Full text data of MPP1
MPP1
(DXS552E, EMP55)
[Confidence: high (present in two of the MS resources)]
55 kDa erythrocyte membrane protein; p55 (Membrane protein, palmitoylated 1)
55 kDa erythrocyte membrane protein; p55 (Membrane protein, palmitoylated 1)
hRBCD
IPI00215610
IPI00215610 55 kDa erythrocyte membrane protein 55 kDa erythrocyte membrane protein membrane 4 1 12 1 11 6 12 3 43 6 16 1 n/a 11 8 4 9 15 11 15 membrane bound n/a found at its expected molecular weight found at molecular weight
IPI00215610 55 kDa erythrocyte membrane protein 55 kDa erythrocyte membrane protein membrane 4 1 12 1 11 6 12 3 43 6 16 1 n/a 11 8 4 9 15 11 15 membrane bound n/a found at its expected molecular weight found at molecular weight
UniProt
Q00013
ID EM55_HUMAN Reviewed; 466 AA.
AC Q00013; B4DZV5; G3XAI1; Q2TSB6; Q5J7V5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 2.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=55 kDa erythrocyte membrane protein;
DE Short=p55;
DE AltName: Full=Membrane protein, palmitoylated 1;
GN Name=MPP1; Synonyms=DXS552E, EMP55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP PALMITOYLATION.
RC TISSUE=Reticulocyte;
RX PubMed=1713685; DOI=10.1073/pnas.88.15.6595;
RA Ruff P., Speicher D.W., Husain-Chishti A.;
RT "Molecular identification of a major palmitoylated erythrocyte
RT membrane protein containing the src homology 3 motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6595-6599(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1301163; DOI=10.1093/hmg/1.2.97;
RA Metzenberg A.B., Gitschier J.;
RT "The gene encoding the palmitoylated erythrocyte membrane protein,
RT p55, originates at the CpG island 3' to the factor VIII gene.";
RL Hum. Mol. Genet. 1:97-101(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung cancer;
RA Kim J.W.;
RT "Identification of a human migration-related gene.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Cerebellum, Cervix, and Thymus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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] (ISOFORM 3).
RC TISSUE=Umbilical cord;
RA Kim J.W.;
RT "Identification of a human aging-related gene.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH MPP5 AND WHRN, AND
RP TISSUE SPECIFICITY.
RX PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT "MPP1 links the Usher protein network and the Crumbs protein complex
RT in the retina.";
RL Hum. Mol. Genet. 16:1993-2003(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-57 AND SER-243,
RP AND MASS SPECTROMETRY.
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 INTERACTION WITH NF2, AND SUBCELLULAR LOCATION.
RX PubMed=19144871; DOI=10.3181/0809-RM-275;
RA Seo P.-S., Quinn B.J., Khan A.A., Zeng L., Takoudis C.G., Hanada T.,
RA Bolis A., Bolino A., Chishti A.H.;
RT "Identification of erythrocyte p55/MPP1 as a binding partner of NF2
RT tumor suppressor protein/Merlin.";
RL Exp. Biol. Med. 234:255-262(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP PALMITOYLATION BY ZDHHC17, AND SUBCELLULAR LOCATION.
RX PubMed=22496366; DOI=10.1074/jbc.M111.332981;
RA Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J.,
RA Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J.,
RA Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F.;
RT "Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is
RT crucial for lateral membrane organization in erythroid cells.";
RL J. Biol. Chem. 287:18974-18984(2012).
RN [15]
RP STRUCTURE BY NMR OF 69-153.
RX PubMed=16741958; DOI=10.1002/prot.21028;
RA Kusunoki H., Kohno T.;
RT "Solution structure of human erythroid p55 PDZ domain.";
RL Proteins 64:804-807(2006).
CC -!- FUNCTION: Essential regulator of neutrophil polarity. Regulates
CC neutrophil polarization by regulating AKT1 phosphorylation through
CC a mechanism that is independent of PIK3CG activity (By
CC similarity).
CC -!- SUBUNIT: Heterodimer with MPP5. Interacts with DLG5 and NF2.
CC Interacts (via guanylate kinase-like domain) with WHRN (via third
CC PDZ domain).
CC -!- INTERACTION:
CC Q96CV9:OPTN; NbExp=2; IntAct=EBI-711788, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cell projection,
CC stereocilium (By similarity). Note=Colocalizes with WHRN at
CC stereocilium tip during hair cell development (By similarity).
CC Colocalizes with MPP5 in the retina, at the outer limiting
CC membrane (OLM). Colocalizes with WHRN in the retina, at the outer
CC limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies
CC and at the connecting cilium (CC). Colocalizes with NF2 in non-
CC myelin-forming Schwann cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q00013-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00013-2; Sequence=VSP_042675;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q00013-3; Sequence=VSP_044634;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Extensively palmitoylated by ZDHHC17, palmitoylation is
CC essential for membrane organization and is crucial for proper
CC erythrocytes morphology.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; M64925; AAA60059.1; -; mRNA.
