Q6PKG0 (LARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
La-related protein 1

Alternative name(s):
La ribonucleoprotein domain family member 1

Gene names

Name:	LARP1
Synonyms:	KIAA0731, LARP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1096 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Belongs to the LARP family. Contains 1 HTH La-type RNA-binding domain.
Sequence caution	The sequence AAH33856.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA34451.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q6PKG0-1)

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: Q6PKG0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.
     78-144: PLQLPGAEGP...VLTTVNGQSP → MLWRVLLSKR...PFPVLAPFSN

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 1096	1095	La-related protein 1		PRO_0000207609
Regions
	Domain	397 – 487	91	HTH La-type RNA-binding
	Compositional bias	1044 – 1050	7	Poly-Gly
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3 Ref.19
	Modified residue	75	1	Phosphoserine Ref.16 Ref.21
	Modified residue	90	1	Phosphoserine Ref.7 Ref.10 Ref.16 Ref.18 Ref.20 Ref.21
	Modified residue	143	1	Phosphoserine Ref.18
	Modified residue	165	1	Phosphoserine Ref.18
	Modified residue	228	1	Phosphoserine By similarity
	Modified residue	324	1	Phosphoserine By similarity
	Modified residue	327	1	Phosphoserine By similarity
	Modified residue	517	1	Phosphoserine Ref.7 Ref.11 Ref.18 Ref.19 Ref.20
	Modified residue	521	1	Phosphoserine Ref.7 Ref.11 Ref.15 Ref.18 Ref.19 Ref.20
	Modified residue	526	1	Phosphothreonine Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	546	1	Phosphoserine Ref.20
	Modified residue	548	1	Phosphoserine Ref.6 Ref.17 Ref.19 Ref.20 Ref.21
	Modified residue	622	1	Phosphothreonine Ref.11 Ref.19 Ref.20
	Modified residue	624	1	Phosphothreonine Ref.11 Ref.19
	Modified residue	627	1	Phosphoserine Ref.6 Ref.7 Ref.11 Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	631	1	Phosphoserine Ref.7 Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	633	1	Phosphotyrosine Ref.19
	Modified residue	649	1	Phosphothreonine Ref.9 Ref.18
	Modified residue	724	1	Phosphothreonine Ref.18 Ref.19 Ref.21
	Modified residue	766	1	Phosphoserine Ref.7 Ref.16 Ref.18 Ref.19 Ref.20
	Modified residue	774	1	Phosphoserine Ref.3 Ref.6 Ref.7 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21
	Modified residue	785	1	Phosphothreonine Ref.8 Ref.11
	Modified residue	788	1	Phosphothreonine Ref.8 Ref.11
	Modified residue	823	1	Phosphoserine Ref.16
	Modified residue	824	1	Phosphoserine Ref.7 Ref.16 Ref.18 Ref.21
	Modified residue	845	1	Phosphothreonine Ref.18
	Modified residue	847	1	Phosphoserine Ref.13 Ref.19
	Modified residue	849	1	Phosphoserine Ref.19
	Modified residue	850	1	Phosphoserine Ref.19
	Modified residue	851	1	Phosphoserine Ref.13 Ref.18 Ref.19
	Modified residue	853	1	Phosphoserine Ref.18 Ref.19
	Modified residue	862	1	Phosphotyrosine Ref.19
	Modified residue	892	1	N6-acetyllysine Ref.22
	Modified residue	1017	1	N6-acetyllysine Ref.22
	Modified residue	1056	1	Phosphoserine Ref.12
	Modified residue	1071	1	Phosphothreonine Ref.7 Ref.12
Natural variations
	Alternative sequence	1 – 77	77	Missing in isoform 2.		VSP_015114
	Alternative sequence	78 – 144	67	PLQLP…NGQSP → MLWRVLLSKRPPFPHPELDF QEAPIPSCPGRLPGRKNSVA LAAAPRKEPTGDREKPLPFP VLAPFSN in isoform 2.		VSP_015115
Experimental info
	Sequence conflict	778 – 780	3	RNT → TRP in AAH33856. Ref.1
	Sequence conflict	979	1	V → L in CAB61364. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: CA3E9D30BBC101B7	FASTA	1,096	123,510
