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O95777 (NAA38_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
N-alpha-acetyltransferase 38, NatC auxiliary subunit
Alternative name(s):
U6 snRNA-associated Sm-like protein LSm8
Gene names
Name:NAA38
Synonyms:LSM8
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length96 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds specifically to the 3'-terminal U-tract of U6 snRNA.

Subunit structure

LSm subunits form a heteromer with a donut shape.

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the snRNP Sm proteins family.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processnuclear mRNA splicing, via spliceosome

Non-traceable author statement. Source: UniProtKB

   Cellular componentnucleus

Non-traceable author statement. Source: UniProtKB

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionU6 snRNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 9695N-alpha-acetyltransferase 38, NatC auxiliary subunit
PRO_0000125582

Amino acid modifications

Modified residue21N-acetylthreonine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O95777 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 15D26E6B75AA2EE1

FASTA9610,403
        10         20         30         40         50         60 
MTSALENYIN RTVAVITSDG RMIVGTLKGF DQTINLILDE SHERVFSSSQ GVEQVVLGLY 

        70         80         90 
IVRGDNVAVI GEIDEETDSA LDLGNIRAEP LNSVAH 

« Hide

References

« Hide 'large scale' references
[1]"A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro."
Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., Luehrmann R.
EMBO J. 18:5789-5802(1999) [PubMed: 10523320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed: 12853948] [Abstract]
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].
Tissue: Brain and Uterus.
[4]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 29-44 AND 88-96, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[5]"A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates."
Polevoda B., Arnesen T., Sherman F.
BMC Proc. 3:S2-S2(2009) [PubMed: 19660095] [Abstract]
Cited for: NOMENCLATURE.
[6]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182294 mRNA. Translation: AAD56232.1.
AC006389 Genomic DNA. Translation: AAD15542.1.
BC002742 mRNA. Translation: AAH02742.1.
BC022440 mRNA. Translation: AAH22440.1.
IPIIPI00219871.
RefSeqNP_057284.1. NM_016200.4.
UniGeneHs.655046.

3D structure databases

ProteinModelPortalO95777.
SMRO95777. Positions 3-73.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31195N.
IntActO95777. 45 interactions.
MINTMINT-1032595.
STRINGO95777.

Proteomic databases

PeptideAtlasO95777.
PRIDEO95777.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249299; ENSP00000249299; ENSG00000128534.
GeneID51691.
KEGGhsa:51691.
UCSCuc003vjg.1. human.

Organism-specific databases

CTD51691.
GeneCardsGC07P117824.
H-InvDBHIX0007025.
HGNCHGNC:20471. NAA38.
HPAHPA020116.
MIM607288. gene.
neXtProtNX_O95777.
PharmGKBPA134930584.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00570000079167.
HOGENOMHBG749684.
HOVERGENHBG105578.
InParanoidO95777.
OMANHTVSII.
OrthoDBEOG48SGVN.
PhylomeDBO95777.

Gene expression databases

ArrayExpressO95777.
BgeeO95777.
CleanExHS_LSM8.
GenevestigatorO95777.
GermOnlineENSG00000128534. Homo sapiens.

Family and domain databases

InterProIPR010920. LSM-related_domain.
IPR001163. LSM_domain.
IPR006649. LSM_domain_euk/arc.
[Graphical view]
KOK12627.
PfamPF01423. LSM. 1 hit.
[Graphical view]
SMARTSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMSSF50182. Sm_like_riboprot. 1 hit.
ProtoNetSearch...

Other

NextBio55698.
SOURCESearch...

Entry information

Entry nameNAA38_HUMAN
AccessionPrimary (citable) accession number: O95777
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 108 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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families