MYADM_HUMAN
ID MYADM_HUMAN Reviewed; 322 AA.
AC Q96S97; B2RE58; Q542Z1; Q7Z507; Q8N9R4; Q96CS6; Q96SK9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Myeloid-associated differentiation marker;
DE AltName: Full=Protein SB135;
GN Name=MYADM; ORFNames=UNQ553/PRO1110;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=12075932; DOI=10.1023/a:1015288412047;
RA Cui W., Yu L., He H., Chu Y., Gao J., Wan B., Tang L., Zhao S.;
RT "Cloning of human myeloid-associated differentiation marker (MYADM) gene
RT whose expression was up-regulated in NB4 cells induced by all-trans
RT retinoic acid.";
RL Mol. Biol. Rep. 28:123-138(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li N., Wan T., Zhang W., Cao X.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- INTERACTION:
CC Q96S97; P11912: CD79A; NbExp=3; IntAct=EBI-13301517, EBI-7797864;
CC Q96S97; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-13301517, EBI-781551;
CC Q96S97; Q9Y624: F11R; NbExp=3; IntAct=EBI-13301517, EBI-742600;
CC Q96S97; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-13301517, EBI-18304435;
CC Q96S97; Q96LL3: FIMP; NbExp=3; IntAct=EBI-13301517, EBI-12887376;
CC Q96S97; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-13301517, EBI-12142257;
CC Q96S97; P15941-11: MUC1; NbExp=3; IntAct=EBI-13301517, EBI-17263240;
CC Q96S97; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-13301517, EBI-716063;
CC Q96S97; P60201-2: PLP1; NbExp=3; IntAct=EBI-13301517, EBI-12188331;
CC Q96S97; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-13301517, EBI-2821497;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Not detected in thymus.
CC {ECO:0000269|PubMed:12075932}.
CC -!- SIMILARITY: Belongs to the MAL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97182.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB55302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF087882; AAP97182.1; ALT_FRAME; mRNA.
DR EMBL; AY037147; AAK67628.2; -; mRNA.
DR EMBL; AY358582; AAQ88945.1; -; mRNA.
DR EMBL; AK027693; BAB55302.1; ALT_INIT; mRNA.
DR EMBL; AK093999; BAC04265.1; -; mRNA.
DR EMBL; AK075276; BAC11513.1; -; mRNA.
DR EMBL; AK316566; BAG38155.1; -; mRNA.
DR EMBL; CH471135; EAW72159.1; -; Genomic_DNA.
DR EMBL; BC013995; AAH13995.1; -; mRNA.
DR EMBL; BC095412; AAH95412.1; -; mRNA.
DR CCDS; CCDS12866.1; -.
DR RefSeq; NP_001018654.1; NM_001020818.2.
DR RefSeq; NP_001018655.1; NM_001020819.2.
DR RefSeq; NP_001018656.1; NM_001020820.2.
DR RefSeq; NP_001018657.1; NM_001020821.2.
DR RefSeq; NP_001277117.1; NM_001290188.1.
DR RefSeq; NP_001277118.1; NM_001290189.1.
DR RefSeq; NP_001277119.1; NM_001290190.1.
DR RefSeq; NP_001277120.1; NM_001290191.1.
DR RefSeq; NP_001277121.1; NM_001290192.1.
DR RefSeq; NP_001277122.1; NM_001290193.1.
DR RefSeq; NP_001277123.1; NM_001290194.1.
DR RefSeq; NP_612382.1; NM_138373.4.
DR AlphaFoldDB; Q96S97; -.
DR BioGRID; 124862; 114.
DR IntAct; Q96S97; 34.
DR STRING; 9606.ENSP00000375649; -.
DR TCDB; 1.A.64.3.1; the plasmolipin (plasmolipin) family.
DR iPTMnet; Q96S97; -.
DR PhosphoSitePlus; Q96S97; -.
DR SwissPalm; Q96S97; -.
DR BioMuta; MYADM; -.
DR DMDM; 21263793; -.
DR EPD; Q96S97; -.
