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Q96HR8 (NAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
H/ACA ribonucleoprotein complex non-core subunit NAF1

Short name=hNAF1
Gene names
Name:NAF1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disapears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4. Ref.5

Subunit structure

During assembly of the complex, component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) which contains NOLA2/NHP2, NOLA3/NOP10, NAF1 and DKC1/NOLA4. Interacts directly with DKC1/NOLA4. Ref.5 Ref.6

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and the nucleus. Absent from the nucleolus By similarity. Ref.5 Ref.6 Ref.7

Sequence similarities

Belongs to the NAF1 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494H/ACA ribonucleoprotein complex non-core subunit NAF1
PRO_0000315637

Regions

Compositional bias110 – 14839Ser-rich
Compositional bias417 – 48165Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue3151Phosphoserine Ref.4 Ref.8 Ref.9

Natural variations

Natural variant431P → S.
Corresponds to variant rs12331663 [ dbSNP | Ensembl ].
VAR_057795
Natural variant1621I → V. Ref.3
Corresponds to variant rs4691896 [ dbSNP | Ensembl ].
VAR_063101

Secondary structure

................. 494
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96HR8 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 5A0C9B635A982A62

FASTA49453,717
        10         20         30         40         50         60 
MEVVEAAAAQ LETLKFNGTD FGVGEGPAAP SPGSAPVPGT QPPLQSFEGS PDAGQTVEVK 

        70         80         90        100        110        120 
PAGEQPLQPV LNAVAAGTPA PQPQPPAESP ACGDCVTSPG AAEPARAPDS LETSDSDSDS 

       130        140        150        160        170        180 
DSETDSDSSS SSSSSSSSSS SSSSSCISLP PVLSDGDDDL QIEKENKNFP LKTKDELLLN 

       190        200        210        220        230        240 
ELPSVEELTI ILPEDIELKP LGMVSSIIEQ LVIIESMTNL PPVNEETVIF KSDRQAAGKI 

       250        260        270        280        290        300 
FEIFGPVAHP FYVLRFNSSD HIESKGIKIK ETMYFAPSMK DFTQYIFTEK LKQDKGSDAS 

       310        320        330        340        350        360 
WKNDQEPPPE ALDFSDDEKE KEAKQRKKSQ IQGRKKLKSE FNEPGEDFTE VHQNWNAHSS 

       370        380        390        400        410        420 
ASEHAKGYRN REFTRGFSRA RYPRSCHGRP PPQHFYNSEH MVSQETSGFP SQRQNNPIMP 

       430        440        450        460        470        480 
QYPFPLPVFD MHNFPLRPPP PPPPPPVNMG WATPNMAAHP LLNLPYSLPP PPPPPPLPPP 

       490 
PSSGDSNSHF GPYY 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT VAL-162.
Tissue: Placenta.
[4]"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-315, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells."
Darzacq X., Kittur N., Roy S., Shav-Tal Y., Singer R.H., Meier U.T.
J. Cell Biol. 173:207-218(2006) [PubMed: 16618814] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DKC1.
[6]"hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs, and telomerase."
Hoareau-Aveilla C., Bonoli M., Caizergues-Ferrer M., Henry Y.
RNA 12:832-840(2006) [PubMed: 16601202] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DKC1 AND NOLA3.
[7]"Dynamic association and localization of human H/ACA RNP proteins."
Kittur N., Darzacq X., Roy S., Singer R.H., Meier U.T.
RNA 12:2057-2062(2006) [PubMed: 17135485] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[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 SER-315, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"Solution structure of the NAF1 domain of hypothetical protein BC008207 [Homo sapiens]."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 181-276.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC022272 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04843.1.
CH471056 Genomic DNA. Translation: EAX04844.1.
BC008207 mRNA. Translation: AAH08207.1.
IPIIPI00063219.
RefSeqNP_001122403.1. NM_001128931.1.
NP_612395.2. NM_138386.2.
UniGeneHs.129095.
Hs.672113.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQNNMR-A181-276[»]
ProteinModelPortalQ96HR8.
SMRQ96HR8. Positions 181-276.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96HR8. 1 interaction.
STRINGQ96HR8.

PTM databases

PhosphoSiteQ96HR8.

Polymorphism databases

DMDM296439238.

Proteomic databases

PRIDEQ96HR8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274054; ENSP00000274054; ENSG00000145414.
GeneID92345.
KEGGhsa:92345.
UCSCuc003iqj.1. human.

Organism-specific databases

CTD92345.
GeneCardsGC04M164047.
H-InvDBHIX0004605.
HGNCHGNC:25126. NAF1.
HPAHPA036242.
neXtProtNX_Q96HR8.
PharmGKBPA162396775.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18125.
GeneTreeENSGT00390000004697.
HOVERGENHBG108169.
InParanoidQ96HR8.
OMAMHNFSLP.
PhylomeDBQ96HR8.

Gene expression databases

ArrayExpressQ96HR8.
BgeeQ96HR8.
CleanExHS_NAF1.
GenevestigatorQ96HR8.

Family and domain databases

InterProIPR007504. H/ACA_rnp_Gar1/Naf1.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
KOK14763.
PfamPF04410. Gar1. 1 hit.
[Graphical view]
SUPFAMSSF50447. Translat_factor. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNAF1_HUMAN
AccessionPrimary (citable) accession number: Q96HR8
Secondary accession number(s): D3DP28
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 18, 2010
Last modified: January 25, 2012
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

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Human chromosome 4: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families