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Unconventional myosin-Ig [Cleaved into: Minor histocompatibility antigen HA-2 (mHag HA-2)]

 MYO1G_HUMAN             Reviewed;        1018 AA.
B0I1T2; Q8TEI9; Q8TES2; Q96BE2; Q96RI5; Q96RI6;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 85.
RecName: Full=Unconventional myosin-Ig;
Contains:
RecName: Full=Minor histocompatibility antigen HA-2 {ECO:0000303|PubMed:11544309};
Short=mHag HA-2;
Name=MYO1G; Synonyms=HA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 193-1018 (ISOFORM 3), AND VARIANT
THR-489.
TISSUE=Spleen;
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
"The nucleotide sequence of a long cDNA clone isolated from human
spleen.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
THR-489 AND ARG-861.
TISSUE=Spleen;
Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
"Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
recombination: preparation of full-length cDNA clones encoding motor
proteins.";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-665 (ISOFORM 4), IDENTIFICATION AS
THE MINOR HISTOCOMPATIBILITY ANTIGEN HA-2, VARIANTS HA-2M MET-49 AND
THR-489, CHARACTERIZATION OF VARIANT HA-2M MET-49, AND TISSUE
SPECIFICITY.
PubMed=11544309; DOI=10.4049/jimmunol.167.6.3223;
Pierce R.A., Field E.D., Mutis T., Golovina T.N., Von Kap-Herr C.,
Wilke M., Pool J., Shabanowitz J., Pettenati M.J., Eisenlohr L.C.,
Hunt D.F., Goulmy E., Engelhard V.H.;
"The HA-2 minor histocompatibility antigen is derived from a diallelic
gene encoding a novel human class I myosin protein.";
J. Immunol. 167:3223-3230(2001).
[5]
PROTEIN SEQUENCE OF 41-49 (ISOFORM 1).
PubMed=7539551; DOI=10.1126/science.7539551;
den Haan J.M.M., Sherman N.E., Blokland E., Huczko E., Koning F.,
Drijfhout J.W., Skipper J., Shabanowitz J., Hunt D.F., Engelhard V.H.,
Goulmy E.;
"Identification of a graft versus host disease-associated human minor
histocompatibility antigen.";
Science 268:1476-1480(1995).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-1018 (ISOFORM 1), AND
VARIANT ARG-861.
TISSUE=B-cell;
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).
[7]
SUBCELLULAR LOCATION.
PubMed=19968988; DOI=10.1016/j.febslet.2009.11.096;
Olety B., Walte M., Honnert U., Schillers H., Bahler M.;
"Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises
to the plasma membrane and regulates cell elasticity.";
FEBS Lett. 584:493-499(2010).
[8]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-815;
ARG-826; ARG-876; ARG-880; ARG-885; LYS-898; ARG-903; ARG-906;
ARG-909; ARG-934; ARG-945; ARG-947 AND ARG-953.
PubMed=20071333; DOI=10.1074/jbc.M109.086959;
Patino-Lopez G., Aravind L., Dong X., Kruhlak M.J., Ostap E.M.,
Shaw S.;
"Myosin 1G is an abundant class I myosin in lymphocytes whose
localization at the plasma membrane depends on its ancient divergent
pleckstrin homology (PH) domain (Myo1PH).";
J. Biol. Chem. 285:8675-8686(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Unconventional myosin required during immune response
for detection of rare antigen-presenting cells by regulating T-
cell migration. Unconventional myosins are actin-based motor
molecules with ATPase activity and serve in intracellular
movements. Acts as a regulator of T-cell migration by generating
membrane tension, enforcing cell-intrinsic meandering search,
thereby enhancing detection of rare antigens during lymph-node
surveillance, enabling pathogen eradication. Also required in B-
cells, where it regulates different membrane/cytoskeleton-
dependent processes. Involved in Fc-gamma receptor (Fc-gamma-R)
phagocytosis. {ECO:0000250|UniProtKB:Q5SUA5}.
