CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018320
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein L-like 
Protein Synonyms/Alias
 hnRNPLL; Stromal RNA-regulating factor 
Gene Name
 HNRNPLL 
Gene Synonyms/Alias
 HNRPLL; SRRF; BLOCK24 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71EAGGSHHKVSVSPVVubiquitination[1, 2]
222VLCAQKAKAALNGADubiquitination[3]
261NDSWDYTKPYLGRRDubiquitination[1, 2, 3]
491KYKVFDAKPSAKTLSubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. 
Sequence Annotation
 DOMAIN 76 150 RRM 1.
 DOMAIN 166 244 RRM 2.
 DOMAIN 335 409 RRM 3.
 MOD_RES 68 68 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 542 AA 
Protein Sequence
MSSSSSSPRE TYEEDREYES QAKRLKTEEG EIDYSAEEGE NRREATPRGG GDGGGGGRSF 60
SQPEAGGSHH KVSVSPVVHV RGLCESVVEA DLVEALEKFG TICYVMMMPF KRQALVEFEN 120
IDSAKECVTF AADEPVYIAG QQAFFNYSTS KRITRPGNTD DPSGGNKVLL LSIQNPLYPI 180
TVDVLYTVCN PVGKVQRIVI FKRNGIQAMV EFESVLCAQK AKAALNGADI YAGCCTLKIE 240
YARPTRLNVI RNDNDSWDYT KPYLGRRDRG KGRQRQAILG EHPSSFRHDG YGSHGPLLPL 300
PSRYRMGSRD TPELVAYPLP QASSSYMHGG NPSGSVVMVS GLHQLKMNCS RVFNLFCLYG 360
NIEKVKFMKT IPGTALVEMG DEYAVERAVT HLNNVKLFGK RLNVCVSKQH SVVPSQIFEL 420
EDGTSSYKDF AMSKNNRFTS AGQASKNIIQ PPSCVLHYYN VPLCVTEETF TKLCNDHEVL 480
TFIKYKVFDA KPSAKTLSGL LEWECKTDAV EALTALNHYQ IRVPNGSNPY TLKLCFSTSS 540
HL 542 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0006397; P:mRNA processing; IEA:InterPro.
 GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB. 
Interpro
 IPR006536; HnRNP-L_PTB.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
  
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS