Full text data of DBNL
DBNL
(CMAP, SH3P7)
[Confidence: low (only semi-automatic identification from reviews)]
Drebrin-like protein (Cervical SH3P7; Cervical mucin-associated protein; Drebrin-F; HPK1-interacting protein of 55 kDa; HIP-55; SH3 domain-containing protein 7)
Drebrin-like protein (Cervical SH3P7; Cervical mucin-associated protein; Drebrin-F; HPK1-interacting protein of 55 kDa; HIP-55; SH3 domain-containing protein 7)
UniProt
Q9UJU6
ID DBNL_HUMAN Reviewed; 430 AA.
AC Q9UJU6; A4D2I9; P84070; Q6IAI8; Q96F30; Q96K74; Q9HBN8; Q9NR72;
read moreDT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Cervical SH3P7;
DE AltName: Full=Cervical mucin-associated protein;
DE AltName: Full=Drebrin-F;
DE AltName: Full=HPK1-interacting protein of 55 kDa;
DE Short=HIP-55;
DE AltName: Full=SH3 domain-containing protein 7;
GN Name=DBNL; Synonyms=CMAP, SH3P7; ORFNames=PP5423;
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), AND INTERACTION WITH MAP4K1.
RX PubMed=10567356; DOI=10.1074/jbc.274.48.33945;
RA Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.;
RT "A novel src homology 3 domain-containing adaptor protein, HIP-55,
RT that interacts with hematopoietic progenitor kinase 1.";
RL J. Biol. Chem. 274:33945-33950(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang W., Yuan Z., Wan T., He L., Cao X.;
RT "Molecular cloning of cDNA encoding drebrin F.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RA Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L.,
RA Spurr-Michaud S., Keutmann H.T., Hill J.A., Gipson I.K.;
RT "Expression cloning of a novel cervical mucin-associated protein
RT (CMAP).";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 [10]
RP IDENTIFICATION.
RX PubMed=9891087;
RA Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J.,
RA Wienands J.;
RT "SH3P7 is a cytoskeleton adapter protein and is coupled to signal
RT transduction from lymphocyte antigen receptors.";
RL Mol. Cell. Biol. 19:1539-1546(1999).
RN [11]
RP DEGRADATION BY CASPASES.
RX PubMed=11689006; DOI=10.1006/bbrc.2001.5862;
RA Chen Y.-R., Kori R., John B., Tan T.-H.;
RT "Caspase-mediated cleavage of actin-binding and SH3-domain-containing
RT proteins cortactin, HS1, and HIP-55 during apoptosis.";
RL Biochem. Biophys. Res. Commun. 288:981-989(2001).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP FUNCTION.
RX PubMed=14729663; DOI=10.1074/jbc.M312659200;
RA Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O.,
RA Deckert M.;
RT "Recruitment of the actin-binding protein HIP-55 to the immunological
RT synapse regulates T cell receptor signaling and endocytosis.";
RL J. Biol. Chem. 279:15550-15560(2004).
RN [14]
RP INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF
RP ASP-361.
RX PubMed=15637062; DOI=10.1074/jbc.M413564200;
RA Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.;
RT "PRAM-1 potentiates arsenic trioxide-induced JNK activation.";
RL J. Biol. Chem. 280:9043-9048(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, AND
RP 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 [20]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, AND
RP MASS SPECTROMETRY.
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, AND
RP MASS 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP STRUCTURE BY NMR OF 1-133.
RX PubMed=19768801; DOI=10.1002/pro.248;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M.,
RA Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.;
RT "NMR solution structures of actin depolymerizing factor homology
RT domains.";
RL Protein Sci. 18:2384-2392(2009).
CC -!- FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby
CC plays a role in receptor-mediated endocytosis. Plays a role in the
CC reorganization of the actin cytoskeleton, formation of cell
CC projections, such as neurites, in neuron morphogenesis and synapse
CC formation via its interaction with WASL and COBL. Does not bind G-
CC actin and promote actin polymerization by itself. Required for the
CC formation of organized podosome rosettes (By similarity). May act
CC as a common effector of antigen receptor-signaling pathways in
CC leukocytes. Acts as a key component of the immunological synapse
CC that regulates T-cell activation by bridging TCRs and the actin
CC cytoskeleton to gene activation and endocytic processes.
