NIBA2_HUMAN
ID NIBA2_HUMAN Reviewed; 746 AA.
AC Q96TA1; Q4LE55; Q5VVW6; Q5VVW7; Q9BUS2; Q9NT35;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein Niban 2 {ECO:0000305};
DE AltName: Full=Meg-3;
DE AltName: Full=Melanoma invasion by ERK {ECO:0000303|PubMed:21148485};
DE Short=MINERVA {ECO:0000303|PubMed:21148485};
DE AltName: Full=Niban-like protein 1;
DE AltName: Full=Protein FAM129B;
GN Name=NIBAN2 {ECO:0000312|HGNC:HGNC:25282};
GN Synonyms=C9orf88, FAM129B {ECO:0000303|PubMed:21148485};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Miyata T., Inagi R., Yasuda Y., Kurokawa K.;
RT "Homo sapiens meg-3 mRNA, complete cds.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yamane S., Toyosaki-Maeda T., Tsuruta Y., Suzuki R., Ochi T.;
RT "Differential screening of human osteoclast maturation associated genes.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-746 (ISOFORM 1).
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-733.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-733.
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 637-650 AND 688-698, IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-641;
RP SER-646; SER-665; SER-681; SER-692 AND SER-696, AND MUTAGENESIS OF SER-641;
RP SER-646; SER-665; SER-681; SER-692 AND SER-696.
RX PubMed=19362540; DOI=10.1016/j.molcel.2009.03.007;
RA Old W.M., Shabb J.B., Houel S., Wang H., Couts K.L., Yen C.Y., Litman E.S.,
RA Croy C.H., Meyer-Arendt K., Miranda J.G., Brown R.A., Witze E.S.,
RA Schweppe R.E., Resing K.A., Ahn N.G.;
RT "Functional proteomics identifies targets of phosphorylation by B-Raf
RT signaling in melanoma.";
RL Mol. Cell 34:115-131(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646; SER-665 AND SER-681, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574; SER-601; SER-603;
RP THR-606; SER-609; SER-638; SER-641; SER-646; SER-692 AND SER-696, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624; SER-641; SER-646;
RP SER-665; SER-692 AND SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-646; SER-665 AND
RP SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21148485; DOI=10.1074/jbc.m110.175273;
RA Chen S., Evans H.G., Evans D.R.;
RT "FAM129B/MINERVA, a novel adherens junction-associated protein, suppresses
RT apoptosis in HeLa cells.";
RL J. Biol. Chem. 286:10201-10209(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665 AND SER-681, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665; SER-681; SER-692 AND
RP SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638; SER-646; SER-692 AND
RP SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [20]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
CC -!- FUNCTION: May play a role in apoptosis suppression. May promote
CC melanoma cell invasion in vitro. {ECO:0000269|PubMed:19362540,
CC ECO:0000269|PubMed:21148485}.
CC -!- INTERACTION:
CC Q96TA1; Q14145: KEAP1; NbExp=9; IntAct=EBI-2514593, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell junction, adherens
CC junction. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=In
CC exponentially growing cells, exclusively cytoplasmic. Cell membrane
CC localization is observed when cells reach confluency and during
CC telophase. In melanoma cells, targeting to the plasma membrane may be
CC impaired by C-terminal phosphorylation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96TA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96TA1-2; Sequence=VSP_041810;
CC -!- PTM: Phosphorylated at Ser-641, Ser-646, Ser-692 and Ser-696 by the
CC BRAF/MKK/ERK signaling cascade. In melanoma cells, the C-terminal
CC phosphorylation may prevent targeting to the plasma membrane.
CC {ECO:0000269|PubMed:19362540}.
CC -!- PTM: As apoptosis proceeds, degraded via an proteasome-independent
CC pathway, probably by caspases. {ECO:0000269|PubMed:21148485}.
CC -!- SIMILARITY: Belongs to the Niban family. {ECO:0000305}.
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DR EMBL; AF151783; AAK57556.1; -; mRNA.
DR EMBL; AF192911; AAQ13825.1; -; mRNA.
DR EMBL; AL445222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87675.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87677.1; -; Genomic_DNA.
DR EMBL; AB210016; BAE06098.1; -; mRNA.
DR EMBL; AL137555; CAB70809.1; -; mRNA.
DR EMBL; BC001979; AAH01979.2; -; mRNA.
