHHHHHHHH		37.60-
172UbiquitinationSEEEEFLKLPRLKLE
CCHHHHHCCCCCEEE		62.8629967540
197UbiquitinationSNGKLYTKVINWVQR
CCCEEHHHHHHHHHH		27.79-
246PhosphorylationGQAEVFGSDDDHIQF
CCEEECCCCCCCEEE		26.8025159151
256UbiquitinationDHIQFVQKKPPRENG
CCEEEECCCCCCCCC		63.0429967540
259UbiquitinationQFVQKKPPRENGHKQ
EEECCCCCCCCCCCC		66.1621890473
262UbiquitinationQKKPPRENGHKQISS
CCCCCCCCCCCCCCC		60.1822817900
265UbiquitinationPPRENGHKQISSSST
CCCCCCCCCCCCCCC		51.2129967540
266UbiquitinationPRENGHKQISSSSTG
CCCCCCCCCCCCCCC		34.8121890473
268PhosphorylationENGHKQISSSSTGCL
CCCCCCCCCCCCCCC		22.9825159151
269PhosphorylationNGHKQISSSSTGCLS
CCCCCCCCCCCCCCC		29.9125159151
269UbiquitinationNGHKQISSSSTGCLS
CCCCCCCCCCCCCCC		29.9122817900
270PhosphorylationGHKQISSSSTGCLSS
CCCCCCCCCCCCCCC		25.7325159151
271PhosphorylationHKQISSSSTGCLSSP
CCCCCCCCCCCCCCC		30.6625159151
272PhosphorylationKQISSSSTGCLSSPN
CCCCCCCCCCCCCCC		33.5825159151
276PhosphorylationSSSTGCLSSPNATVQ
CCCCCCCCCCCCEEC		48.0725159151
277PhosphorylationSSTGCLSSPNATVQS
CCCCCCCCCCCEECC		14.8225159151
281PhosphorylationCLSSPNATVQSPKHE
CCCCCCCEECCCCCE		26.2220068231
284PhosphorylationSPNATVQSPKHEWKI
CCCCEECCCCCEEEE		31.4220068231
286UbiquitinationNATVQSPKHEWKIVA
CCEECCCCCEEEEEE		60.4429967540
290UbiquitinationQSPKHEWKIVASEKT
CCCCCEEEEEEEEEC		25.0729967540
322PhosphorylationIFLHGRNSPQSSPTS
EEECCCCCCCCCCCC		23.9729255136
325PhosphorylationHGRNSPQSSPTSTPK
CCCCCCCCCCCCCCC		41.4923663014
326PhosphorylationGRNSPQSSPTSTPKL
CCCCCCCCCCCCCCH		27.2716964243
328PhosphorylationNSPQSSPTSTPKLSK
CCCCCCCCCCCCHHH		47.3721955146
329PhosphorylationSPQSSPTSTPKLSKS
CCCCCCCCCCCHHHC		46.2023663014
330PhosphorylationPQSSPTSTPKLSKSL
CCCCCCCCCCHHHCC		27.2421955146
334PhosphorylationPTSTPKLSKSLSFEM
CCCCCCHHHCCCCEE		26.7329116813
336PhosphorylationSTPKLSKSLSFEMQQ
CCCCHHHCCCCEECH		26.3525159151
338PhosphorylationPKLSKSLSFEMQQDE
CCHHHCCCCEECHHH		26.6725159151
352PhosphorylationELIEKPMSPMQYARS
HHHHCCCCHHHHHHC		26.2525159151
356PhosphorylationKPMSPMQYARSGLGT
CCCCHHHHHHCCCCC		9.5723663014
363PhosphorylationYARSGLGTAEMNGKL
HHHCCCCCHHHCCEE		25.20-
369UbiquitinationGTAEMNGKLIAAGGY
CCHHHCCEEEEECCC		31.54-
395UbiquitinationYNPHTDHWSFLAPMR
CCCCCCCCCHHCCCC		8.1221890473
398UbiquitinationHTDHWSFLAPMRTPR
CCCCCCHHCCCCCHH		4.3422817900
464UbiquitinationGVCALNGKLYIVGGS
CEEEECCEEEEEECC		36.72-
471PhosphorylationKLYIVGGSDPYGQKG
EEEEEECCCCCCCCC		29.5028152594
474PhosphorylationIVGGSDPYGQKGLKN
EEECCCCCCCCCCCC		36.8628152594
477UbiquitinationGSDPYGQKGLKNCDV
CCCCCCCCCCCCCCC		62.9422817900
480UbiquitinationPYGQKGLKNCDVFDP
CCCCCCCCCCCCCCC		65.2922817900
484UbiquitinationKGLKNCDVFDPVTKL
CCCCCCCCCCCHHHH		6.8021890473
487UbiquitinationKNCDVFDPVTKLWTS
CCCCCCCCHHHHHHH		24.9822817900
