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Alsin (Amyotrophic lateral sclerosis 2 protein homolog)

 ALS2_MOUSE              Reviewed;        1651 AA.
Q920R0; G5E868; Q8JZR1; Q9CXJ3;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
05-DEC-2018, entry version 152.
RecName: Full=Alsin;
AltName: Full=Amyotrophic lateral sclerosis 2 protein homolog;
Name=Als2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:BAB69016.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11586298; DOI=10.1038/ng1001-166;
Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R.,
Figlewicz D.A., Kwiatkowski T., Hosler B.A., Sagie T., Skaug J.,
Nasir J., Brown R.H. Jr., Scherer S.W., Rouleau G.A., Hayden M.R.,
Ikeda J.-E.;
"A gene encoding a putative GTPase regulator is mutated in familial
amyotrophic lateral sclerosis 2.";
Nat. Genet. 29:166-173(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH46828.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH46828.1}, and
Mammary gland {ECO:0000312|EMBL:AAH31479.1};
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 847-1651 (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-486, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-486, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-527, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: May act as a GTPase regulator. Controls survival and
growth of spinal motoneurons. {ECO:0000250}.
-!- SUBUNIT: Forms a heteromeric complex with ALS2CL. Interacts with
ALS2CL (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000305};
IsoId=Q920R0-1; Sequence=Displayed;
Name=2 {ECO:0000305};
IsoId=Q920R0-2; Sequence=VSP_050525, VSP_050526;
Note=No experimental confirmation available. {ECO:0000305};
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EMBL; AB053307; BAB69016.1; -; mRNA.
EMBL; AC153652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466548; EDL00124.1; -; Genomic_DNA.
EMBL; BC031479; AAH31479.1; -; mRNA.
EMBL; BC046828; AAH46828.1; -; mRNA.
EMBL; AK014320; BAB29271.2; -; mRNA.
CCDS; CCDS35583.1; -. [Q920R0-1]
RefSeq; NP_001153420.2; NM_001159948.2. [Q920R0-1]
RefSeq; NP_082993.4; NM_028717.6. [Q920R0-1]
RefSeq; NP_666221.1; NM_146109.3.
UniGene; Mm.272078; -.
UniGene; Mm.474049; -.
BioGrid; 216427; 4.
STRING; 10090.ENSMUSP00000027178; -.
iPTMnet; Q920R0; -.
PhosphoSitePlus; Q920R0; -.
EPD; Q920R0; -.
PaxDb; Q920R0; -.
PeptideAtlas; Q920R0; -.
PRIDE; Q920R0; -.
Ensembl; ENSMUST00000027178; ENSMUSP00000027178; ENSMUSG00000026024. [Q920R0-1]
Ensembl; ENSMUST00000163058; ENSMUSP00000125753; ENSMUSG00000026024. [Q920R0-1]
GeneID; 74018; -.
KEGG; mmu:74018; -.
UCSC; uc007bdm.2; mouse. [Q920R0-1]
UCSC; uc007bdn.2; mouse. [Q920R0-2]
CTD; 57679; -.
MGI; MGI:1921268; Als2.
eggNOG; KOG0231; Eukaryota.
eggNOG; KOG1426; Eukaryota.
eggNOG; COG4642; LUCA.
GeneTree; ENSGT00940000155861; -.
HOGENOM; HOG000033908; -.
HOVERGEN; HBG037320; -.
InParanoid; Q920R0; -.
KO; K04575; -.
OMA; ATCFEVT; -.
OrthoDB; EOG091G00CU; -.
TreeFam; TF331793; -.
Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; Als2; mouse.
PRO; PR:Q920R0; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026024; Expressed in 107 organ(s), highest expression level in cerebellum.
ExpressionAtlas; Q920R0; baseline and differential.
Genevisible; Q920R0; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; ISS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; ISO:MGI.
GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISO:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0008219; P:cell death; ISO:MGI.
GO; GO:0016197; P:endosomal transport; IMP:MGI.
GO; GO:0007032; P:endosome organization; ISO:MGI.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0007041; P:lysosomal transport; ISO:MGI.
GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0016601; P:Rac protein signal transduction; ISO:MGI.
GO; GO:0001881; P:receptor recycling; IMP:MGI.
