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Protein Page:
RBM17 (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
RBM17 Splice factor that binds to the single stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia. Note: This description may include information from UniProtKB.
Protein type: RNA splicing; Spliceosome; RNA-binding
Chromosomal Location of Human Ortholog: 10p15.1
Molecular Function: protein binding
Biological Process: alternative nuclear mRNA splicing, via spliceosome
Reference #:  Q96I25 (UniProtKB)
Alt. Names/Synonyms: 45 kDa-splicing factor; DKFZp686F13131; MGC14439; RBM17; RNA binding motif protein 17; RNA-binding motif protein 17; SPF45; Splicing factor 45; splicing factor 45kDa
Gene Symbols: RBM17
Molecular weight: 44,962 Da
Basal Isoelectric point: 5.76  Predict pI for various phosphorylation states
Select Structure to View Below

RBM17

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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Sites Implicated In
RNA splicing, altered: S48‑p, S62‑p, S202‑p, S204‑p, S222‑p, S266‑p, S288‑p, S291‑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

 
0 5 S2‑p ______MsLYDDLGV
0 1 T11 YDDLGVETSDSKTEG
0 1 S12 DDLGVETSDSKTEGW
0 1 S14 LGVETSDSKTEGWSk
0 1 K21‑ac SKTEGWSkNFkLLQs
0 1 K24‑sm EGWSkNFkLLQsQLQ
0 2 S28‑p kNFkLLQsQLQVKKA
1 0 S48‑p KSQRTKQsTVLAPVI
0 2 K58‑ac LAPVIDLkRGGsSDD
1 2 S62‑p IDLkRGGsSDDRQIV
1 23 T71‑p DDRQIVDtPPHVAAG
0 1 S85‑p GLKDPVPsGFSAGEV
0 1 K129‑ac QRELERQkEIEEREK
0 361 S155‑p ARRPDPDsDEDEDyE
0 244 Y161‑p DsDEDEDyERERRKR
0 27 S169‑p ERERRKRsMGGAAIA
0 1 T179‑p GAAIAPPtsLVEKDK
0 1 S180‑p AAIAPPtsLVEKDKE
0 11 Y194‑p ELPRDFPyEEDSRPR
1 0 S202‑p EEDSRPRsQsSKAAI
1 1 S204‑p DSRPRsQsSKAAIPP
0 7 Y214‑p AAIPPPVyEEQDRPR
2 29 S222‑p EEQDRPRsPtGPsNs
0 9 T224‑p QDRPRsPtGPsNsFL
0 5 S227‑p PRsPtGPsNsFLANM
0 3 S229‑p sPtGPsNsFLANMGG
0 2 T237‑p FLANMGGtVAHKIMQ
0 1 K256‑ac REGQGLGkHEQGLST
1 3 S266‑p QGLSTALsVEKTSKR
0 1 K285‑ac IVGDATEkDAsKKsD
1 0 S288‑p DATEkDAsKKsDsNP
1 2 S291‑p EkDAsKKsDsNPLTE
0 4 S293‑p DAsKKsDsNPLTEIL
0 1 T304‑p TEILKCPtKVVLLRN
0 1 K327 EDLEVETKEECEKYG
0 1 K332 ETKEECEKYGKVGKC
0 1 K338 EKYGKVGKCVIFEIP
0 1 K391‑ac ACFYNLDkFRVLDLA
  mouse

 
S2‑p ______MsLYDDLGV
T11‑p YDDLGVEtsDsKTEG
S12‑p DDLGVEtsDsKTEGW
S14‑p LGVEtsDsKTEGWSK
K21 sKTEGWSKNFKLLQS
K24 EGWSKNFKLLQSQLQ
S28 KNFKLLQSQLQVKKA
S48 KSQRTKQSTVLAPVI
K58‑ac LAPVIDLkRGGsSDD
S62‑p IDLkRGGsSDDRQIA
T71‑p DDRQIADtPPHVAAG
S85 GLKDPVPSGFSAGEV
K129 QRELERQKEIEEREK
S155‑p SRRPDPDsDEDEDyE
Y161‑p DsDEDEDyERERRKR
S169‑p ERERRKRsMGGAAIA
T179 GAAIAPPTSLVEKDK
S180 AAIAPPTSLVEKDKE
Y194 ELPRDFPYEEDSRPR
S202 EEDSRPRSQSSKAAI
S204 DSRPRSQSSKAAIPP
Y214‑p AAIPPPVyEEPDRPR
S222‑p EEPDRPRsPtGPsNs
T224‑p PDRPRsPtGPsNsFL
S227‑p PRsPtGPsNsFLANM
S229‑p sPtGPsNsFLANMGG
T237‑p FLANMGGtVAHKIMQ
K256 REGQGLGKHEQGLST
S266 QGLSTALSVEKTSKR
K285 IVGDATEKGEAQDAS
S292 KGEAQDASKKSDSNP
S295 AQDASKKSDSNPLTE
S297 DASKKSDSNPLTEIL
T308 TEILKCPTKVVLLRN
K331‑ac EDLEVETkEECEkYG
K336‑ac ETkEECEkYGKVGkC
K342‑ac EkYGKVGkCVIFEIP
K395 ACFYNLDKFRVLDLA
  rat

 
S2‑p ______MsLYDDLGV
T11 YDDLGVETSDSKTEG
S12 DDLGVETSDSKTEGW
S14 LGVETSDSKTEGWSK
K21 SKTEGWSKNFKLLQS
K24 EGWSKNFKLLQSQLQ
S28 KNFKLLQSQLQVKKA
S48 KSQRTKQSTVLAPVI
K58 LAPVIDLKRGGSSDD
S62 IDLKRGGSSDDRQIV
T71‑p DDRQIVDtPPHVAAG
S85 GLKDPVPSGFSAGEV
K129 QRELERQKEIEEREK
S155‑p SRRPDPDsDEDEDYE
Y161 DsDEDEDYERERRKR
S169‑p ERERRKRsMGGAAIA
T179 GAAIAPPTSLVEKDK
S180 AAIAPPTSLVEKDKE
Y194 ELPRDFPYEEDSRPR
S202 EEDSRPRSQSSKAAI
S204 DSRPRSQSSKAAIPP
Y214 AAIPPPVYEEPDRPR
S222‑p EEPDRPRsPTGPSNS
T224 PDRPRsPTGPSNSFL
S227 PRsPTGPSNSFLANM
S229 sPTGPSNSFLANMGG
T237 FLANMGGTVAHKIMQ
K256 REGQGLGKHEQGLST
S266 QGLSTALSVEKTSKR
K285 IVGDATEKGESQDAS
S292 KGESQDASKKSDSNP
S295 SQDASKKSDSNPLTE
S297 DASKKSDSNPLTEIL
T308 TEILKCPTKVVLLRN
K331 EDLEVETKEECEKYG
K336 ETKEECEKYGKVGKC
K342 EKYGKVGKCVIFEIP
K395 ACFYNLDKFRVLDLA
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