CC -!- SUBUNIT: Interacts with SHANK2, SHANK3 and SYN1. Interacts with
CC FGD1 and DNM1. Interacts with ANKRD54. Interacts with COBL.
CC Interacts with WASL and WIPF1 (By similarity). Interacts with
CC MAP4K1 and PRAM1.
CC -!- INTERACTION:
CC Q9H788:SH2D4A; NbExp=3; IntAct=EBI-751783, EBI-747035;
CC P78314:SH3BP2; NbExp=7; IntAct=EBI-751783, EBI-727062;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC lamellipodium. Cell projection, ruffle (By similarity). Cytoplasm,
CC cell cortex (By similarity). Cytoplasm, cytosol (By similarity).
CC Cell junction, synapse (By similarity). Cell projection (By
CC similarity). Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side (By similarity). Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic
CC side (By similarity). Golgi apparatus membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Cell
CC projection, podosome (By similarity). Note=Detected in neuron cell
CC body and cell projections, such as neurites. Colocalizes with
CC cytosolic dynamin in hippocampus neurons (By similarity). Cortical
CC actin cytoskeleton. Associates with lamellipodial actin and
CC membrane ruffles. Colocalizes with actin and cortactin at podosome
CC dots and podosome rosettes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJU6-2; Sequence=VSP_011398;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 232;
CC Name=3;
CC IsoId=Q9UJU6-3; Sequence=VSP_011398, VSP_011399;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 232;
CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3
CC and PRAM1.
CC -!- PTM: Degraded by caspases during apoptosis.
CC -!- SIMILARITY: Belongs to the ABP1 family.
CC -!- SIMILARITY: Contains 1 ADF-H domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; AF197060; AAF13701.1; -; mRNA.
DR EMBL; AF077353; AAF80228.1; -; mRNA.
DR EMBL; AF250287; AAF81273.1; -; mRNA.
DR EMBL; AF151364; AAG13120.1; -; mRNA.
DR EMBL; AF218020; AAG17262.2; -; mRNA.
DR EMBL; AK027367; BAB55065.1; -; mRNA.
DR EMBL; CR457167; CAG33448.1; -; mRNA.
DR EMBL; CH236960; EAL23770.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61132.1; -; Genomic_DNA.
DR EMBL; BC011677; AAH11677.1; -; mRNA.
DR EMBL; BC031687; AAH31687.1; -; mRNA.
DR RefSeq; NP_001014436.1; NM_001014436.2.
DR RefSeq; NP_001116428.1; NM_001122956.1.
DR RefSeq; NP_001271242.1; NM_001284313.1.
DR RefSeq; NP_001271244.1; NM_001284315.1.
DR RefSeq; NP_054782.2; NM_014063.6.
DR UniGene; Hs.436500; -.
DR PDB; 1X67; NMR; -; A=1-133.
DR PDBsum; 1X67; -.
DR ProteinModelPortal; Q9UJU6; -.
DR SMR; Q9UJU6; 1-133, 373-428.
DR IntAct; Q9UJU6; 4.
DR MINT; MINT-1474845; -.
DR STRING; 9606.ENSP00000407950; -.
DR PhosphoSite; Q9UJU6; -.
DR DMDM; 51316115; -.
DR OGP; Q9UJU6; -.
DR PaxDb; Q9UJU6; -.
DR PRIDE; Q9UJU6; -.
DR DNASU; 28988; -.
DR Ensembl; ENST00000448521; ENSP00000411701; ENSG00000136279.
DR Ensembl; ENST00000468694; ENSP00000417653; ENSG00000136279.
DR Ensembl; ENST00000494774; ENSP00000419992; ENSG00000136279.
DR GeneID; 28988; -.
DR KEGG; hsa:28988; -.
DR UCSC; uc003tjp.4; human.
DR CTD; 28988; -.
DR GeneCards; GC07P044084; -.
DR HGNC; HGNC:2696; DBNL.
DR HPA; HPA020265; -.
DR HPA; HPA027735; -.
DR MIM; 610106; gene.
