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P55769

- NH2L1_HUMAN

UniProt

P55769 - NH2L1_HUMAN

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Protein

NHP2-like protein 1

Gene

NHP2L1

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

Functioni

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.2 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: Reactome
  3. ribosome biogenesis Source: InterPro
  4. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:NHP2L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:7819. NHP2L1.

Subcellular locationi

Nucleusnucleolus 3 Publications
Note: Concentrated in the dense fibrillar component of the nucleolus.

GO - Cellular componenti

  1. box C/D snoRNP complex Source: BHF-UCL
  2. nucleolus Source: ProtInc
  3. nucleoplasm Source: Reactome
  4. nucleus Source: ProtInc
  5. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381G → K: Abolishes completely RNA-binding. 1 Publication
Mutagenesisi57 – 571A → F: Abolishes completely RNA-binding. 1 Publication
Mutagenesisi80 – 801Y → A: Abolishes 50% of RNA-binding. 1 Publication
Mutagenesisi96 – 12833Missing: Abolishes completely RNA-binding. Add
BLAST

Organism-specific databases

PharmGKBiPA31621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128128NHP2-like protein 1PRO_0000423260Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 128127NHP2-like protein 1, N-terminally processedPRO_0000136778Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylthreonine; in NHP2-like protein 1, N-terminally processed2 Publications
Modified residuei21 – 211N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP55769.
PaxDbiP55769.
PeptideAtlasiP55769.
PRIDEiP55769.

2D gel databases

SWISS-2DPAGEP55769.

PTM databases

PhosphoSiteiP55769.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP55769.
CleanExiHS_NHP2L1.
ExpressionAtlasiP55769. baseline and differential.
GenevestigatoriP55769.

Organism-specific databases

HPAiHPA029199.

Interactioni

Subunit structurei

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 PRPF31.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
gagP045912EBI-712228,EBI-6179727From a different organism.
NUFIP1Q9UHK02EBI-712228,EBI-2563549

Protein-protein interaction databases

BioGridi110874. 114 interactions.
IntActiP55769. 18 interactions.
MINTiMINT-1382515.
STRINGi9606.ENSP00000215956.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Helixi16 – 3116Combined sources
Beta strandi35 – 384Combined sources
Helixi39 – 4810Combined sources
Beta strandi51 – 577Combined sources
Helixi63 – 653Combined sources
Helixi68 – 769Combined sources
Beta strandi80 – 845Combined sources
Helixi86 – 927Combined sources
Beta strandi100 – 1056Combined sources
Helixi113 – 12412Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP55769.
SMRiP55769. Positions 3-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55769.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7Ae family.Curated

Phylogenomic databases

eggNOGiCOG1358.
HOGENOMiHOG000055226.
HOVERGENiHBG000328.
InParanoidiP55769.
KOiK12845.
OrthoDBiEOG78WKTT.
PhylomeDBiP55769.
TreeFamiTF300184.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR002415. 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]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
PRINTSiPR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiPS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55769 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEADVNPKA YPLADAHLTK KLLDLVQQSC NYKQLRKGAN EATKTLNRGI
60 70 80 90 100
SEFIVMAADA EPLEIILHLP LLCEDKNVPY VFVRSKQALG RACGVSRPVI
110 120
ACSVTIKEGS QLKQQIQSIQ QSIERLLV
Length:128
Mass (Da):14,174
Last modified:January 23, 2007 - v3
Checksum:i78849EBB497089ED
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191T → N.
Corresponds to variant rs1802521 [ dbSNP | Ensembl ].
VAR_034155

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14022.1.
CCDS33653.1.
RefSeqiNP_001003796.1. NM_001003796.1.
NP_004999.1. NM_005008.3.
UniGeneiHs.182255.

Genome annotation databases

EnsembliENST00000215956; ENSP00000215956; ENSG00000100138.
ENST00000355257; ENSP00000347401; ENSG00000100138.
ENST00000401959; ENSP00000383949; ENSG00000100138.
GeneIDi4809.
KEGGihsa:4809.
UCSCiuc003bat.4. human.

Polymorphism databases

DMDMi2500345.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14022.1.
CCDS33653.1.
RefSeqi NP_001003796.1. NM_001003796.1.
NP_004999.1. NM_005008.3.
UniGenei Hs.182255.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E7K X-ray 2.90 A/B 1-128 [» ]
2JNB NMR - A 1-128 [» ]
2OZB X-ray 2.60 A/D 1-128 [» ]
3SIU X-ray 2.63 A/D 1-128 [» ]
3SIV X-ray 3.30 A/D/G/J 1-128 [» ]
ProteinModelPortali P55769.
SMRi P55769. Positions 3-128.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110874. 114 interactions.
IntActi P55769. 18 interactions.
MINTi MINT-1382515.
STRINGi 9606.ENSP00000215956.

PTM databases

PhosphoSitei P55769.

Polymorphism databases

DMDMi 2500345.

2D gel databases

SWISS-2DPAGE P55769.

Proteomic databases

MaxQBi P55769.
PaxDbi P55769.
PeptideAtlasi P55769.
PRIDEi P55769.

Protocols and materials databases

DNASUi 4809.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215956 ; ENSP00000215956 ; ENSG00000100138 .
ENST00000355257 ; ENSP00000347401 ; ENSG00000100138 .
ENST00000401959 ; ENSP00000383949 ; ENSG00000100138 .
GeneIDi 4809.
KEGGi hsa:4809.
UCSCi uc003bat.4. human.

Organism-specific databases

CTDi 4809.
GeneCardsi GC22M042069.
HGNCi HGNC:7819. NHP2L1.
HPAi HPA029199.
MIMi 601304. gene.
601876. gene.
neXtProti NX_P55769.
PharmGKBi PA31621.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1358.
HOGENOMi HOG000055226.
HOVERGENi HBG000328.
InParanoidi P55769.
KOi K12845.
OrthoDBi EOG78WKTT.
PhylomeDBi P55769.
TreeFami TF300184.

Enzyme and pathway databases

Reactomei REACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi NHP2L1. human.
EvolutionaryTracei P55769.
GeneWikii NHP2L1.
GenomeRNAii 4809.
NextBioi 18532.
PROi P55769.
SOURCEi Search...

Gene expression databases

Bgeei P55769.
CleanExi HS_NHP2L1.
ExpressionAtlasi P55769. baseline and differential.
Genevestigatori P55769.

Family and domain databases

Gene3Di 3.30.1330.30. 1 hit.
InterProi IPR002415. 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 ]
Pfami PF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view ]
PRINTSi PR00881. L7ARS6FAMILY.
PR00883. NUCLEARHMG.
SUPFAMi SSF55315. SSF55315. 1 hit.
PROSITEi PS01082. RIBOSOMAL_L7AE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiNH2L1_HUMAN
AccessioniPrimary (citable) accession number: P55769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 153 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3