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Niban-like protein 1 (Meg-3) (Melanoma invasion by ERK) (MINERVA) (Protein FAM129B)

 NIBL1_HUMAN             Reviewed;         746 AA.
Q96TA1; Q4LE55; Q5VVW6; Q5VVW7; Q9BUS2; Q9NT35;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 3.
22-NOV-2017, entry version 140.
RecName: Full=Niban-like protein 1;
AltName: Full=Meg-3;
AltName: Full=Melanoma invasion by ERK;
Short=MINERVA;
AltName: Full=Protein FAM129B;
Name=FAM129B; Synonyms=C9orf88;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Miyata T., Inagi R., Yasuda Y., Kurokawa K.;
"Homo sapiens meg-3 mRNA, complete cds.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yamane S., Toyosaki-Maeda T., Tsuruta Y., Suzuki R., Ochi T.;
"Differential screening of human osteoclast maturation associated
genes.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-746 (ISOFORM 1).
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-733.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-733.
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 637-650 AND 688-698, IDENTIFICATION BY 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.
PubMed=19362540; DOI=10.1016/j.molcel.2009.03.007;
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.;
"Functional proteomics identifies targets of phosphorylation by B-Raf
signaling in melanoma.";
Mol. Cell 34:115-131(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646; SER-665 AND
SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574; SER-601; SER-603;
THR-606; SER-609; SER-638; SER-641; SER-646; SER-692 AND SER-696, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624; SER-641; SER-646;
SER-665; SER-692 AND SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-646; SER-665
AND SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21148485; DOI=10.1074/jbc.M110.175273;
Chen S., Evans H.G., Evans D.R.;
"FAM129B/MINERVA, a novel adherens junction-associated protein,
suppresses apoptosis in HeLa cells.";
J. Biol. Chem. 286:10201-10209(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665 AND SER-681, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665; SER-681; SER-692
AND SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638; SER-646; SER-692
AND SER-696, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[20]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
-!- FUNCTION: May play a role in apoptosis suppression. May promote
melanoma cell invasion in vitro. {ECO:0000269|PubMed:19362540,
ECO:0000269|PubMed:21148485}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell junction, adherens
junction. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Note=In exponentially growing cells, exclusively cytoplasmic. Cell
membrane localization is observed when cells reach confluency and
during telophase. In melanoma cells, targeting to the plasma
membrane may be impaired by C-terminal phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96TA1-1; Sequence=Displayed;
Name=2;
IsoId=Q96TA1-2; Sequence=VSP_041810;
-!- PTM: Phosphorylated at Ser-641, Ser-646, Ser-692 and Ser-696 by
the BRAF/MKK/ERK signaling cascade. In melanoma cells, the C-
terminal phosphorylation may prevent targeting to the plasma
membrane. {ECO:0000269|PubMed:19362540}.
-!- PTM: As apoptosis proceeds, degraded via an proteasome-independent
pathway, probably by caspases. {ECO:0000269|PubMed:21148485}.
-!- SIMILARITY: Belongs to the Niban family. {ECO:0000305}.
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EMBL; AF151783; AAK57556.1; -; mRNA.
EMBL; AF192911; AAQ13825.1; -; mRNA.
EMBL; AL445222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL390116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87675.1; -; Genomic_DNA.
EMBL; CH471090; EAW87677.1; -; Genomic_DNA.
EMBL; AB210016; BAE06098.1; -; mRNA.
EMBL; AL137555; CAB70809.1; -; mRNA.
EMBL; BC001979; AAH01979.2; -; mRNA.
CCDS; CCDS35144.1; -. [Q96TA1-2]
CCDS; CCDS35145.1; -. [Q96TA1-1]
PIR; T46394; T46394.
RefSeq; NP_001030611.1; NM_001035534.2. [Q96TA1-2]
RefSeq; NP_073744.2; NM_022833.3. [Q96TA1-1]
UniGene; Hs.522401; -.
ProteinModelPortal; Q96TA1; -.
SMR; Q96TA1; -.
BioGrid; 122328; 35.
IntAct; Q96TA1; 6.
MINT; MINT-1193681; -.
STRING; 9606.ENSP00000362409; -.
iPTMnet; Q96TA1; -.
PhosphoSitePlus; Q96TA1; -.
SwissPalm; Q96TA1; -.
BioMuta; FAM129B; -.
DMDM; 347595791; -.
EPD; Q96TA1; -.
MaxQB; Q96TA1; -.
PaxDb; Q96TA1; -.
PeptideAtlas; Q96TA1; -.
PRIDE; Q96TA1; -.