DR neXtProt; NX_Q9UJU6; -.
DR PharmGKB; PA27164; -.
DR eggNOG; NOG265859; -.
DR HOVERGEN; HBG051316; -.
DR OMA; FQDTGPQ; -.
DR OrthoDB; EOG7X3QR9; -.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; Q9UJU6; -.
DR ChiTaRS; DBNL; human.
DR EvolutionaryTrace; Q9UJU6; -.
DR GeneWiki; Drebrin-like; -.
DR GenomeRNAi; 28988; -.
DR NextBio; 51899; -.
DR PMAP-CutDB; Q9UJU6; -.
DR PRO; PR:Q9UJU6; -.
DR ArrayExpress; Q9UJU6; -.
DR Bgee; Q9UJU6; -.
DR CleanEx; HS_DBNL; -.
DR Genevestigator; Q9UJU6; -.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Adaptive immunity;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endocytosis; Golgi apparatus; Immunity; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Synapse; Transport.
FT CHAIN 1 430 Drebrin-like protein.
FT /FTId=PRO_0000079793.
FT DOMAIN 4 133 ADF-H.
FT DOMAIN 371 430 SH3.
FT COILED 176 231 Potential.
FT SITE 361 362 Cleavage; by caspase-3.
FT MOD_RES 176 176 N6-acetyllysine.
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 269 269 Phosphoserine.
FT MOD_RES 283 283 Phosphoserine.
FT MOD_RES 288 288 N6-acetyllysine.
FT MOD_RES 334 334 Phosphotyrosine (By similarity).
FT MOD_RES 344 344 Phosphotyrosine (By similarity).
FT VAR_SEQ 234 234 Q -> QS (in isoform 2 and isoform 3).
FT /FTId=VSP_011398.
FT VAR_SEQ 251 251 Q -> QGSTCASLQ (in isoform 3).
FT /FTId=VSP_011399.
FT MUTAGEN 361 361 D->A: Abolishes cleavage by caspase-3.
FT CONFLICT 8 8 N -> K (in Ref. 4; AAG17262).
FT CONFLICT 98 98 A -> S (in Ref. 3; AAF81273/AAG13120).
FT CONFLICT 235 235 R -> S (in Ref. 3; AAF81273/AAG13120).
FT CONFLICT 430 430 E -> D (in Ref. 6; CAG33448).
FT HELIX 9 20
FT STRAND 22 25
FT STRAND 27 38
FT STRAND 40 48
FT HELIX 50 56
FT STRAND 61 70
FT STRAND 72 74
FT STRAND 76 85
FT HELIX 91 107
FT TURN 108 110
FT STRAND 111 115
FT HELIX 120 123
FT HELIX 125 133
SQ SEQUENCE 430 AA; 48207 MW; 7E8C42ED047257AE CRC64;
MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE
EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW
AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ
QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE
PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI
DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM
FPANYVELIE
//
ID DBNL_HUMAN Reviewed; 430 AA.
AC Q9UJU6; A4D2I9; P84070; Q6IAI8; Q96F30; Q96K74; Q9HBN8; Q9NR72;
read moreDT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Cervical SH3P7;
DE AltName: Full=Cervical mucin-associated protein;
DE AltName: Full=Drebrin-F;
DE AltName: Full=HPK1-interacting protein of 55 kDa;
DE Short=HIP-55;
DE AltName: Full=SH3 domain-containing protein 7;
GN Name=DBNL; Synonyms=CMAP, SH3P7; ORFNames=PP5423;
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), AND INTERACTION WITH MAP4K1.
RX PubMed=10567356; DOI=10.1074/jbc.274.48.33945;
RA Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.;
RT "A novel src homology 3 domain-containing adaptor protein, HIP-55,
RT that interacts with hematopoietic progenitor kinase 1.";
RL J. Biol. Chem. 274:33945-33950(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang W., Yuan Z., Wan T., He L., Cao X.;
RT "Molecular cloning of cDNA encoding drebrin F.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RA Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L.,
RA Spurr-Michaud S., Keutmann H.T., Hill J.A., Gipson I.K.;
RT "Expression cloning of a novel cervical mucin-associated protein
RT (CMAP).";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 [10]
RP IDENTIFICATION.