DR EMBL; M87059; AAA60060.1; -; Genomic_DNA.
DR EMBL; U39611; AAD14835.1; -; Genomic_DNA.
DR EMBL; AY423731; AAS00494.1; -; mRNA.
DR EMBL; AK290246; BAF82935.1; -; mRNA.
DR EMBL; AK303111; BAG64217.1; -; mRNA.
DR EMBL; AK312296; BAG35223.1; -; mRNA.
DR EMBL; AK315957; BAH14328.1; -; mRNA.
DR EMBL; AY634686; AAV35469.1; -; mRNA.
DR EMBL; AC109993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72655.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72656.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72660.1; -; Genomic_DNA.
DR EMBL; BC002392; AAH02392.1; -; mRNA.
DR PIR; A39599; A39599.
DR RefSeq; NP_001159932.1; NM_001166460.1.
DR RefSeq; NP_001159933.1; NM_001166461.1.
DR RefSeq; NP_001159934.1; NM_001166462.1.
DR RefSeq; NP_002427.1; NM_002436.3.
DR UniGene; Hs.496984; -.
DR PDB; 2EJY; NMR; -; A=69-153.
DR PDB; 2EV8; NMR; -; A=69-153.
DR PDB; 3NEY; X-ray; 2.26 A; A/B/C/D/E/F=282-460.
DR PDBsum; 2EJY; -.
DR PDBsum; 2EV8; -.
DR PDBsum; 3NEY; -.
DR ProteinModelPortal; Q00013; -.
DR SMR; Q00013; 69-153, 162-461.
DR IntAct; Q00013; 15.
DR MINT; MINT-1402557; -.
DR STRING; 9606.ENSP00000358547; -.
DR PhosphoSite; Q00013; -.
DR DMDM; 1346575; -.
DR PaxDb; Q00013; -.
DR PeptideAtlas; Q00013; -.
DR PRIDE; Q00013; -.
DR DNASU; 4354; -.
DR Ensembl; ENST00000369534; ENSP00000358547; ENSG00000130830.
DR Ensembl; ENST00000393531; ENSP00000377165; ENSG00000130830.
DR Ensembl; ENST00000413259; ENSP00000400155; ENSG00000130830.
DR Ensembl; ENST00000595966; ENSP00000470051; ENSG00000269326.
DR Ensembl; ENST00000597401; ENSP00000472560; ENSG00000269326.
DR Ensembl; ENST00000599769; ENSP00000471445; ENSG00000269326.
DR GeneID; 4354; -.
DR KEGG; hsa:4354; -.
DR UCSC; uc010nvg.2; human.
DR CTD; 4354; -.
DR GeneCards; GC0XM154006; -.
DR HGNC; HGNC:7219; MPP1.
DR HPA; HPA000884; -.
DR MIM; 305360; gene.
DR neXtProt; NX_Q00013; -.
DR PharmGKB; PA30924; -.
DR eggNOG; COG0194; -.
DR HOGENOM; HOG000233034; -.
DR HOVERGEN; HBG001858; -.
DR InParanoid; Q00013; -.
DR OMA; IPNQQSR; -.
DR PhylomeDB; Q00013; -.
DR EvolutionaryTrace; Q00013; -.
DR GeneWiki; MPP1; -.
DR GenomeRNAi; 4354; -.
DR NextBio; 17130; -.
DR PRO; PR:Q00013; -.
DR ArrayExpress; Q00013; -.
DR Bgee; Q00013; -.
DR CleanEx; HS_MPP1; -.
DR Genevestigator; Q00013; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005622; C:intracellular; IDA:LIFEdb.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR011511; SH3_2.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection;
KW Complete proteome; Direct protein sequencing; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
KW SH3 domain.
FT CHAIN 1 466 55 kDa erythrocyte membrane protein.
FT /FTId=PRO_0000094565.
FT DOMAIN 71 152 PDZ.
FT DOMAIN 158 228 SH3.
FT DOMAIN 282 451 Guanylate kinase-like.
FT REGION 268 466 Interaction with MPP5.
FT MOD_RES 49 49 Phosphothreonine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 110 110 Phosphoserine.
FT MOD_RES 243 243 Phosphoserine.
FT VAR_SEQ 1 34 MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPE -> MES
FT W (in isoform 2).
FT /FTId=VSP_042675.
FT VAR_SEQ 161 180 Missing (in isoform 3).
FT /FTId=VSP_044634.
FT VARIANT 448 448 E -> Q (in dbSNP:rs14092).
FT /FTId=VAR_011914.
FT CONFLICT 204 204 Q -> R (in Ref. 5; AAV35469).