	10 20 30 40 50 60 MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC 70 80 90 100 110 120 AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP 130 140 150 160 170 180 PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG 190 200 210 220 230 240 EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR 250 260 270 280 290 300 GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA 310 320 330 340 350 360 PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD 370 380 390 400 410 420 YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL 430 440 450 460 470 480 ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP 490 500 510 520 530 540 EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT 550 560 570 580 590 600 LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD 610 620 630 640 650 660 EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD 670 680 690 700 710 720 RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF 730 740 750 760 770 780 DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT 790 800 810 820 830 840 RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE 850 860 870 880 890 900 HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE 910 920 930 940 950 960 RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY 970 980 990 1000 1010 1020 GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR 1030 1040 1050 1060 1070 1080 LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE 1090 DAKWTSQHSN TQTLGK
	Isoform 2 [UniParc]. Checksum: 64982CA22171B0E6	FASTA	1,019	116,465
	10 20 30 40 50 60 MLWRVLLSKR PPFPHPELDF QEAPIPSCPG RLPGRKNSVA LAAAPRKEPT GDREKPLPFP 70 80 90 100 110 120 VLAPFSNPEH SAPAKVVRAA VPKQRKGSKV GDFGDAINWP TPGEIAHKSV QPQSHKPQPT 130 140 150 160 170 180 RKLPPKKDMK EQEKGEGSDS KESPKTKSDE SGEEKNGDED CQRGGQKKKG NKHKWVPLQI 190 200 210 220 230 240 DMKPEVPREK LASRPTRPPE PRHIPANRGE IKGSESATYV PVAPPTPAWQ PEIKPEPAWH 250 260 270 280 290 300 DQDETSSVKS DGAGGARASF RGRGRGRGRG RGRGRGGTRT HFDYQFGYRK FDGVEGPRTP 310 320 330 340 350 360 KYMNNITYYF DNVSSTELYS VDQELLKDYI KRQIEYYFSV DNLERDFFLR RKMDADGFLP 370 380 390 400 410 420 ITLIASFHRV QALTTDISLI FAALKDSKVV EIVDEKVRRR EEPEKWPLPP IVDYSQTDFS 430 440 450 460 470 480 QLLNCPEFVP RQHYQKETES APGSPRAVTP VPTKTEEVSN LKTLPKGLSA SLPDLDSENW 490 500 510 520 530 540 IEVKKRPRPS PARPKKSEES RFSHLTSLPQ QLPSQQLMSK DQDEQEELDF LFDEEMEQMD 550 560 570 580 590 600 GRKNTFTAWS DEESDYEIDD RDVNKILIVT QTPHYMRRHP GGDRTGNHTS RAKMSAELAK 610 620 630 640 650 660 VINDGLFYYE QDLWAEKFEP EYSQIKQEVE NFKKVNMISR EQFDTLTPEP PVDPNQEVPP 670 680 690 700 710 720 GPPRFQQVPT DALANKLFGA PEPSTIARSL PTTVPESPNY RNTRTPRTPR TPQLKDSSQT 730 740 750 760 770 780 SRFYPVVKEG RTLDAKMPRK RKTRHSSNPP LESHVGWVMD SREHRPRTAS ISSSPSEGTP 790 800 810 820 830 840 TVGSYGCTPQ SLPKFQHPSH ELLKENGFTQ HVYHKYRRRC LNERKRLGIG QSQEMNTLFR 850 860 870 880 890 900 FWSFFLRDHF NKKMYEEFKQ LALEDAKEGY RYGLECLFRY YSYGLEKKFR LDIFKDFQEE 910 920 930 940 950 960 TVKDYEAGQL YGLEKFWAFL KYSKAKNLDI DPKLQEYLGK FRRLEDFRVD PPMGEEGNHK 970 980 990 1000 1010 RHSVVAGGGG GEGRKRCPSQ SSSRPAAMIS QPPTPPTGQP VREDAKWTSQ HSNTQTLGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 2). Tissue: Cervix and Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1). Tissue: Brain.
[3]	Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W., Heiserich L., Boulahbel H., Gottlieb E. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422; 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924; 937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, MASS SPECTROMETRY. Tissue: Cervix carcinoma, Colon carcinoma and Mammary carcinoma.
[4]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed: 9872452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1). Tissue: Brain.
