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Q9NX24 (NHP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 subunit 2
Alternative name(s):
Nucleolar protein family A member 2
snoRNP protein NHP2
Gene names
Name:NHP2
Synonyms:NOLA2
ORF Names:HSPC286
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. Ref.10

Subunit structure

Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1, NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic subunit. The complex contains a stable core formed by binding of one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently binds to this core via DKC1. The complex binds a box H/ACA small nucleolar RNA (snoRNA), which may target the specific site of modification within the RNA substrate. During assembly, the complex contains NAF1 instead of GAR1/NOLA1. The complex also interacts with TERC, which contains a 3'-terminal domain related to the box H/ACA snoRNAs. Specific interactions with snoRNAs or TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140. H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or SMN2, GEMIN2/SIP1, DDX20/GEMIN3, and GEMIN4. This is mediated by interaction between GAR1 and SMN1 or SMN2. The SMN complex may be required for correct assembly of the H/ACA snoRNP complex. Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Ref.1 Ref.11

Subcellular location

Nucleusnucleolus. NucleusCajal body. Note: Also localized to Cajal bodies (coiled bodies). Ref.1 Ref.8 Ref.9

Tissue specificity

Expressed in brain, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus. Also expressed at lower levels in the liver. Ref.2

Developmental stage

Transcript peaks at G1/S transition. Ref.2

Involvement in disease

Dyskeratosis congenita, autosomal recessive, 2 (DKCB2) [MIM:613987]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Belongs to the ribosomal protein L7Ae family.

Sequence caution

The sequence AAF28964.1 differs from that shown. Reason: Frameshift at positions 37, 119 and 120.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 153153H/ACA ribonucleoprotein complex subunit 2
PRO_0000136763

Amino acid modifications

Modified residue191Phosphoserine Ref.13
Cross-link5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12

Natural variations

Natural variant1181A → T. Ref.16
Corresponds to variant rs139588879 [ dbSNP | Ensembl ].
VAR_065870
Natural variant1261V → M in DKCB2. Ref.16
Corresponds to variant rs121908090 [ dbSNP | Ensembl ].
VAR_065871
Natural variant1391Y → H in DKCB2. Ref.16
Corresponds to variant rs121908089 [ dbSNP | Ensembl ].
VAR_065872

Sequences

Sequence LengthMass (Da)Tools
Q9NX24 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7658FDFF88AF3178

FASTA15317,201
        10         20         30         40         50         60 
MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI 

        70         80         90        100        110        120 
RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTDLGAAAGS 

       130        140        150 
KRPTCVIMVK PHEEYQEAYD ECLEEVQSLP LPL 

« Hide

References

« Hide 'large scale' references
[1]"Human H/ACA small nucleolar RNPs and telomerase share evolutionarily conserved proteins NHP2 and NOP10."
Pogacic V., Dragon F., Filipowicz W.
Mol. Cell. Biol. 20:9028-9040(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GAR1; SMALL NUCLEOLAR RNAS AND TERC, SUBCELLULAR LOCATION.
[2]"Expression of the human homologue of the small nucleolar RNA-binding protein NHP2 gene during monocytic differentiation of U937 cells."
Kang H.S., Jung H.M., Jun D., Huh T.L., Kim Y.H.
Biochim. Biophys. Acta 1575:31-39(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"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. expand/collapse author list , 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].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Muscle and Placenta.
[8]"Directed proteomic analysis of the human nucleolus."
Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I.
Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[9]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins."
Wang C., Meier U.T.
EMBO J. 23:1857-1867(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF THE H/ACA SNORNP COMPLEX.
[11]"A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
[12]"A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58."
Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E., Lamond A.I.
Mol. Cell 39:618-631(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-5.
[13]"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-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Mutations in the telomerase component NHP2 cause the premature ageing syndrome dyskeratosis congenita."
Vulliamy T., Beswick R., Kirwan M., Marrone A., Digweed M., Walne A., Dokal I.
Proc. Natl. Acad. Sci. U.S.A. 105:8073-8078(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DKCB2 MET-126 AND HIS-139, VARIANT THR-118.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ293309 mRNA. Translation: CAC08452.1.
AF401219 mRNA. Translation: AAL02175.1.
AF161404 mRNA. Translation: AAF28964.1. Frameshift.
AK000486 mRNA. Translation: BAA91198.1.
CR457238 mRNA. Translation: CAG33519.1.
AC136632 Genomic DNA. No translation available.
BC000009 mRNA. Translation: AAH00009.1.
BC006387 mRNA. Translation: AAH06387.1.
RefSeqNP_001030005.1. NM_001034833.1.
NP_060308.1. NM_017838.3.
UniGeneHs.744074.

3D structure databases

ProteinModelPortalQ9NX24.
SMRQ9NX24. Positions 40-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120783. 19 interactions.
IntActQ9NX24. 9 interactions.
MINTMINT-3077751.
STRING9606.ENSP00000274606.

PTM databases

PhosphoSiteQ9NX24.

Polymorphism databases

DMDM68565945.

2D gel databases

SWISS-2DPAGEQ9NX24.

Proteomic databases

PaxDbQ9NX24.
PeptideAtlasQ9NX24.
PRIDEQ9NX24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274606; ENSP00000274606; ENSG00000145912.
GeneID55651.
KEGGhsa:55651.
UCSCuc003mir.2. human.

Organism-specific databases

CTD55651.
GeneCardsGC05M177510.
HGNCHGNC:14377. NHP2.
HPAHPA044171.
HPA050400.
MIM606470. gene.
613987. phenotype.
neXtProtNX_Q9NX24.
Orphanet1775. Dyskeratosis congenita.
PharmGKBPA164723898.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1358.
HOGENOMHOG000055227.
HOVERGENHBG000328.
InParanoidQ9NX24.
KOK11129.
OMAPVDIMCH.
OrthoDBEOG7288T8.
PhylomeDBQ9NX24.
TreeFamTF105839.

Gene expression databases

ArrayExpressQ9NX24.
BgeeQ9NX24.
CleanExHS_NHP2.
GenevestigatorQ9NX24.

Family and domain databases

InterProIPR002415. H/ACA_rnp_Nhp2_euk.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
[Graphical view]
PfamPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSPR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.
ProtoNetSearch...

Other

ChiTaRSNHP2. human.
GeneWikiNOLA2.
GenomeRNAi55651.
NextBio60350.
PROQ9NX24.
SOURCESearch...

Entry information

Entry nameNHP2_HUMAN
AccessionPrimary (citable) accession number: Q9NX24
Secondary accession number(s): A6NKY8, Q9P095
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 123 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM