Reviewed, UniProtKB/Swiss-Prot Q4G0J3 (LARP7_HUMAN)

Names and origin

Protein names

Recommended name:
    La-related protein 7
Alternative name(s):
    La ribonucleoprotein domain family member 7
    P-TEFb-interaction protein for 7SK stability
      Short name=PIP7S

Gene names

Name:	LARP7
ORF Names:	HDCMA18P

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (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. Ref.1 Ref.6
Subunit structure	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 Ref.1.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Ref.7 Ref.8 Ref.9 Ref.11 Ref.13
Sequence similarities	Contains 1 HTH La-type RNA-binding domain. Contains 1 RRM (RNA recognition motif) domain.
Sequence caution	The sequence ACD13786.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence EAX06284.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from electronic annotation. Source: InterPro
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q4G0J3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q4G0J3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-368: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 582	582	La-related protein 7		PRO_0000281143
Regions
	Domain	28 – 122	95	HTH La-type RNA-binding
	Domain	125 – 203	79	RRM
	Compositional bias	202 – 368	167	Lys-rich
Amino acid modifications
	Modified residue	254	1	Phosphoserine Ref.11
	Modified residue	257	1	Phosphothreonine Ref.8 Ref.11
	Modified residue	258	1	Phosphoserine Ref.8 Ref.11
	Modified residue	261	1	Phosphoserine Ref.8 Ref.11
	Modified residue	265	1	Phosphoserine Ref.11
	Modified residue	273	1	Phosphoserine Ref.8
	Modified residue	298	1	Phosphoserine
	Modified residue	300	1	Phosphoserine Ref.11
	Modified residue	337	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13
	Modified residue	338	1	Phosphothreonine Ref.7 Ref.8 Ref.9 Ref.13
	Modified residue	440	1	Phosphothreonine By similarity
	Modified residue	574	1	N6-acetyllysine Ref.14
Natural variations
	Alternative sequence	1 – 368	368	Missing in isoform 2.		VSP_024021
Experimental info
	Mutagenesis	128	1	Y → D: Loss of 7SK RNA-binding and marked decrease in 7SK RNP complex formation. Ref.6
	Sequence conflict	295	1	R → G in AAI07710. Ref.4
	Sequence conflict	516	1	K → R in AAF65503. Ref.2
	Sequence conflict	516	1	K → R in CAB43230. Ref.5
	Sequence conflict	560	1	K → Q in CAB43230. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 30, 2005. Version 1. Checksum: 04209B8159A5738C	FASTA	582	66,899
	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
	Isoform 2. Checksum: 12A03DED56668BA7	FASTA	214	24,488
	10 20 30 40 50 60 MGEEVIPLRV LSKSEWMDLK KEYLALQKAS MASLKKTISQ IKSESEMETD SGVPQNTGMK 70 80 90 100 110 120 NEKTANREEC RTQEKVNATG PQFVSGVIVK IISTEPLPGR KQVRDTLAAI SEVLYVDLLE 130 140 150 160 170 180 GDTECHARFK TPEDAQAVIN AYTEINKKHC WKLEILSGDH EQRYWQKILV DRQAKLNQPR 190 200 210 EKKRGTEKLI TKAEKIRLAK TQQASKHIRF SEYD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes." Markert A., Grimm M., Martinez J., Wiesner J., Meyerhans A., Meyuhas O., Sickmann A., Fischer U. EMBO Rep. 9:569-575(2008) [PubMed: 18483487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
[2]	"A novel gene from human dendritic cell." Zhao Z., Huang X., Li N., Zhu X., Cao X. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Dendritic cell.
[3]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-582 (ISOFORM 1). Tissue: Fetal brain.
[6]	"A La-related protein modulates 7SK snRNP integrity to suppress P-TEFb-dependent transcriptional elongation and tumorigenesis." He N., Jahchan N.S., Hong E., Li Q., Bayfield M.A., Maraia R.J., Luo K., Zhou Q. Mol. Cell 29:588-599(2008) [PubMed: 18249148] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-128.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-258; SER-261; SER-273; SER-337 AND THR-338, MASS SPECTROMETRY.
[9]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, MASS SPECTROMETRY. Tissue: Liver.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-257; SER-258; SER-261; SER-265 AND SER-300, MASS SPECTROMETRY.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, MASS SPECTROMETRY. Tissue: T-cell.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-574, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU667388 mRNA. Translation: ACD13786.1. Different initiation. AF068284 mRNA. Translation: AAF65503.1. CH471057 Genomic DNA. Translation: EAX06284.1. Different initiation. BC066945 mRNA. Translation: AAH66945.1. BC107709 mRNA. Translation: AAI07710.2. AL049996 mRNA. Translation: CAB43230.1.
IPI	IPI00294742. IPI00395536.
PIR	T08692.
RefSeq	NP_056269.1. NP_057732.2.
UniGene	Hs.713663
3D structure databases
HSSP	HSSP built from PDB template 1ZH5 based on UniProtKB P05455.
SMR	Q4G0J3. Positions 34-115, 92-190, 451-552.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4G0J3.
PTM databases
PhosphoSite	Q4G0J3.
Proteomic databases
PRIDE	Q4G0J3.
Genome annotation databases
Ensembl	ENST00000324052; ENSP00000314311; ENSG00000174720; Homo sapiens. [Genome view] ENST00000344442; ENSP00000344950; ENSG00000174720; Homo sapiens. [Genome view]
GeneID	51574.
KEGG	hsa:51574.
UCSC	uc003iay.1. human.
Organism-specific databases
CTD	51574.
GeneCards	GC04P113777.
HGNC	HGNC:24912. LARP7.
HPA	HPA017600.
MIM	612026. gene.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05972.
HOGENOM	HBG716691.
HOVERGEN	Q4G0J3.
InParanoid	Q4G0J3.
OMA	EVVYVDL.
OrthoDB	EOG9RBT3W.
PhylomeDB	Q4G0J3.
Gene expression databases
ArrayExpress	Q4G0J3.
Bgee	Q4G0J3.
CleanEx	HS_LARP7.
Genevestigator	Q4G0J3.
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. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF05383. La. 1 hit. PF00076. RRM_1. 1 hit. PF08777. RRM_3. 1 hit. [Graphical view]
PRINTS	PR00302. LUPUSLA.
SMART	SM00715. LA. 1 hit. SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50961. HTH_LA. 1 hit. PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	55403.
SOURCE	Search...

Entry information

Entry name

LARP7_HUMAN

Accession

Primary (citable) accession number: Q4G0J3
Secondary accession number(s): B2ZHN6 , Q3B7A9, Q9P1S7, Q9Y3Z8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	August 30, 2005
Last modified:	February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.