-!- FUNCTION: Minor histocompatibility antigen HA-2: Constitutes the
minor histocompatibility antigen HA-2. More generally, minor
histocompatibility antigens (mHags) refer to immunogenic peptide
which, when complexed with MHC, can generate an immune response
after recognition by specific T-cells. The peptides are derived
from polymorphic intracellular proteins, which are cleaved by
normal pathways of antigen processing. The binding of these
peptides to MHC class I or class II molecules and their expression
on the cell surface can stimulate T-cell responses and thereby
trigger graft rejection or graft-versus-host disease (GVHD) after
hematopoietic stem cell transplantation from HLA-identical sibling
donor. GVHD is a frequent complication after bone marrow
transplantation (BMT), due to mismatch of minor histocompatibility
antigen in HLA-matched sibling marrow transplants. HA-2 is
restricted to MHC class I HLA-A*0201.
{ECO:0000269|PubMed:11544309, ECO:0000305}.
-!- SUBUNIT: Interacts with calmodulin; via its IQ motifs.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19968988,
ECO:0000269|PubMed:20071333}; Peripheral membrane protein
{ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333}. Cell
projection, phagocytic cup {ECO:0000250|UniProtKB:Q5SUA5}.
Note=Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup.
In T-cells, transiently accumulates in discrete areas at the
plasma membrane of migrating cells or when membranes are deformed
(By similarity). Localization at the membrane is not highly
dependent on phosphatidylinositol 4,5-bisphosphate levels.
Released from the membrane in the presence of ATP. May be enriched
in peripheral processes, such as microvilli or ruffles.
{ECO:0000250|UniProtKB:Q5SUA5, ECO:0000269|PubMed:20071333}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=B0I1T2-1; Sequence=Displayed;
Name=2;
IsoId=B0I1T2-2; Sequence=VSP_034208, VSP_034209;
Note=No experimental confirmation available.;
Name=3;
IsoId=B0I1T2-3; Sequence=VSP_034210;
Note=No experimental confirmation available.;
Name=4;
IsoId=B0I1T2-4; Sequence=VSP_034211, VSP_034212;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells.
{ECO:0000269|PubMed:11544309, ECO:0000269|PubMed:20071333}.
-!- DOMAIN: The myosin tail domain mediates binding to
phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2),
phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and
phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) and
binds to membranous compartments. It is required for recruitment
to Fc-gamma receptor (Fc-gamma-R) phagocytic cups.
{ECO:0000250|UniProtKB:Q5SUA5}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- CAUTION: Represents an unconventional myosin. This protein should
not be confused with the conventional myosin-1 (MYH1).
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB84876.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK074050; BAB84876.1; ALT_SEQ; mRNA.
EMBL; AK074135; BAB84961.1; -; mRNA.
EMBL; AB290179; BAG06733.1; -; mRNA.
EMBL; AC004847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF380932; AAK58092.1; -; mRNA.
EMBL; AF380933; AAK58093.1; -; mRNA.
EMBL; BC015693; AAH15693.2; -; mRNA.
CCDS; CCDS34629.1; -. [B0I1T2-1]
RefSeq; NP_149043.2; NM_033054.2. [B0I1T2-1]
UniGene; Hs.37617; -.
ProteinModelPortal; B0I1T2; -.
SMR; B0I1T2; -.
BioGrid; 122031; 7.
IntAct; B0I1T2; 8.
MINT; MINT-7307233; -.
STRING; 9606.ENSP00000258787; -.
iPTMnet; B0I1T2; -.
PhosphoSitePlus; B0I1T2; -.
SwissPalm; B0I1T2; -.
BioMuta; MYO1G; -.
EPD; B0I1T2; -.
MaxQB; B0I1T2; -.
PaxDb; B0I1T2; -.
PRIDE; B0I1T2; -.
Ensembl; ENST00000258787; ENSP00000258787; ENSG00000136286. [B0I1T2-1]
GeneID; 64005; -.
KEGG; hsa:64005; -.
UCSC; uc003tmh.3; human. [B0I1T2-1]
CTD; 64005; -.
DisGeNET; 64005; -.