DR CCDS; CCDS35144.1; -. [Q96TA1-2]
DR CCDS; CCDS35145.1; -. [Q96TA1-1]
DR PIR; T46394; T46394.
DR RefSeq; NP_001030611.1; NM_001035534.2. [Q96TA1-2]
DR RefSeq; NP_073744.2; NM_022833.3. [Q96TA1-1]
DR PDB; 7CTP; X-ray; 1.80 A; A=2-560.
DR PDBsum; 7CTP; -.
DR AlphaFoldDB; Q96TA1; -.
DR SMR; Q96TA1; -.
DR BioGRID; 122328; 120.
DR IntAct; Q96TA1; 21.
DR MINT; Q96TA1; -.
DR STRING; 9606.ENSP00000362409; -.
DR GlyGen; Q96TA1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96TA1; -.
DR MetOSite; Q96TA1; -.
DR PhosphoSitePlus; Q96TA1; -.
DR SwissPalm; Q96TA1; -.
DR BioMuta; FAM129B; -.
DR DMDM; 347595791; -.
DR CPTAC; CPTAC-75; -.
DR CPTAC; CPTAC-968; -.
DR EPD; Q96TA1; -.
DR jPOST; Q96TA1; -.
DR MassIVE; Q96TA1; -.
DR MaxQB; Q96TA1; -.
DR PaxDb; Q96TA1; -.
DR PeptideAtlas; Q96TA1; -.
DR PRIDE; Q96TA1; -.
DR ProteomicsDB; 78220; -. [Q96TA1-1]
DR ProteomicsDB; 78221; -. [Q96TA1-2]
DR Antibodypedia; 17013; 133 antibodies from 28 providers.
DR DNASU; 64855; -.
DR Ensembl; ENST00000373312.4; ENSP00000362409.3; ENSG00000136830.12. [Q96TA1-1]
DR Ensembl; ENST00000373314.7; ENSP00000362411.3; ENSG00000136830.12. [Q96TA1-2]
DR GeneID; 64855; -.
DR KEGG; hsa:64855; -.
DR MANE-Select; ENST00000373312.4; ENSP00000362409.3; NM_022833.4; NP_073744.2.
DR UCSC; uc004brh.5; human. [Q96TA1-1]
DR CTD; 64855; -.
DR DisGeNET; 64855; -.
DR GeneCards; NIBAN2; -.
DR HGNC; HGNC:25282; NIBAN2.
DR HPA; ENSG00000136830; Tissue enhanced (esophagus).
DR MIM; 614045; gene.
DR neXtProt; NX_Q96TA1; -.
DR OpenTargets; ENSG00000136830; -.
DR PharmGKB; PA162385984; -.
DR VEuPathDB; HostDB:ENSG00000136830; -.
DR eggNOG; ENOG502QV2S; Eukaryota.
DR GeneTree; ENSGT00940000154149; -.
DR HOGENOM; CLU_009718_1_1_1; -.
DR InParanoid; Q96TA1; -.
DR OMA; TPIDWGE; -.
DR OrthoDB; 138545at2759; -.
DR PhylomeDB; Q96TA1; -.
DR TreeFam; TF333351; -.
DR PathwayCommons; Q96TA1; -.
DR SignaLink; Q96TA1; -.
DR BioGRID-ORCS; 64855; 23 hits in 1089 CRISPR screens.
DR ChiTaRS; FAM129B; human.
DR GenomeRNAi; 64855; -.
DR Pharos; Q96TA1; Tbio.
DR PRO; PR:Q96TA1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96TA1; protein.
DR Bgee; ENSG00000136830; Expressed in pancreatic ductal cell and 177 other tissues.
DR ExpressionAtlas; Q96TA1; baseline and differential.
DR Genevisible; Q96TA1; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0032274; P:gonadotropin secretion; IMP:UniProtKB.