RX PubMed=9891087;
RA Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J.,
RA Wienands J.;
RT "SH3P7 is a cytoskeleton adapter protein and is coupled to signal
RT transduction from lymphocyte antigen receptors.";
RL Mol. Cell. Biol. 19:1539-1546(1999).
RN [11]
RP DEGRADATION BY CASPASES.
RX PubMed=11689006; DOI=10.1006/bbrc.2001.5862;
RA Chen Y.-R., Kori R., John B., Tan T.-H.;
RT "Caspase-mediated cleavage of actin-binding and SH3-domain-containing
RT proteins cortactin, HS1, and HIP-55 during apoptosis.";
RL Biochem. Biophys. Res. Commun. 288:981-989(2001).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP FUNCTION.
RX PubMed=14729663; DOI=10.1074/jbc.M312659200;
RA Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O.,
RA Deckert M.;
RT "Recruitment of the actin-binding protein HIP-55 to the immunological
RT synapse regulates T cell receptor signaling and endocytosis.";
RL J. Biol. Chem. 279:15550-15560(2004).
RN [14]
RP INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF
RP ASP-361.
RX PubMed=15637062; DOI=10.1074/jbc.M413564200;
RA Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.;
RT "PRAM-1 potentiates arsenic trioxide-induced JNK activation.";
RL J. Biol. Chem. 280:9043-9048(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, AND
RP 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 [20]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, AND
RP MASS SPECTROMETRY.
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, AND
RP MASS 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 [24]
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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP STRUCTURE BY NMR OF 1-133.
RX PubMed=19768801; DOI=10.1002/pro.248;
RA Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M.,
RA Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.;
RT "NMR solution structures of actin depolymerizing factor homology
RT domains.";
RL Protein Sci. 18:2384-2392(2009).
CC -!- FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby
CC plays a role in receptor-mediated endocytosis. Plays a role in the
CC reorganization of the actin cytoskeleton, formation of cell
CC projections, such as neurites, in neuron morphogenesis and synapse
CC formation via its interaction with WASL and COBL. Does not bind G-
CC actin and promote actin polymerization by itself. Required for the
CC formation of organized podosome rosettes (By similarity). May act
CC as a common effector of antigen receptor-signaling pathways in
CC leukocytes. Acts as a key component of the immunological synapse
CC that regulates T-cell activation by bridging TCRs and the actin
CC cytoskeleton to gene activation and endocytic processes.
CC -!- SUBUNIT: Interacts with SHANK2, SHANK3 and SYN1. Interacts with
CC FGD1 and DNM1. Interacts with ANKRD54. Interacts with COBL.
CC Interacts with WASL and WIPF1 (By similarity). Interacts with
CC MAP4K1 and PRAM1.
CC -!- INTERACTION:
CC Q9H788:SH2D4A; NbExp=3; IntAct=EBI-751783, EBI-747035;
CC P78314:SH3BP2; NbExp=7; IntAct=EBI-751783, EBI-727062;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC lamellipodium. Cell projection, ruffle (By similarity). Cytoplasm,
CC cell cortex (By similarity). Cytoplasm, cytosol (By similarity).
CC Cell junction, synapse (By similarity). Cell projection (By
CC similarity). Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side (By similarity). Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane; Peripheral membrane protein; Cytoplasmic
CC side (By similarity). Golgi apparatus membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Cell
CC projection, podosome (By similarity). Note=Detected in neuron cell
CC body and cell projections, such as neurites. Colocalizes with
CC cytosolic dynamin in hippocampus neurons (By similarity). Cortical
CC actin cytoskeleton. Associates with lamellipodial actin and
CC membrane ruffles. Colocalizes with actin and cortactin at podosome
CC dots and podosome rosettes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UJU6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJU6-2; Sequence=VSP_011398;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 232;
CC Name=3;
CC IsoId=Q9UJU6-3; Sequence=VSP_011398, VSP_011399;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 232;
CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3
CC and PRAM1.
CC -!- PTM: Degraded by caspases during apoptosis.
CC -!- SIMILARITY: Belongs to the ABP1 family.
