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Protein Page:
DROSHA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DROSHA a nuclear type-III RNase that, along with the DGCR8, executes the initial step of microRNA (miRNA) processing in the nucleus. Cleaves the local hairpin structures embedded in long primary microRNA transcripts (pri-miRNAs) into pre-miRNAs. Involved in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Interacts with Sp1. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: RNA processing; RNA-binding; EC 3.1.26.3; Nucleolus; Ribonuclease
Chromosomal Location of Human Ortholog: 5p13.3
Cellular Component: nucleolus; nucleoplasm
Molecular Function: double-stranded RNA binding; lipopolysaccharide binding; metal ion binding; protein binding; protein homodimerization activity; ribonuclease III activity
Biological Process: defense response to Gram-negative bacterium; defense response to Gram-positive bacterium; gene expression; pre-microRNA processing; primary microRNA processing; ribosome biogenesis and assembly; RNA interference, production of siRNA; RNA-mediated gene silencing; rRNA catabolic process
Reference #:  Q9NRR4 (UniProtKB)
Alt. Names/Synonyms: Drosha; drosha, double-stranded RNA-specific endoribonuclease; drosha, ribonuclease type III; ETOHI2; HSA242976; nuclear RNase III Drosha; p241; putative protein p241 which interacts with transcription factor Sp1; putative ribonuclease III; RANSE3L; Ribonuclease 3; Ribonuclease III; ribonuclease III, nuclear; ribonuclease type III, nuclear; RN3; RNase III; RNASE3L; RNASEN; RNC
Gene Symbols: DROSHA
Molecular weight: 159,316 Da
Basal Isoelectric point: Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DROSHA

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: S300‑p, S302‑p
molecular association, regulation: S221‑p, S255‑p, T274‑p, S300‑p, S355‑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


 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
1 3 S221‑p KAPSERRsPERLKHy
0 5 Y228‑p sPERLKHyDDHRHRD
0 2 S237‑p DHRHRDHsHGRGERH
1 0 S255‑p DRRERGRsPDRRRQD
0 1 S267‑p RQDSRYRsDyDRGRt
0 1 Y269‑p DSRYRsDyDRGRtPs
1 1 T274‑p sDyDRGRtPsRHRSY
0 1 S276‑p yDRGRtPsRHRSYER
3 11 S300‑p RHRDNRRsPsLERSy
2 8 S302‑p RDNRRsPsLERSyKK
0 1 S306 RsPsLERSyKKEYKR
0 1 Y307‑p sPsLERSyKKEYKRS
0 1 S317‑p EYKRSGRsYGLSVVP
1 8 S355‑p LEIVNHRsPsREKKR
0 7 S357‑p IVNHRsPsREKKRAR
0 9 S373‑p EEEKDRWsDNQSSGK
0 1 S491‑p ECESDEDsTCSSSSD
0 1 S698‑p DGGKEVLsMHQILLy
0 1 Y705‑p sMHQILLyLLRCSKA
0 1 T747‑p MIVTNPGtKPSSVRI
0 1 S796‑p QYQKLWKsYVKLRHL
0 5 S807‑p LRHLLANsPKVKQTD
0 1 K1250‑ub VCFFPRLkEFILNQD
0 1 S1293‑p TLQTVGPsHARTYTV
  DROSHA iso2  
S221 KAPSERRSPERLKHY
Y228 SPERLKHYDDHRHRD
S237 DHRHRDHSHGRGERH
S255 DRRERGRSPDRRRQD
S267 RQDSRYRSDYDRGRT
Y269 DSRYRSDYDRGRTPS
T274 SDYDRGRTPSRHRSY
S276 YDRGRTPSRHRSYER
- gap
- gap
- gap
- gap
- gap
S287 SYERSSRSPSREKKR
S289 ERSSRSPSREKKRAR
S305 EEEKDRWSDNQSSGK
S423 ECESDEDSTCSSSSD
S630 DGGKEVLSMHQILLY
Y637 SMHQILLYLLRCSKA
T679 MIVTNPGTKPSSVRI
S728 QYQKLWKSYVKLRHL
S739 LRHLLANSPKVKQTD
K1182 VCFFPRLKEFILNQD
S1225 TLQTVGPSHARTYTV
  DROSHA iso3  
S221 KAPSERRSPERLKHY
Y228 SPERLKHYDDHRHRD
S237 DHRHRDHSHGRGERH
S255 DRRERGRSPDRRRQD
S267 RQDSRYRSDYDRGRT
Y269 DSRYRSDYDRGRTPS
T274 SDYDRGRTPSRHRSY
S276 YDRGRTPSRHRSYER
S300 RHRDNRRSPSLERSY
S302 RDNRRSPSLERSYKK
S306 RSPSLERSYKKEYKR
Y307 SPSLERSYKKEYKRS
- gap
S318 YKRSGSRSPSREKKR
S320 RSGSRSPSREKKRAR
S336 EEEKDRWSDNQSSGK
S454 ECESDEDSTCSSSSD
S661 DGGKEVLSMHQILLY
Y668 SMHQILLYLLRCSKA
T710 MIVTNPGTKPSSVRI
S759 QYQKLWKSYVKLRHL
S770 LRHLLANSPKVKQTD
- gap
- gap
  DROSHA iso4  
S221 KAPSERRSPERLKHY
Y228 SPERLKHYDDHRHRD
S237 DHRHRDHSHGRGERH
S255 DRRERGRSPDRRRQD
S267 RQDSRYRSDYDRGRT
Y269 DSRYRSDYDRGRTPS
T274 SDYDRGRTPSRHRSY
S276 YDRGRTPSRHRSYER
S300 RHRDNRRSPSLERSY
S302 RDNRRSPSLERSYKK
S306 RSPSLERSYKKEYKR
Y307 SPSLERSYKKEYKRS
- gap
S318 YKRSGSRSPSREKKR
S320 RSGSRSPSREKKRAR
S336 EEEKDRWSDNQSSGK
S454 ECESDEDSTCSSSSD
S661 DGGKEVLSMHQILLY
Y668 SMHQILLYLLRCSKA
T710 MIVTNPGTKPSSVRI
S759 QYQKLWKSYVKLRHL
S770 LRHLLANSPKVKQTD
K1213 VCFFPRLKEFILNQD
S1256 TLQTVGPSHARTYTV
  mouse

