Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
DBN1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DBN1 a cytoplasmic actin-binding protein thought to play a role in the process of neuronal growth. It is a member of the drebrin family of proteins that are developmentally regulated in the brain. A decrease in the amount of this protein in the brain has been implicated as a possible contributing factor in the pathogenesis of memory disturbance in Alzheimer's disease. Expressed in brain neurons, heart, placenta, skeletal muscle, kidney and pancreas. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Cytoskeletal protein; Actin binding protein; Motility/polarity/chemotaxis
Cellular Component: dendrite; cytoplasm; gap junction; plasma membrane; actomyosin; cell cortex; actin cytoskeleton
Molecular Function: protein binding; actin binding; profilin binding
Biological Process: maintenance of cellular protein localization; regulation of dendrite development; actin filament organization; regulation of neuronal synaptic plasticity
Reference #:  Q16643 (UniProtKB)
Alt. Names/Synonyms: D0S117E; DBN1; Developmentally-regulated brain protein; DKFZp434D064; DREB; Drebrin; drebrin 1; drebrin E; drebrin E2; drebrin-1
Gene Symbols: DBN1
Molecular weight: 71,429 Da
Basal Isoelectric point: 4.41  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DBN1

Protein Structure Not Found.


STRING  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
cytoskeletal reorganization: S142‑p
molecular association, regulation: S142‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 3 S5-p ___MAGVsFsGHRLE
0 4 S7-p _MAGVsFsGHRLELL
0 1 Y32-p SAADWALyTYEDGSD
0 2 Y65-p FENQKVMyGFCSVkD
0 3 K71-ub MyGFCSVkDsQAALP
0 5 S73-p GFCSVkDsQAALPKY
0 3 S134-p GAIGQRLsNGLARLs
1 14 S141-p sNGLARLssPVLHRL
2 75 S142-p NGLARLssPVLHRLR
0 5 T162-p NAEPVGTtyQKTdAA
0 77 Y163-p AEPVGTtyQKTdAAV
0 1 K165 PVGTtyQKTdAAVEM
0 1 D167-ca GTtyQKTdAAVEMKR
0 1 K173 TdAAVEMKRINREQF
0 4 T241-p EHRRKQQtLEAEEAK
0 5 S274-p THMKKSEsEVEEAAA
0 1 K295-sc DNPREFFkQQERVAS
0 1 S307-p VASASAGsCDVPsPF
0 5 S312-p AGsCDVPsPFNHRPG
0 1 - gap
0 1 - gap
1 5 - gap
0 4 S320-p PFNHRPGsHLDsHRR
0 2 S324-p RPGsHLDsHRRMAPt
0 22 T331-p sHRRMAPtPIPtRsP
0 22 T335-p MAPtPIPtRsPsDss
0 34 S337-p PtPIPtRsPsDsstA
0 44 S339-p PIPtRsPsDsstAst
0 8 S341-p PtRsPsDsstAstPV
0 15 S342-p tRsPsDsstAstPVA
0 10 T343-p RsPsDsstAstPVAE
0 19 S345-p PsDsstAstPVAEQI
0 52 T346-p sDsstAstPVAEQIE
0 2 T377-p PPPPAQEtQEPsPIL
0 2 S381-p AQEtQEPsPILDSEE
0 1 S416-p APPRGPGsPAEDLMF
0 3 T497-p QGEPRAPtPPSGTEV
0 1 T559-p ESLAAPQtPTLPSAL
0 2 S594-p QKEGTQAsEGyFsQs
0 63 Y597-p GTQAsEGyFsQsQEE
0 4 S599-p QAsEGyFsQsQEEEF
1 20 S601-p sEGyFsQsQEEEFAQ
0 1 S609-p QEEEFAQsEELCAKA
0 30 Y622-p KAPPPVFyNKPPEID
  DBN1 iso3  
S5 ___MAGVSFSGHRLE
S7 _MAGVSFSGHRLELL
Y32 SAADWALYTYEDGSD
Y65 FENQKVMYGFCSVKD
K71 MYGFCSVKDSQAALP
S73 GFCSVKDSQAALPKY
S134 GAIGQRLSNGLARLS
S141 SNGLARLSsPVLHRL
S142-p NGLARLSsPVLHRLR
T162 NAEPVGTTYQKTDAA
Y163 AEPVGTTYQKTDAAV
K165 PVGTTYQKTDAAVEM
D167 GTTYQKTDAAVEMKR
K173 TDAAVEMKRINREQF
T241 EHRRKQQTLEAEEAK
S274 THMKKSESEVEEAAA
K295 DNPREFFKQQERVAS
S307 VASASAGSCDVPSPF
S312 AGSCDVPSPFNHRPG
S334 KASDSGPSSSSSSSS
S340 PSSSSSSSSsPPRTP
S342-p SSSSSSSsPPRTPFP
S366 LSSSLPCSHLDSHRR
S370 LPCSHLDSHRRMAPT
T377 SHRRMAPTPIPTRSP
T381 MAPTPIPTRSPSDSS
S383 PTPIPTRSPSDSSTA
S385 PIPTRSPSDSSTAST
S387 PTRSPSDSSTASTPV
S388 TRSPSDSSTASTPVA
T389 RSPSDSSTASTPVAE
S391 PSDSSTASTPVAEQI
T392 SDSSTASTPVAEQIE
T423 PPPPAQETQEPSPIL
S427 AQETQEPSPILDSEE
S462 APPRGPGSPAEDLMF
T543 QGEPRAPTPPSGTEV
T605 ESLAAPQTPTLPSAL
S640 QKEGTQASEGYFSQS
Y643 GTQASEGYFSQSQEE
S645 QASEGYFSQSQEEEF
S647 SEGYFSQSQEEEFAQ
S655 QEEEFAQSEELCAKA
Y668 KAPPPVFYNKPPEID
  mouse

