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Q9Y312 (AAR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Protein AAR2 homolog
Alternative name(s):
AAR2 splicing factor homolog
Gene names
Name:AAR2
Synonyms:C20orf4
ORF Names:CGI-23, PRO0225
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the AAR2 family.

Sequence caution

The sequence AAF29578.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 384383Protein AAR2 homolog
PRO_0000209706

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.9 Ref.10

Natural variations

Natural variant1241P → T.
Corresponds to variant rs6121183 [ dbSNP | Ensembl ].
VAR_048127

Experimental info

Sequence conflict451F → L in CAB55913. Ref.2
Sequence conflict701E → K in AAD27732. Ref.1
Sequence conflict921S → N in AAD27732. Ref.1
Sequence conflict1461E → K in CAB55913. Ref.2
Sequence conflict2401L → H in CAB55913. Ref.2
Sequence conflict2411N → I in AAD27732. Ref.1
Sequence conflict2791N → H in AAD27732. Ref.1
Sequence conflict2991I → M in AAD27732. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y312 [UniParc].

Last modified October 19, 2002. Version 2.
Checksum: 01194E1DEC644F4D

FASTA38443,472
        10         20         30         40         50         60 
MAAVQMDPEL AKRLFFEGAT VVILNMPKGT EFGIDYNSWE VGPKFRGVKM IPPGIHFLHY 

        70         80         90        100        110        120 
SSVDKANPKE VGPRMGFFLS LHQRGLTVLR WSTLREEVDL SPAPESEVEA MRANLQELDQ 

       130        140        150        160        170        180 
FLGPYPYATL KKWISLTNFI SEATVEKLQP ENRQICAFSD VLPVLSMKHT KDRVGQNLPR 

       190        200        210        220        230        240 
CGIECKSYQE GLARLPEMKP RAGTEIRFSE LPTQMFPEGA TPAEITKHSM DLSYALETVL 

       250        260        270        280        290        300 
NKQFPSSPQD VLGELQFAFV CFLLGNVYEA FEHWKRLLNL LCRSEAAMMK HHTLYINLIS 

       310        320        330        340        350        360 
ILYHQLGEIP ADFFVDIVSQ DNFLTSTLQV FFSSACSIAV DATLRKKAEK FQAHLTKKFR 

       370        380 
WDFAAEPEDC APVVVELPEG IEMG 

« Hide

References

[1]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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 Skin.
[6]"Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 228-384.
Tissue: Fetal liver.
[7]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132957 mRNA. Translation: AAD27732.1.
AL117419 mRNA. Translation: CAB55913.1.
AL121895 Genomic DNA. Translation: CAC09921.1.
CH471077 Genomic DNA. Translation: EAW76141.1.
CH471077 Genomic DNA. Translation: EAW76142.1.
CH471077 Genomic DNA. Translation: EAW76143.1.
BC001751 mRNA. Translation: AAH01751.1.
BC019311 mRNA. Translation: AAH19311.1.
AF113672 mRNA. Translation: AAF29578.1. Different initiation.
CCDSCCDS13273.1.
PIRT17223.
RefSeqNP_001258803.1. NM_001271874.1.
NP_056326.2. NM_015511.4.
XP_005260442.1. XM_005260385.2.
XP_006723833.1. XM_006723770.1.
UniGeneHs.11314.
Hs.744306.

3D structure databases

ProteinModelPortalQ9Y312.
SMRQ9Y312. Positions 20-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117464. 10 interactions.
IntActQ9Y312. 5 interactions.
MINTMINT-1454200.
STRING9606.ENSP00000313674.

PTM databases

PhosphoSiteQ9Y312.

Polymorphism databases

DMDM24211603.

Proteomic databases

MaxQBQ9Y312.
PaxDbQ9Y312.
PRIDEQ9Y312.

Protocols and materials databases

DNASU25980.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320849; ENSP00000313674; ENSG00000131043.
ENST00000373932; ENSP00000363043; ENSG00000131043.
GeneID25980.
KEGGhsa:25980.
UCSCuc002xfc.3. human.

Organism-specific databases

CTD25980.
GeneCardsGC20P034825.
H-InvDBHIX0203050.
HGNCHGNC:15886. AAR2.
HPACAB034220.
HPA048645.
neXtProtNX_Q9Y312.
PharmGKBPA25753.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319701.
HOGENOMHOG000225103.
HOVERGENHBG051148.
KOK13205.
OMAPGVHFVY.
PhylomeDBQ9Y312.
TreeFamTF315089.

Gene expression databases

ArrayExpressQ9Y312.
BgeeQ9Y312.
CleanExHS_C20orf4.
GenevestigatorQ9Y312.

Family and domain databases

InterProIPR007946. AAR2.
[Graphical view]
PANTHERPTHR12689. PTHR12689. 1 hit.
PfamPF05282. AAR2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi25980.
NextBio47638.
PROQ9Y312.

Entry information

Entry nameAAR2_HUMAN
AccessionPrimary (citable) accession number: Q9Y312
Secondary accession number(s): E1P5S7 expand/collapse secondary AC list , Q9H4F9, Q9P1P3, Q9UFK9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: July 9, 2014
This is version 102 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

SIMILARITY comments

Index of protein domains and families

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 20

Human chromosome 20: entries, gene names and cross-references to MIM