Full text data of EHBP1L1
EHBP1L1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
EH domain-binding protein 1-like protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
EH domain-binding protein 1-like protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8N3D4
ID EH1L1_HUMAN Reviewed; 1523 AA.
AC Q8N3D4; Q8TB89; Q9H7M7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=EH domain-binding protein 1-like protein 1;
GN Name=EHBP1L1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-1523, AND VARIANTS
RP LEU-133 AND VAL-569.
RC TISSUE=Melanoma;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1523, AND VARIANTS
RP LEU-133; GLN-307; GLY-538 AND VAL-569.
RC TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1281-1523.
RC TISSUE=Muscle;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-1257, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-173; SER-191;
RP SER-285 AND SER-1168, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1273, 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 [10]
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).
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AP001362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834433; CAD39093.1; -; mRNA.
DR EMBL; AK024451; BAB15741.1; -; mRNA.
DR EMBL; BC024207; AAH24207.2; -; mRNA.
DR RefSeq; NP_001092879.1; NM_001099409.1.
DR UniGene; Hs.502867; -.
DR ProteinModelPortal; Q8N3D4; -.
DR SMR; Q8N3D4; 1029-1143.
DR IntAct; Q8N3D4; 3.
DR PhosphoSite; Q8N3D4; -.
DR DMDM; 146286137; -.
DR PaxDb; Q8N3D4; -.
DR PRIDE; Q8N3D4; -.
DR Ensembl; ENST00000309295; ENSP00000312671; ENSG00000173442.
DR GeneID; 254102; -.
DR KEGG; hsa:254102; -.
DR UCSC; uc001oeo.4; human.
DR CTD; 254102; -.
DR GeneCards; GC11P065343; -.
DR H-InvDB; HIX0009801; -.
DR HGNC; HGNC:30682; EHBP1L1.
DR HPA; HPA039479; -.
DR neXtProt; NX_Q8N3D4; -.
DR PharmGKB; PA134871712; -.
DR eggNOG; COG5069; -.
DR HOGENOM; HOG000112349; -.
DR HOVERGEN; HBG056787; -.
DR InParanoid; Q8N3D4; -.
DR OMA; LGTQKTE; -.
DR ChiTaRS; EHBP1L1; human.
DR GenomeRNAi; 254102; -.
DR NextBio; 92259; -.
DR PRO; PR:Q8N3D4; -.
DR ArrayExpress; Q8N3D4; -.
DR Bgee; Q8N3D4; -.
DR CleanEx; HS_EHBP1L1; -.
DR Genevestigator; Q8N3D4; -.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR022735; DUF3585.
DR InterPro; IPR019448; NT-C2.
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; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1523 EH domain-binding protein 1-like protein
FT 1.
FT /FTId=PRO_0000285204.
FT DOMAIN 1037 1139 CH.
FT COILED 1363 1515 Potential.
FT COMPBIAS 222 226 Poly-Glu.
FT COMPBIAS 561 890 Glu-rich.
FT COMPBIAS 1153 1158 Poly-Gly.
FT COMPBIAS 1247 1250 Poly-Gly.
FT COMPBIAS 1308 1311 Poly-Ala.
FT COMPBIAS 1316 1347 Pro-rich.
FT MOD_RES 170 170 Phosphoserine.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 191 191 Phosphoserine.
FT MOD_RES 285 285 Phosphoserine.
FT MOD_RES 310 310 Phosphoserine.
FT MOD_RES 1168 1168 Phosphoserine.
FT MOD_RES 1257 1257 Phosphoserine.
FT MOD_RES 1273 1273 Phosphoserine.
FT VARIANT 133 133 V -> L (in dbSNP:rs1194100).
FT /FTId=VAR_061645.
FT VARIANT 307 307 R -> Q (in dbSNP:rs3741380).
FT /FTId=VAR_031993.
FT VARIANT 538 538 V -> G (in dbSNP:rs6591182).
FT /FTId=VAR_031994.
FT VARIANT 569 569 D -> V (in dbSNP:rs1194099).
FT /FTId=VAR_031995.
FT VARIANT 599 599 T -> I (in dbSNP:rs7931052).