DR GO; GO:0044029; P:hypomethylation of CpG island; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR026088; Niban-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR14392; PTHR14392; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cytoplasm;
KW Direct protein sequencing; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..746
FT /note="Protein Niban 2"
FT /id="PRO_0000213121"
FT DOMAIN 68..192
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 590..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19362540,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19362540,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19362540,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19362540,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19362540,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19362540,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT VAR_SEQ 1..18
FT /note="MGDVLSTHLDDARRQHIA -> MGWMG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_041810"
FT MUTAGEN 641
FT /note="S->A: Loss of melanoma cell invasion; when
FT associated with A-646; A-665; A-681; A-679 and A-683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 641
FT /note="S->D,E: Promotes melanoma cell invasion; when
FT associated with D/E-633; D/E-652; D/E-668; D/E-679 and D/E-
FT 683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 646
FT /note="S->A: Loss of melanoma cell invasion; when
FT associated with A-641; A-665; A-681; A-679 and A-683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 646
FT /note="S->D,E: Promotes melanoma cell invasion; when
FT associated with D/E-628; D/E-652; D/E-668; D/E-679 and D/E-
FT 683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 665
FT /note="S->A: Loss of melanoma cell invasion; when
FT associated with A-641; A-646; A-681; A-679 and A-683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 665
FT /note="S->D,E: Promotes melanoma cell invasion; when
FT associated with D/E-628; D/E-633; D/E-668; D/E-679 and D/E-
FT 683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 681
FT /note="S->A: Loss of melanoma cell invasion; when
FT associated with A-641; A-646; A-665; A-679 and A-683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 681
FT /note="S->D,E: Promotes melanoma cell invasion; when
FT associated with D/E-628; D/E-633; D/E-652; D/E-679 and D/E-
FT 683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 692
FT /note="S->A: Loss of melanoma cell invasion; when
FT associated with A-641; A-646; A-665; A-668 and A-683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 692
FT /note="S->D,E: Promotes melanoma cell invasion; when
FT associated with D/E-628; D/E-633; D/E-652; D/E-668 and D/E-
FT 683."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 696
FT /note="S->A: Loss of melanoma cell invasion; when
FT associated with A-641; A-646; A-665; A-668 and A-679."
FT /evidence="ECO:0000269|PubMed:19362540"
FT MUTAGEN 696
FT /note="S->D,E: Promotes melanoma cell invasion; when
FT associated with D/E-628; D/E-633; D/E-652; D/E-668 and D/E-
FT 679."
FT /evidence="ECO:0000269|PubMed:19362540"
FT CONFLICT 318
FT /note="H -> L (in Ref. 1; AAK57556)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="P -> L (in Ref. 7; AAH01979)"
FT /evidence="ECO:0000305"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 11..49
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:7CTP"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:7CTP"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 177..195
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 233..253
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 261..338
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 343..379
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:7CTP"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 407..411
FT /evidence="ECO:0007829|PDB:7CTP"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 423..456
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 465..512
FT /evidence="ECO:0007829|PDB:7CTP"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:7CTP"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:7CTP"
FT HELIX 533..556
FT /evidence="ECO:0007829|PDB:7CTP"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:7CTP"
SQ SEQUENCE 746 AA; 84138 MW; 2049835F08356944 CRC64;
MGDVLSTHLD DARRQHIAEK TGKILTEFLQ FYEDQYGVAL FNSMRHEIEG TGLPQAQLLW
RKVPLDERIV FSGNLFQHQE DSKKWRNRFS LVPHNYGLVL YENKAAYERQ VPPRAVINSA
GYKILTSVDQ YLELIGNSLP GTTAKSGSAP ILKCPTQFPL ILWHPYARHY YFCMMTEAEQ
DKWQAVLQDC IRHCNNGIPE DSKVEGPAFT DAIRMYRQSK ELYGTWEMLC GNEVQILSNL
VMEELGPELK AELGPRLKGK PQERQRQWIQ ISDAVYHMVY EQAKARFEEV LSKVQQVQPA
MQAVIRTDMD QIITSKEHLA SKIRAFILPK AEVCVRNHVQ PYIPSILEAL MVPTSQGFTE
VRDVFFKEVT DMNLNVINEG GIDKLGEYME KLSRLAYHPL KMQSCYEKME SLRLDGLQQR
FDVSSTSVFK QRAQIHMREQ MDNAVYTFET LLHQELGKGP TKEELCKSIQ RVLERVLKKY
DYDSSSVRKR FFREALLQIS IPFLLKKLAP TCKSELPRFQ ELIFEDFARF ILVENTYEEV
VLQTVMKDIL QAVKEAAVQR KHNLYRDSMV MHNSDPNLHL LAEGAPIDWG EEYSNSGGGG
SPSPSTPESA TLSEKRRRAK QVVSVVQDEE VGLPFEASPE SPPPASPDGV TEIRGLLAQG
LRPESPPPAG PLLNGAPAGE SPQPKAAPEA SSPPASPLQH LLPGKAVDLG PPKPSDQETG
EQVSSPSSHP ALHTTTEDSA GVQTEF