GO; GO:0051036; P:regulation of endosome size; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; IDA:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
GO; GO:0016050; P:vesicle organization; IDA:MGI.
Gene3D; 1.20.1050.80; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.130.10.30; -; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR003409; MORN.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
InterPro; IPR003123; VPS9.
InterPro; IPR037191; VPS9_dom_sf.
Pfam; PF02493; MORN; 7.
Pfam; PF00415; RCC1; 4.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF02204; VPS9; 1.
PRINTS; PR00633; RCCNDNSATION.
SMART; SM00698; MORN; 8.
SUPFAM; SSF109993; SSF109993; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50985; SSF50985; 2.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS00626; RCC1_2; 2.
PROSITE; PS50012; RCC1_3; 4.
PROSITE; PS51205; VPS9; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Guanine-nucleotide releasing factor; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1651 Alsin.
/FTId=PRO_0000080904.
REPEAT 59 108 RCC1 1. {ECO:0000305}.
REPEAT 109 167 RCC1 2. {ECO:0000305}.
REPEAT 169 218 RCC1 3. {ECO:0000305}.
REPEAT 519 570 RCC1 4. {ECO:0000305}.
REPEAT 572 621 RCC1 5. {ECO:0000305}.
DOMAIN 684 879 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 895 1001 PH. {ECO:0000305}.
REPEAT 1043 1065 MORN 1.
REPEAT 1066 1088 MORN 2.
REPEAT 1094 1116 MORN 3.
REPEAT 1117 1139 MORN 4.
REPEAT 1145 1167 MORN 5.
REPEAT 1169 1191 MORN 6.
REPEAT 1192 1214 MORN 7.
REPEAT 1215 1238 MORN 8.
DOMAIN 1507 1651 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000250|UniProtKB:Q96Q42}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:Q96Q42}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 504 504 Phosphothreonine.
{ECO:0000250|UniProtKB:P0C5Y8}.
MOD_RES 527 527 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1329 1329 Phosphoserine.
{ECO:0000250|UniProtKB:P0C5Y8}.
VAR_SEQ 855 928 TSPEYQKLQDSSSCYESLALHLGKKRKEAEYTLSFWKTFPG
KMTDSLRKPERRLLCESSNRALSLQHAGRFSVN -> VGFV
CAPPNTREAKSQSSLFALSLLKMLGPGAGEMAQWVRAPDCS
SEGLEFKSQQPHGGSQPPVMRSDALFWSV (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_050525.
VAR_SEQ 929 1651 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_050526.
CONFLICT 318 318 V -> I (in Ref. 1; BAB69016 and 4;
AAH31479). {ECO:0000305}.
CONFLICT 469 469 L -> S (in Ref. 1; BAB69016 and 4;
AAH31479). {ECO:0000305}.
CONFLICT 764 764 V -> F (in Ref. 4; AAH46828).
{ECO:0000305}.
CONFLICT 1206 1206 V -> L (in Ref. 5; BAB29271).
{ECO:0000305}.
CONFLICT 1296 1296 R -> H (in Ref. 1; BAB69016).
{ECO:0000305}.
CONFLICT 1452 1452 S -> L (in Ref. 1; BAB69016).
{ECO:0000305}.
SEQUENCE 1651 AA; 182566 MW; F9A9DBCA1ED423B2 CRC64;
MDSKKKSSTE AEGSKERGLV HVWQAGSFSL TPERLPGWGG KTVLQAALGV RHGVLLTEDG
EVYSFGTLPW KSESAEICPS SPLLESALVG HHVITVATGS FHSGAVTESG VVYMWGENAA
GQCAVANQQY VPEPSPVSIS DSETSPSLAV RILQLACGEE HTLALSLSRE IWAWGTGCQL
GLITTTFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PPQDLKPVPE RCNQCSQLLI
TMTDKEDHVI ISDSHCCPLG VTLSESQAEK HASPAPSPHP EALDEQGEVF ENTVVEAELN
MGSSQTTSGS AISTQQNVVG TAEVSSARTA PSYPDTHAVT AYLQKLSEHS MRENHEPGEK
PPQVQPLVEE AVPDLHSPPT TSTSALNSLV VSCASAVGVR VAATYEAGAL SLKKVMNFYS
TAPCETAAQS GSASTGPESL KDLREEQVKQ ESLQGKKSSS LMDIREEELE GGSRRLSLPG
LLSQVSPRLL RKAARVKTRT VVLTPTYSGE ADALLPSLRT EVWTWGKGKE GQLGHGDVLP
RLQPLCVKCL DGKEVIHLEA GGSHSLALTA KSQVYSWGSN TFGQLGHSEF PTTVPRLSKV
SSENGVWSVA AGQDYSLFLV DTEDFQPGLY YSGRQDRAEG DTLPENPSGT KTPVLLSCSK
LGYISRVTAG KDSYLALVDK NIMGYIASLH ELASTERRFY SKLSEIKSQI LRPLLSLENL
GTVTTVQLLQ EVASRFSKLC YLIGQHGASL SSYLQGMKEA SSLVIMKHSS LFLDSYTEYC
TSVSNFLVMG GFQLLAKPAI DFLNKNQELL QDLSEVNDEN TQLMEILNML FFLPIRRLHN
YAKVLLKLAT CFEVTSPEYQ KLQDSSSCYE SLALHLGKKR KEAEYTLSFW KTFPGKMTDS
LRKPERRLLC ESSNRALSLQ HAGRFSVNWF ILFNDALVHA QFSTHHVFPL ATLWAEPLSE
EAGSVNGLKI TTPEEQFTLI SSTPQEKTKW LRAISQAVDQ ALRGTSDFPL YGGGSSVQRQ
EPPISRSAKY TFYKDTRLKD ATYDGRWLSG KPHGRGVLKW PDGKMYSGMF RNGLEDGYGE
YRIPNKALNK EDHYVGHWKE GKMCGQGVYS YASGEVFEGC FQDNMRHGHG LLRSGKLTSS
SPSMFIGQWV MDKKAGYGVF DDITRGEKYM GMWQDDVCQG NGVVVTQFGL YYEGNFHLNK
MMGNGVLLSE DDTIYEGEFS DDWTLSGKGT LTMPHGDYIE GYFSGEWGSG IKITGTYFKP
SLYESDKDKP KAFRKLGNLA VAADEKWRAV FEECWRQLGC ESPGQGEVWK AWDNIAVALT
TNRRQHKDSP EILSRSQTQT LESLEYIPQH IGAFSVEKYD DIKKYLIKAC DTPLHPLGRL
VETLVAVYRM TYVGVGANRR LLQEAVKEIK SYLKRIFQLV RFLFPELPEE GSTIPLSAPL
PTGRRSFCTG KSDSRSESPE PGYVVTSSGL LLPVLLPRLY PPLFMLYALD NDREEDIYWE
CVLRLNKQPD IALLGFLGVQ KKFWPATLSI LGESKKVLST TKDACFASAV ECLQQISTTF
TPSDKLKVIQ QTFEEISQSV LASLQEDFLW SMDDLFPVFL YVVLRARIRN LGSEVHLIED
LMDPFLQHGE QGIMFTTLKA CYFQIQREKL N


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EIAAB29887 ALS2CR19,Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein,Homo sapiens,Human,PAR3B,PAR3-beta,PAR3L,PAR3-L protein,PARD3B,Partitioning defective 3 homolog B,Partitioning def
E1328c Human ELISA Kit FOR Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein 96T
PN-7100a-9 Rabbit anti_Human Amyotrophic lateral sclerosis protein 2 (ALS2) IgG fraction polyclonal antibody 1mg
PN-7100a-9 Rabbit anti_Human Amyotrophic lateral sclerosis protein 2 (ALS2) IgG fraction polyclonal antibody 1 mg
CSB-EL001639RA Rat Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein(ALS2CR12) ELISA kit 96T
CSB-EL001642MO Mouse Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 8 protein(ALS2CR8) ELISA kit 96T
CSB-EL001639RA Rat Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein(ALS2CR12) ELISA kit SpeciesRat 96T
CSB-EL001639MO Mouse Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein(ALS2CR12) ELISA kit 96T
CSB-EL001638HU Human Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 11 protein(ALS2CR11) ELISA kit 96T


 

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