FT /FTId=VAR_031996.
FT VARIANT 648 648 T -> I (in dbSNP:rs7931269).
FT /FTId=VAR_031997.
FT CONFLICT 1235 1235 P -> L (in Ref. 2; CAD39093).
FT CONFLICT 1378 1378 D -> E (in Ref. 2; CAD39093).
SQ SEQUENCE 1523 AA; 161854 MW; 5F0DD06B15131597 CRC64;
MTSVWKRLQR VGKRAAKFQF VACYHELVLE CTKKWQPDKL VVVWTRRNRR ICSKAHSWQP
GIQNPYRGTV VWMVPENVDI SVTLYRDPHV DQYEAKEWTF IIENESKGQR KVLATAEVDL
ARHAGPVPVQ VPVRLRLKPK SVKVVQAELS LTLSGVLLRE GRATDDDMQS LASLMSVKPS
DVGNLDDFAE SDEDEAHGPG APEARARVPQ PDPSRELKTL CEEEEEGQGR PQQAVASPSN
AEDTSPAPVS APAPPARTSR GQGSERANEA GGQVGPEAPR PPETSPEMRS SRQPAQDTAP
TPAPRLRKGS DALRPPVPQG EDEVPKASGA PPAGLGSARE TQAQACPQEG TEAHGARLGP
SIEDKGSGDP FGRQRLKAEE MDTEDRPEAS GVDTEPRSGG REANTKRSGV RAGEAEESSA
VCQVDAEQRS KVRHVDTKGP EATGVMPEAR CRGTPEAPPR GSQGRLGVRT RDEAPSGLSL
PPAEPAGHSG QLGDLEGARA AAGQEREGAE VRGGAPGIEG TGLEQGPSVG AISTRPQVSS
WQGALLSTAQ GAISRGLGGW EAEAGGSGDL ETETEVVGLE VLGTQEKEVE GSGFPETRTL
EIEILGALEK EAARSRVLES EVAGTAQCEG LETQETEVGV IETPGTETEV LGTQKTEAGG
SGVLQTRTTI AETEVLVTQE ISGDLGPLKI EDTIQSEMLG TQETEVEASR VPESEAEGTE
AKILGTQEIT ARDSGVREIE AEIAESDILV AQEIEVGLLG VLGIETGAAE GAILGTQEIA
SRDSGVPGLE ADTTGIQVKE VGGSEVPEIA TGTAETEILG TQEIASRSSG VPGLESEVAG
AQETEVGGSG ISGPEAGMAE ARVLMTRKTE IIVPEAEKEE AQTSGVQEAE TRVGSALKYE
ALRAPVTQPR VLGSQEAKAE ISGVQGSETQ VLRVQEAEAG VWGMSEGKSG AWGAQEAEMK
VLESPENKSG TFKAQEAEAG VLGNEKGKEA EGSLTEASLP EAQVASGAGA GAPRASSPEK
AEEDRRLPGS QAPPALVSSS QSLLEWCQEV TTGYRGVRIT NFTTSWRNGL AFCAILHRFY
PDKIDYASLD PLNIKQNNKQ AFDGFAALGV SRLLEPADMV LLSVPDKLIV MTYLCQIRAF
CTGQELQLVQ LEGGGGAGTY RVGSAQPSPP DDLDAGGLAQ RLRGHGAEGP QEPKEAADRA
DGAAPGVASR NAVAGRASKD GGAEAPRESR PAEVPAEGLV NGAGAPGGGG VRLRRPSVNG
EPGSVPPPRA HGSFSHVRDA DLLKKRRSRL RNSSSFSMDD PDAGAMGAAA AEGQAPDPSP
APGPPTAADS QQPPGGSSPS EEPPPSPGEE AGLQRFQDTS QYVCAELQAL EQEQRQIDGR
AAEVEMQLRS LMESGANKLQ EEVLIQEWFT LVNKKNALIR RQDQLQLLME EQDLERRFEL
LSRELRAMLA IEDWQKTSAQ QHREQLLLEE LVSLVNQRDE LVRDLDHKER IALEEDERLE
RGLEQRRRKL SRQLSRRERC VLS
//
ID EH1L1_HUMAN Reviewed; 1523 AA.
