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Q9UJU6 (DBNL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Drebrin-like protein
Alternative name(s):
Cervical SH3P7
Cervical mucin-associated protein
Drebrin-F
HPK1-interacting protein of 55 kDa
Short name=HIP-55
SH3 domain-containing protein 7
Gene names
Name:DBNL
Synonyms:CMAP, SH3P7
ORF Names:PP5423
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes By similarity. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. Ref.13

Subunit structure

Interacts with SHANK2, SHANK3 and SYN1. Interacts with FGD1 and DNM1. Interacts with ANKRD54. Interacts with COBL. Interacts with WASL and WIPF1 By similarity. Interacts with MAP4K1 and PRAM1. Ref.1 Ref.14

Subcellular location

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle By similarity. Cytoplasmcell cortex By similarity. Cytoplasmcytosol By similarity. Cell junctionsynapse By similarity. Cell projection By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicleclathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionpodosome By similarity. Note: Detected in neuron cell body and cell projections, such as neurites. Colocalizes with cytosolic dynamin in hippocampus neurons By similarity. Cortical actin cytoskeleton. Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes By similarity.

Domain

The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1.

Post-translational modification

Degraded by caspases during apoptosis.

Sequence similarities

Belongs to the ABP1 family.

Contains 1 ADF-H domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Endocytosis
Immunity
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Golgi apparatus
Membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

activation of JUN kinase activity

Traceable author statement Ref.1. Source: ProtInc

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

podosome assembly

Inferred from sequence or structural similarity. Source: UniProtKB

synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

podosome

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionactin binding

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme activator activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SH2D4AQ9H7883EBI-751783,EBI-747035
SH3BP2P783147EBI-751783,EBI-727062

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJU6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UJU6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     234-234: Q → QS
Note: No experimental confirmation available. Contains a phosphoserine at position 232.
Isoform 3 (identifier: Q9UJU6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     234-234: Q → QS
     251-251: Q → QGSTCASLQ
Note: No experimental confirmation available. Contains a phosphoserine at position 232.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Drebrin-like protein
PRO_0000079793

Regions

Domain4 – 133130ADF-H
Domain371 – 43060SH3
Coiled coil176 – 23156 Potential

Sites

Site361 – 3622Cleavage; by caspase-3

Amino acid modifications

Modified residue1761N6-acetyllysine Ref.22
Modified residue2321Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.25
Modified residue2691Phosphoserine Ref.19 Ref.21 Ref.23
Modified residue2831Phosphoserine Ref.12 Ref.16
Modified residue2881N6-acetyllysine Ref.22
Modified residue3341Phosphotyrosine By similarity
Modified residue3441Phosphotyrosine By similarity

Natural variations

Alternative sequence2341Q → QS in isoform 2 and isoform 3.
VSP_011398
Alternative sequence2511Q → QGSTCASLQ in isoform 3.
VSP_011399

Experimental info

Mutagenesis3611D → A: Abolishes cleavage by caspase-3. Ref.14
Sequence conflict81N → K in AAG17262. Ref.4
Sequence conflict981A → S in AAF81273. Ref.3
Sequence conflict981A → S in AAG13120. Ref.3
Sequence conflict2351R → S in AAF81273. Ref.3
Sequence conflict2351R → S in AAG13120. Ref.3
Sequence conflict4301E → D in CAG33448. Ref.6

Secondary structure

......................... 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7E8C42ED047257AE

FASTA43048,207
        10         20         30         40         50         60 
MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG 

        70         80         90        100        110        120 
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE 

       130        140        150        160        170        180 
EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW 

       190        200        210        220        230        240 
AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ 

       250        260        270        280        290        300 
QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE 

       310        320        330        340        350        360 
PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI 

       370        380        390        400        410        420 
DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM 

       430 
FPANYVELIE 

« Hide

Isoform 2 [UniParc].

Checksum: D18F9D316FFD0B4E
Show »

FASTA43148,294
Isoform 3 [UniParc].