EuPathDB; HostDB:ENSG00000136286.14; -.
GeneCards; MYO1G; -.
H-InvDB; HIX0006659; -.
HGNC; HGNC:13880; MYO1G.
HPA; HPA021252; -.
MIM; 600642; gene.
neXtProt; NX_B0I1T2; -.
OpenTargets; ENSG00000136286; -.
eggNOG; KOG0160; Eukaryota.
eggNOG; KOG0164; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00900000140778; -.
HOGENOM; HOG000260264; -.
HOVERGEN; HBG062373; -.
InParanoid; B0I1T2; -.
KO; K10356; -.
OMA; TLARWRC; -.
OrthoDB; EOG091G0136; -.
PhylomeDB; B0I1T2; -.
TreeFam; TF312960; -.
GenomeRNAi; 64005; -.
PRO; PR:B0I1T2; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000136286; -.
CleanEx; HS_MYO1G; -.
ExpressionAtlas; B0I1T2; baseline and differential.
Genevisible; B0I1T2; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0031256; C:leading edge membrane; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0003774; F:motor activity; IEA:InterPro.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0071976; P:cell gliding; IEA:Ensembl.
GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
GO; GO:0006887; P:exocytosis; IEA:Ensembl.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; ISS:UniProtKB.
GO; GO:0002456; P:T cell mediated immunity; ISS:UniProtKB.
GO; GO:0072678; P:T cell migration; ISS:UniProtKB.
CDD; cd01378; MYSc_Myo1; 1.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR010926; Myosin_TH1.
InterPro; IPR036072; MYSc_Myo1.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF06017; Myosin_TH1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS51757; TH1; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Adaptive immunity; Alternative splicing;
ATP-binding; Calmodulin-binding; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Immunity; Lipid-binding;
Membrane; Motor protein; Myosin; Nucleotide-binding; Polymorphism;
Reference proteome.
CHAIN 1 1018 Unconventional myosin-Ig.
/FTId=PRO_0000340316.
PEPTIDE 41 49 Minor histocompatibility antigen HA-2.
{ECO:0000269|PubMed:7539551}.
/FTId=PRO_0000340317.
DOMAIN 9 707 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 710 739 IQ.
DOMAIN 824 1017 TH1. {ECO:0000255|PROSITE-
ProRule:PRU01093}.
NP_BIND 102 109 ATP. {ECO:0000250}.
REGION 584 606 Actin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:25944712}.
VAR_SEQ 207 230 LLRGSEDKQLHELHLERNPAVYNF -> VSPEGKGRWKNGV
GKGRAASWTSL (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_034208.
VAR_SEQ 231 1018 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_034209.
VAR_SEQ 526 1018 Missing (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_034210.
VAR_SEQ 652 722 KMTCEYTWPNHLLGSDKAAVSALLEQHGLQGDVAFGHSKLF
IRSPRTLVTLEQSRARLIPIIVLLLQKAWR -> WHLTPIT
PWAIVPVWSPRGRSRGSPNSTSQTSIQAGTSTLLASRHQNI
WEDMCVSTCMWGHTGGNMGMRAV (in isoform 4).
{ECO:0000303|PubMed:11544309}.
/FTId=VSP_034211.
VAR_SEQ 723 1018 Missing (in isoform 4).
{ECO:0000303|PubMed:11544309}.
/FTId=VSP_034212.
VARIANT 49 49 V -> M (in allele HA-2M; the HA-2V allele
constitute the HA-2 epitope while HA-2M
is not recognized by HA-2 cytotoxic T
lymphocytes; dbSNP:rs61739531).
{ECO:0000269|PubMed:11544309}.
/FTId=VAR_044013.
VARIANT 489 489 M -> T (in dbSNP:rs3735485).
{ECO:0000269|PubMed:11544309,
ECO:0000269|Ref.1, ECO:0000269|Ref.2}.
/FTId=VAR_044014.
VARIANT 798 798 R -> Q (in dbSNP:rs2107737).
/FTId=VAR_050212.
