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Protein Page:
HNRPLL (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
HNRPLL RNA-binding protein that functions as regulator of alternative splicing for multiple target mRNAs, including PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC. Interacts with HNRNPL. Up-regulated in stimulated T-cells. Widely expressed. Detected in bone marrow stroma cells, skeletal muscle, heart, placenta, pancreas, kidney and lung. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Unknown function
Cellular Component: ribonucleoprotein complex; nucleus
Molecular Function: mRNA binding; protein binding; nucleotide binding
Biological Process: mRNA processing; positive regulation of RNA splicing
Reference #:  Q8WVV9 (UniProtKB)
Alt. Names/Synonyms: Heterogeneous nuclear ribonucleoprotein L-like; HNRLL; hnRNPLL; HNRPLL; SRRF; stromal RNA regulating factor; Stromal RNA-regulating factor
Gene Symbols: HNRPLL
Molecular weight: 60,083 Da
Basal Isoelectric point: 7.83  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HNRPLL

Protein Structure Not Found.


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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

 
0 1 - gap
0 1 S2 ______MSSSSSSPR
0 1 S3 _____MSSSSSSPRE
0 2 S4 ____MSSSSSSPRET
0 2 S5 ___MSSSSSSPRETY
0 1 S7 _MSSSSSSPRETYEE
0 1 T11 SSSSPRETYEEDREy
0 4 Y18-p TYEEDREyESQAKRL
0 1 S20 EEDREyESQAKRLKT
0 1 Y34-p TEEGEIDysAEEGEN
0 13 S35-p EEGEIDysAEEGENR
0 5 T46-p GENRREAtPRGGGDG
0 1 - gap
0 1 - gap
0 3 S59-p DGGGGGRsFsQPEAG
0 12 S61-p GGGGRsFsQPEAGGs
0 5 S68-p sQPEAGGsHHkVSVs
0 1 K71-u EAGGsHHkVSVsPVV
0 1 S75-p sHHkVSVsPVVHVRG
0 1 K261-u NDSWDYTkPYLGRRD
0 1 S411-p VCVSKQHsVVPSQIF
0 1 K434 YKDFAMSKNNRFTSA
0 1 E504 LSGLLEWECKTDAVE
0 3 Y530 VPNGSNPYTLKLCFS
0 1 - gap
  mouse

► Hide Isoforms
 
S2-p ______MsssssSsP
S3-p _____MsssssSsPK
S4-p ____MsssssSsPKE
S5-p ___MsssssSsPKEE
S6-p __MsssssSsPKEEt
S8-p MsssssSsPKEEtYE
T13-p sSsPKEEtYEEDREF
F20 tYEEDREFEsQAKRL
S22-p EEDREFEsQAKRLKT
Y36 TEEGEIVYsAEESEN
S37-p EEGEIVYsAEESENR
T48 SENRQEATPQAGSDs
S55-p TPQAGSDsDSGGGDG
S94 GDGDEGGSGGDEGGS
S107 GSGGGPRSMPLSTEG
P109 GGGPRSMPLSTEGGG
S117 LSTEGGGSHHKVSVS
K120 EGGGSHHKVSVSPVV
S124 SHHKVSVSPVVHVRG
K310 NDSWDYTKPYLGRRD
S460 VCVSKQHSVVPSQIF
K483-u YKDFAMSkNNRFTSA
K553-u LSGLLEWkCKTDAVE
Y579-p VPNGSNPyTLKLCFS
- gap
  HNRPLL iso5  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S64-p YVYVVFHsSASFENF
  rat

 
- gap
S2 ______MSSTSSSPK
S3 _____MSSTSSSPKE
T4 ____MSSTSSSPKEE
S5 ___MSSTSSSPKEET
S7 _MSSTSSSPKEETYE
T12 SSSPKEETYEEDREF
F19 TYEEDREFESQAKRL
S21 EEDREFESQAKRLKT
Y35 TEEGEIVYsAEESEN
S36-p EEGEIVYsAEESENR
T47 SENRQEATPQAGSDS
S54 TPQAGSDSDSGGGDR
S94-p GDGDERGsGGDEGGS
S107 GSGGGPRSMPPSTEG
P109 GGGPRSMPPSTEGGG
S117 PSTEGGGSHHKVSVS
K120 EGGGSHHKVSVSPVV
S124 SHHKVSVSPVVHVRG
K310 NDSWDYTKPYLGRRD
S460 VCVSKQHSVVPSQIF
K483 YKDFAMSKNNRFTSA
K553 LSGLLEWKCKTDAVE
Y579 VPNGSNPYTLKLCFS
- gap
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