 
S219 KAQNERRSPERLKHY
Y226 SPERLKHYDDHRHRD
S235‑p DHRHRDHsHGRGERH
S253 ERRERGRSPERRRPE
S265 RPESRYRSDYDRGRT
Y267 ESRYRSDYDRGRTPP
T272 SDYDRGRTPPPRHRS
P275 DRGRTPPPRHRSYER
S299‑p RHREARRsPsLERsY
S301‑p REARRsPsLERsYKK
S305‑p RsPsLERsYKKEYKR
Y306 sPsLERsYKKEYKRS
S316 EYKRSGRSYALPVAP
S354‑p PENVNHRsPsREKKR
S356‑p NVNHRsPsREKKRAR
S372‑p EEEKDRWsDSQGSGK
S490 ECETDDDSTCSSSSD
S697 DGGKEVLSMHQILLY
Y704 SMHQILLYLLRCSKA
T746 MIVTNPGTKPSSVRI
S795 QYQKLWKSYVKLRHL
S806‑p LRHLLANsPKVKQTD
K1249 VCFFPRLKEFILNQD
S1292 TLQTVGPSHARTYTV
  rat

 
S213 KAQSERRSPERLKHY
Y220 SPERLKHYDDHRHRD
S229 DHRHRDHSHGRGERH
S247 ERRERGRSPERRRPE
S259 RPESRYRSEYDRGRT
Y261 ESRYRSEYDRGRTPP
T266 SEYDRGRTPPPRHRS
P269 DRGRTPPPRHRSYER
S293‑p RHRENRRsPsLERAY
S295‑p RENRRsPsLERAYKK
A299 RsPsLERAYKKEYKR
Y300 sPsLERAYKKEYKRS
S310 EYKRSGRSYGLPVTP
S348 QENVNHRSPSREKKR
S350 NVNHRSPSREKKRAR
S366 EEEKDRWSDSQSSGK
S484 ECETDEDSTCSSSSD
S691 DGGKEVLSMHQILLY
Y698 SMHQILLYLLRCSKA
T740 MIVTNPGTKPSSVRI
S789 QYQKLWKSYVKLRHL
S800 LRHLLANSPKVKQTD
- gap
- gap
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