FT STRAND 70 76
FT STRAND 78 80
FT STRAND 83 88
FT STRAND 94 99
FT STRAND 101 103
FT HELIX 104 108
FT STRAND 116 120
FT TURN 125 127
FT HELIX 131 139
FT STRAND 142 149
FT STRAND 284 288
FT HELIX 295 305
FT TURN 307 309
FT HELIX 336 344
FT STRAND 348 354
FT STRAND 357 362
FT HELIX 363 371
FT STRAND 375 379
FT HELIX 382 384
FT HELIX 385 388
FT TURN 391 393
FT STRAND 395 402
FT STRAND 405 407
FT HELIX 410 426
FT HELIX 427 429
FT STRAND 431 437
FT HELIX 439 452
SQ SEQUENCE 466 AA; 52296 MW; DC68AA68EF48A26E CRC64;
MTLKASEGES GGSMHTALSD LYLEHLLQKR SRPEAVSHPL NTVTEDMYTN GSPAPGSPAQ
VKGQEVRKVR LIQFEKVTEE PMGITLKLNE KQSCTVARIL HGGMIHRQGS LHVGDEILEI
NGTNVTNHSV DQLQKAMKET KGMISLKVIP NQQSRLPALQ MFMRAQFDYD PKKDNLIPCK
EAGLKFATGD IIQIINKDDS NWWQGRVEGS SKESAGLIPS PELQEWRVAS MAQSAPSEAP
SCSPFGKKKK YKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
ALLSQNPEKF VYPVPYTTRP PRKSEEDGKE YHFISTEEMT RNISANEFLE FGSYQGNMFG
TKFETVHQIH KQNKIAILDI EPQTLKIVRT AELSPFIVFI APTDQGTQTE ALQQLQKDSE
AIRSQYAHYF DLSLVNNGVD ETLKKLQEAF DQACSSPQWV PVSWVY
//
ID EM55_HUMAN Reviewed; 466 AA.
AC Q00013; B4DZV5; G3XAI1; Q2TSB6; Q5J7V5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1996, sequence version 2.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=55 kDa erythrocyte membrane protein;
DE Short=p55;
DE AltName: Full=Membrane protein, palmitoylated 1;
GN Name=MPP1; Synonyms=DXS552E, EMP55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP PALMITOYLATION.
RC TISSUE=Reticulocyte;
RX PubMed=1713685; DOI=10.1073/pnas.88.15.6595;
RA Ruff P., Speicher D.W., Husain-Chishti A.;
RT "Molecular identification of a major palmitoylated erythrocyte
RT membrane protein containing the src homology 3 motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6595-6599(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1301163; DOI=10.1093/hmg/1.2.97;
RA Metzenberg A.B., Gitschier J.;
RT "The gene encoding the palmitoylated erythrocyte membrane protein,
RT p55, originates at the CpG island 3' to the factor VIII gene.";
RL Hum. Mol. Genet. 1:97-101(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung cancer;
RA Kim J.W.;
RT "Identification of a human migration-related gene.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Cerebellum, Cervix, and Thymus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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] (ISOFORM 3).
RC TISSUE=Umbilical cord;
RA Kim J.W.;
RT "Identification of a human aging-related gene.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH MPP5 AND WHRN, AND
RP TISSUE SPECIFICITY.
RX PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT "MPP1 links the Usher protein network and the Crumbs protein complex
RT in the retina.";
RL Hum. Mol. Genet. 16:1993-2003(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-57 AND SER-243,
RP AND MASS SPECTROMETRY.
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 INTERACTION WITH NF2, AND SUBCELLULAR LOCATION.
RX PubMed=19144871; DOI=10.3181/0809-RM-275;
RA Seo P.-S., Quinn B.J., Khan A.A., Zeng L., Takoudis C.G., Hanada T.,
RA Bolis A., Bolino A., Chishti A.H.;
RT "Identification of erythrocyte p55/MPP1 as a binding partner of NF2
RT tumor suppressor protein/Merlin.";
RL Exp. Biol. Med. 234:255-262(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., 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 [14]
RP PALMITOYLATION BY ZDHHC17, AND SUBCELLULAR LOCATION.
RX PubMed=22496366; DOI=10.1074/jbc.M111.332981;
RA Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J.,
RA Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J.,
RA Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F.;
RT "Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is
RT crucial for lateral membrane organization in erythroid cells.";
RL J. Biol. Chem. 287:18974-18984(2012).
RN [15]
RP STRUCTURE BY NMR OF 69-153.
RX PubMed=16741958; DOI=10.1002/prot.21028;
RA Kusunoki H., Kohno T.;
RT "Solution structure of human erythroid p55 PDZ domain.";
RL Proteins 64:804-807(2006).
CC -!- FUNCTION: Essential regulator of neutrophil polarity. Regulates
CC neutrophil polarization by regulating AKT1 phosphorylation through
CC a mechanism that is independent of PIK3CG activity (By
CC similarity).
CC -!- SUBUNIT: Heterodimer with MPP5. Interacts with DLG5 and NF2.
CC Interacts (via guanylate kinase-like domain) with WHRN (via third
CC PDZ domain).
CC -!- INTERACTION:
CC Q96CV9:OPTN; NbExp=2; IntAct=EBI-711788, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cell projection,
CC stereocilium (By similarity). Note=Colocalizes with WHRN at
CC stereocilium tip during hair cell development (By similarity).
CC Colocalizes with MPP5 in the retina, at the outer limiting
CC membrane (OLM). Colocalizes with WHRN in the retina, at the outer
CC limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies
CC and at the connecting cilium (CC). Colocalizes with NF2 in non-
CC myelin-forming Schwann cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q00013-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00013-2; Sequence=VSP_042675;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q00013-3; Sequence=VSP_044634;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Extensively palmitoylated by ZDHHC17, palmitoylation is
CC essential for membrane organization and is crucial for proper
CC erythrocytes morphology.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; M64925; AAA60059.1; -; mRNA.
DR EMBL; M87059; AAA60060.1; -; Genomic_DNA.
DR EMBL; U39611; AAD14835.1; -; Genomic_DNA.
DR EMBL; AY423731; AAS00494.1; -; mRNA.
DR EMBL; AK290246; BAF82935.1; -; mRNA.
DR EMBL; AK303111; BAG64217.1; -; mRNA.
DR EMBL; AK312296; BAG35223.1; -; mRNA.
DR EMBL; AK315957; BAH14328.1; -; mRNA.
DR EMBL; AY634686; AAV35469.1; -; mRNA.
DR EMBL; AC109993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72655.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72656.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72660.1; -; Genomic_DNA.
DR EMBL; BC002392; AAH02392.1; -; mRNA.
DR PIR; A39599; A39599.
DR RefSeq; NP_001159932.1; NM_001166460.1.
DR RefSeq; NP_001159933.1; NM_001166461.1.
DR RefSeq; NP_001159934.1; NM_001166462.1.
DR RefSeq; NP_002427.1; NM_002436.3.
DR UniGene; Hs.496984; -.
DR PDB; 2EJY; NMR; -; A=69-153.
DR PDB; 2EV8; NMR; -; A=69-153.
DR PDB; 3NEY; X-ray; 2.26 A; A/B/C/D/E/F=282-460.
DR PDBsum; 2EJY; -.
DR PDBsum; 2EV8; -.
DR PDBsum; 3NEY; -.
DR ProteinModelPortal; Q00013; -.
DR SMR; Q00013; 69-153, 162-461.
DR IntAct; Q00013; 15.
DR MINT; MINT-1402557; -.
DR STRING; 9606.ENSP00000358547; -.
DR PhosphoSite; Q00013; -.
DR DMDM; 1346575; -.
DR PaxDb; Q00013; -.
DR PeptideAtlas; Q00013; -.
DR PRIDE; Q00013; -.
DR DNASU; 4354; -.
DR Ensembl; ENST00000369534; ENSP00000358547; ENSG00000130830.
DR Ensembl; ENST00000393531; ENSP00000377165; ENSG00000130830.
DR Ensembl; ENST00000413259; ENSP00000400155; ENSG00000130830.
DR Ensembl; ENST00000595966; ENSP00000470051; ENSG00000269326.
DR Ensembl; ENST00000597401; ENSP00000472560; ENSG00000269326.
DR Ensembl; ENST00000599769; ENSP00000471445; ENSG00000269326.
DR GeneID; 4354; -.
DR KEGG; hsa:4354; -.
DR UCSC; uc010nvg.2; human.
DR CTD; 4354; -.
DR GeneCards; GC0XM154006; -.
DR HGNC; HGNC:7219; MPP1.
DR HPA; HPA000884; -.
DR MIM; 305360; gene.
DR neXtProt; NX_Q00013; -.
DR PharmGKB; PA30924; -.
DR eggNOG; COG0194; -.
DR HOGENOM; HOG000233034; -.
DR HOVERGEN; HBG001858; -.
DR InParanoid; Q00013; -.
DR OMA; IPNQQSR; -.
DR PhylomeDB; Q00013; -.
DR EvolutionaryTrace; Q00013; -.
DR GeneWiki; MPP1; -.
DR GenomeRNAi; 4354; -.
DR NextBio; 17130; -.
DR PRO; PR:Q00013; -.
DR ArrayExpress; Q00013; -.
DR Bgee; Q00013; -.
DR CleanEx; HS_MPP1; -.
DR Genevestigator; Q00013; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005622; C:intracellular; IDA:LIFEdb.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR011511; SH3_2.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection;
KW Complete proteome; Direct protein sequencing; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
KW SH3 domain.