CC -!- SIMILARITY: Contains 1 ADF-H domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; AF197060; AAF13701.1; -; mRNA.
DR EMBL; AF077353; AAF80228.1; -; mRNA.
DR EMBL; AF250287; AAF81273.1; -; mRNA.
DR EMBL; AF151364; AAG13120.1; -; mRNA.
DR EMBL; AF218020; AAG17262.2; -; mRNA.
DR EMBL; AK027367; BAB55065.1; -; mRNA.
DR EMBL; CR457167; CAG33448.1; -; mRNA.
DR EMBL; CH236960; EAL23770.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61132.1; -; Genomic_DNA.
DR EMBL; BC011677; AAH11677.1; -; mRNA.
DR EMBL; BC031687; AAH31687.1; -; mRNA.
DR RefSeq; NP_001014436.1; NM_001014436.2.
DR RefSeq; NP_001116428.1; NM_001122956.1.
DR RefSeq; NP_001271242.1; NM_001284313.1.
DR RefSeq; NP_001271244.1; NM_001284315.1.
DR RefSeq; NP_054782.2; NM_014063.6.
DR UniGene; Hs.436500; -.
DR PDB; 1X67; NMR; -; A=1-133.
DR PDBsum; 1X67; -.
DR ProteinModelPortal; Q9UJU6; -.
DR SMR; Q9UJU6; 1-133, 373-428.
DR IntAct; Q9UJU6; 4.
DR MINT; MINT-1474845; -.
DR STRING; 9606.ENSP00000407950; -.
DR PhosphoSite; Q9UJU6; -.
DR DMDM; 51316115; -.
DR OGP; Q9UJU6; -.
DR PaxDb; Q9UJU6; -.
DR PRIDE; Q9UJU6; -.
DR DNASU; 28988; -.
DR Ensembl; ENST00000448521; ENSP00000411701; ENSG00000136279.
DR Ensembl; ENST00000468694; ENSP00000417653; ENSG00000136279.
DR Ensembl; ENST00000494774; ENSP00000419992; ENSG00000136279.
DR GeneID; 28988; -.
DR KEGG; hsa:28988; -.
DR UCSC; uc003tjp.4; human.
DR CTD; 28988; -.
DR GeneCards; GC07P044084; -.
DR HGNC; HGNC:2696; DBNL.
DR HPA; HPA020265; -.
DR HPA; HPA027735; -.
DR MIM; 610106; gene.
DR neXtProt; NX_Q9UJU6; -.
DR PharmGKB; PA27164; -.
DR eggNOG; NOG265859; -.
DR HOVERGEN; HBG051316; -.
DR OMA; FQDTGPQ; -.
DR OrthoDB; EOG7X3QR9; -.
DR Reactome; REACT_578; Apoptosis.
DR SignaLink; Q9UJU6; -.
DR ChiTaRS; DBNL; human.
DR EvolutionaryTrace; Q9UJU6; -.
DR GeneWiki; Drebrin-like; -.
DR GenomeRNAi; 28988; -.
DR NextBio; 51899; -.
DR PMAP-CutDB; Q9UJU6; -.
DR PRO; PR:Q9UJU6; -.
DR ArrayExpress; Q9UJU6; -.
DR Bgee; Q9UJU6; -.
DR CleanEx; HS_DBNL; -.
DR Genevestigator; Q9UJU6; -.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
DR GO; GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Adaptive immunity;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endocytosis; Golgi apparatus; Immunity; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Synapse; Transport.
FT CHAIN 1 430 Drebrin-like protein.
FT /FTId=PRO_0000079793.
FT DOMAIN 4 133 ADF-H.
FT DOMAIN 371 430 SH3.
FT COILED 176 231 Potential.
FT SITE 361 362 Cleavage; by caspase-3.
FT MOD_RES 176 176 N6-acetyllysine.
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 269 269 Phosphoserine.
FT MOD_RES 283 283 Phosphoserine.
FT MOD_RES 288 288 N6-acetyllysine.
FT MOD_RES 334 334 Phosphotyrosine (By similarity).
FT MOD_RES 344 344 Phosphotyrosine (By similarity).
FT VAR_SEQ 234 234 Q -> QS (in isoform 2 and isoform 3).
