EHBP1_HUMAN
ID EHBP1_HUMAN Reviewed; 1231 AA.
AC Q8NDI1; O94977; Q53TG7; Q53TV6; Q580X2; Q6NX72; Q6PIT3; Q6QNV2; Q9NWI9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=EH domain-binding protein 1;
GN Name=EHBP1; Synonyms=KIAA0903, NACSIN;
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 2), FUNCTION, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INTERACTION WITH EHD2.
RX PubMed=14676205; DOI=10.1074/jbc.m307702200;
RA Guilherme A., Soriano N.A., Bose S., Holik J., Bose A., Pomerleau D.P.,
RA Furcinitti P., Leszyk J., Corvera S., Czech M.P.;
RT "EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to
RT the actin cytoskeleton.";
RL J. Biol. Chem. 279:10593-10605(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Castellano-Munoz M., Fernandez-Chacon R.;
RT "Functional analysis of NACSIN (KIAA0903) in membrane trafficking.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-341 (ISOFORM 2).
RC TISSUE=Adipose tissue;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1231.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174; SER-177;
RP SER-432; SER-436; SER-710; SER-964 AND SER-1058, AND IDENTIFICATION BY MASS
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174; SER-432 AND
RP SER-436, AND 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174 AND SER-436, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-1058, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-302; SER-307;
RP SER-408; SER-428; SER-436; THR-694; SER-781 AND SER-1058, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-432; SER-436;
RP SER-854 AND SER-1058, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INTERACTION WITH RAB8A; RAB10; RAB13 AND RAB15, DOMAIN, FUNCTION,
RP ISOPRENYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=27552051; DOI=10.7554/elife.18675;
RA Rai A., Oprisko A., Campos J., Fu Y., Friese T., Itzen A., Goody R.S.,
RA Gazdag E.M., Muller M.P.;
RT "bMERB domains are bivalent Rab8 family effectors evolved by gene
RT duplication.";
RL Elife 5:E18675-E18675(2016).
RN [18]
RP STRUCTURE BY NMR OF 443-548.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain from human EH domain binding protein
RT 1.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [19]
RP VARIANT [LARGE SCALE ANALYSIS] THR-395.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [20]
RP INVOLVEMENT IN SUSCEPTIBILITY TO HEREDITARY PROSTATE CANCER.
RX PubMed=18264098; DOI=10.1038/ng.89;
RA Gudmundsson J., Sulem P., Rafnar T., Bergthorsson J.T., Manolescu A.,
RA Gudbjartsson D., Agnarsson B.A., Sigurdsson A., Benediktsdottir K.R.,
RA Blondal T., Jakobsdottir M., Stacey S.N., Kostic J., Kristinsson K.T.,
RA Birgisdottir B., Ghosh S., Magnusdottir D.N., Thorlacius S.,
RA Thorleifsson G., Zheng S.L., Sun J., Chang B.-L., Elmore J.B., Breyer J.P.,
RA McReynolds K.M., Bradley K.M., Yaspan B.L., Wiklund F., Stattin P.,
RA Lindstroem S., Adami H.-O., McDonnell S.K., Schaid D.J., Cunningham J.M.,
RA Wang L., Cerhan J.R., St Sauver J.L., Isaacs S.D., Wiley K.E., Partin A.W.,
RA Walsh P.C., Polo S., Ruiz-Echarri M., Navarrete S., Fuertes F., Saez B.,
RA Godino J., Weijerman P.C., Swinkels D.W., Aben K.K., Witjes J.A.,
RA Suarez B.K., Helfand B.T., Frigge M.L., Kristjansson K., Ober C.,
RA Jonsson E., Einarsson G.V., Xu J., Gronberg H., Smith J.R., Thibodeau S.N.,
RA Isaacs W.B., Catalona W.J., Mayordomo J.I., Kiemeney L.A.,
RA Barkardottir R.B., Gulcher J.R., Thorsteinsdottir U., Kong A.,
RA Stefansson K.;
RT "Common sequence variants on 2p15 and Xp11.22 confer susceptibility to
RT prostate cancer.";
RL Nat. Genet. 40:281-283(2008).
CC -!- FUNCTION: May play a role in actin reorganization. Links clathrin-
CC mediated endocytosis to the actin cytoskeleton. May act as Rab effector
CC protein and play a role in vesicle trafficking (PubMed:14676205,
CC PubMed:27552051). Required for perinuclear sorting and insulin-
CC regulated recycling of SLC2A4/GLUT4 in adipocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q69ZW3, ECO:0000269|PubMed:14676205,
CC ECO:0000305|PubMed:27552051}.
CC -!- SUBUNIT: Interacts with EHD1 (By similarity). Interacts with EHD2.
CC Interacts with RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound
CC forms); at least in case of RAB8A may bind 2 molecules of RAB8A
CC simultaneously through a high and a low affinity binding site,
CC respectively. {ECO:0000250|UniProtKB:Q69ZW3,
CC ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:27552051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14676205}. Membrane
CC {ECO:0000269|PubMed:14676205}. Endosome {ECO:0000305|PubMed:27552051}.
CC Note=Mostly found in cytosol and plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NDI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDI1-2; Sequence=VSP_024834;
CC Name=3;
CC IsoId=Q8NDI1-3; Sequence=VSP_024834, VSP_024835;
CC -!- DOMAIN: The CAAX motif is a signal for prenylation and required for
CC endosomal colocalization with Rab8 and Rab10.
CC {ECO:0000269|PubMed:27552051}.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to Rab8, Rab10, Rab10, Rab13 and Rab15 (in their GTP-bound
CC forms). {ECO:0000269|PubMed:27552051}.
CC -!- PTM: Prenylated (Probable). Farnelysation (predominant) and
CC geranylgeranylation has been observed in vitro.
CC {ECO:0000269|PubMed:27552051}.
CC -!- DISEASE: Prostate cancer, hereditary, 12 (HPC12) [MIM:611868]: A
CC condition associated with familial predisposition to cancer of the
CC prostate. Most prostate cancers are adenocarcinomas that develop in the
CC acini of the prostatic ducts. Other rare histopathologic types of
CC prostate cancer that occur in approximately 5% of patients include
CC small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma,
CC transitional cell carcinoma, squamous cell carcinoma, basal cell
CC carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell
CC carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:18264098}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91391.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY531390; AAS48537.1; -; mRNA.
DR EMBL; AY331186; AAQ97141.1; -; mRNA.
DR EMBL; AL833968; CAD38814.1; -; mRNA.
DR EMBL; AC007098; AAY14789.1; -; Genomic_DNA.
DR EMBL; AC009501; AAY24356.1; -; Genomic_DNA.
DR EMBL; AC092567; AAX82024.1; -; Genomic_DNA.
DR EMBL; BC029477; AAH29477.1; -; mRNA.
DR EMBL; BC067215; AAH67215.1; -; mRNA.
DR EMBL; AK000828; BAA91391.1; ALT_SEQ; mRNA.
DR EMBL; AB020710; BAA74926.1; -; mRNA.
DR CCDS; CCDS1872.1; -. [Q8NDI1-1]
DR CCDS; CCDS46299.1; -. [Q8NDI1-2]
DR CCDS; CCDS46300.1; -. [Q8NDI1-3]
DR RefSeq; NP_001136086.1; NM_001142614.1. [Q8NDI1-2]
DR RefSeq; NP_001136087.1; NM_001142615.2. [Q8NDI1-3]
DR RefSeq; NP_001136088.1; NM_001142616.1. [Q8NDI1-3]
DR RefSeq; NP_056067.2; NM_015252.3. [Q8NDI1-1]
DR RefSeq; XP_005264282.1; XM_005264225.2.
DR RefSeq; XP_005264283.1; XM_005264226.2. [Q8NDI1-1]
DR RefSeq; XP_005264284.1; XM_005264227.1. [Q8NDI1-2]
DR RefSeq; XP_011531015.1; XM_011532713.2.
DR RefSeq; XP_011531016.1; XM_011532714.2.
DR RefSeq; XP_011531017.1; XM_011532715.2. [Q8NDI1-1]
DR RefSeq; XP_016859132.1; XM_017003643.1.
DR RefSeq; XP_016859133.1; XM_017003644.1.
DR RefSeq; XP_016859136.1; XM_017003647.1.
DR RefSeq; XP_016859137.1; XM_017003648.1.
DR RefSeq; XP_016859138.1; XM_017003649.1.
DR RefSeq; XP_016859140.1; XM_017003651.1.
DR PDB; 2D89; NMR; -; A=443-548.
DR PDB; 6ZSH; X-ray; 2.20 A; A/C=1060-1162, B/D=440-550.
DR PDB; 6ZSI; X-ray; 1.91 A; C/D=1060-1212.
DR PDB; 6ZSJ; X-ray; 2.00 A; C/D=1060-1212.