FT CHAIN 1 466 55 kDa erythrocyte membrane protein.
FT /FTId=PRO_0000094565.
FT DOMAIN 71 152 PDZ.
FT DOMAIN 158 228 SH3.
FT DOMAIN 282 451 Guanylate kinase-like.
FT REGION 268 466 Interaction with MPP5.
FT MOD_RES 49 49 Phosphothreonine.
FT MOD_RES 57 57 Phosphoserine.
FT MOD_RES 110 110 Phosphoserine.
FT MOD_RES 243 243 Phosphoserine.
FT VAR_SEQ 1 34 MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPE -> MES
FT W (in isoform 2).
FT /FTId=VSP_042675.
FT VAR_SEQ 161 180 Missing (in isoform 3).
FT /FTId=VSP_044634.
FT VARIANT 448 448 E -> Q (in dbSNP:rs14092).
FT /FTId=VAR_011914.
FT CONFLICT 204 204 Q -> R (in Ref. 5; AAV35469).
FT STRAND 70 76
FT STRAND 78 80
FT STRAND 83 88
FT STRAND 94 99
FT STRAND 101 103
FT HELIX 104 108
FT STRAND 116 120
FT TURN 125 127
FT HELIX 131 139
FT STRAND 142 149
FT STRAND 284 288
FT HELIX 295 305
FT TURN 307 309
FT HELIX 336 344
FT STRAND 348 354
FT STRAND 357 362
FT HELIX 363 371
FT STRAND 375 379
FT HELIX 382 384
FT HELIX 385 388
FT TURN 391 393
FT STRAND 395 402
FT STRAND 405 407
FT HELIX 410 426
FT HELIX 427 429
FT STRAND 431 437
FT HELIX 439 452
SQ SEQUENCE 466 AA; 52296 MW; DC68AA68EF48A26E CRC64;
MTLKASEGES GGSMHTALSD LYLEHLLQKR SRPEAVSHPL NTVTEDMYTN GSPAPGSPAQ
VKGQEVRKVR LIQFEKVTEE PMGITLKLNE KQSCTVARIL HGGMIHRQGS LHVGDEILEI
NGTNVTNHSV DQLQKAMKET KGMISLKVIP NQQSRLPALQ MFMRAQFDYD PKKDNLIPCK
EAGLKFATGD IIQIINKDDS NWWQGRVEGS SKESAGLIPS PELQEWRVAS MAQSAPSEAP
SCSPFGKKKK YKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
ALLSQNPEKF VYPVPYTTRP PRKSEEDGKE YHFISTEEMT RNISANEFLE FGSYQGNMFG
TKFETVHQIH KQNKIAILDI EPQTLKIVRT AELSPFIVFI APTDQGTQTE ALQQLQKDSE
AIRSQYAHYF DLSLVNNGVD ETLKKLQEAF DQACSSPQWV PVSWVY
//
MIM
305360
*RECORD*
*FIELD* NO
305360
*FIELD* TI
*305360 MEMBRANE PROTEIN, PALMITOYLATED 1; MPP1
;;ERYTHROCYTE MEMBRANE PROTEIN p55; EMP55;;
read morePALMITOYLATED ERYTHROCYTE MEMBRANE PROTEIN; PEMP
*FIELD* TX
DESCRIPTION
EMP55 is the prototype of a family of membrane-associated proteins
termed MAGUKs (membrane-associated guanylate kinase homologs). MAGUKs
interact with the cytoskeleton and regulate cell proliferation,
signaling pathways, and intracellular junctions (Kim et al., 1996).
CLONING
Ruff et al. (1991) deduced the complete amino acid sequence of a 55-kD
erythrocyte membrane protein from cDNA clones isolated from a human
reticulocyte library. This protein, p55, was copurified during the
isolation of dematin, an actin-bundling protein of the erythrocyte
membrane cytoskeleton. Its tight association with the plasma membrane
was reminiscent of an integral membrane protein. Protein p55 is the most
extensively palmitoylated protein of the erythrocyte membrane. Predicted
primary structure of p55 contained a conserved sequence, called the SH3
(src homology 3) motif, found in several other proteins that associate
with the cytoskeleton and are suspected to play important roles in
signal transduction.
Metzenberg and Gitschier (1992) found a gene located in a CpG island 30
kb 3-prime to the factor VIII gene (F8; 300841). The 2-kb transcript
encoded a previously described palmitoylated membrane protein, p55,
containing an src homology motif, SH3. Although originally described in
reticulocytes (Ruff et al., 1991), Metzenberg and Gitschier (1992) found
that the transcript was expressed in a wide variety of human tissues.
