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Protein

Drebrin

Gene

DBN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.1 Publication

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • profilin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ16643.

Names & Taxonomyi

Protein namesi
Recommended name:
Drebrin
Alternative name(s):
Developmentally-regulated brain protein
Gene namesi
Name:DBN1
Synonyms:D0S117E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:2695. DBN1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • actomyosin Source: UniProtKB
  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • dendrite Source: UniProtKB
  • gap junction Source: Ensembl
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27163.

Polymorphism and mutation databases

BioMutaiDBN1.
DMDMi215274247.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 649648DrebrinPRO_0000080008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei141 – 1411Phosphoserine2 Publications
Modified residuei142 – 1421Phosphoserine4 Publications
Modified residuei331 – 3311Phosphothreonine2 Publications
Modified residuei335 – 3351Phosphothreonine1 Publication
Modified residuei337 – 3371Phosphoserine2 Publications
Modified residuei339 – 3391Phosphoserine1 Publication
Modified residuei346 – 3461Phosphothreonine2 Publications
Modified residuei416 – 4161Phosphoserine1 Publication
Modified residuei497 – 4971Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ16643.
PaxDbiQ16643.
PRIDEiQ16643.

2D gel databases

OGPiQ16643.

PTM databases

PhosphoSiteiQ16643.

Expressioni

Tissue specificityi

Brain neurons. Also found in the heart, placenta, skeletal muscle, kidney and pancreas. Expressed in peripheral blood lymphocytes, including T-cells (at protein level).1 Publication

Gene expression databases

BgeeiQ16643.
CleanExiHS_DBN1.
ExpressionAtlasiQ16643. baseline and differential.
GenevisibleiQ16643. HS.

Organism-specific databases

HPAiHPA051452.
HPA056940.

Interactioni

Subunit structurei

Binds F-actin. Interacts with CXCR4; this interaction is enhanced by antigenic stimulation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CXCR4P610735EBI-351394,EBI-489411
DBN1Q16643-12EBI-351394,EBI-8757328
GRB2P629934EBI-351394,EBI-401755
MLLT4P551964EBI-351394,EBI-365875
Mllt4O358893EBI-351394,EBI-6654073From a different organism.
PTENP604845EBI-351394,EBI-696162

Protein-protein interaction databases

BioGridi107995. 55 interactions.
IntActiQ16643. 36 interactions.
MINTiMINT-1149054.
STRINGi9606.ENSP00000292385.

Structurei

3D structure databases

ProteinModelPortaliQ16643.
SMRiQ16643. Positions 13-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 134132ADF-HPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ADF-H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG329456.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000015304.
HOVERGENiHBG000823.
InParanoidiQ16643.
OMAiCSHLDSH.
OrthoDBiEOG7X3QR9.
PhylomeDBiQ16643.
TreeFamiTF318935.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028438. Drebrin.
[Graphical view]
PANTHERiPTHR10829:SF1. PTHR10829:SF1. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16643-1) [UniParc]FASTAAdd to basket

Also known as: Drebrin E, drebrin E2, Embryonic drebrin

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.

« Hide

        10         20         30         40         50
MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG
60 70 80 90 100
LQELSGHFEN QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS
110 120 130 140 150
HVAKVAEFFQ GVDVIVNASS VEDIDAGAIG QRLSNGLARL SSPVLHRLRL
160 170 180 190 200
REDENAEPVG TTYQKTDAAV EMKRINREQF WEQAKKEEEL RKEEERKKAL
210 220 230 240 250
DERLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ TLEAEEAKRR
260 270 280 290 300
LKEQSIFGDH RDEEEETHMK KSESEVEEAA AIIAQRPDNP REFFKQQERV
310 320 330 340 350
ASASAGSCDV PSPFNHRPGS HLDSHRRMAP TPIPTRSPSD SSTASTPVAE
360 370 380 390 400
QIERALDEVT SSQPPPLPPP PPPAQETQEP SPILDSEETR AAAPQAWAGP
410 420 430 440 450
MEEPPQAQAP PRGPGSPAED LMFMESAEQA VLAAPVEPAT ADATEIHDAA
460 470 480 490 500
DTIETDTATA DTTVANNVPP AATSLIDLWP GNGEGASTLQ GEPRAPTPPS
510 520 530 540 550
GTEVTLAEVP LLDEVAPEPL LPAGEGCATL LNFDELPEPP ATFCDPEEVE
560 570 580 590 600
GESLAAPQTP TLPSALEELE QEQEPEPHLL TNGETTQKEG TQASEGYFSQ
610 620 630 640
SQEEEFAQSE ELCAKAPPPV FYNKPPEIDI TCWDADPVPE EEEGFEGGD
Length:649
Mass (Da):71,429
Last modified:November 25, 2008 - v4
Checksum:iA7DF1AE3776C0BEA
GO
Isoform 2 (identifier: Q16643-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     4-29: VSFSGHRLELLAAYEEVIREESAADW → HPWHGTAALASSQAWRDGRERQALVSCR

Note: No experimental confirmation available.
Show »
Length:651
Mass (Da):71,599
Checksum:i89DA14954246C0A3
GO
Isoform 3 (identifier: Q16643-3) [UniParc]FASTAAdd to basket

Also known as: Drebrin A

The sequence of this isoform differs from the canonical sequence as follows:
     319-319: G → GRPYCPFIKASDSGPSSSSSSSSSPPRTPFPYITCHRTPNLSSSLPC

Note: No experimental confirmation available.
Show »
Length:695
Mass (Da):76,300
Checksum:iC4E1FEC8D932603C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti278 – 2781E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035910
Natural varianti446 – 4461I → V.4 Publications
Corresponds to variant rs2544809 [ dbSNP | Ensembl ].
VAR_047365
Natural varianti553 – 5531S → P.4 Publications
Corresponds to variant rs28538572 [ dbSNP | Ensembl ].
VAR_047366
Natural varianti640 – 6401E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035911

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei4 – 2926VSFSG…SAADW → HPWHGTAALASSQAWRDGRE RQALVSCR in isoform 2. 1 PublicationVSP_028175Add
BLAST
Alternative sequencei319 – 3191G → GRPYCPFIKASDSGPSSSSS SSSSPPRTPFPYITCHRTPN LSSSLPC in isoform 3. 1 PublicationVSP_053443

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC114553 mRNA. No translation available.
CCDSiCCDS4420.1. [Q16643-1]
CCDS4421.1. [Q16643-2]
PIRiJN0809.
T14763.
RefSeqiNP_004386.2. NM_004395.3.
NP_543157.1. NM_080881.2.
XP_005265884.1. XM_005265827.2. [Q16643-3]
UniGeneiHs.130316.

Genome annotation databases

EnsembliENST00000292385; ENSP00000292385; ENSG00000113758. [Q16643-2]
ENST00000309007; ENSP00000308532; ENSG00000113758.
ENST00000393565; ENSP00000377195; ENSG00000113758. [Q16643-3]
GeneIDi1627.
KEGGihsa:1627.
UCSCiuc003mgx.2. human. [Q16643-2]
uc003mgy.2. human. [Q16643-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC114553 mRNA. No translation available.
CCDSiCCDS4420.1. [Q16643-1]
CCDS4421.1. [Q16643-2]
PIRiJN0809.
T14763.
RefSeqiNP_004386.2. NM_004395.3.
NP_543157.1. NM_080881.2.
XP_005265884.1. XM_005265827.2. [Q16643-3]
UniGeneiHs.130316.

3D structure databases

ProteinModelPortaliQ16643.
SMRiQ16643. Positions 13-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107995. 55 interactions.
IntActiQ16643. 36 interactions.
MINTiMINT-1149054.
STRINGi9606.ENSP00000292385.

PTM databases

PhosphoSiteiQ16643.

Polymorphism and mutation databases

BioMutaiDBN1.
DMDMi215274247.

2D gel databases

OGPiQ16643.

Proteomic databases

MaxQBiQ16643.
PaxDbiQ16643.
PRIDEiQ16643.

Protocols and materials databases

DNASUi1627.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292385; ENSP00000292385; ENSG00000113758. [Q16643-2]
ENST00000309007; ENSP00000308532; ENSG00000113758.
ENST00000393565; ENSP00000377195; ENSG00000113758. [Q16643-3]
GeneIDi1627.
KEGGihsa:1627.
UCSCiuc003mgx.2. human. [Q16643-2]
uc003mgy.2. human. [Q16643-1]

Organism-specific databases

CTDi1627.
GeneCardsiGC05M176883.
H-InvDBHIX0005464.
HGNCiHGNC:2695. DBN1.
HPAiHPA051452.
HPA056940.
MIMi126660. gene.
neXtProtiNX_Q16643.
PharmGKBiPA27163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG329456.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000015304.
HOVERGENiHBG000823.
InParanoidiQ16643.
OMAiCSHLDSH.
OrthoDBiEOG7X3QR9.
PhylomeDBiQ16643.
TreeFamiTF318935.

Enzyme and pathway databases

SignaLinkiQ16643.

Miscellaneous databases

ChiTaRSiDBN1. human.
GeneWikiiDBN1.
GenomeRNAii1627.
NextBioi35464922.
PROiQ16643.
SOURCEiSearch...

Gene expression databases

BgeeiQ16643.
CleanExiHS_DBN1.
ExpressionAtlasiQ16643. baseline and differential.
GenevisibleiQ16643. HS.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028438. Drebrin.
[Graphical view]
PANTHERiPTHR10829:SF1. PTHR10829:SF1. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-521 (ISOFORM 3), 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; THR-331; THR-335; SER-337 AND THR-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. Cited for: FUNCTION, INTERACTION WITH CXCR4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND THR-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-278 AND GLN-640.

Entry informationi

Entry nameiDREB_HUMAN
AccessioniPrimary (citable) accession number: Q16643
Secondary accession number(s): A8MV58, B2RBG0, Q9UFZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: July 22, 2015
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.