NIBL1_HUMAN - dbPTM
NIBL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIBL1_HUMAN
UniProt AC Q96TA1
Protein Name Niban-like protein 1
Gene Name FAM129B
Organism Homo sapiens (Human).
Sequence Length 746
Subcellular Localization Cytoplasm, cytosol. Cell junction, adherens junction. Membrane
Lipid-anchor . In exponentially growing cells, exclusively cytoplasmic. Cell membrane localization is observed when cells reach confluency and during telophase. In melanoma cells, targe
Protein Description May play a role in apoptosis suppression. May promote melanoma cell invasion in vitro..
Protein Sequence MGDVLSTHLDDARRQHIAEKTGKILTEFLQFYEDQYGVALFNSMRHEIEGTGLPQAQLLWRKVPLDERIVFSGNLFQHQEDSKKWRNRFSLVPHNYGLVLYENKAAYERQVPPRAVINSAGYKILTSVDQYLELIGNSLPGTTAKSGSAPILKCPTQFPLILWHPYARHYYFCMMTEAEQDKWQAVLQDCIRHCNNGIPEDSKVEGPAFTDAIRMYRQSKELYGTWEMLCGNEVQILSNLVMEELGPELKAELGPRLKGKPQERQRQWIQISDAVYHMVYEQAKARFEEVLSKVQQVQPAMQAVIRTDMDQIITSKEHLASKIRAFILPKAEVCVRNHVQPYIPSILEALMVPTSQGFTEVRDVFFKEVTDMNLNVINEGGIDKLGEYMEKLSRLAYHPLKMQSCYEKMESLRLDGLQQRFDVSSTSVFKQRAQIHMREQMDNAVYTFETLLHQELGKGPTKEELCKSIQRVLERVLKKYDYDSSSVRKRFFREALLQISIPFLLKKLAPTCKSELPRFQELIFEDFARFILVENTYEEVVLQTVMKDILQAVKEAAVQRKHNLYRDSMVMHNSDPNLHLLAEGAPIDWGEEYSNSGGGGSPSPSTPESATLSEKRRRAKQVVSVVQDEEVGLPFEASPESPPPASPDGVTEIRGLLAQGLRPESPPPAGPLLNGAPAGESPQPKAAPEASSPPASPLQHLLPGKAVDLGPPKPSDQETGEQVSSPSSHPALHTTTEDSAGVQTEF
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
91UbiquitinationKWRNRFSLVPHNYGL
HHHHHCCCCCCCCEE		6.8021890473
132UbiquitinationLTSVDQYLELIGNSL
HHCHHHHHHHHCCCC		3.4321890473
303UbiquitinationQVQPAMQAVIRTDMD
HHHHHHHHHHHCCHH		5.8921890473
303UbiquitinationQVQPAMQAVIRTDMD
HHHHHHHHHHHCCHH		5.8921890473
316UbiquitinationMDQIITSKEHLASKI
HHHHHCCHHHHHHHH		40.2721890473
316UbiquitinationMDQIITSKEHLASKI
HHHHHCCHHHHHHHH		40.2721890473
322AcetylationSKEHLASKIRAFILP
CHHHHHHHHHHHHCC		30.5125953088
330AcetylationIRAFILPKAEVCVRN
HHHHHCCCHHHHHHC		54.4526051181
371UbiquitinationVFFKEVTDMNLNVIN
HHHHHHCCCCCCEEC		29.1921890473
378UbiquitinationDMNLNVINEGGIDKL
CCCCCEECCCCHHHH		37.2621890473
388UbiquitinationGIDKLGEYMEKLSRL
CHHHHHHHHHHHHHH		14.5821890473
388UbiquitinationGIDKLGEYMEKLSRL
CHHHHHHHHHHHHHH		14.5821890473
401UbiquitinationRLAYHPLKMQSCYEK
HHHCCHHHHHHHHHH		39.0721890473
401AcetylationRLAYHPLKMQSCYEK
HHHCCHHHHHHHHHH		39.0726051181
401UbiquitinationRLAYHPLKMQSCYEK
HHHCCHHHHHHHHHH		39.0721890473
408AcetylationKMQSCYEKMESLRLD
HHHHHHHHHHHHCCC		22.8426051181
417UbiquitinationESLRLDGLQQRFDVS
HHHCCCCHHHHCCCC		3.8121890473
417UbiquitinationESLRLDGLQQRFDVS
HHHCCCCHHHHCCCC		3.8121890473
430AcetylationVSSTSVFKQRAQIHM
CCCHHHHHHHHHHHH		36.4027452117
430UbiquitinationVSSTSVFKQRAQIHM
CCCHHHHHHHHHHHH		36.4021890473
430UbiquitinationVSSTSVFKQRAQIHM
CCCHHHHHHHHHHHH		36.4021890473
462AcetylationELGKGPTKEELCKSI
HHCCCCCHHHHHHHH		52.9327452117
467AcetylationPTKEELCKSIQRVLE
CCHHHHHHHHHHHHH		64.3226051181
469PhosphorylationKEELCKSIQRVLERV
HHHHHHHHHHHHHHH		1.5318083107
479AcetylationVLERVLKKYDYDSSS
HHHHHHHHCCCCCHH		38.9127452117
541UbiquitinationENTYEEVVLQTVMKD