AC Q8N3D4; Q8TB89; Q9H7M7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=EH domain-binding protein 1-like protein 1;
GN Name=EHBP1L1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-1523, AND VARIANTS
RP LEU-133 AND VAL-569.
RC TISSUE=Melanoma;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1523, AND VARIANTS
RP LEU-133; GLN-307; GLY-538 AND VAL-569.
RC TISSUE=Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1281-1523.
RC TISSUE=Muscle;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-1257, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY 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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-173; SER-191;
RP SER-285 AND SER-1168, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1273, 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 [10]
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).
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AP001362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834433; CAD39093.1; -; mRNA.
DR EMBL; AK024451; BAB15741.1; -; mRNA.
DR EMBL; BC024207; AAH24207.2; -; mRNA.
DR RefSeq; NP_001092879.1; NM_001099409.1.
DR UniGene; Hs.502867; -.
DR ProteinModelPortal; Q8N3D4; -.
DR SMR; Q8N3D4; 1029-1143.
DR IntAct; Q8N3D4; 3.
DR PhosphoSite; Q8N3D4; -.
DR DMDM; 146286137; -.
DR PaxDb; Q8N3D4; -.
DR PRIDE; Q8N3D4; -.
DR Ensembl; ENST00000309295; ENSP00000312671; ENSG00000173442.
DR GeneID; 254102; -.
DR KEGG; hsa:254102; -.
DR UCSC; uc001oeo.4; human.
DR CTD; 254102; -.
DR GeneCards; GC11P065343; -.
DR H-InvDB; HIX0009801; -.
DR HGNC; HGNC:30682; EHBP1L1.
DR HPA; HPA039479; -.
DR neXtProt; NX_Q8N3D4; -.
DR PharmGKB; PA134871712; -.
DR eggNOG; COG5069; -.
DR HOGENOM; HOG000112349; -.
DR HOVERGEN; HBG056787; -.
DR InParanoid; Q8N3D4; -.
DR OMA; LGTQKTE; -.
DR ChiTaRS; EHBP1L1; human.
DR GenomeRNAi; 254102; -.
DR NextBio; 92259; -.
DR PRO; PR:Q8N3D4; -.
DR ArrayExpress; Q8N3D4; -.
DR Bgee; Q8N3D4; -.
DR CleanEx; HS_EHBP1L1; -.
DR Genevestigator; Q8N3D4; -.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR022735; DUF3585.
DR InterPro; IPR019448; NT-C2.
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; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1523 EH domain-binding protein 1-like protein
FT 1.
FT /FTId=PRO_0000285204.
FT DOMAIN 1037 1139 CH.
FT COILED 1363 1515 Potential.
FT COMPBIAS 222 226 Poly-Glu.
FT COMPBIAS 561 890 Glu-rich.
FT COMPBIAS 1153 1158 Poly-Gly.
FT COMPBIAS 1247 1250 Poly-Gly.
FT COMPBIAS 1308 1311 Poly-Ala.
FT COMPBIAS 1316 1347 Pro-rich.
FT MOD_RES 170 170 Phosphoserine.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 191 191 Phosphoserine.
FT MOD_RES 285 285 Phosphoserine.
FT MOD_RES 310 310 Phosphoserine.
FT MOD_RES 1168 1168 Phosphoserine.
FT MOD_RES 1257 1257 Phosphoserine.
FT MOD_RES 1273 1273 Phosphoserine.
FT VARIANT 133 133 V -> L (in dbSNP:rs1194100).
FT /FTId=VAR_061645.
FT VARIANT 307 307 R -> Q (in dbSNP:rs3741380).
FT /FTId=VAR_031993.
FT VARIANT 538 538 V -> G (in dbSNP:rs6591182).
FT /FTId=VAR_031994.
FT VARIANT 569 569 D -> V (in dbSNP:rs1194099).
FT /FTId=VAR_031995.
FT VARIANT 599 599 T -> I (in dbSNP:rs7931052).
FT /FTId=VAR_031996.