The gene was also found in the mouse where it was expressed in all
tissues examined. The EMP55 gene did not appear to be developmentally
regulated in erythrocytes; p55 is constitutively and abundantly
expressed in erythroid cells during their development from stem cells to
fully differentiated reticulocytes. In contrast, other red cell
membrane-associated proteins such as 4.1, ankyrin, and band 3 are
expressed late in erythropoiesis. These results suggested that the p55
protein may have a housekeeping function. Other work indicated that it
is a peripheral membrane protein. Bryant and Woods (1992) demonstrated
that p55 is homologous to the yeast guanylate kinase and to the product
of a Drosophila tumor suppressor gene.
Elder et al. (1996) cloned and sequenced the mouse MPP1 gene. The mouse
gene shares 89% sequence identity with the coding sequence of human
MPP1. The coding region size and intron/exon structures of the mouse and
human genes are identical. The human and mouse sequences and structures
are highly homologous to the MPP1 gene of fish (Fugu), suggesting that
the gene serves an essential function in development.
GENE FUNCTION
By yeast 2-hybrid analysis of a mouse embryo cDNA library, Mburu et al.
(2006) found that whirlin (WHRN; 607928) interacted with p55. p55 was
expressed in mouse outer hair cells in long stereocilia that made up the
stereocilia bundle and in surrounding shorter stereocilia structures.
Since p55 and protein 4.1R (EPB41; 130500) form complexes critical for
actin cytoskeletal assembly in erythrocytes, Mburu et al. (2006)
proposed that p55 and whirlin may have a similar role in hair cell
stereocilia.
GENE STRUCTURE
Metzenberg and Gitschier (1992) estimated that the EMP55 gene spans 20
to 30 kb.
Kim et al. (1996) reported the complete intron/exon map of the human
erythroid p55 gene. The structure of the p55 gene was determined from
cosmid clones isolated from a cosmid library specific for the human X
chromosome. There is a single copy of the p55 gene, composed of 12 exons
and spanning approximately 28 kb in the Xq28 region. Several of the exon
boundaries corresponded to the boundaries of functional domains in the
p55 protein. These domains include an SH3 motif and a region that binds
to cytoskeletal protein 4.1.
MAPPING
Metzenberg and Gitschier (1992) identified the EMP55 gene in a CpG
island 30 kb 3-prime to the factor VIII gene (300841). They confirmed
the Xq28 localization of the EMP55 gene by study of hybrid cell lines
containing various parts of the human X chromosome in rodent
backgrounds. They proved that the gene is located between the F8 and
glucose-6 phosphate dehydrogenase (G6PD; 305900) genes by hybridization
to a YAC clone that extends approximately 60 kb beyond the F8C gene. The
EMP55 gene appeared to be transcribed in the same direction as F8C. No
known factor VIII gene deletions extended into the EMP55 gene. Since the
function of the p55 protein was not known, the gene was formally a
candidate for any of the many disease genes that are closely linked
genetically to the F8C gene.
MOLECULAR GENETICS
Metzenberg et al. (1994) failed to find evidence of mutation in the
EMP55 gene in either of 2 disorders that on the grounds of phenotype and
map location are candidate disorders: dyskeratosis congenita (305000)
and Emery-Dreifuss muscular dystrophy (310300).
Liu et al. (1997) reported a method of determination of clonality using
allele-specific PCR (ASPCR) to detect exonic polymorphisms in p55 and
G6PD (305900). They demonstrated a significant sex difference in allele
frequencies in African Americans but not in Caucasians, and linkage
disequilibrium for the p55 and G6PD alleles in Caucasians but not in
African Americans.
*FIELD* RF
1. Bryant, P. J.; Woods, D. F.: A major palmitoylated membrane protein
of human erythrocytes shows homology to yeast guanylate kinase and
to the product of a Drosophila tumor suppressor gene. Cell 68: 621-622,
1992.
2. Elder, B.; Kuo, K.; Gitschier, J.; Kim, A.; Chishti, A.; Metzenberg,
A.: cDNA sequence and genomic structure of the murine p55 (Mpp1)
gene. Genomics 38: 231-234, 1996.
3. Kim, A. C.; Metzenberg, A. B.; Sahr, K. E.; Marfatia, S. M.; Chisti,
A. H.: Complete genomic organization of the human erythroid p55 gene
(MPP1), a membrane-associated guanylate kinase homologue. Genomics 31:
223-229, 1996.
4. Liu, Y.; Phelan, J.; Go, R. C. P.; Prchal, J. F.; Prchal, J. T.
: Rapid determination of clonality by detection of two closely-linked
X chromosome exonic polymorphisms using allele-specific PCR. J. Clin.
Invest. 99: 1984-1990, 1997.
5. Mburu, P.; Kikkawa, Y.; Townsend, S.; Romero, R.; Yonekawa, H.;
Brown, S. D. M.: Whirlin complexes with p55 at the stereocilia tip
during hair cell development. Proc. Nat. Acad. Sci. 103;-10973-10978,
2006.