Ensembl; ENST00000373312; ENSP00000362409; ENSG00000136830. [Q96TA1-1]
Ensembl; ENST00000373314; ENSP00000362411; ENSG00000136830. [Q96TA1-2]
GeneID; 64855; -.
KEGG; hsa:64855; -.
UCSC; uc004brh.5; human. [Q96TA1-1]
CTD; 64855; -.
DisGeNET; 64855; -.
EuPathDB; HostDB:ENSG00000136830.11; -.
GeneCards; FAM129B; -.
H-InvDB; HIX0008401; -.
HGNC; HGNC:25282; FAM129B.
HPA; HPA021284; -.
HPA; HPA021417; -.
HPA; HPA023261; -.
HPA; HPA024312; -.
MIM; 614045; gene.
neXtProt; NX_Q96TA1; -.
OpenTargets; ENSG00000136830; -.
PharmGKB; PA162385984; -.
eggNOG; ENOG410IFR1; Eukaryota.
eggNOG; ENOG41102BB; LUCA.
GeneTree; ENSGT00530000063284; -.
HOGENOM; HOG000220836; -.
HOVERGEN; HBG026217; -.
InParanoid; Q96TA1; -.
OMA; RHCNNGI; -.
OrthoDB; EOG091G02BX; -.
PhylomeDB; Q96TA1; -.
TreeFam; TF333351; -.
ChiTaRS; FAM129B; human.
GenomeRNAi; 64855; -.
PRO; PR:Q96TA1; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136830; -.
CleanEx; HS_FAM129B; -.
ExpressionAtlas; Q96TA1; baseline and differential.
Genevisible; Q96TA1; HS.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
GO; GO:0032274; P:gonadotropin secretion; IMP:UniProtKB.
GO; GO:0044029; P:hypomethylation of CpG island; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:UniProtKB.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0034337; P:RNA folding; IDA:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR026088; Niban-like.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR14392; PTHR14392; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Complete proteome; Cytoplasm;
Direct protein sequencing; Lipoprotein; Membrane; Myristate;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CHAIN 2 746 Niban-like protein 1.
/FTId=PRO_0000213121.
DOMAIN 68 192 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 574 574 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 601 601 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 603 603 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 606 606 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 638 638 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 641 641 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:19362540}.
MOD_RES 646 646 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19362540}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19362540}.
MOD_RES 681 681 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19362540}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19362540}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19362540}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
VAR_SEQ 1 18 MGDVLSTHLDDARRQHIA -> MGWMG (in isoform
2). {ECO:0000303|Ref.1}.
/FTId=VSP_041810.
MUTAGEN 641 641 S->A: Loss of melanoma cell invasion;
when associated with A-646; A-665; A-681;
A-679 and A-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 641 641 S->D,E: Promotes melanoma cell invasion;
when associated with D/E-633; D/E-652;
D/E-668; D/E-679 and D/E-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 646 646 S->A: Loss of melanoma cell invasion;
when associated with A-641; A-665; A-681;
A-679 and A-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 646 646 S->D,E: Promotes melanoma cell invasion;
when associated with D/E-628; D/E-652;
D/E-668; D/E-679 and D/E-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 665 665 S->A: Loss of melanoma cell invasion;
when associated with A-641; A-646; A-681;
A-679 and A-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 665 665 S->D,E: Promotes melanoma cell invasion;
when associated with D/E-628; D/E-633;
D/E-668; D/E-679 and D/E-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 681 681 S->A: Loss of melanoma cell invasion;
when associated with A-641; A-646; A-665;
A-679 and A-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 681 681 S->D,E: Promotes melanoma cell invasion;
when associated with D/E-628; D/E-633;
D/E-652; D/E-679 and D/E-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 692 692 S->A: Loss of melanoma cell invasion;
when associated with A-641; A-646; A-665;
A-668 and A-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 692 692 S->D,E: Promotes melanoma cell invasion;
when associated with D/E-628; D/E-633;
D/E-652; D/E-668 and D/E-683.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 696 696 S->A: Loss of melanoma cell invasion;
when associated with A-641; A-646; A-665;
A-668 and A-679.
{ECO:0000269|PubMed:19362540}.
MUTAGEN 696 696 S->D,E: Promotes melanoma cell invasion;
when associated with D/E-628; D/E-633;
D/E-652; D/E-668 and D/E-679.
{ECO:0000269|PubMed:19362540}.
CONFLICT 318 318 H -> L (in Ref. 1; AAK57556).
{ECO:0000305}.
CONFLICT 677 677 P -> L (in Ref. 7; AAH01979).
{ECO:0000305}.
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


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