EM55_HUMAN
ID EM55_HUMAN Reviewed; 466 AA.
AC Q00013; B4DZV5; G3XAI1; Q2TSB6; Q5J7V5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 214.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 membrane
RT 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, p55,
RT 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., 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] (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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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., 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 (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP SUBUNIT, INTERACTION WITH PALS1 AND WHRN, AND 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 in the
RT retina.";
RL Hum. Mol. Genet. 16:1993-2003(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-57 AND SER-243, AND
RP IDENTIFICATION BY 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 [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 tumor
RT suppressor protein/Merlin.";
RL Exp. Biol. Med. 234:255-262(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 RETRACTED PAPER.
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 crucial
RT for lateral membrane organization in erythroid cells.";
RL J. Biol. Chem. 287:18974-18984(2012).
RN [15]
RP RETRACTION NOTICE OF PUBMED:22496366.
RX PubMed=29475958; DOI=10.1074/jbc.w118.002209;
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 crucial
RT for lateral membrane organization in erythroid cells.";
RL J. Biol. Chem. 293:2786-2786(2018).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-19; SER-57; SER-110
RP AND SER-243, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [18]
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 a
CC mechanism that is independent of PIK3CG activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with PALS1. Interacts with DLG5 and NF2. Interacts
CC (via guanylate kinase-like domain) with WHRN (via third PDZ domain).
CC {ECO:0000269|PubMed:17584769, ECO:0000269|PubMed:19144871}.
CC -!- INTERACTION:
CC Q00013; O15439: ABCC4; NbExp=10; IntAct=EBI-711788, EBI-4319622;
CC Q00013; Q8TDN7: ACER1; NbExp=3; IntAct=EBI-711788, EBI-13074986;
CC Q00013; Q5QJU3-2: ACER2; NbExp=3; IntAct=EBI-711788, EBI-13319881;
CC Q00013; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-711788, EBI-2803601;
CC Q00013; Q96CW1: AP2M1; NbExp=5; IntAct=EBI-711788, EBI-297683;
CC Q00013; Q96BI3: APH1A; NbExp=3; IntAct=EBI-711788, EBI-2606935;
CC Q00013; Q6UW56-2: ATRAID; NbExp=3; IntAct=EBI-711788, EBI-12830308;
CC Q00013; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-711788, EBI-11519926;
CC Q00013; Q9GZP9: DERL2; NbExp=3; IntAct=EBI-711788, EBI-7962814;
CC Q00013; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-711788, EBI-12831978;
CC Q00013; Q9ULA0: DNPEP; NbExp=6; IntAct=EBI-711788, EBI-748356;
CC Q00013; P22607: FGFR3; NbExp=3; IntAct=EBI-711788, EBI-348399;
CC Q00013; P06396: GSN; NbExp=3; IntAct=EBI-711788, EBI-351506;
CC Q00013; Q0VD86: INCA1; NbExp=3; IntAct=EBI-711788, EBI-6509505;
CC Q00013; Q53G59: KLHL12; NbExp=6; IntAct=EBI-711788, EBI-740929;
CC Q00013; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-711788, EBI-16439278;
CC Q00013; Q96CV9: OPTN; NbExp=2; IntAct=EBI-711788, EBI-748974;
CC Q00013; Q8TEZ7: PAQR8; NbExp=3; IntAct=EBI-711788, EBI-12847818;
CC Q00013; Q96LW4: PRIMPOL; NbExp=3; IntAct=EBI-711788, EBI-10044038;
CC Q00013; Q9NS64: RPRM; NbExp=3; IntAct=EBI-711788, EBI-1052363;
CC Q00013; Q96K37: SLC35E1; NbExp=3; IntAct=EBI-711788, EBI-720094;
CC Q00013; R4GMP8: SRSF10; NbExp=3; IntAct=EBI-711788, EBI-16433464;
CC Q00013; O43761: SYNGR3; NbExp=3; IntAct=EBI-711788, EBI-11321949;
CC Q00013; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-711788, EBI-11528917;
CC Q00013; Q9UBK9: UXT; NbExp=3; IntAct=EBI-711788, EBI-357355;
CC Q00013; Q9UID6: ZNF639; NbExp=3; IntAct=EBI-711788, EBI-947476;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19144871};
CC Lipid-anchor {ECO:0000305|PubMed:1713685}. Cell projection,
CC stereocilium {ECO:0000250|UniProtKB:P70290}. Note=Colocalizes with WHRN
CC at stereocilium tip during hair cell development (By similarity).
CC Colocalizes with PALS1 in the retina, at the outer limiting membrane
CC (OLM) (By similarity). Colocalizes with WHRN in the retina, at the
CC outer limiting membrane (OLM), outer plexifirm layer (OPL), basal
CC bodies and at the connecting cilium (CC) (By similarity). Colocalizes
CC with NF2 in non-myelin-forming Schwann cells (PubMed:19144871).
CC {ECO:0000250|UniProtKB:P70290, ECO:0000269|PubMed:19144871}.
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 Name=3;
CC IsoId=Q00013-3; Sequence=VSP_044634;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17584769}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:1713685}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
CC -!- CAUTION: Thought to be palmitoylated by ZDHHC17 (PubMed:22496366). This
CC work was later retracted due to image manipulation (PubMed:29475958).
CC {ECO:0000269|PubMed:22496366, ECO:0000269|PubMed:29475958}.
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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 CCDS; CCDS14762.1; -. [Q00013-1]
DR CCDS; CCDS55544.1; -. [Q00013-2]
DR CCDS; CCDS55545.1; -. [Q00013-3]
DR PIR; A39599; A39599.
DR RefSeq; NP_001159932.1; NM_001166460.1.
DR RefSeq; NP_001159933.1; NM_001166461.1. [Q00013-3]
DR RefSeq; NP_001159934.1; NM_001166462.1. [Q00013-2]
DR RefSeq; NP_002427.1; NM_002436.3. [Q00013-1]
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 AlphaFoldDB; Q00013; -.
DR SMR; Q00013; -.
DR BioGRID; 110494; 101.
DR CORUM; Q00013; -.
DR ELM; Q00013; -.
DR IntAct; Q00013; 71.
DR MINT; Q00013; -.
DR STRING; 9606.ENSP00000358547; -.
DR iPTMnet; Q00013; -.
DR MetOSite; Q00013; -.
DR PhosphoSitePlus; Q00013; -.
DR SwissPalm; Q00013; -.
DR BioMuta; MPP1; -.
DR DMDM; 1346575; -.
DR EPD; Q00013; -.
DR jPOST; Q00013; -.
DR MassIVE; Q00013; -.
DR MaxQB; Q00013; -.
DR PaxDb; Q00013; -.
DR PeptideAtlas; Q00013; -.
DR PRIDE; Q00013; -.
DR ProteomicsDB; 33755; -.
DR ProteomicsDB; 57837; -. [Q00013-1]
DR ProteomicsDB; 57838; -. [Q00013-2]
DR Antibodypedia; 419; 349 antibodies from 33 providers.
DR DNASU; 4354; -.
DR Ensembl; ENST00000369534.8; ENSP00000358547.3; ENSG00000130830.15. [Q00013-1]
DR Ensembl; ENST00000393531.5; ENSP00000377165.1; ENSG00000130830.15. [Q00013-3]
DR Ensembl; ENST00000413259.7; ENSP00000400155.3; ENSG00000130830.15. [Q00013-2]
DR GeneID; 4354; -.
DR KEGG; hsa:4354; -.
DR MANE-Select; ENST00000369534.8; ENSP00000358547.3; NM_002436.4; NP_002427.1.
DR UCSC; uc004fmp.3; human. [Q00013-1]
DR CTD; 4354; -.
DR DisGeNET; 4354; -.
DR GeneCards; MPP1; -.
DR HGNC; HGNC:7219; MPP1.
DR HPA; ENSG00000130830; Tissue enhanced (bone).
DR MIM; 305360; gene.
DR neXtProt; NX_Q00013; -.
DR OpenTargets; ENSG00000130830; -.
DR PharmGKB; PA30924; -.
DR VEuPathDB; HostDB:ENSG00000130830; -.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000158744; -.
DR HOGENOM; CLU_001715_5_1_1; -.
DR InParanoid; Q00013; -.
DR OMA; QAPNAMT; -.
DR OrthoDB; 95102at2759; -.
DR PhylomeDB; Q00013; -.
DR TreeFam; TF314263; -.
DR PathwayCommons; Q00013; -.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q00013; -.
DR BioGRID-ORCS; 4354; 9 hits in 701 CRISPR screens.
DR ChiTaRS; MPP1; human.
DR EvolutionaryTrace; Q00013; -.
DR GeneWiki; MPP1; -.
DR GenomeRNAi; 4354; -.
DR Pharos; Q00013; Tbio.
DR PRO; PR:Q00013; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q00013; protein.
DR Bgee; ENSG00000130830; Expressed in monocyte and 203 other tissues.
DR ExpressionAtlas; Q00013; baseline and differential.
DR Genevisible; Q00013; HS.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd12080; SH3_MPP1; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR035475; MPP1_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00018; SH3_1; 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; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Direct protein sequencing; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..466
FT /note="55 kDa erythrocyte membrane protein"
FT /id="PRO_0000094565"
FT DOMAIN 71..152
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 158..228
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 282..451
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 268..466
FT /note="Interaction with PALS1"
FT /evidence="ECO:0000269|PubMed:17584769"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70290"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..34
FT /note="MTLKASEGESGGSMHTALSDLYLEHLLQKRSRPE -> MESW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042675"
FT VAR_SEQ 161..180
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044634"
FT VARIANT 448
FT /note="E -> Q (in dbSNP:rs14092)"
FT /id="VAR_011914"
FT CONFLICT 204
FT /note="Q -> R (in Ref. 5; AAV35469)"
FT /evidence="ECO:0000305"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2EJY"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2EJY"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2EV8"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:2EJY"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:3NEY"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 336..344
FT /evidence="ECO:0007829|PDB:3NEY"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:3NEY"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:3NEY"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3NEY"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:3NEY"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:3NEY"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 410..426
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:3NEY"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:3NEY"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:3NEY"
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