6. Metzenberg, A. B.; Gitschier, J.: The gene encoding the palmitoylated
erythrocyte membrane protein, p55, originates at the CpG island 3-prime
to the factor VIII gene. Hum. Molec. Genet. 1: 97-101, 1992.
7. Metzenberg, A. B.; Pan, Y.; Das, S.; Pai, G. S.; Gitschier, J.
: Molecular evidence that the p55 gene is not responsible for either
of two Xq28-linked disorders: Emery-Dreifuss muscular dystrophy and
dyskeratosis congenita. (Letter) Am. J. Hum. Genet. 54: 920-922,
1994.
8. Ruff, P.; Speicher, D. W.; Husain-Chishti, A.: Molecular identification
of a major palmitoylated erythrocyte membrane protein containing the
src homology 3 motif. Proc. Nat. Acad. Sci. 88: 6595-6599, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 10/5/2006
Michael J. Wright - updated: 9/25/1997
Jennifer P. Macke - updated: 7/12/1997
*FIELD* CD
Victor A. McKusick: 10/2/1992
*FIELD* ED
carol: 04/07/2011
mgross: 10/5/2006
carol: 4/2/2002
alopez: 11/11/1997
jenny: 9/2/1997
jenny: 8/13/1997
mark: 3/18/1996
terry: 3/6/1996
jason: 7/26/1994
carol: 2/17/1993
carol: 1/8/1993
carol: 1/4/1993
carol: 10/21/1992
carol: 10/2/1992
*RECORD*
*FIELD* NO
305360
*FIELD* TI
*305360 MEMBRANE PROTEIN, PALMITOYLATED 1; MPP1
;;ERYTHROCYTE MEMBRANE PROTEIN p55; EMP55;;
read morePALMITOYLATED ERYTHROCYTE MEMBRANE PROTEIN; PEMP
*FIELD* TX
DESCRIPTION
EMP55 is the prototype of a family of membrane-associated proteins
termed MAGUKs (membrane-associated guanylate kinase homologs). MAGUKs
interact with the cytoskeleton and regulate cell proliferation,
signaling pathways, and intracellular junctions (Kim et al., 1996).
CLONING
Ruff et al. (1991) deduced the complete amino acid sequence of a 55-kD
erythrocyte membrane protein from cDNA clones isolated from a human
reticulocyte library. This protein, p55, was copurified during the
isolation of dematin, an actin-bundling protein of the erythrocyte
membrane cytoskeleton. Its tight association with the plasma membrane
was reminiscent of an integral membrane protein. Protein p55 is the most
extensively palmitoylated protein of the erythrocyte membrane. Predicted
primary structure of p55 contained a conserved sequence, called the SH3
(src homology 3) motif, found in several other proteins that associate
with the cytoskeleton and are suspected to play important roles in
signal transduction.
Metzenberg and Gitschier (1992) found a gene located in a CpG island 30
kb 3-prime to the factor VIII gene (F8; 300841). The 2-kb transcript
encoded a previously described palmitoylated membrane protein, p55,
containing an src homology motif, SH3. Although originally described in
reticulocytes (Ruff et al., 1991), Metzenberg and Gitschier (1992) found
that the transcript was expressed in a wide variety of human tissues.
The gene was also found in the mouse where it was expressed in all
tissues examined. The EMP55 gene did not appear to be developmentally
regulated in erythrocytes; p55 is constitutively and abundantly
expressed in erythroid cells during their development from stem cells to
fully differentiated reticulocytes. In contrast, other red cell
membrane-associated proteins such as 4.1, ankyrin, and band 3 are
expressed late in erythropoiesis. These results suggested that the p55
protein may have a housekeeping function. Other work indicated that it
is a peripheral membrane protein. Bryant and Woods (1992) demonstrated
that p55 is homologous to the yeast guanylate kinase and to the product
of a Drosophila tumor suppressor gene.
Elder et al. (1996) cloned and sequenced the mouse MPP1 gene. The mouse
gene shares 89% sequence identity with the coding sequence of human
MPP1. The coding region size and intron/exon structures of the mouse and
human genes are identical. The human and mouse sequences and structures
are highly homologous to the MPP1 gene of fish (Fugu), suggesting that
the gene serves an essential function in development.
GENE FUNCTION
By yeast 2-hybrid analysis of a mouse embryo cDNA library, Mburu et al.
(2006) found that whirlin (WHRN; 607928) interacted with p55. p55 was
expressed in mouse outer hair cells in long stereocilia that made up the
stereocilia bundle and in surrounding shorter stereocilia structures.
Since p55 and protein 4.1R (EPB41; 130500) form complexes critical for
actin cytoskeletal assembly in erythrocytes, Mburu et al. (2006)
proposed that p55 and whirlin may have a similar role in hair cell
stereocilia.
GENE STRUCTURE
Metzenberg and Gitschier (1992) estimated that the EMP55 gene spans 20
to 30 kb.
Kim et al. (1996) reported the complete intron/exon map of the human
erythroid p55 gene. The structure of the p55 gene was determined from
cosmid clones isolated from a cosmid library specific for the human X
chromosome. There is a single copy of the p55 gene, composed of 12 exons
and spanning approximately 28 kb in the Xq28 region. Several of the exon
boundaries corresponded to the boundaries of functional domains in the
p55 protein. These domains include an SH3 motif and a region that binds
to cytoskeletal protein 4.1.
MAPPING
Metzenberg and Gitschier (1992) identified the EMP55 gene in a CpG
island 30 kb 3-prime to the factor VIII gene (300841). They confirmed
the Xq28 localization of the EMP55 gene by study of hybrid cell lines
containing various parts of the human X chromosome in rodent
backgrounds. They proved that the gene is located between the F8 and
glucose-6 phosphate dehydrogenase (G6PD; 305900) genes by hybridization
to a YAC clone that extends approximately 60 kb beyond the F8C gene. The
EMP55 gene appeared to be transcribed in the same direction as F8C. No
known factor VIII gene deletions extended into the EMP55 gene. Since the
function of the p55 protein was not known, the gene was formally a
candidate for any of the many disease genes that are closely linked
genetically to the F8C gene.
MOLECULAR GENETICS
Metzenberg et al. (1994) failed to find evidence of mutation in the
EMP55 gene in either of 2 disorders that on the grounds of phenotype and
map location are candidate disorders: dyskeratosis congenita (305000)
and Emery-Dreifuss muscular dystrophy (310300).
Liu et al. (1997) reported a method of determination of clonality using
allele-specific PCR (ASPCR) to detect exonic polymorphisms in p55 and
G6PD (305900). They demonstrated a significant sex difference in allele
frequencies in African Americans but not in Caucasians, and linkage
disequilibrium for the p55 and G6PD alleles in Caucasians but not in
African Americans.
*FIELD* RF
1. Bryant, P. J.; Woods, D. F.: A major palmitoylated membrane protein
of human erythrocytes shows homology to yeast guanylate kinase and
to the product of a Drosophila tumor suppressor gene. Cell 68: 621-622,
1992.
2. Elder, B.; Kuo, K.; Gitschier, J.; Kim, A.; Chishti, A.; Metzenberg,
A.: cDNA sequence and genomic structure of the murine p55 (Mpp1)
gene. Genomics 38: 231-234, 1996.
3. Kim, A. C.; Metzenberg, A. B.; Sahr, K. E.; Marfatia, S. M.; Chisti,
A. H.: Complete genomic organization of the human erythroid p55 gene
(MPP1), a membrane-associated guanylate kinase homologue. Genomics 31:
223-229, 1996.
4. Liu, Y.; Phelan, J.; Go, R. C. P.; Prchal, J. F.; Prchal, J. T.
: Rapid determination of clonality by detection of two closely-linked
X chromosome exonic polymorphisms using allele-specific PCR. J. Clin.
Invest. 99: 1984-1990, 1997.
5. Mburu, P.; Kikkawa, Y.; Townsend, S.; Romero, R.; Yonekawa, H.;
Brown, S. D. M.: Whirlin complexes with p55 at the stereocilia tip
during hair cell development. Proc. Nat. Acad. Sci. 103;-10973-10978,
2006.
6. Metzenberg, A. B.; Gitschier, J.: The gene encoding the palmitoylated
erythrocyte membrane protein, p55, originates at the CpG island 3-prime
to the factor VIII gene. Hum. Molec. Genet. 1: 97-101, 1992.
7. Metzenberg, A. B.; Pan, Y.; Das, S.; Pai, G. S.; Gitschier, J.
: Molecular evidence that the p55 gene is not responsible for either
of two Xq28-linked disorders: Emery-Dreifuss muscular dystrophy and
dyskeratosis congenita. (Letter) Am. J. Hum. Genet. 54: 920-922,
1994.
8. Ruff, P.; Speicher, D. W.; Husain-Chishti, A.: Molecular identification
of a major palmitoylated erythrocyte membrane protein containing the
src homology 3 motif. Proc. Nat. Acad. Sci. 88: 6595-6599, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 10/5/2006
Michael J. Wright - updated: 9/25/1997
Jennifer P. Macke - updated: 7/12/1997
*FIELD* CD
Victor A. McKusick: 10/2/1992
*FIELD* ED
carol: 04/07/2011
mgross: 10/5/2006
carol: 4/2/2002
alopez: 11/11/1997
jenny: 9/2/1997
jenny: 8/13/1997
mark: 3/18/1996
terry: 3/6/1996
jason: 7/26/1994
carol: 2/17/1993
carol: 1/8/1993
carol: 1/4/1993
carol: 10/21/1992
carol: 10/2/1992