FT /FTId=VSP_011398.
FT VAR_SEQ 251 251 Q -> QGSTCASLQ (in isoform 3).
FT /FTId=VSP_011399.
FT MUTAGEN 361 361 D->A: Abolishes cleavage by caspase-3.
FT CONFLICT 8 8 N -> K (in Ref. 4; AAG17262).
FT CONFLICT 98 98 A -> S (in Ref. 3; AAF81273/AAG13120).
FT CONFLICT 235 235 R -> S (in Ref. 3; AAF81273/AAG13120).
FT CONFLICT 430 430 E -> D (in Ref. 6; CAG33448).
FT HELIX 9 20
FT STRAND 22 25
FT STRAND 27 38
FT STRAND 40 48
FT HELIX 50 56
FT STRAND 61 70
FT STRAND 72 74
FT STRAND 76 85
FT HELIX 91 107
FT TURN 108 110
FT STRAND 111 115
FT HELIX 120 123
FT HELIX 125 133
SQ SEQUENCE 430 AA; 48207 MW; 7E8C42ED047257AE CRC64;
MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE
EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW
AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ
QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE
PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI
DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM
FPANYVELIE
//
MIM
610106
*RECORD*
*FIELD* NO
610106
*FIELD* TI
*610106 DREBRIN-LIKE; DBNL
;;HPK1-INTERACTING PROTEIN, 55-KD; HIP55
*FIELD* TX
CLONING
read more
By yeast 2-hybrid screening of a HeLa cell cDNA library using GLK
(MAP4K3; 604921) as bait, followed by EST database analysis, Ensenat et
al. (1999) cloned DBNL, which they called HIP55. The predicted 430-amino
acid protein has a calculated molecular mass of 48 kD. The N terminus of
HIP55 contains a putative actin-binding domain found in drebrins (see
DBN1; 126660), which are involved in brain development, and the C
terminus contains an SH3 domain. Western blot analysis detected a 55-kD
protein. Northern blot analysis revealed ubiquitous expression of a
2.3-kb transcript, with highest levels in spleen and peripheral blood
leukocytes.
GENE FUNCTION
By yeast 2-hybrid analysis, Ensenat et al. (1999) found that HIP55
interacted with GLK and HPK1 (MAP4K1; 601983). They confirmed the
interaction with HPK1 both in vitro and in vivo. The interaction was
dependent on the SH3 domain of HIP55 and the second proline-rich domain
of HPK1. When cotransfected, HIP55 increased HPK1 kinase activity and
JNK1 (MAPK8; 601158) kinase activity. Ensenat et al. (1999) concluded
that HIP55 binds HPK1 and regulates the JNK1 signaling cascade.
Using confocal microscopy, RNA interference, and overexpression
experiments in mouse and human cell lines, Le Bras et al. (2004) found
that HIP55 did not contribute to early formation of T
cell-antigen-presenting cell (APC) conjugates. However, they identified
HIP55 as a key constituent of the immunologic synapse, regulating T-cell
activation by bridging T-cell receptors and the actin cytoskeleton to
gene activation and endocytic processes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DBNL
gene to chromosome 7 (TMAP D7S2634).
ANIMAL MODEL
Han et al. (2005) found that Hip55 -/- mice were viable and fertile, but
they showed decreased body weight and increased frequency of death
within the first 4 weeks after birth. Lymphoid organs of Hip55 -/- mice
showed normal cellularity and T-cell development. However, Hip55 -/- T
cells proliferated at a reduced level, with lower cytokine production
and lower expression of activation markers after T-cell receptor
stimulation.
*FIELD* RF
1. Ensenat, D.; Yao, Z.; Wang, X. S.; Kori, R.; Zhou, G.; Lee, S.
C.; Tan, T.-H.: A novel Src homology 3 domain-containing adaptor
protein, HIP-55, that interacts with hematopoietic progenitor kinase
1. J. Biol. Chem. 274: 33945-33950, 1999. Note: Erratum: J. Biol.
Chem. 275: 14004 only, 2000.
2. Han, J.; Shui, J.-W.; Zhang, X.; Zheng, B.; Han, S.; Tan, T.-H.
: HIP-55 is important for T-cell proliferation, cytokine production,
and immune responses. Molec. Cell. Biol. 25: 6869-6878, 2005.
3. Le Bras, S.; Foucault, I.; Foussat, A.; Brignone, C.; Acuto, O.;
Deckert, M.: Recruitment of the actin-binding protein HIP-55 to the
immunological synapse regulates T cell receptor signaling and endocytosis. J.
Biol. Chem. 279: 15550-15560, 2004.
*FIELD* CD
Paul J. Converse: 5/10/2006
*FIELD* ED
terry: 07/03/2012
mgross: 5/10/2006
*RECORD*
*FIELD* NO
610106
*FIELD* TI
*610106 DREBRIN-LIKE; DBNL
;;HPK1-INTERACTING PROTEIN, 55-KD; HIP55
*FIELD* TX
CLONING
read more
By yeast 2-hybrid screening of a HeLa cell cDNA library using GLK
(MAP4K3; 604921) as bait, followed by EST database analysis, Ensenat et
al. (1999) cloned DBNL, which they called HIP55. The predicted 430-amino
acid protein has a calculated molecular mass of 48 kD. The N terminus of
HIP55 contains a putative actin-binding domain found in drebrins (see
DBN1; 126660), which are involved in brain development, and the C
terminus contains an SH3 domain. Western blot analysis detected a 55-kD
protein. Northern blot analysis revealed ubiquitous expression of a
2.3-kb transcript, with highest levels in spleen and peripheral blood
leukocytes.
GENE FUNCTION
By yeast 2-hybrid analysis, Ensenat et al. (1999) found that HIP55
interacted with GLK and HPK1 (MAP4K1; 601983). They confirmed the
interaction with HPK1 both in vitro and in vivo. The interaction was
dependent on the SH3 domain of HIP55 and the second proline-rich domain
of HPK1. When cotransfected, HIP55 increased HPK1 kinase activity and
JNK1 (MAPK8; 601158) kinase activity. Ensenat et al. (1999) concluded
that HIP55 binds HPK1 and regulates the JNK1 signaling cascade.
Using confocal microscopy, RNA interference, and overexpression
experiments in mouse and human cell lines, Le Bras et al. (2004) found
that HIP55 did not contribute to early formation of T
cell-antigen-presenting cell (APC) conjugates. However, they identified
HIP55 as a key constituent of the immunologic synapse, regulating T-cell
activation by bridging T-cell receptors and the actin cytoskeleton to
gene activation and endocytic processes.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DBNL
gene to chromosome 7 (TMAP D7S2634).
ANIMAL MODEL
Han et al. (2005) found that Hip55 -/- mice were viable and fertile, but
they showed decreased body weight and increased frequency of death
within the first 4 weeks after birth. Lymphoid organs of Hip55 -/- mice
showed normal cellularity and T-cell development. However, Hip55 -/- T
cells proliferated at a reduced level, with lower cytokine production
and lower expression of activation markers after T-cell receptor
stimulation.
*FIELD* RF
1. Ensenat, D.; Yao, Z.; Wang, X. S.; Kori, R.; Zhou, G.; Lee, S.
C.; Tan, T.-H.: A novel Src homology 3 domain-containing adaptor
protein, HIP-55, that interacts with hematopoietic progenitor kinase
1. J. Biol. Chem. 274: 33945-33950, 1999. Note: Erratum: J. Biol.
Chem. 275: 14004 only, 2000.
2. Han, J.; Shui, J.-W.; Zhang, X.; Zheng, B.; Han, S.; Tan, T.-H.
: HIP-55 is important for T-cell proliferation, cytokine production,
and immune responses. Molec. Cell. Biol. 25: 6869-6878, 2005.
3. Le Bras, S.; Foucault, I.; Foussat, A.; Brignone, C.; Acuto, O.;
Deckert, M.: Recruitment of the actin-binding protein HIP-55 to the
immunological synapse regulates T cell receptor signaling and endocytosis. J.
Biol. Chem. 279: 15550-15560, 2004.
*FIELD* CD
Paul J. Converse: 5/10/2006
*FIELD* ED
terry: 07/03/2012
mgross: 5/10/2006