► Hide Isoforms
 
S5 ___MAGVSFsGHRLE
S7-p _MAGVSFsGHRLELL
Y32 SAADWALYTYEDGSD
Y65 FENQKVMYGFCSVKD
K71 MYGFCSVKDsQAALP
S73-p GFCSVKDsQAALPKY
S134-p GAIGQRLsNGLARLs
S141-p sNGLARLssPVLHRL
S142-p NGLARLssPVLHRLR
T162-p NAEPVGTtyQkTDAA
Y163-p AEPVGTtyQkTDAAV
K165-ac PVGTtyQkTDAAVEM
D167 GTtyQkTDAAVEMkR
K173-ac TDAAVEMkRINREQF
S241-p EHRRKQQsLEAEEAK
S274-p SQMKKSEsEVEEAAA
R295 DNPREFFRQQERVAS
S307 VASASGGSCDAPAPA
- gap
S336-p KASDSGPsSSSSSsS
S342-p PsSSSSSsSsPPRTP
S344-p SSSSSsSsPPRTPFP
S368 LSSSLPCSHLDSHRR
S372 LPCSHLDSHRRMAPt
T379-p SHRRMAPtPIPtRsP
T383-p MAPtPIPtRsPsDss
S385-p PtPIPtRsPsDsstA
S387-p PIPtRsPsDsstAst
S389-p PtRsPsDsstAstPI
S390-p tRsPsDsstAstPIA
T391-p RsPsDsstAstPIAE
S393-p PsDsstAstPIAEQI
T394-p sDsstAstPIAEQIE
A425 PPPPTQEAQETTPSL
T429 TQEAQETTPSLDEEL
S468 EPPLLQSSPLEDSMC
T550-p QAEPRVPtPPSGAEA
V612 ETLAASQVLTMPSAL
S651 QKEGTQASEGyFsQs
Y654-p GTQASEGyFsQsQEE
S656-p QASEGyFsQsQEEEF
S658-p SEGyFsQsQEEEFAQ
S666 QEEEFAQSEEPCAKV
Y679 KVPPPVFYNKPPEID
  DBN1 iso3  
S5 ___MAGVSFSGHRLE
S7 _MAGVSFSGHRLELL
Y32 SAADWALYTYEDGSD
Y65 FENQKVMYGFCSVKD
K71 MYGFCSVKDSQAALP
S73 GFCSVKDSQAALPKY
S134 GAIGQRLSNGLARLS
S141 SNGLARLSSPVLHRL
S142 NGLARLSSPVLHRLR
T162 NAEPVGTTYQKTDAA
Y163 AEPVGTTYQKTDAAV
K165 PVGTTYQKTDAAVEM
D167 GTTYQKTDAAVEMKR
K173 TDAAVEMKRINREQF
S241 EHRRKQQSLEAEEAK
S274 SQMKKSESEVEEAAA
R295 DNPREFFRQQERVAS
S307 VASASGGSCDAPAPA
- gap
- gap
- gap
- gap
S322 PFNHRPGSHLDsHRR
S326-p RPGSHLDsHRRMAPT
T333 sHRRMAPTPIPTRSP
T337 MAPTPIPTRSPSDSS
S339 PTPIPTRSPSDSSTA
S341 PIPTRSPSDSSTAST
S343 PTRSPSDSSTASTPI
S344 TRSPSDSSTASTPIA
T345 RSPSDSSTASTPIAE
S347 PSDSSTASTPIAEQI
T348 SDSSTASTPIAEQIE
A379 PPPPTQEAQETTPSL
T383 TQEAQETTPSLDEEL
S422 EPPLLQSSPLEDSMC
T504 QAEPRVPTPPSGAEA
V566 ETLAASQVLTMPSAL
S605 QKEGTQASEGYFSQS
Y608 GTQASEGYFSQSQEE
S610 QASEGYFSQSQEEEF
S612 SEGYFSQSQEEEFAQ
S620 QEEEFAQSEEPCAKV
Y633 KVPPPVFYNKPPEID
  rat