[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 538-1096. Tissue: Mammary cancer.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; SER-548; SER-627 AND SER-774, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-90; SER-517; SER-521; THR-526; SER-627; SER-631; SER-766; SER-774; SER-824 AND THR-1071, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; THR-785 AND THR-788, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND THR-649, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-526, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-521; THR-526; THR-622; THR-624; SER-627; THR-785 AND THR-788, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056 AND THR-1071, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; SER-847 AND SER-851, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND SER-774, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-766; SER-774; SER-823 AND SER-824, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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 SER-90; SER-143; SER-165; SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724; SER-766; SER-774; SER-824; THR-845; SER-851 AND SER-853, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-521; THR-526; SER-548; THR-622; THR-624; SER-627; SER-631; TYR-633; THR-724; SER-766; SER-774; SER-847; SER-849; SER-850; SER-851; SER-853 AND TYR-862, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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-90; SER-517; SER-521; THR-526; SER-546; SER-548; THR-622; SER-627; SER-631; SER-766 AND SER-774, MASS SPECTROMETRY.
[21]	"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-75; SER-90; THR-526; SER-548; SER-627; SER-631; THR-724; SER-774 AND SER-824, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"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-892 AND LYS-1017, MASS SPECTROMETRY.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC001460 mRNA. Translation: AAH01460.2. BC033856 mRNA. Translation: AAH33856.1. Different initiation. AK091465 mRNA. Translation: BAC03668.1. AB018274 mRNA. Translation: BAA34451.1. Sequence problems. AL133034 mRNA. Translation: CAB61364.1.
IPI	IPI00185919. IPI00411690.
PIR	T42646.
RefSeq	NP_056130.2. NM_015315.3.
UniGene	Hs.292078.
3D structure databases
ProteinModelPortal	Q6PKG0.
SMR	Q6PKG0. Positions 403-477.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6PKG0. 8 interactions.
MINT	MINT-1631511.
STRING	Q6PKG0.
PTM databases
PhosphoSite	Q6PKG0.
Polymorphism databases
DMDM	73621135.
Proteomic databases
PRIDE	Q6PKG0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377643; ENSP00000366871; ENSG00000155506.
GeneID	23367.
KEGG	hsa:23367.
UCSC	uc003lvo.1. human. uc003lvp.1. human.
Organism-specific databases
CTD	23367.
GeneCards	GC05P154092.
HGNC	HGNC:29531. LARP1.
HPA	CAB015222.
MIM	612059. gene.
neXtProt	NX_Q6PKG0.
PharmGKB	PA142671564.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11099.
GeneTree	ENSGT00390000000523.
HOGENOM	HBG713047.
HOVERGEN	HBG054322.
InParanoid	Q6PKG0.
OMA	NARTPRT.
PhylomeDB	Q6PKG0.
Gene expression databases
ArrayExpress	Q6PKG0.
CleanEx	HS_LARP1.
Genevestigator	Q6PKG0.
GermOnline	ENSG00000155506. Homo sapiens.
Family and domain databases
InterPro	IPR006607. DM15. IPR006630. Lupus_La_RNA-bd. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF05383. La. 1 hit. [Graphical view]
SMART	SM00684. DM15. 3 hits. SM00715. LA. 1 hit. [Graphical view]
PROSITE	PS50961. HTH_LA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	45430.
PMAP-CutDB	Q6PKG0.
SOURCE	Search...

Entry information

Entry name

LARP1_HUMAN

Accession

Primary (citable) accession number: Q6PKG0
Secondary accession number(s): O94836 , Q8N4M2, Q8NB73, Q9UFD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	August 16, 2005
Last modified:	January 25, 2012
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.