VARIANT 861 861 Q -> R (in dbSNP:rs7792760).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2}.
/FTId=VAR_044015.
MUTAGEN 815 815 K->A: Reduced membrane association.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 826 826 R->A: Reduced membrane association.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 876 876 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 880 880 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 883 883 K->A: No effect on membrane localization;
when associated with R-885.
MUTAGEN 885 885 R->A: No effect on membrane localization;
when associated with K-883.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 898 898 K->A: Reduced membrane association.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 903 903 R->A: No effect on membrane localization;
when associated with R-906.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 906 906 R->A: No effect on membrane localization;
when associated with R-903.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 909 909 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 934 934 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 945 945 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 947 947 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
MUTAGEN 953 953 R->A: No effect on membrane localization.
{ECO:0000269|PubMed:20071333}.
CONFLICT 369 369 N -> K (in Ref. 1; BAB84961).
{ECO:0000305}.
CONFLICT 377 377 P -> L (in Ref. 4; AAK58092/AAK58093).
{ECO:0000305}.
SEQUENCE 1018 AA; 116442 MW; 3EB4ACC3D99A86E9 CRC64;
MEDEEGPEYG KPDFVLLDQV TMEDFMRNLQ LRFEKGRIYT YIGEVLVSVN PYQELPLYGP
EAIARYQGRE LYERPPHLYA VANAAYKAMK HRSRDTCIVI SGESGAGKTE ASKHIMQYIA
AVTNPSQRAE VERVKDVLLK STCVLEAFGN ARTNRNHNSS RFGKYMDINF DFKGDPIGGH
IHSYLLEKSR VLKQHVGERN FHAFYQLLRG SEDKQLHELH LERNPAVYNF THQGAGLNMT
VHSALDSDEQ SHQAVTEAMR VIGFSPEEVE SVHRILAAIL HLGNIEFVET EEGGLQKEGL
AVAEEALVDH VAELTATPRD LVLRSLLART VASGGRELIE KGHTAAEASY ARDACAKAVY
QRLFEWVVNR INSVMEPRGR DPRRDGKDTV IGVLDIYGFE VFPVNSFEQF CINYCNEKLQ
QLFIQLILKQ EQEEYEREGI TWQSVEYFNN ATIVDLVERP HRGILAVLDE ACSSAGTITD
RIFLQTLDMH HRHHLHYTSR QLCPTDKTME FGRDFRIKHY AGDVTYSVEG FIDKNRDFLF
QDFKRLLYNS TDPTLRAMWP DGQQDITEVT KRPLTAGTLF KNSMVALVEN LASKEPFYVR
CIKPNEDKVA GKLDENHCRH QVAYLGLLEN VRVRRAGFAS RQPYSRFLLR YKMTCEYTWP
NHLLGSDKAA VSALLEQHGL QGDVAFGHSK LFIRSPRTLV TLEQSRARLI PIIVLLLQKA
WRGTLARWRC RRLRAIYTIM RWFRRHKVRA HLAELQRRFQ AARQPPLYGR DLVWPLPPAV
LQPFQDTCHA LFCRWRARQL VKNIPPSDMP QIKAKVAAMG ALQGLRQDWG CRRAWARDYL
SSATDNPTAS SLFAQRLKTL QDKDGFGAVL FSSHVRKVNR FHKIRNRALL LTDQHLYKLD
PDRQYRVMRA VPLEAVTGLS VTSGGDQLVV LHARGQDDLV VCLHRSRPPL DNRVGELVGV
LAAHCQGEGR TLEVRVSDCI PLSHRGVRRL ISVEPRPEQP EPDFRCARGS FTLLWPSR


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18-003-43570 Pumilio domain-containing protein KIAA0020 - HBV X-transactivated gene 5 protein; Minor histocompatibility antigen HA-8; HLA-HA8 Polyclonal 0.1 mg Protein A
EIAAB37817 H47,Minor histocompatibility antigen H47,Mouse,Mus musculus,Selenoprotein S,SelS,Sels,VCP-interacting membrane protein,Vimp


 

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