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Protein

La-related protein 4B

Gene

LARP4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Stimulates mRNA translation.1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • positive regulation of translation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
La-related protein 4B
Alternative name(s):
La ribonucleoprotein domain family member 4B
La ribonucleoprotein domain family member 5
La-related protein 5
Gene namesi
Name:LARP4B
Synonyms:KIAA0217, LARP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:28987. LARP4B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoplasmic stress granule Source: UniProtKB
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • polysomal ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165548762.

Polymorphism and mutation databases

DMDMi134034150.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 738738La-related protein 4BPRO_0000281139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei424 – 4241PhosphoserineCombined sources
Modified residuei434 – 4341PhosphoserineCombined sources
Modified residuei451 – 4511PhosphoserineCombined sources
Modified residuei488 – 4881PhosphoserineCombined sources
Modified residuei498 – 4981PhosphoserineBy similarity
Modified residuei518 – 5181PhosphothreonineCombined sources
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei556 – 5561PhosphoserineCombined sources
Modified residuei566 – 5661PhosphothreonineCombined sources
Modified residuei568 – 5681PhosphoserineCombined sources
Modified residuei601 – 6011PhosphoserineCombined sources
Modified residuei664 – 6641PhosphoserineCombined sources
Modified residuei718 – 7181PhosphoserineCombined sources
Modified residuei724 – 7241N6-acetyllysineCombined sources
Modified residuei727 – 7271PhosphoserineCombined sources
Modified residuei732 – 7321PhosphothreonineBy similarity
Modified residuei736 – 7361PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ92615.
MaxQBiQ92615.
PaxDbiQ92615.
PeptideAtlasiQ92615.
PRIDEiQ92615.

PTM databases

iPTMnetiQ92615.
PhosphoSiteiQ92615.

Expressioni

Gene expression databases

BgeeiQ92615.
CleanExiHS_LARP5.
ExpressionAtlasiQ92615. baseline and differential.
GenevisibleiQ92615. HS.

Organism-specific databases

HPAiHPA036566.
HPA042738.

Interactioni

Subunit structurei

Interacts with PABPC1 and RACK1. Associates with polysomes via the 40S ribosomal subunit.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
E9KL353EBI-1052558,EBI-8456500

Protein-protein interaction databases

BioGridi116795. 28 interactions.
IntActiQ92615. 20 interactions.
STRINGi9606.ENSP00000326128.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PTHX-ray1.70B55-69[»]
ProteinModelPortaliQ92615.
SMRiQ92615. Positions 152-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini150 – 23990HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini240 – 30768RRMAdd
BLAST

Sequence similaritiesi

Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IN3Y. Eukaryota.
ENOG4111REM. LUCA.
GeneTreeiENSGT00530000063417.
HOGENOMiHOG000004803.
HOVERGENiHBG055137.
InParanoidiQ92615.
KOiK18763.
OMAiICQRTTK.
OrthoDBiEOG74J971.
PhylomeDBiQ92615.
TreeFamiTF321960.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSDQDAKVV AEPQTQRVQE GKDSAHLMNG PISQTTSQTS SIPPLSQVPA
60 70 80 90 100
TKVSELNPNA EVWGAPVLHL EASSAADGVS AAWEEVAGHH ADRGPQGSDA
110 120 130 140 150
NGDGDQGHEN AALPDPQESD PADMNALALG PSEYDSLPEN SETGGNESQP
160 170 180 190 200
DSQEDPREVL KKTLEFCLSR ENLASDMYLI SQMDSDQYVP ITTVANLDHI
210 220 230 240 250
KKLSTDVDLI VEVLRSLPLV QVDEKGEKVR PNQNRCIVIL REISESTPVE
260 270 280 290 300
EVEALFKGDN LPKFINCEFA YNDNWFITFE TEADAQQAYK YLREEVKTFQ
310 320 330 340 350
GKPIKARIKA KAIAINTFLP KNGFRPLDVS LYAQQRYATS FYFPPMYSPQ
360 370 380 390 400
QQFPLYSLIT PQTWSATHSY LDPPLVTPFP NTGFINGFTS PAFKPAASPL
410 420 430 440 450
TSLRQYPPRS RNPSKSHLRH AIPSAERGPG LLESPSIFNF TADRLINGVR
460 470 480 490 500
SPQTRQAGQT RTRIQNPSAY AKREAGPGRV EPGSLESSPG LGRGRKNSFG
510 520 530 540 550
YRKKREEKFT SSQTQSPTPP KPPSPSFELG LSSFPPLPGA AGNLKTEDLF
560 570 580 590 600
ENRLSSLIIG PSKERTLSAD ASVNTLPVVV SREPSVPASC AVSATYERSP
610 620 630 640 650
SPAHLPDDPK VAEKQRETHS VDRLPSALTA TACKSVQVNG AATELRKPSY
660 670 680 690 700
AEICQRTSKE PPSSPLQPQK EQKPNTVGCG KEEKKLAEPA ERYREPPALK
710 720 730
STPGAPRDQR RPAGGRPSPS AMGKRLSREQ STPPKSPQ
Length:738
Mass (Da):80,552
Last modified:March 20, 2007 - v3
Checksum:iA0E5D44ECA58265D
GO