DR PDBsum; 2D89; -.
DR PDBsum; 6ZSH; -.
DR PDBsum; 6ZSI; -.
DR PDBsum; 6ZSJ; -.
DR AlphaFoldDB; Q8NDI1; -.
DR BMRB; Q8NDI1; -.
DR SMR; Q8NDI1; -.
DR BioGRID; 116893; 105.
DR CORUM; Q8NDI1; -.
DR ELM; Q8NDI1; -.
DR IntAct; Q8NDI1; 28.
DR MINT; Q8NDI1; -.
DR STRING; 9606.ENSP00000263991; -.
DR iPTMnet; Q8NDI1; -.
DR MetOSite; Q8NDI1; -.
DR PhosphoSitePlus; Q8NDI1; -.
DR BioMuta; EHBP1; -.
DR DMDM; 223590228; -.
DR EPD; Q8NDI1; -.
DR jPOST; Q8NDI1; -.
DR MassIVE; Q8NDI1; -.
DR MaxQB; Q8NDI1; -.
DR PaxDb; Q8NDI1; -.
DR PeptideAtlas; Q8NDI1; -.
DR PRIDE; Q8NDI1; -.
DR ProteomicsDB; 73032; -. [Q8NDI1-1]
DR ProteomicsDB; 73033; -. [Q8NDI1-2]
DR ProteomicsDB; 73034; -. [Q8NDI1-3]
DR Antibodypedia; 30724; 88 antibodies from 23 providers.
DR DNASU; 23301; -.
DR Ensembl; ENST00000263991.9; ENSP00000263991.5; ENSG00000115504.15. [Q8NDI1-1]
DR Ensembl; ENST00000405015.7; ENSP00000384143.3; ENSG00000115504.15. [Q8NDI1-3]
DR Ensembl; ENST00000405289.5; ENSP00000385524.1; ENSG00000115504.15. [Q8NDI1-2]
DR Ensembl; ENST00000431489.6; ENSP00000403783.1; ENSG00000115504.15. [Q8NDI1-3]
DR GeneID; 23301; -.
DR KEGG; hsa:23301; -.
DR MANE-Select; ENST00000431489.6; ENSP00000403783.1; NM_001142616.3; NP_001136088.1. [Q8NDI1-3]
DR UCSC; uc002sby.4; human. [Q8NDI1-1]
DR CTD; 23301; -.
DR DisGeNET; 23301; -.
DR GeneCards; EHBP1; -.
DR HGNC; HGNC:29144; EHBP1.
DR HPA; ENSG00000115504; Low tissue specificity.
DR MalaCards; EHBP1; -.
DR MIM; 609922; gene.
DR MIM; 611868; phenotype.
DR neXtProt; NX_Q8NDI1; -.
DR OpenTargets; ENSG00000115504; -.
DR PharmGKB; PA128394620; -.
DR VEuPathDB; HostDB:ENSG00000115504; -.
DR eggNOG; KOG0035; Eukaryota.
DR GeneTree; ENSGT00940000157597; -.
DR HOGENOM; CLU_004178_1_1_1; -.
DR InParanoid; Q8NDI1; -.
DR OMA; ILMTRRQ; -.
DR OrthoDB; 165311at2759; -.
DR PhylomeDB; Q8NDI1; -.
DR TreeFam; TF105382; -.
DR PathwayCommons; Q8NDI1; -.
DR SignaLink; Q8NDI1; -.
DR BioGRID-ORCS; 23301; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; EHBP1; human.
DR EvolutionaryTrace; Q8NDI1; -.
DR GenomeRNAi; 23301; -.
DR Pharos; Q8NDI1; Tbio.
DR PRO; PR:Q8NDI1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NDI1; protein.
DR Bgee; ENSG00000115504; Expressed in sural nerve and 207 other tissues.
DR ExpressionAtlas; Q8NDI1; baseline and differential.
DR Genevisible; Q8NDI1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR029944; EHBP1.
DR InterPro; IPR019448; NT-C2.
