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Protein

La-related protein 7

Gene

LARP7

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. RNA processing Source: InterPro
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:LARP7
ORF Names:HDCMA18P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24912. LARP7.

Subcellular locationi

  1. Nucleusnucleoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. Golgi apparatus Source: HPA
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
  5. ribonucleoprotein complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Alazami syndrome (ALAZS)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndromic form of primordial dwarfism, a condition characterized by severe growth restriction that has its onset in utero, and results in short stature and undersize. ALAZS patients manifest severe intellectual disability and distinct facial features including malar hypoplasia, deep-set eyes, broad nose, short philtrum, and macrostomia. Some patients have non-specific and inconsistent skeletal findings, for example, scoliosis and mild epiphyseal changes in the proximal phalanges, but no frank dysplasia.

See also OMIM:615071

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281Y → D: Loss of 7SK RNA-binding and marked decrease in 7SK RNP complex formation. 1 Publication

Keywords - Diseasei

Dwarfism, Mental retardation

Organism-specific databases

MIMi615071. phenotype.
Orphaneti319671. Microcephalic primordial dwarfism, Alazami type.
PharmGKBiPA145148525.

Polymorphism and mutation databases

BioMutaiLARP7.
DMDMi121945944.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582La-related protein 7PRO_0000281143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei257 – 2571Phosphothreonine1 Publication
Modified residuei258 – 2581Phosphoserine3 Publications
Modified residuei261 – 2611Phosphoserine4 Publications
Modified residuei273 – 2731Phosphoserine1 Publication
Modified residuei337 – 3371Phosphoserine5 Publications
Modified residuei338 – 3381Phosphothreonine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ4G0J3.
PaxDbiQ4G0J3.
PRIDEiQ4G0J3.

PTM databases

PhosphoSiteiQ4G0J3.

Expressioni

Gene expression databases

BgeeiQ4G0J3.
CleanExiHS_LARP7.
ExpressionAtlasiQ4G0J3. baseline and differential.
GenevestigatoriQ4G0J3.

Organism-specific databases

HPAiHPA017600.
HPA026842.
HPA027930.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK9P507507EBI-2371923,EBI-1383449
HEXIM1O949925EBI-2371923,EBI-2832510

Protein-protein interaction databases

BioGridi119619. 51 interactions.
DIPiDIP-47624N.
IntActiQ4G0J3. 18 interactions.
MINTiMINT-4540675.
STRINGi9606.ENSP00000314311.

Structurei

3D structure databases

ProteinModelPortaliQ4G0J3.
SMRiQ4G0J3. Positions 36-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 12295HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 20379RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi202 – 368167Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5193.
GeneTreeiENSGT00760000119314.
HOGENOMiHOG000113284.
HOVERGENiHBG081891.
InParanoidiQ4G0J3.
KOiK15191.
OMAiLSKTEWM.
OrthoDBiEOG72C50R.
PhylomeDBiQ4G0J3.
TreeFamiTF314476.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.70.330. 2 hits.
InterProiIPR002344. Lupus_La.
IPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR014886. RRM_3.
IPR000504. RRM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
PF00076. RRM_1. 1 hit.
PF08777. RRM_3. 1 hit.
[Graphical view]
PRINTSiPR00302. LUPUSLA.
SMARTiSM00715. LA. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50961. HTH_LA. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q4G0J3-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
METESGNQEK VMEEESTEKK KEVEKKKRSR VKQVLADIAK QVDFWFGDAN
60 70 80 90 100
LHKDRFLREQ IEKSRDGYVD ISLLVSFNKM KKLTTDGKLI ARALRSSAVV
110 120 130 140 150
ELDLEGTRIR RKKPLGERPK DEDERTVYVE LLPKNVNHSW IERVFGKCGN
160 170 180 190 200
VVYISIPHYK STGDPKGFAF VEFETKEQAA KAIEFLNNPP EEAPRKPGIF
210 220 230 240 250
PKTVKNKPIP ALRVVEEKKK KKKKKGRMKK EDNIQAKEEN MDTSNTSISK
260 270 280 290 300
MKRSRPTSEG SDIESTEPQK QCSKKKKKRD RVEASSLPEV RTGKRKRSSS
310 320 330 340 350
EDAESLAPRS KVKKIIQKDI IKEASEASKE NRDIEISTEE EKDTGDLKDS
360 370 380 390 400
SLLKTKRKHK KKHKERHKMG EEVIPLRVLS KSEWMDLKKE YLALQKASMA
410 420 430 440 450
SLKKTISQIK SESEMETDSG VPQNTGMKNE KTANREECRT QEKVNATGPQ
460 470 480 490 500
FVSGVIVKII STEPLPGRKQ VRDTLAAISE VLYVDLLEGD TECHARFKTP
510 520 530 540 550
EDAQAVINAY TEINKKHCWK LEILSGDHEQ RYWQKILVDR QAKLNQPREK
560 570 580
KRGTEKLITK AEKIRLAKTQ QASKHIRFSE YD
Length:582
Mass (Da):66,899
Last modified:August 30, 2005 - v1
Checksum:i04209B8159A5738C
GO
Isoform 2 (identifier: Q4G0J3-2) [UniParc]FASTAAdd to basket

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

Show »
Length:214
Mass (Da):24,488
Checksum:i12A03DED56668BA7
GO
Isoform 3 (identifier: Q4G0J3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MIPNIEGM

Show »
Length:589
Mass (Da):67,654
Checksum:iCD532FEBA691906E
GO

Sequence cautioni

The sequence AAH66945.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951R → G in AAI07710 (PubMed:15489334).Curated
Sequence conflicti516 – 5161K → R in AAF65503 (Ref. 2) Curated
Sequence conflicti516 – 5161K → R in CAB43230 (PubMed:17974005).Curated
Sequence conflicti560 – 5601K → Q in CAB43230 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 368368Missing in isoform 2. 1 PublicationVSP_024021Add
BLAST
Alternative sequencei1 – 11M → MIPNIEGM in isoform 3. 2 PublicationsVSP_047390

