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Q16643 (DREB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Drebrin
Alternative name(s):
Developmentally-regulated brain protein
Gene names
Name:DBN1
Synonyms:D0S117E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites, respectively.

Subunit structure

Binds F-actin.

Subcellular location

Cytoplasm.

Tissue specificity

Brain neurons. Also found in the heart, placenta, skeletal muscle, kidney and pancreas.

Sequence similarities

Contains 1 ADF-H domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandActin-binding
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from sequence or structural similarity. Source: UniProtKB

cell communication by chemical coupling

Inferred from electronic annotation. Source: Compara

cell communication by electrical coupling

Inferred from electronic annotation. Source: Compara

maintenance of protein location in cell

Inferred from electronic annotation. Source: Compara

neural precursor cell proliferation

Inferred from electronic annotation. Source: Compara

regulation of dendrite development

Non-traceable author statement PubMed 12009525. Source: UniProtKB

regulation of neuronal synaptic plasticity

Non-traceable author statement PubMed 12009525. Source: UniProtKB

   Cellular_componentactomyosin

Non-traceable author statement PubMed 12761245. Source: UniProtKB

cytoplasm

Non-traceable author statement PubMed 12009525. Source: UniProtKB

dendrite

Non-traceable author statement PubMed 12009525. Source: UniProtKB

gap junction

Inferred from electronic annotation. Source: Compara

plasma membrane

Inferred from electronic annotation. Source: Compara

   Molecular_functionactin binding

Non-traceable author statement PubMed 12761245. Source: UniProtKB

profilin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16643-1)

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: Q16643-2)

The sequence of this isoform differs from the canonical sequence as follows:
     4-29: VSFSGHRLELLAAYEEVIREESAADW → HPWHGTAALASSQAWRDGRERQALVSCR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 649648Drebrin
PRO_0000080008

Regions

Domain3 – 134132ADF-H

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.8
Modified residue1341Phosphoserine By similarity
Modified residue1411Phosphoserine Ref.15 Ref.17
Modified residue1421Phosphoserine Ref.8 Ref.13 Ref.15 Ref.17
Modified residue3311Phosphothreonine Ref.13 Ref.14
Modified residue3351Phosphothreonine Ref.13
Modified residue3371Phosphoserine Ref.13 Ref.17
Modified residue3391Phosphoserine Ref.17
Modified residue3421Phosphoserine By similarity
Modified residue3461Phosphothreonine Ref.13 Ref.14

Natural variations

Alternative sequence4 – 2926VSFSG…SAADW → HPWHGTAALASSQAWRDGRE RQALVSCR in isoform 2.
VSP_028175
Natural variant2781E → K in a breast cancer sample; somatic mutation. Ref.18
VAR_035910
Natural variant4461I → V. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs2544809 [ dbSNP | Ensembl ].
VAR_047365
Natural variant5531S → P. Ref.1 Ref.2 Ref.4 Ref.6
Corresponds to variant rs28538572 [ dbSNP | Ensembl ].
VAR_047366
Natural variant6401E → Q in a breast cancer sample; somatic mutation. Ref.18
VAR_035911

Sequences

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

Last modified November 25, 2008. Version 4.
Checksum: A7DF1AE3776C0BEA

FASTA64971,429
        10         20         30         40         50         60 
MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG LQELSGHFEN 

        70         80         90        100        110        120 
QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS HVAKVAEFFQ GVDVIVNASS 

       130        140        150        160        170        180 
VEDIDAGAIG QRLSNGLARL SSPVLHRLRL REDENAEPVG TTYQKTDAAV EMKRINREQF 

       190        200        210        220        230        240 
WEQAKKEEEL RKEEERKKAL DERLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ 

       250        260        270        280        290        300 
TLEAEEAKRR LKEQSIFGDH RDEEEETHMK KSESEVEEAA AIIAQRPDNP REFFKQQERV 

       310        320        330        340        350        360 
ASASAGSCDV PSPFNHRPGS HLDSHRRMAP TPIPTRSPSD SSTASTPVAE QIERALDEVT 

       370        380        390        400        410        420 
SSQPPPLPPP PPPAQETQEP SPILDSEETR AAAPQAWAGP MEEPPQAQAP PRGPGSPAED 

       430        440        450        460        470        480 
LMFMESAEQA VLAAPVEPAT ADATEIHDAA DTIETDTATA DTTVANNVPP AATSLIDLWP 

       490        500        510        520        530        540 
GNGEGASTLQ GEPRAPTPPS GTEVTLAEVP LLDEVAPEPL LPAGEGCATL LNFDELPEPP 

       550        560        570        580        590        600 
ATFCDPEEVE GESLAAPQTP TLPSALEELE QEQEPEPHLL TNGETTQKEG TQASEGYFSQ 

       610        620        630        640 
SQEEEFAQSE ELCAKAPPPV FYNKPPEIDI TCWDADPVPE EEEGFEGGD 

« Hide

Isoform 2 [UniParc].

Checksum: 89DA14954246C0A3
Show »

FASTA65171,599

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNA encoding human drebrin E and chromosomal mapping of its gene."
Toda M., Shirao T., Minoshima S., Shimizu N., Toya S., Uyemura K.
Biochem. Biophys. Res. Commun. 196:468-472(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-446 AND PRO-553.
Tissue: Fetal brain.
[2]"Human drebrin: cDNA sequence, mRNA tissue distribution and chromosomal localization."
Fisher L.W., McBride O.W., Filpula D., Ibaraki K., Young M.F.
Neurosci. Res. Commun. 14:35-42(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-446 AND PRO-553.
Tissue: Osteoblast.
[3]"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 1).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS VAL-446 AND PRO-553.
Tissue: Testis.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1), VARIANTS VAL-446 AND PRO-553.
Tissue: Eye and Muscle.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
Tissue: Platelet.
[8]Bienvenut W.V., Dozynkiewicz M., Norman J.C.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10; 43-62; 140-147; 150-165; 272-299 AND 328-390, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-142, MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[9]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 80-94, MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"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-142; THR-331; THR-335; SER-337 AND THR-346, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"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 THR-331 AND THR-346, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[15]"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-141 AND SER-142, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[16]"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].
[17]"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-141; SER-142; SER-337 AND SER-339, MASS SPECTROMETRY.
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-278 AND GLN-640.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17530 mRNA. Translation: BAA04480.1.
U00802 mRNA. Translation: AAA16256.1.
AK314645 mRNA. Translation: BAG37207.1.
AL110225 mRNA. Translation: CAB53683.1.
AC145098 Genomic DNA. No translation available.
BC000283 mRNA. Translation: AAH00283.1.
BC007281 mRNA. Translation: AAH07281.1.
BC007567 mRNA. Translation: AAH07567.1.
IPIIPI00003406.
IPI00295624.
PIRJN0809.
T14763.
RefSeqNP_004386.2. NM_004395.3.
NP_543157.1. NM_080881.2.
UniGeneHs.130316.

3D structure databases

ProteinModelPortalQ16643.
ModBaseSearch...

Protein-protein interaction databases

IntActQ16643. 11 interactions.
MINTMINT-1149054.
STRING9606.ENSP00000292385.

PTM databases

PhosphoSiteQ16643.

Polymorphism databases

DMDM215274247.

2D gel databases

OGPQ16643.

Proteomic databases

PaxDbQ16643.
PRIDEQ16643.

Protocols and materials databases

DNASU1627.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292385; ENSP00000292385; ENSG00000113758.
ENST00000309007; ENSP00000308532; ENSG00000113758.
GeneID1627.
KEGGhsa:1627.
UCSCuc003mgx.2. human.
uc003mgy.2. human.

Organism-specific databases

CTD1627.
GeneCardsGC05M176883.
H-InvDBHIX0005464.
HGNCHGNC:2695. DBN1.
HPACAB008367.
MIM126660. gene.
neXtProtNX_Q16643.
PharmGKBPA27163.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329456.
HOGENOMHOG000015304.
HOVERGENHBG000823.
OrthoDBEOG4R502Q.

Gene expression databases

ArrayExpressQ16643.
BgeeQ16643.
CleanExHS_DBN1.
GenevestigatorQ16643.
GermOnlineENSG00000113758. Homo sapiens.

Family and domain databases

InterProIPR002108. Actin-bd_cofilin/tropomyosin.
[Graphical view]
PfamPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTSM00102. ADF. 1 hit.
[Graphical view]
PROSITEPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDBN1. human.
GenomeRNAi1627.
NextBio6674.
SOURCESearch...

Entry information

Entry nameDREB_HUMAN
AccessionPrimary (citable) accession number: Q16643
Secondary accession number(s): B2RBG0, Q9UFZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: May 1, 2013
This is version 125 of the entry and version 4 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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families