 
S5 ___MAGVSFsGHRLE
S7-p _MAGVSFsGHRLELL
Y32 SAADWALYTYEDGSD
Y65 FENQKVMYGFCSVKD
K71 MYGFCSVKDSQAALP
S73 GFCSVKDSQAALPKY
S134 GAIGQRLSNGLARLS
S141 SNGLARLSsPVLHRL
S142-p NGLARLSsPVLHRLR
T162 NAEPVGTTYQKTDAA
Y163 AEPVGTTYQKTDAAV
K165 PVGTTYQKTDAAVEM
D167 GTTYQKTDAAVEMKR
K173 TDAAVEMKRINREQF
S241 EHRRKQQSLEAEEAK
S274 SQMKKSESEVEEAAA
R295 DNPREFFRQQERVAS
S307 VASASGGSCDAPSPF
S312 GGSCDAPSPFNHRPG
S334 KASDSGPSSSSSSSS
S340 PSSSSSSSSsPPRTP
S342-p SSSSSSSsPPRTPFP
S366 LSSSLPCSHLDSHRR
S370 LPCSHLDSHRRMAPT
T377 SHRRMAPTPIPTRsP
T381 MAPTPIPTRsPsDSS
S383-p PTPIPTRsPsDSSTA
S385-p PIPTRsPsDSSTASt
S387 PTRsPsDSSTAStPI
S388 TRsPsDSSTAStPIT
T389 RsPsDSSTAStPITE
S391 PsDSSTAStPITEQI
T392-p sDSSTAStPITEQIE
A423 PPPPAQEAQESAPRL
A427 AQEAQESAPRLDGEE
S467 EPPLLQSSPTEDLMC
T549 QAEPRVPTPPSGAEA
V612 EPLAASQVLTMPSAL
S652 KEGTQQASEGYFSQs
Y655 TQQASEGYFSQsQEE
S657 QASEGYFSQsQEEEF
S659-p SEGYFSQsQEEEFAQ
S667 QEEEFAQSEEPCAKA
Y680 KAPPPVFYNKPPEID
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.