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Protein Page:
HNRPLL (mouse)
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
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; nucleic acid binding; RNA binding; nucleotide binding
Biological Process: mRNA processing; positive regulation of RNA splicing
Reference #:  Q921F4 (UniProtKB)
Alt. Names/Synonyms: 2510028H02Rik; 2810036L13Rik; AI256697; AI852082; Heterogeneous nuclear ribonucleoprotein L-like; HNRLL; Hnrpll
Gene Symbols: Hnrpll
Molecular weight: 64,125 Da
Basal Isoelectric point: 5.57  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.


       mouse

► Hide Isoforms
 
0 1 S2-p ______MsssssSsP
0 1 S3-p _____MsssssSsPK
0 1 S4-p ____MsssssSsPKE
0 2 S5-p ___MsssssSsPKEE
0 2 S6-p __MsssssSsPKEEt
0 1 S8-p MsssssSsPKEEtYE
0 1 T13-p sSsPKEEtYEEDREF
0 4 F20 tYEEDREFEsQAKRL
0 1 S22-p EEDREFEsQAKRLKT
0 1 Y36 TEEGEIVYsAEESEN
0 15 S37-p EEGEIVYsAEESENR
0 6 T48 SENRQEATPQAGSDs
0 1 S55-p TPQAGSDsDSGGGDG
0 1 S94 GDGDEGGSGGDEGGS
0 4 S107 GSGGGPRSMPLSTEG
0 14 P109 GGGPRSMPLSTEGGG
0 7 S117 LSTEGGGSHHKVSVS
0 1 K120 EGGGSHHKVSVSPVV
0 1 S124 SHHKVSVSPVVHVRG
0 1 K310-ac NDSWDYTkPYLGRRD
0 1 K310 NDSWDYTKPYLGRRD
0 1 S333 AILGDHPSSFRHDGY
0 1 S460 VCVSKQHSVVPSQIF
0 1 K483-ub YKDFAMSkNNRFTSA
0 1 K553-ub LSGLLEWkCKTDAVE
0 3 Y579-p VPNGSNPyTLKLCFS
0 1 - gap
  HNRPLL iso5  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- under review  
- gap
- gap
- gap
- gap
- gap
- gap
S64-p YVYVVFHsSASFENF
  human

 
- gap
S2 ______MSSSSSSPR
S3 _____MSSSSSSPRE
S4 ____MSSSSSSPRET
S5 ___MSSSSSSPRETY
S7 _MSSSSSSPRETYEE
T11 SSSSPRETYEEDREy
Y18-p TYEEDREyESQAKRL
S20 EEDREyESQAKRLKT
Y34-p TEEGEIDysAEEGEN
S35-p EEGEIDysAEEGENR
T46-p GENRREAtPRGGGDG
- gap
- gap
S59-p DGGGGGRsFsQPEAG
S61-p GGGGRsFsQPEAGGs
S68-p sQPEAGGsHHkVSVs
K71-ub EAGGsHHkVSVsPVV
S75-p sHHkVSVsPVVHVRG
K261-ac NDSWDYTkPYLGRRD
K261-ub NDSWDYTkPYLGRRD
S284-p AILGEHPsSFRHDGY
S411-p VCVSKQHsVVPSQIF
K434 YKDFAMSKNNRFTSA
E504 LSGLLEWECKTDAVE
Y530 VPNGSNPYTLKLCFS
- gap
  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
K310 NDSWDYTKPYLGRRD
S333 AILGDHPSSFRHDGY
S460 VCVSKQHSVVPSQIF
K483 YKDFAMSKNNRFTSA
K553 LSGLLEWKCKTDAVE
Y579 VPNGSNPYTLKLCFS
- gap
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