Sequence cautioni

The sequence BAA13207.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86971 mRNA. Translation: BAA13207.2. Different initiation.
AK292946 mRNA. Translation: BAF85635.1.
AL359878, AL157709 Genomic DNA. Translation: CAI13663.2.
AL157709, AL359878 Genomic DNA. Translation: CAI39596.2.
AL359878 Genomic DNA. Translation: CAI13661.1.
AL359878 Genomic DNA. Translation: CAI13662.1.
CH471072 Genomic DNA. Translation: EAW86530.1.
BC131630 mRNA. Translation: AAI31631.1.
BC152443 mRNA. Translation: AAI52444.1.
CR749653 mRNA. Translation: CAH18446.1.
CCDSiCCDS31131.1.
RefSeqiNP_055970.1. NM_015155.2.
UniGeneiHs.159069.
Hs.215766.

Genome annotation databases

EnsembliENST00000316157; ENSP00000326128; ENSG00000107929.
ENST00000612396; ENSP00000482767; ENSG00000107929.
GeneIDi23185.
KEGGihsa:23185.
UCSCiuc031ptb.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86971 mRNA. Translation: BAA13207.2. Different initiation.
AK292946 mRNA. Translation: BAF85635.1.
AL359878, AL157709 Genomic DNA. Translation: CAI13663.2.
AL157709, AL359878 Genomic DNA. Translation: CAI39596.2.
AL359878 Genomic DNA. Translation: CAI13661.1.
AL359878 Genomic DNA. Translation: CAI13662.1.
CH471072 Genomic DNA. Translation: EAW86530.1.
BC131630 mRNA. Translation: AAI31631.1.
BC152443 mRNA. Translation: AAI52444.1.
CR749653 mRNA. Translation: CAH18446.1.
CCDSiCCDS31131.1.
RefSeqiNP_055970.1. NM_015155.2.
UniGeneiHs.159069.
Hs.215766.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PTHX-ray1.70B55-69[»]
ProteinModelPortaliQ92615.
SMRiQ92615. Positions 152-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116795. 28 interactions.
IntActiQ92615. 20 interactions.
STRINGi9606.ENSP00000326128.

PTM databases

iPTMnetiQ92615.
PhosphoSiteiQ92615.

Polymorphism and mutation databases

DMDMi134034150.

Proteomic databases

EPDiQ92615.
MaxQBiQ92615.
PaxDbiQ92615.
PeptideAtlasiQ92615.
PRIDEiQ92615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316157; ENSP00000326128; ENSG00000107929.
ENST00000612396; ENSP00000482767; ENSG00000107929.
GeneIDi23185.
KEGGihsa:23185.
UCSCiuc031ptb.1. human.

Organism-specific databases

CTDi23185.
GeneCardsiLARP4B.
HGNCiHGNC:28987. LARP4B.
HPAiHPA036566.
HPA042738.
MIMi616513. gene.
neXtProtiNX_Q92615.
PharmGKBiPA165548762.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IN3Y. Eukaryota.
ENOG4111REM. LUCA.
GeneTreeiENSGT00530000063417.
HOGENOMiHOG000004803.
HOVERGENiHBG055137.
InParanoidiQ92615.
KOiK18763.
OMAiICQRTTK.
OrthoDBiEOG74J971.
PhylomeDBiQ92615.
TreeFamiTF321960.

Miscellaneous databases

ChiTaRSiLARP4B. human.
GenomeRNAii23185.
PROiQ92615.
SOURCEiSearch...

Gene expression databases

BgeeiQ92615.
CleanExiHS_LARP5.
ExpressionAtlasiQ92615. baseline and differential.
GenevisibleiQ92615. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Trachea.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-738.
    Tissue: Fetal kidney.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND THR-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424; SER-434; SER-451; SER-524; SER-727 AND SER-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424; THR-518 AND SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-724, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "A stimulatory role for the La-related protein 4B in translation."
    Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.
    RNA 16:1488-1499(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PABPC1 AND RACK1.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-488; SER-524; SER-556; SER-568; SER-601; SER-664 AND SER-718, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLAR4B_HUMAN
AccessioniPrimary (citable) accession number: Q92615
Secondary accession number(s): A7MD20
, Q5T3R3, Q5T3R4, Q5T3R5, Q68CY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: July 6, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.