DR PANTHER; PTHR23167:SF43; PTHR23167:SF43; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF10358; NT-C2; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS51840; C2_NT; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Endocytosis;
KW Endosome; Lipoprotein; Membrane; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1231
FT /note="EH domain-binding protein 1"
FT /id="PRO_0000285202"
FT DOMAIN 8..158
FT /note="C2 NT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01186"
FT DOMAIN 443..548
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1056..1212
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 264..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..210
FT /evidence="ECO:0000255"
FT COILED 808..879
FT /evidence="ECO:0000255"
FT COILED 1076..1100
FT /evidence="ECO:0000255"
FT COILED 1136..1230
FT /evidence="ECO:0000255"
FT MOTIF 1228..1231
FT /note="CAAX motif"
FT /evidence="ECO:0000305|PubMed:27552051"
FT COMPBIAS 296..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZW3"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZW3"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZW3"
FT MOD_RES 694
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 212..246
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14676205,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_024834"
FT VAR_SEQ 905..940
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024835"
FT VARIANT 395
FT /note="R -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035913"
FT VARIANT 755
FT /note="K -> Q (in dbSNP:rs17432615)"
FT /id="VAR_031992"
FT CONFLICT 105
FT /note="E -> V (in Ref. 5; AAH29477)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="K -> R (in Ref. 2; AAQ97141 and 3; CAD38814)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="E -> G (in Ref. 2; AAQ97141 and 3; CAD38814)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="D -> V (in Ref. 2; AAQ97141 and 3; CAD38814)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> G (in Ref. 2; AAQ97141 and 3; CAD38814)"
FT /evidence="ECO:0000305"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:6ZSH"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6ZSH"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 476..485
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:2D89"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 522..528
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 533..547
FT /evidence="ECO:0007829|PDB:6ZSH"
FT HELIX 1076..1101
FT /evidence="ECO:0007829|PDB:6ZSI"
FT HELIX 1110..1160
FT /evidence="ECO:0007829|PDB:6ZSI"
FT HELIX 1164..1166
FT /evidence="ECO:0007829|PDB:6ZSI"
FT HELIX 1169..1198
FT /evidence="ECO:0007829|PDB:6ZSI"
FT TURN 1199..1201
FT /evidence="ECO:0007829|PDB:6ZSI"
SQ SEQUENCE 1231 AA; 140017 MW; FFF39B65BCC0FC0A CRC64;
MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP
GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN
MKQYASPMPT QTDVKLKFKP LSKKVVSAAL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ
ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TEIVNQLNAL SSLDEDQDDC IKQANMRSAK
SASSSEELIN KLNFLDEAEK DLATVNSNPF DDPDAAELNP FGDPDSEEPI TETASPRKTE
DSFYNNSYNP FKEVQTPQYL NPFDEPEAFV TIKDSPPQST KRKNIRPVDM SKYLYADSSK
TEEEELDESN PFYEPKSTPP PNNLVNPVQE LETERRVKRK APAPPVLSPK TGVLNENTVS
AGKDLSTSPK PSPIPSPVLG RKPNASQSLL VWCKEVTKNY RGVKITNFTT SWRNGLSFCA
ILHHFRPDLI DYKSLNPQDI KENNKKAYDG FASIGISRLL EPSDMVLLAI PDKLTVMTYL
YQIRAHFSGQ ELNVVQIEEN SSKSTYKVGN YETDTNSSVD QEKFYAELSD LKREPELQQP
ISGAVDFLSQ DDSVFVNDSG VGESESEHQT PDDHLSPSTA SPYCRRTKSD TEPQKSQQSS
GRTSGSDDPG ICSNTDSTQA QVLLGKKRLL KAETLELSDL YVSDKKKDMS PPFICEETDE
QKLQTLDIGS NLEKEKLENS RSLECRSDPE SPIKKTSLSP TSKLGYSYSR DLDLAKKKHA
SLRQTESDPD ADRTTLNHAD HSSKIVQHRL LSRQEELKER ARVLLEQARR DAALKAGNKH
NTNTATPFCN RQLSDQQDEE RRRQLRERAR QLIAEARSGV KMSELPSYGE MAAEKLKERS
KASGDENDNI EIDTNEEIPE GFVVGGGDEL TNLENDLDTP EQNSKLVDLK LKKLLEVQPQ
VANSPSSAAQ KAVTESSEQD MKSGTEDLRT ERLQKTTERF RNPVVFSKDS TVRKTQLQSF
SQYIENRPEM KRQRSIQEDT KKGNEEKAAI TETQRKPSED EVLNKGFKDT SQYVVGELAA
LENEQKQIDT RAALVEKRLR YLMDTGRNTE EEEAMMQEWF MLVNKKNALI RRMNQLSLLE
KEHDLERRYE LLNRELRAML AIEDWQKTEA QKRREQLLLD ELVALVNKRD ALVRDLDAQE
KQAEEEDEHL ERTLEQNKGK MAKKEEKCVL Q
