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P55769 (NH2L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NHP2-like protein 1
Alternative name(s):
High mobility group-like nuclear protein 2 homolog 1
OTK27
SNU13 homolog
Short name=hSNU13
U4/U6.U5 tri-snRNP 15.5 kDa protein

Cleaved into the following chain:

  1. NHP2-like protein 1, N-terminally processed
Gene names
Name:NHP2L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding. Ref.2 Ref.15

Subunit structure

Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Interacts with RAD17 and PRPF31. Ref.8 Ref.10

Subcellular location

Nucleusnucleolus. Note: Concentrated in the dense fibrillar component of the nucleolus. Ref.7 Ref.8 Ref.9

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the ribosomal protein L7Ae family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gagP045912EBI-712228,EBI-6179727From a different organism.
NUFIP1Q9UHK02EBI-712228,EBI-2563549

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 128128NHP2-like protein 1
PRO_0000423260
Initiator methionine11Removed; alternate Ref.7
Chain2 – 128127NHP2-like protein 1, N-terminally processed
PRO_0000136778

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue21N-acetylthreonine; in NHP2-like protein 1, N-terminally processed Ref.7 Ref.11
Modified residue211N6-acetyllysine By similarity

Natural variations

Natural variant191T → N.
Corresponds to variant rs1802521 [ dbSNP | Ensembl ].
VAR_034155

Experimental info

Mutagenesis381G → K: Abolishes completely RNA-binding. Ref.2
Mutagenesis571A → F: Abolishes completely RNA-binding. Ref.2
Mutagenesis801Y → A: Abolishes 50% of RNA-binding. Ref.2
Mutagenesis96 – 12833Missing: Abolishes completely RNA-binding.

Secondary structure

...................... 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55769 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 78849EBB497089ED

FASTA12814,174
        10         20         30         40         50         60 
MTEADVNPKA YPLADAHLTK KLLDLVQQSC NYKQLRKGAN EATKTLNRGI SEFIVMAADA 

        70         80         90        100        110        120 
EPLEIILHLP LLCEDKNVPY VFVRSKQALG RACGVSRPVI ACSVTIKEGS QLKQQIQSIQ 


QSIERLLV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and mapping of a human novel cDNA (NHP2L1) that encodes a protein highly homologous to yeast nuclear protein NHP2."
Saito H., Fujiwara T., Shin S., Okui K., Nakamura Y.
Cytogenet. Cell Genet. 72:191-193(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA."
Nottrott S., Hartmuth K., Fabrizio P., Urlaub H., Vidovic I., Ficner R., Luehrmann R.
EMBO J. 18:6119-6133(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-7 AND 92-106, FUNCTION, MUTAGENESIS OF GLY-38; ALA-57 AND TYR-80.
[3]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Lung and Urinary bladder.
[7]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-20; 22-33; 77-84 AND 114-125, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"HRad17 colocalizes with NHP2L1 in the nucleolus and redistributes after UV irradiation."
Chang M.-S., Sasaki H., Campbell M.S., Kraeft S.-K., Sutherland R., Yang C.-Y., Liu Y., Auclair D., Hao L., Sonoda H., Ferland L.H., Chen L.B.
J. Biol. Chem. 274:36544-36549(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RAD17.
[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]"The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment."
Vidovic I., Nottrott S., Hartmuth K., Luehrmann R., Ficner R.
Mol. Cell 6:1331-1342(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[14]"Functional implications for a prototypical K-turn binding protein from structural and dynamical studies of 15.5K."
Soss S.E., Flynn P.F.
Biochemistry 46:14979-14986(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[15]"Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP."
Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Luehrmann R., Carlomagno T., Wahl M.C.
Science 316:115-120(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PRPF31 AND STEM-LOOP RNA OF U4 SNRNA, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50420 mRNA. Translation: BAA23363.1.
AF155235 mRNA. Translation: AAF06959.1.
AF091076 mRNA. Translation: AAC72945.1.
CR456531 mRNA. Translation: CAG30417.1.
Z83840 Genomic DNA. Translation: CAB46207.1.
BC005358 mRNA. Translation: AAH05358.1.
BC019282 mRNA. Translation: AAH19282.1.
CCDSCCDS14022.1.
CCDS33653.1.
RefSeqNP_001003796.1. NM_001003796.1.
NP_004999.1. NM_005008.3.
UniGeneHs.182255.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7KX-ray2.90A/B1-128[»]
2JNBNMR-A1-128[»]
2OZBX-ray2.60A/D1-128[»]
3SIUX-ray2.63A/D1-128[»]
3SIVX-ray3.30A/D/G/J1-128[»]
ProteinModelPortalP55769.
SMRP55769. Positions 3-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110874. 113 interactions.
IntActP55769. 18 interactions.
MINTMINT-1382515.
STRING9606.ENSP00000215956.

PTM databases

PhosphoSiteP55769.

Polymorphism databases

DMDM2500345.

2D gel databases

SWISS-2DPAGEP55769.

Proteomic databases

MaxQBP55769.
PaxDbP55769.
PeptideAtlasP55769.
PRIDEP55769.

Protocols and materials databases

DNASU4809.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215956; ENSP00000215956; ENSG00000100138.
ENST00000355257; ENSP00000347401; ENSG00000100138.
ENST00000401959; ENSP00000383949; ENSG00000100138.
GeneID4809.
KEGGhsa:4809.
UCSCuc003bat.4. human.

Organism-specific databases

CTD4809.
GeneCardsGC22M042069.
HGNCHGNC:7819. NHP2L1.
HPAHPA029199.
MIM601304. gene.
601876. gene.
neXtProtNX_P55769.
PharmGKBPA31621.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1358.
HOGENOMHOG000055226.
HOVERGENHBG000328.
KOK12845.
OrthoDBEOG78WKTT.
PhylomeDBP55769.
TreeFamTF300184.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP55769.
BgeeP55769.
CleanExHS_NHP2L1.
GenevestigatorP55769.

Family and domain databases

Gene3D3.30.1330.30. 1 hit.
InterProIPR002415. H/ACA_rnp_Nhp2_euk.
IPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
[Graphical view]
PfamPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSPR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.
SUPFAMSSF55315. SSF55315. 1 hit.
PROSITEPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNHP2L1. human.
EvolutionaryTraceP55769.
GeneWikiNHP2L1.
GenomeRNAi4809.
NextBio18532.
PROP55769.
SOURCESearch...

Entry information

Entry nameNH2L1_HUMAN
AccessionPrimary (citable) accession number: P55769
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 22

Human chromosome 22: entries, gene names and cross-references to MIM