Checksum: 8C044FBD0E82C6D5
Show »

FASTA43949,042

References

« Hide 'large scale' references
[1]"A novel src homology 3 domain-containing adaptor protein, HIP-55, that interacts with hematopoietic progenitor kinase 1."
Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.
J. Biol. Chem. 274:33945-33950(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP4K1.
[2]"Molecular cloning of cDNA encoding drebrin F."
Zhang W., Yuan Z., Wan T., He L., Cao X.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Expression cloning of a novel cervical mucin-associated protein (CMAP)."
Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L., Spurr-Michaud S., Keutmann H.T., Hill J.A., Gipson I.K.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix.
[4]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Mammary gland.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Eye.
[10]"SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors."
Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J., Wienands J.
Mol. Cell. Biol. 19:1539-1546(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[11]"Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis."
Chen Y.-R., Kori R., John B., Tan T.-H.
Biochem. Biophys. Res. Commun. 288:981-989(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEGRADATION BY CASPASES.
[12]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Recruitment of the actin-binding protein HIP-55 to the immunological synapse regulates T cell receptor signaling and endocytosis."
Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O., Deckert M.
J. Biol. Chem. 279:15550-15560(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"PRAM-1 potentiates arsenic trioxide-induced JNK activation."
Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.
J. Biol. Chem. 280:9043-9048(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-361.
[15]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"NMR solution structures of actin depolymerizing factor homology domains."
Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M., Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.
Protein Sci. 18:2384-2392(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-133.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF197060 mRNA. Translation: AAF13701.1.
AF077353 mRNA. Translation: AAF80228.1.
AF250287 mRNA. Translation: AAF81273.1.
AF151364 mRNA. Translation: AAG13120.1.
AF218020 mRNA. Translation: AAG17262.2.
AK027367 mRNA. Translation: BAB55065.1.
CR457167 mRNA. Translation: CAG33448.1.
CH236960 Genomic DNA. Translation: EAL23770.1.
CH471128 Genomic DNA. Translation: EAW61132.1.
BC011677 mRNA. Translation: AAH11677.1.
BC031687 mRNA. Translation: AAH31687.1.
RefSeqNP_001014436.1. NM_001014436.2.
NP_001116428.1. NM_001122956.1.
NP_001271242.1. NM_001284313.1.
NP_001271244.1. NM_001284315.1.
NP_054782.2. NM_014063.6.
UniGeneHs.436500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X67NMR-A1-133[»]
ProteinModelPortalQ9UJU6.
SMRQ9UJU6. Positions 1-133, 373-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118809. 43 interactions.
IntActQ9UJU6. 4 interactions.
MINTMINT-1474845.
STRING9606.ENSP00000407950.

PTM databases

PhosphoSiteQ9UJU6.

Polymorphism databases

DMDM51316115.

2D gel databases

OGPQ9UJU6.

Proteomic databases

PaxDbQ9UJU6.
PRIDEQ9UJU6.

Protocols and materials databases

DNASU28988.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000448521; ENSP00000411701; ENSG00000136279. [Q9UJU6-1]
ENST00000468694; ENSP00000417653; ENSG00000136279. [Q9UJU6-3]
ENST00000494774; ENSP00000419992; ENSG00000136279. [Q9UJU6-2]
GeneID28988.
KEGGhsa:28988.
UCSCuc003tjo.4. human. [Q9UJU6-2]
uc003tjp.4. human. [Q9UJU6-1]
uc003tjq.4. human. [Q9UJU6-3]

Organism-specific databases

CTD28988.
GeneCardsGC07P044084.
HGNCHGNC:2696. DBNL.
HPAHPA020265.
HPA027735.
MIM610106. gene.
neXtProtNX_Q9UJU6.
PharmGKBPA27164.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265859.
HOVERGENHBG051316.
OMAFQDTGPQ.
OrthoDBEOG7X3QR9.
PhylomeDBQ9UJU6.
TreeFamTF318935.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
SignaLinkQ9UJU6.

Gene expression databases

ArrayExpressQ9UJU6.
BgeeQ9UJU6.
CleanExHS_DBNL.
GenevestigatorQ9UJU6.

Family and domain databases

InterProIPR002108. ADF-H.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTSM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDBNL. human.
EvolutionaryTraceQ9UJU6.
GeneWikiDrebrin-like.
GenomeRNAi28988.
NextBio51899.
PMAP-CutDBQ9UJU6.
PROQ9UJU6.
SOURCESearch...

Entry information

Entry nameDBNL_HUMAN
AccessionPrimary (citable) accession number: Q9UJU6
Secondary accession number(s): A4D2I9 expand/collapse secondary AC list , P84070, Q6IAI8, Q96F30, Q96K74, Q9HBN8, Q9NR72
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM