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UniProtKB/Swiss-Prot entry Q4G0J3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LARP7_HUMAN
Primary accession number Q4G0J3
Secondary accession numbers B2ZHN6 Q3B7A9 Q9P1S7 Q9Y3Z8
Integrated into Swiss-Prot on March 20, 2007
Sequence was last modified on August 30, 2005 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 43)
Name and origin of the protein
Protein name La-related protein 7
Synonyms La ribonucleoprotein domain family member 7
P-TEFb-interaction protein for 7SK stability
PIP7S
Gene name
Name: LARP7
ORFNames: HDCMA18P
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
DOI=10.1038/embor.2008.72; PubMed=18483487 [NCBI, ExPASy, EBI, Israel, Japan]
Markert A., Grimm M., Martinez J., Wiesner J., Meyerhans A., Meyuhas O., Sickmann A., Fischer U.;
"The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes.";
EMBO Rep. 9:569-575(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Dendritic cell;
Zhao Z., Huang X., Li N., Zhu X., Cao X.;
"A novel gene from human dendritic cell.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-582 (ISOFORM 1).
TISSUE=Fetal brain;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
FUNCTION, AND MUTAGENESIS OF TYR-128.
DOI=10.1016/j.molcel.2008.01.003; PubMed=18249148 [NCBI, ExPASy, EBI, Israel, Japan]
He N., Jahchan N.S., Hong E., Li Q., Bayfield M.A., Maraia R.J., Luo K., Zhou Q.;
"A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis.";
Mol. Cell 29:588-599(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-258; SER-261; SER-273; SER-337 AND THR-338, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Negative transcriptional regulator of polymerase II genes, acting by means of the 7SK RNP system. Within the 7SK RNP complex, the positive transcription elongation factor b (P-TEFb) is sequestered in an inactive form, preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation.
  • SUBUNIT: Integral part of the 7SK RNP complex. Specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA. On stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex.
  • SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ4G0J3-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ4G0J3-2
    Features which should be applied to build the isoform sequence: VSP_024021.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
  • SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
  • SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
  • SEQUENCE CAUTION:
    • Sequence=ACD13786.1; Type=Erroneous initiation; Note=Translation N-terminally shortened
    • Sequence=EAX06284.1; Type=Erroneous initiation; Note=Translation N-terminally shortened
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
EU667388; ACD13786.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF068284; AAF65503.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471057; EAX06284.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066945; AAH66945.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107709; AAI07710.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049996; CAB43230.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00294742; -.
IPI00395536; -.
PIR T08692; T08692.
RefSeq NP_056269.1; -.
NP_057732.2; -.
UniGene Hs.713663
3D structure databases
ModBase Q4G0J3.
PTM databases
PhosphoSite Q4G0J3; -.
Organism-specific databases
GeneCards GC04P113777; -.
HGNC HGNC:24912; LARP7.
GenAtlas LARP7.
HPA HPA017600; -.
MIM 612026; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress Q4G0J3; -.
Bgee Q4G0J3; -.
CleanEx HS_LARP7; -.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0030529; Cellular component: ribonucleoprotein complex (inferred from electronic annotation from InterPro).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006396; Biological process: RNA processing (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR002344; Lupus_La.
IPR006630; Lupus_La_RNA_bd.
IPR014886; RRM_3.
IPR000504; RRM_RNP1.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF05383; La; 1.
PF00076; RRM_1; 1.
PF08777; RRM_3; 1.
Pfam graphical view of domain structure.
PRINTS PR00302; LUPUSLA.
SMART SM00715; LA; 1.
SM00360; RRM; 1.
SMART graphical view of domain structure.
PROSITE PS50961; HTH_LA; 1.
PS50102; RRM; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q4G0J3; -.
Genome annotation databases
Ensembl ENSG00000174720; Homo sapiens. [Contig view]
GeneID 51574; -.
KEGG hsa:51574; -.
Phylogenomic databases
HOVERGEN Q4G0J3; -.
OMA Q4G0J3; AKLNQPR.
Other
NextBio 55403; -.
SOURCE LARP7; Homo sapiens.
ProtoNet Q4G0J3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Nucleus; Phosphoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   582  582     La-related protein 7. PRO_0000281143
DOMAIN   28   122  95     HTH La-type RNA-binding. 
DOMAIN   125   203  79     RRM. 
COMPBIAS   202   368  167     Lys-rich. 
MOD_RES   257   257        Phosphothreonine. 
MOD_RES   258   258        Phosphoserine. 
MOD_RES   261   261        Phosphoserine. 
MOD_RES   273   273        Phosphoserine. 
MOD_RES   337   337        Phosphoserine. 
MOD_RES   338   338        Phosphothreonine. 
MOD_RES   440   440        Phosphothreonine (By similarity). 
VAR_SEQ   1   368        Missing (in isoform 2). VSP_024021
MUTAGEN   128   128        Y->D: Loss of 7SK RNA-binding and marked decrease in 7SK RNP complex formation. 
CONFLICT   295   295        R -> G (in Ref. 4; AAI07710). 
CONFLICT   516   516        K -> R (in Ref. 2; AAF65503 and 5; CAB43230). 
CONFLICT   560   560        K -> Q (in Ref. 5; CAB43230). 
Sequence information
Length: 582 AA [This is the length of the unprocessed precursor] Molecular weight: 66899 Da [This is the MW of the unprocessed precursor] CRC64: 04209B8159A5738C [This is a checksum on the sequence]
        10         20         30         40         50         60 
METESGNQEK VMEEESTEKK KEVEKKKRSR VKQVLADIAK QVDFWFGDAN LHKDRFLREQ 

        70         80         90        100        110        120 
IEKSRDGYVD ISLLVSFNKM KKLTTDGKLI ARALRSSAVV ELDLEGTRIR RKKPLGERPK 

       130        140        150        160        170        180 
DEDERTVYVE LLPKNVNHSW IERVFGKCGN VVYISIPHYK STGDPKGFAF VEFETKEQAA 

       190        200        210        220        230        240 
KAIEFLNNPP EEAPRKPGIF PKTVKNKPIP ALRVVEEKKK KKKKKGRMKK EDNIQAKEEN 

       250        260        270        280        290        300 
MDTSNTSISK MKRSRPTSEG SDIESTEPQK QCSKKKKKRD RVEASSLPEV RTGKRKRSSS 

       310        320        330        340        350        360 
EDAESLAPRS KVKKIIQKDI IKEASEASKE NRDIEISTEE EKDTGDLKDS SLLKTKRKHK 

       370        380        390        400        410        420 
KKHKERHKMG EEVIPLRVLS KSEWMDLKKE YLALQKASMA SLKKTISQIK SESEMETDSG 

       430        440        450        460        470        480 
VPQNTGMKNE KTANREECRT QEKVNATGPQ FVSGVIVKII STEPLPGRKQ VRDTLAAISE 

       490        500        510        520        530        540 
VLYVDLLEGD TECHARFKTP EDAQAVINAY TEINKKHCWK LEILSGDHEQ RYWQKILVDR 

       550        560        570        580 
QAKLNQPREK KRGTEKLITK AEKIRLAKTQ QASKHIRFSE YD 

Q4G0J3 in FASTA format

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