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU667388 mRNA. Translation: ACD13786.1.
AF068284 mRNA. Translation: AAF65503.1.
AC106864 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06284.1.
BC066945 mRNA. Translation: AAH66945.1. Different initiation.
BC107709 mRNA. Translation: AAI07710.2.
AL049996 mRNA. Translation: CAB43230.1.
CCDSiCCDS3701.2. [Q4G0J3-1]
CCDS58924.1. [Q4G0J3-3]
PIRiT08692.
RefSeqiNP_001253968.1. NM_001267039.1. [Q4G0J3-3]
NP_056269.1. NM_015454.2. [Q4G0J3-1]
NP_057732.2. NM_016648.3. [Q4G0J3-1]
UniGeneiHs.713663.

Genome annotation databases

EnsembliENST00000324052; ENSP00000314311; ENSG00000174720. [Q4G0J3-1]
ENST00000344442; ENSP00000344950; ENSG00000174720. [Q4G0J3-1]
ENST00000509061; ENSP00000422626; ENSG00000174720. [Q4G0J3-3]
GeneIDi51574.
KEGGihsa:51574.
UCSCiuc003iay.4. human. [Q4G0J3-1]

Polymorphism and mutation databases

BioMutaiLARP7.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU667388 mRNA. Translation: ACD13786.1.
AF068284 mRNA. Translation: AAF65503.1.
AC106864 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06284.1.
BC066945 mRNA. Translation: AAH66945.1. Different initiation.
BC107709 mRNA. Translation: AAI07710.2.
AL049996 mRNA. Translation: CAB43230.1.
CCDSiCCDS3701.2. [Q4G0J3-1]
CCDS58924.1. [Q4G0J3-3]
PIRiT08692.
RefSeqiNP_001253968.1. NM_001267039.1. [Q4G0J3-3]
NP_056269.1. NM_015454.2. [Q4G0J3-1]
NP_057732.2. NM_016648.3. [Q4G0J3-1]
UniGeneiHs.713663.

3D structure databases

ProteinModelPortaliQ4G0J3.
SMRiQ4G0J3. Positions 36-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119619. 51 interactions.
DIPiDIP-47624N.
IntActiQ4G0J3. 18 interactions.
MINTiMINT-4540675.
STRINGi9606.ENSP00000314311.

PTM databases

PhosphoSiteiQ4G0J3.

Polymorphism and mutation databases

BioMutaiLARP7.
DMDMi121945944.

Proteomic databases

MaxQBiQ4G0J3.
PaxDbiQ4G0J3.
PRIDEiQ4G0J3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324052; ENSP00000314311; ENSG00000174720. [Q4G0J3-1]
ENST00000344442; ENSP00000344950; ENSG00000174720. [Q4G0J3-1]
ENST00000509061; ENSP00000422626; ENSG00000174720. [Q4G0J3-3]
GeneIDi51574.
KEGGihsa:51574.
UCSCiuc003iay.4. human. [Q4G0J3-1]

Organism-specific databases

CTDi51574.
GeneCardsiGC04P113559.
HGNCiHGNC:24912. LARP7.
HPAiHPA017600.
HPA026842.
HPA027930.
MIMi612026. gene.
615071. phenotype.
neXtProtiNX_Q4G0J3.
Orphaneti319671. Microcephalic primordial dwarfism, Alazami type.
PharmGKBiPA145148525.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5193.
GeneTreeiENSGT00760000119314.
HOGENOMiHOG000113284.
HOVERGENiHBG081891.
InParanoidiQ4G0J3.
KOiK15191.
OMAiLSKTEWM.
OrthoDBiEOG72C50R.
PhylomeDBiQ4G0J3.
TreeFamiTF314476.

Miscellaneous databases

ChiTaRSiLARP7. human.
GenomeRNAii51574.
NextBioi55403.
PROiQ4G0J3.
SOURCEiSearch...

Gene expression databases

BgeeiQ4G0J3.
CleanExiHS_LARP7.
ExpressionAtlasiQ4G0J3. baseline and differential.
GenevestigatoriQ4G0J3.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.70.330. 2 hits.
InterProiIPR002344. Lupus_La.
IPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR014886. RRM_3.
IPR000504. RRM_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
PF00076. RRM_1. 1 hit.
PF08777. RRM_3. 1 hit.
[Graphical view]
PRINTSiPR00302. LUPUSLA.
SMARTiSM00715. LA. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50961. HTH_LA. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), 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. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 3).
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-582 (ISOFORM 1).
    Tissue: Fetal brain.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-128.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-258; SER-261; SER-273; SER-337 AND THR-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-261; SER-337 AND THR-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: INVOLVEMENT IN ALAZS.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-261; SER-337 AND THR-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Loss of function mutation in LARP7, chaperone of 7SK ncRNA, causes a syndrome of facial dysmorphism, intellectual disability, and primordial dwarfism."
    Alazami A.M., Al-Owain M., Alzahrani F., Shuaib T., Al-Shamrani H., Al-Falki Y.H., Al-Qahtani S.M., Alsheddi T., Colak D., Alkuraya F.S.
    Hum. Mutat. 33:1429-1434(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ALAZS.
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-261; SER-337 AND THR-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLARP7_HUMAN
AccessioniPrimary (citable) accession number: Q4G0J3
Secondary accession number(s): B2ZHN6
, Q3B7A9, Q9P1S7, Q9Y3Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: August 30, 2005
Last modified: April 29, 2015
This is version 104 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.