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Q16643

- DREB_HUMAN

UniProt

Q16643 - DREB_HUMAN

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Protein
Drebrin
Gene
DBN1, D0S117E
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. actin binding Source: UniProtKB
  2. profilin binding Source: UniProtKB
  3. protein binding Source: IntAct

GO - Biological processi

  1. actin filament organization Source: UniProtKB
  2. cell communication by chemical coupling Source: Ensembl
  3. cell communication by electrical coupling Source: Ensembl
  4. maintenance of protein location in cell Source: Ensembl
  5. neural precursor cell proliferation Source: Ensembl
  6. regulation of dendrite development Source: UniProtKB
  7. regulation of neuronal synaptic plasticity Source: UniProtKB
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: Chromosome 5

Organism-specific databases

HGNCiHGNC:2695. DBN1.

Subcellular locationi

Cytoplasm. Cytoplasmcell cortex. Cell junction
Note: In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC).1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. actomyosin Source: UniProtKB
  3. cell cortex Source: UniProtKB-SubCell
  4. cytoplasm Source: UniProtKB
  5. dendrite Source: UniProtKB
  6. gap junction Source: Ensembl
  7. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 649648Drebrin
PRO_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

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

ArrayExpressiQ16643.
BgeeiQ16643.
CleanExiHS_DBN1.
GenevestigatoriQ16643.

Organism-specific databases

HPAiCAB008367.
HPA051452.

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
MLLT4P551964EBI-351394,EBI-365875
Mllt4O358893EBI-351394,EBI-6654073From a different organism.
PTENP604845EBI-351394,EBI-696162

Protein-protein interaction databases

BioGridi107995. 54 interactions.
IntActiQ16643. 34 interactions.
MINTiMINT-1149054.
STRINGi9606.ENSP00000292385.

Structurei

3D structure databases

ProteinModelPortaliQ16643.
SMRiQ16643. Positions 13-136.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 134132ADF-H
Add
BLAST

Sequence similaritiesi

Contains 1 ADF-H domain.

Phylogenomic databases

eggNOGiNOG329456.
HOGENOMiHOG000015304.
HOVERGENiHBG000823.
OMAiCANLLNF.
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. Align

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

MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG    50
LQELSGHFEN QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS 100
HVAKVAEFFQ GVDVIVNASS VEDIDAGAIG QRLSNGLARL SSPVLHRLRL 150
REDENAEPVG TTYQKTDAAV EMKRINREQF WEQAKKEEEL RKEEERKKAL 200
DERLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ TLEAEEAKRR 250
LKEQSIFGDH RDEEEETHMK KSESEVEEAA AIIAQRPDNP REFFKQQERV 300
ASASAGSCDV PSPFNHRPGS HLDSHRRMAP TPIPTRSPSD SSTASTPVAE 350
QIERALDEVT SSQPPPLPPP PPPAQETQEP SPILDSEETR AAAPQAWAGP 400
MEEPPQAQAP PRGPGSPAED LMFMESAEQA VLAAPVEPAT ADATEIHDAA 450
DTIETDTATA DTTVANNVPP AATSLIDLWP GNGEGASTLQ GEPRAPTPPS 500
GTEVTLAEVP LLDEVAPEPL LPAGEGCATL LNFDELPEPP ATFCDPEEVE 550
GESLAAPQTP TLPSALEELE QEQEPEPHLL TNGETTQKEG TQASEGYFSQ 600
SQEEEFAQSE ELCAKAPPPV FYNKPPEIDI TCWDADPVPE EEEGFEGGD 649
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.
VSP_028175Add
BLAST
Alternative sequencei319 – 3191G → GRPYCPFIKASDSGPSSSSS SSSSPPRTPFPYITCHRTPN LSSSLPC in isoform 3.
VSP_053443

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [Q16643-1]
ENST00000393565; ENSP00000377195; ENSG00000113758. [Q16643-3]
GeneIDi1627.
KEGGihsa:1627.
UCSCiuc003mgx.2. human. [Q16643-2]
uc003mgy.2. human. [Q16643-1]

Polymorphism databases

DMDMi215274247.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS4420.1. [Q16643-1 ]
CCDS4421.1. [Q16643-2 ]
PIRi JN0809.
T14763.
RefSeqi NP_004386.2. NM_004395.3.
NP_543157.1. NM_080881.2.
XP_005265884.1. XM_005265827.2. [Q16643-3 ]
UniGenei Hs.130316.

3D structure databases

ProteinModelPortali Q16643.
SMRi Q16643. Positions 13-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107995. 54 interactions.
IntActi Q16643. 34 interactions.
MINTi MINT-1149054.
STRINGi 9606.ENSP00000292385.

PTM databases

PhosphoSitei Q16643.

Polymorphism databases

DMDMi 215274247.

2D gel databases

OGPi Q16643.

Proteomic databases

MaxQBi Q16643.
PaxDbi Q16643.
PRIDEi Q16643.

Protocols and materials databases

DNASUi 1627.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000292385 ; ENSP00000292385 ; ENSG00000113758 . [Q16643-2 ]
ENST00000309007 ; ENSP00000308532 ; ENSG00000113758 . [Q16643-1 ]
ENST00000393565 ; ENSP00000377195 ; ENSG00000113758 . [Q16643-3 ]
GeneIDi 1627.
KEGGi hsa:1627.
UCSCi uc003mgx.2. human. [Q16643-2 ]
uc003mgy.2. human. [Q16643-1 ]

Organism-specific databases

CTDi 1627.
GeneCardsi GC05M176883.
H-InvDB HIX0005464.
HGNCi HGNC:2695. DBN1.
HPAi CAB008367.
HPA051452.
MIMi 126660. gene.
neXtProti NX_Q16643.
PharmGKBi PA27163.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG329456.
HOGENOMi HOG000015304.
HOVERGENi HBG000823.
OMAi CANLLNF.
OrthoDBi EOG7X3QR9.
PhylomeDBi Q16643.
TreeFami TF318935.

Enzyme and pathway databases

SignaLinki Q16643.

Miscellaneous databases

ChiTaRSi DBN1. human.
GeneWikii DBN1.
GenomeRNAii 1627.
NextBioi 35464922.
PROi Q16643.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16643.
Bgeei Q16643.
CleanExi HS_DBN1.
Genevestigatori Q16643.

Family and domain databases

Gene3Di 3.40.20.10. 1 hit.
InterProi IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028438. Drebrin.
[Graphical view ]
PANTHERi PTHR10829:SF1. PTHR10829:SF1. 1 hit.
Pfami PF00241. Cofilin_ADF. 1 hit.
[Graphical view ]
SMARTi SM00102. ADF. 1 hit.
[Graphical view ]
PROSITEi PS51263. ADF_H. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  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. 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 9, 2014
This is version 137 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

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