CCCHHHHHHHHHHHH		3.5721890473
555PhosphorylationDILQAVKEAAVQRKH
HHHHHHHHHHHHHHH		34.9518669648
561PhosphorylationKEAAVQRKHNLYRDS
HHHHHHHHHCHHHCC		21.5418669648
588PhosphorylationLAEGAPIDWGEEYSN
EECCCCCCCCCCCCC		46.3918669648
590PhosphorylationEGAPIDWGEEYSNSG
CCCCCCCCCCCCCCC		17.7018669648
592PhosphorylationAPIDWGEEYSNSGGG
CCCCCCCCCCCCCCC		50.7718669648
598PhosphorylationEEYSNSGGGGSPSPS
CCCCCCCCCCCCCCC		36.7918669648
625PhosphorylationRAKQVVSVVQDEEVG
HHHHHEEEECCCCCC		2.7918669648
628PhosphorylationQVVSVVQDEEVGLPF
HHEEEECCCCCCCCC		42.2718669648
633PhosphorylationVQDEEVGLPFEASPE
ECCCCCCCCCCCCCC		5.4718669648
652PhosphorylationASPDGVTEIRGLLAQ
CCCCCHHHHHHHHHC		28.4318669648
668PhosphorylationLRPESPPPAGPLLNG
CCCCCCCCCCCCCCC		53.9118669648
678PhosphorylationPLLNGAPAGESPQPK
CCCCCCCCCCCCCCC		33.5716083285
679PhosphorylationLLNGAPAGESPQPKA
CCCCCCCCCCCCCCC		34.5518669648
683PhosphorylationAPAGESPQPKAAPEA
CCCCCCCCCCCCCCC		62.5018669648
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
593YPhosphorylationKinaseEGFRP00533
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIBL1_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 NIBL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDI2_HUMANDDI2physical
22863883
TF2AA_HUMANGTF2A1physical
22863883
H33_HUMANH3F3Aphysical
22863883
NUDC_HUMANNUDCphysical
22863883
PAPOA_HUMANPAPOLAphysical
22863883
SNX2_HUMANSNX2physical
22863883
SNX6_HUMANSNX6physical
22863883
TSN_HUMANTSNphysical
22863883
RASH_HUMANHRASphysical
26721396
RASK_HUMANKRASphysical
26721396
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 NIBL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624; SER-641; SER-646;SER-665; SER-681; SER-692 AND SER-696, AND MASS SPECTROMETRY.
"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-665; SER-681; SER-692AND SER-696, AND MASS 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-601; SER-603; THR-606;SER-638; SER-641; SER-646; SER-665; SER-681; SER-692 AND SER-696, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND MASSSPECTROMETRY.
"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-692 AND SER-696, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665 AND SER-681, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691 AND SER-696, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665; SER-692 ANDSER-696, AND MASS SPECTROMETRY.
"Functional proteomics identifies targets of phosphorylation by B-Rafsignaling in melanoma.";
Old W.M., Shabb J.B., Houel S., Wang H., Couts K.L., Yen C.Y.,Litman E.S., Croy C.H., Meyer-Arendt K., Miranda J.G., Brown R.A.,Witze E.S., Schweppe R.E., Resing K.A., Ahn N.G.;
Mol. Cell 34:115-131(2009).
Cited for: PROTEIN SEQUENCE OF 637-650 AND 688-698, MASS SPECTROMETRY, FUNCTION,SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-641; SER-646; SER-665;SER-681; SER-692 AND SER-696, AND MUTAGENESIS OF SER-641; SER-646;SER-665; SER-681; SER-692 AND SER-696.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-482, AND MASSSPECTROMETRY.

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