ID   LARP7_HUMAN             Reviewed;         582 AA.
AC   Q4G0J3; B2ZHN6; Q3B7A9; Q9P1S7; Q9Y3Z8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=La-related protein 7;
DE   AltName: Full=La ribonucleoprotein domain family member 7;
DE   AltName: Full=P-TEFb-interaction protein for 7SK stability;
DE            Short=PIP7S;
GN   Name=LARP7; ORFNames=HDCMA18P;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, AND IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
RX   PubMed=18483487; DOI=10.1038/embor.2008.72;
RA   Markert A., Grimm M., Martinez J., Wiesner J., Meyerhans A.,
RA   Meyuhas O., Sickmann A., Fischer U.;
RT   "The La-related protein LARP7 is a component of the 7SK
RT   ribonucleoprotein and affects transcription of cellular and viral
RT   polymerase II genes.";
RL   EMBO Rep. 9:569-575(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Dendritic cell;
RA   Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT   "A novel gene from human dendritic cell.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-582 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K.,
RA   Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF TYR-128.
RX   PubMed=18249148; DOI=10.1016/j.molcel.2008.01.003;
RA   He N., Jahchan N.S., Hong E., Li Q., Bayfield M.A., Maraia R.J.,
RA   Luo K., Zhou Q.;
RT   "A La-related protein modulates 7SK snRNP integrity to suppress P-
RT   TEFb-dependent transcriptional elongation and tumorigenesis.";
RL   Mol. Cell 29:588-599(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-258; SER-261;
RP   SER-273; SER-337 AND THR-338, AND MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by
RT   enrichment and fractionation of phosphopeptides with strong anion
RT   exchange chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [10]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Negative transcriptional regulator of polymerase II
CC       genes, acting by means of the 7SK RNP system. Within the 7SK RNP
CC       complex, the positive transcription elongation factor b (P-TEFb)
CC       is sequestered in an inactive form, preventing RNA polymerase II
CC       phosphorylation and subsequent transcriptional elongation.
CC   -!- SUBUNIT: Integral part of the 7SK RNP complex. Specifically binds
CC       to the highly conserved 3'-terminal U-rich stretch of 7SK RNA. On
CC       stimulation, remains associated with 7SK RNA, whereas P-TEFb is
CC       released from the complex.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4G0J3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4G0J3-2; Sequence=VSP_024021;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACD13786.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=EAX06284.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; EU667388; ACD13786.1; ALT_INIT; mRNA.
DR   EMBL; AF068284; AAF65503.1; -; mRNA.
DR   EMBL; CH471057; EAX06284.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC066945; AAH66945.1; -; mRNA.
DR   EMBL; BC107709; AAI07710.1; ALT_INIT; mRNA.
DR   EMBL; AL049996; CAB43230.1; -; mRNA.
DR   IPI; IPI00294742; -.
DR   IPI; IPI00395536; -.
DR   PIR; T08692; T08692.
DR   RefSeq; NP_056269.1; -.
DR   RefSeq; NP_057732.2; -.
DR   UniGene; Hs.713663; -.
DR   PhosphoSite; Q4G0J3; -.
DR   PRIDE; Q4G0J3; -.
DR   Ensembl; ENSG00000174720; Homo sapiens.
DR   GeneID; 51574; -.
DR   KEGG; hsa:51574; -.
DR   GeneCards; GC04P113777; -.
DR   HGNC; HGNC:24912; LARP7.
DR   HPA; HPA017600; -.
DR   MIM; 612026; gene.
DR   HOVERGEN; Q4G0J3; -.
DR   OMA; Q4G0J3; AKLNQPR.
DR   NextBio; 55403; -.
DR   ArrayExpress; Q4G0J3; -.
DR   Bgee; Q4G0J3; -.
DR   CleanEx; HS_LARP7; -.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR012677; a_b_plait_nuc_bd.
DR   InterPro; IPR002344; Lupus_La.
DR   InterPro; IPR006630; Lupus_La_RNA_bd.
DR   InterPro; IPR014886; RRM_3.
DR   InterPro; IPR000504; RRM_RNP1.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF05383; La; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF08777; RRM_3; 1.
DR   PRINTS; PR00302; LUPUSLA.
DR   SMART; SM00715; LA; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50961; HTH_LA; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; RNA-binding.
FT   CHAIN         1    582       La-related protein 7.
FT                                /FTId=PRO_0000281143.
FT   DOMAIN       28    122       HTH La-type RNA-binding.
FT   DOMAIN      125    203       RRM.
FT   COMPBIAS    202    368       Lys-rich.
FT   MOD_RES     257    257       Phosphothreonine.
FT   MOD_RES     258    258       Phosphoserine.
FT   MOD_RES     261    261       Phosphoserine.
FT   MOD_RES     273    273       Phosphoserine.
FT   MOD_RES     337    337       Phosphoserine.
FT   MOD_RES     338    338       Phosphothreonine.
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    368       Missing (in isoform 2).
FT                                /FTId=VSP_024021.
FT   MUTAGEN     128    128       Y->D: Loss of 7SK RNA-binding and marked
FT                                decrease in 7SK RNP complex formation.
FT   CONFLICT    295    295       R -> G (in Ref. 4; AAI07710).
FT   CONFLICT    516    516       K -> R (in Ref. 2; AAF65503 and 5;
FT                                CAB43230).
FT   CONFLICT    560    560       K -> Q (in Ref. 5; CAB43230).
SQ   SEQUENCE   582 AA;  66899 MW;  04209B8159A5738C CRC64;
     METESGNQEK VMEEESTEKK KEVEKKKRSR VKQVLADIAK QVDFWFGDAN LHKDRFLREQ
     IEKSRDGYVD ISLLVSFNKM KKLTTDGKLI ARALRSSAVV ELDLEGTRIR RKKPLGERPK
     DEDERTVYVE LLPKNVNHSW IERVFGKCGN VVYISIPHYK STGDPKGFAF VEFETKEQAA
     KAIEFLNNPP EEAPRKPGIF PKTVKNKPIP ALRVVEEKKK KKKKKGRMKK EDNIQAKEEN
     MDTSNTSISK MKRSRPTSEG SDIESTEPQK QCSKKKKKRD RVEASSLPEV RTGKRKRSSS
     EDAESLAPRS KVKKIIQKDI IKEASEASKE NRDIEISTEE EKDTGDLKDS SLLKTKRKHK
     KKHKERHKMG EEVIPLRVLS KSEWMDLKKE YLALQKASMA SLKKTISQIK SESEMETDSG
     VPQNTGMKNE KTANREECRT QEKVNATGPQ FVSGVIVKII STEPLPGRKQ VRDTLAAISE
     VLYVDLLEGD TECHARFKTP EDAQAVINAY TEINKKHCWK LEILSGDHEQ RYWQKILVDR
     QAKLNQPREK KRGTEKLITK AEKIRLAKTQ QASKHIRFSE YD
//