490UbiquitinationDVFDPVTKLWTSCAP
CCCCCHHHHHHHCCC		42.11-
493PhosphorylationDPVTKLWTSCAPLNI
CCHHHHHHHCCCCCC		25.1026657352
494PhosphorylationPVTKLWTSCAPLNIR
CHHHHHHHCCCCCCH		9.1926657352
638SumoylationNEWSPYTKIFQF---
CCCCCCEEEECC---		35.36-
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 NS1BP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NS1BP_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 NS1BP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VIME_HUMANVIMphysical
16169070
CHD3_HUMANCHD3physical
16169070
PROF2_HUMANPFN2physical
16169070
AHR_HUMANAHRphysical
16582008
ENOA_HUMANENO1physical
17996313
RPA12_HUMANZNRD1physical
21988832
RL6_HUMANRPL6physical
21988832
LC7L2_HUMANLUC7L2physical
22863883
GLYM_HUMANSHMT2physical
22863883
STAT3_HUMANSTAT3physical
22863883
VPS35_HUMANVPS35physical
22863883
GBF1_HUMANGBF1physical
23825951
MYH9_HUMANMYH9physical
23825951
RENT1_HUMANUPF1physical
23825951
LPPRC_HUMANLRPPRCphysical
23825951
DHX9_HUMANDHX9physical
23825951
LARP1_HUMANLARP1physical
23825951
TR150_HUMANTHRAP3physical
23825951
DHX30_HUMANDHX30physical
23825951
HNRPU_HUMANHNRNPUphysical
23825951
ILF3_HUMANILF3physical
23825951
DHX36_HUMANDHX36physical
23825951
PARP1_HUMANPARP1physical
23825951
DDX17_HUMANDDX17physical
23825951
ZCCHV_HUMANZC3HAV1physical
23825951
HS90B_HUMANHSP90AB1physical
23825951
NCBP1_HUMANNCBP1physical
23825951
DDX21_HUMANDDX21physical
23825951
HNRL1_HUMANHNRNPUL1physical
23825951
PABP4_HUMANPABPC4physical
23825951
IF2B1_HUMANIGF2BP1physical
23825951
HSP7C_HUMANHSPA8physical
23825951
HNRPM_HUMANHNRNPMphysical
23825951
NS1BP_HUMANIVNS1ABPphysical
23825951
HNRPR_HUMANHNRNPRphysical
23825951
HNRPL_HUMANHNRNPLphysical
23825951
HNRPK_HUMANHNRNPKphysical
23825951
G3BP2_HUMANG3BP2physical
23825951
STAU1_HUMANSTAU1physical
23825951
YBOX1_HUMANYBX1physical
23825951
HNRPD_HUMANHNRNPDphysical
23825951
ILF2_HUMANILF2physical
23825951
HNRPC_HUMANHNRNPCphysical
23825951
HNRPF_HUMANHNRNPFphysical
23825951
ENOA_HUMANENO1physical
23825951
RBMX_HUMANRBMXphysical
23825951
ROAA_HUMANHNRNPABphysical
23825951
ELAV1_HUMANELAVL1physical
23825951
ACTB_HUMANACTBphysical
23825951
ROA1_HUMANHNRNPA1physical
23825951
RPB1_HUMANPOLR2Aphysical
23825951
KLH20_HUMANKLHL20physical
25619834
DAPK1_HUMANDAPK1physical
25619834
SMC1A_HUMANSMC1Aphysical
27173435
GAPD1_HUMANGAPVD1physical
27173435
ANK3_HUMANANK3physical
27173435
HSF1_HUMANHSF1physical
27173435
PLK1_HUMANPLK1physical
27173435
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 NS1BP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-338, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-338, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.

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