FT VARIANT 648 648 T -> I (in dbSNP:rs7931269).
FT /FTId=VAR_031997.
FT CONFLICT 1235 1235 P -> L (in Ref. 2; CAD39093).
FT CONFLICT 1378 1378 D -> E (in Ref. 2; CAD39093).
SQ SEQUENCE 1523 AA; 161854 MW; 5F0DD06B15131597 CRC64;
MTSVWKRLQR VGKRAAKFQF VACYHELVLE CTKKWQPDKL VVVWTRRNRR ICSKAHSWQP
GIQNPYRGTV VWMVPENVDI SVTLYRDPHV DQYEAKEWTF IIENESKGQR KVLATAEVDL
ARHAGPVPVQ VPVRLRLKPK SVKVVQAELS LTLSGVLLRE GRATDDDMQS LASLMSVKPS
DVGNLDDFAE SDEDEAHGPG APEARARVPQ PDPSRELKTL CEEEEEGQGR PQQAVASPSN
AEDTSPAPVS APAPPARTSR GQGSERANEA GGQVGPEAPR PPETSPEMRS SRQPAQDTAP
TPAPRLRKGS DALRPPVPQG EDEVPKASGA PPAGLGSARE TQAQACPQEG TEAHGARLGP
SIEDKGSGDP FGRQRLKAEE MDTEDRPEAS GVDTEPRSGG REANTKRSGV RAGEAEESSA
VCQVDAEQRS KVRHVDTKGP EATGVMPEAR CRGTPEAPPR GSQGRLGVRT RDEAPSGLSL
PPAEPAGHSG QLGDLEGARA AAGQEREGAE VRGGAPGIEG TGLEQGPSVG AISTRPQVSS
WQGALLSTAQ GAISRGLGGW EAEAGGSGDL ETETEVVGLE VLGTQEKEVE GSGFPETRTL
EIEILGALEK EAARSRVLES EVAGTAQCEG LETQETEVGV IETPGTETEV LGTQKTEAGG
SGVLQTRTTI AETEVLVTQE ISGDLGPLKI EDTIQSEMLG TQETEVEASR VPESEAEGTE
AKILGTQEIT ARDSGVREIE AEIAESDILV AQEIEVGLLG VLGIETGAAE GAILGTQEIA
SRDSGVPGLE ADTTGIQVKE VGGSEVPEIA TGTAETEILG TQEIASRSSG VPGLESEVAG
AQETEVGGSG ISGPEAGMAE ARVLMTRKTE IIVPEAEKEE AQTSGVQEAE TRVGSALKYE
ALRAPVTQPR VLGSQEAKAE ISGVQGSETQ VLRVQEAEAG VWGMSEGKSG AWGAQEAEMK
VLESPENKSG TFKAQEAEAG VLGNEKGKEA EGSLTEASLP EAQVASGAGA GAPRASSPEK
AEEDRRLPGS QAPPALVSSS QSLLEWCQEV TTGYRGVRIT NFTTSWRNGL AFCAILHRFY
PDKIDYASLD PLNIKQNNKQ AFDGFAALGV SRLLEPADMV LLSVPDKLIV MTYLCQIRAF
CTGQELQLVQ LEGGGGAGTY RVGSAQPSPP DDLDAGGLAQ RLRGHGAEGP QEPKEAADRA
DGAAPGVASR NAVAGRASKD GGAEAPRESR PAEVPAEGLV NGAGAPGGGG VRLRRPSVNG
EPGSVPPPRA HGSFSHVRDA DLLKKRRSRL RNSSSFSMDD PDAGAMGAAA AEGQAPDPSP
APGPPTAADS QQPPGGSSPS EEPPPSPGEE AGLQRFQDTS QYVCAELQAL EQEQRQIDGR
AAEVEMQLRS LMESGANKLQ EEVLIQEWFT LVNKKNALIR RQDQLQLLME EQDLERRFEL
LSRELRAMLA IEDWQKTSAQ QHREQLLLEE LVSLVNQRDE LVRDLDHKER IALEEDERLE
RGLEQRRRKL SRQLSRRERC VLS
//