DR jPOST; Q96S97; -.
DR MassIVE; Q96S97; -.
DR MaxQB; Q96S97; -.
DR PaxDb; Q96S97; -.
DR PeptideAtlas; Q96S97; -.
DR PRIDE; Q96S97; -.
DR ProteomicsDB; 78092; -.
DR Antibodypedia; 19206; 229 antibodies from 19 providers.
DR DNASU; 91663; -.
DR Ensembl; ENST00000391768.2; ENSP00000375648.2; ENSG00000179820.16.
DR Ensembl; ENST00000391769.2; ENSP00000375649.2; ENSG00000179820.16.
DR Ensembl; ENST00000391770.9; ENSP00000375650.4; ENSG00000179820.16.
DR Ensembl; ENST00000391771.1; ENSP00000375651.1; ENSG00000179820.16.
DR Ensembl; ENST00000421337.6; ENSP00000398269.2; ENSG00000179820.16.
DR GeneID; 91663; -.
DR KEGG; hsa:91663; -.
DR MANE-Select; ENST00000391770.9; ENSP00000375650.4; NM_138373.5; NP_612382.1.
DR UCSC; uc002qcl.4; human.
DR CTD; 91663; -.
DR DisGeNET; 91663; -.
DR GeneCards; MYADM; -.
DR HGNC; HGNC:7544; MYADM.
DR HPA; ENSG00000179820; Low tissue specificity.
DR MIM; 609959; gene.
DR neXtProt; NX_Q96S97; -.
DR OpenTargets; ENSG00000179820; -.
DR PharmGKB; PA31344; -.
DR VEuPathDB; HostDB:ENSG00000179820; -.
DR eggNOG; KOG4788; Eukaryota.
DR GeneTree; ENSGT00950000182933; -.
DR InParanoid; Q96S97; -.
DR OMA; DCTNMLP; -.
DR OrthoDB; 1056604at2759; -.
DR PhylomeDB; Q96S97; -.
DR TreeFam; TF331088; -.
DR PathwayCommons; Q96S97; -.
DR SignaLink; Q96S97; -.
DR BioGRID-ORCS; 91663; 198 hits in 1078 CRISPR screens.
DR ChiTaRS; MYADM; human.
DR GeneWiki; MYADM; -.
DR GenomeRNAi; 91663; -.
DR Pharos; Q96S97; Tbio.
DR PRO; PR:Q96S97; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96S97; protein.
DR Bgee; ENSG00000179820; Expressed in oviduct epithelium and 189 other tissues.
DR ExpressionAtlas; Q96S97; baseline and differential.
DR Genevisible; Q96S97; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0031579; P:membrane raft organization; IMP:UniProtKB.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0044860; P:protein localization to plasma membrane raft; IMP:UniProtKB.
DR InterPro; IPR008253; Marvel.
DR Pfam; PF01284; MARVEL; 2.
DR PROSITE; PS51225; MARVEL; 2.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..322
FT /note="Myeloid-associated differentiation marker"
FT /id="PRO_0000156816"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 31..163
FT /note="MARVEL 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 168..319
FT /note="MARVEL 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CONFLICT 77..94
FT /note="Missing (in Ref. 4; BAC04265)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="C -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35274 MW; A92142CC63625A4E CRC64;
MPVTVTRTTI TTTTTSSSGL GSPMIVGSPR ALTQPLGLLR LLQLVSTCVA FSLVASVGAW
TGSMGNWSMF TWCFCFSVTL IILIVELCGL QARFPLSWRN FPITFACYAA LFCLSASIIY
PTTYVQFLSH GRSRDHAIAA TFFSCIACVA YATEVAWTRA RPGEITGYMA TVPGLLKVLE
TFVACIIFAF ISDPNLYQHQ PALEWCVAVY AICFILAAIA ILLNLGECTN VLPIPFPSFL
SGLALLSVLL YATALVLWPL YQFDEKYGGQ PRRSRDVSCS RSHAYYVCAW DRRLAVAILT
AINLLAYVAD LVHSAHLVFV KV
