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Q9BXJ9 (NAA15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-alpha-acetyltransferase 15, NatA auxiliary subunit
Alternative name(s):
Gastric cancer antigen Ga19
N-terminal acetyltransferase
NMDA receptor-regulated protein 1
Protein tubedown-1
Tbdn100
Gene names
Name:NAA15
Synonyms:GA19, NARG1, NATH, TBDN100
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length866 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity. The NAT activity may be important for vascular, hematopoietic and neuronal growth and development. Required to control retinal neovascularization in adult ocular endothelial cells. In complex with XRCC6 and XRCC5 (Ku80), up-regulates transcription from the osteocalcin promoter. Ref.2 Ref.9 Ref.10

Subunit structure

Component of the N-terminal acetyltransferase A (NatA) complex composed of NAA10 or probably NAA11 and NAA15. Interacts with XRCC6, NAA50 and XRCC5. Associates with HYPK when in a complex with NAA10. Ref.2 Ref.10 Ref.11 Ref.13 Ref.19

Subcellular location

Cytoplasm. Nucleus. Note: Mainly cytoplasmic, nuclear in some cases. Present in the free cytosolic and cytoskeleton-bound polysomes, but not in the membrane-bound polysomes. Ref.3 Ref.10

Tissue specificity

Expressed at high levels in testis and in ocular endothelial cells. Also found in brain (corpus callosum), heart, colon, bone marrow and at lower levels in most adult tissues, including thyroid, liver, pancreas, mammary and salivary glands, lung, ovary, urogenital system and upper gastrointestinal tract. Overexpressed in gastric cancer, in papillary thyroid carcinomas and in a Burkitt lymphoma cell line (Daudi). Specifically suppressed in abnormal proliferating blood vessels in eyes of patients with proliferative diabetic retinopathy. Ref.1 Ref.3 Ref.9

Post-translational modification

Cleaved by caspases during apoptosis, resulting in a stable 35 kDa fragment.

Sequence similarities

Contains 8 TPR repeats.

Sequence caution

The sequence AAH39818.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
TPR repeat
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein amino acid acetylation

Inferred from direct assay Ref.10. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 19480662. Source: UniProt

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.2. Source: UniProtKB

protein stabilization

Inferred from mutant phenotype PubMed 19480662. Source: UniProt

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNatA complex

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.3Ref.10. Source: UniProtKB

nucleus

Inferred from direct assay Ref.3Ref.2. Source: UniProtKB

transcription factor complex

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionN-acetyltransferase activity

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.10. Source: UniProtKB

ribosome binding

Inferred from direct assay PubMed 19480662. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NAA50Q9GZZ12EBI-1042540,EBI-1052523

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXJ9-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BXJ9-4)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     514-525: HFIEITDDQFDF → KSLMTSLTFIHTV
     526-866: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 866866N-alpha-acetyltransferase 15, NatA auxiliary subunit
PRO_0000106294

Regions

Repeat46 – 7934TPR 1
Repeat80 – 11334TPR 2
Repeat148 – 18437TPR 3
Repeat224 – 25734TPR 4
Repeat374 – 40734TPR 5
Repeat409 – 44133TPR 6
Repeat485 – 51834TPR 7
Repeat672 – 70534TPR 8
Region500 – 866367Interaction with HYPK
Motif612 – 62918Bipartite nuclear localization signal Potential
Compositional bias629 – 6324Poly-Asp

Amino acid modifications

Modified residue2621N6-acetyllysine Ref.18
Modified residue3991Phosphothreonine Ref.17
Modified residue4031Phosphoserine Ref.17
Modified residue5881Phosphoserine Ref.22
Modified residue7351N6-acetyllysine Ref.18
Modified residue7561N6-acetyllysine Ref.18
Modified residue8551Phosphoserine By similarity
Modified residue8561Phosphoserine Ref.20 Ref.22

Natural variations

Alternative sequence514 – 52512HFIEI…DQFDF → KSLMTSLTFIHTV in isoform 2.
VSP_012560
Alternative sequence526 – 866341Missing in isoform 2.
VSP_012561

Experimental info

Sequence conflict4251K → R in AAM48746. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6B4BA23B99D99121

FASTA866101,272
        10         20         30         40         50         60 
MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA MKGLTLNCLG 

        70         80         90        100        110        120 
KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI KCYRNALKWD KDNLQILRDL 

       130        140        150        160        170        180 
SLLQIQMRDL EGYRETRYQL LQLRPAQRAS WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT 

       190        200        210        220        230        240 
SPDKVDYEYS ELLLYQNQVL REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL 

       250        260        270        280        290        300 
EDAADVYRGL QERNPENWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF 

       310        320        330        340        350        360 
LSGEKFKECL DKFLRMNFSK GCPPVFNTLR SLYKDKEKVA IIEELVVGYE TSLKSCRLFN 

       370        380        390        400        410        420 
PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA IESTPTLIEL FLVKAKIYKH 

       430        440        450        460        470        480 
AGNIKEAARW MDEAQALDTA DRFINSKCAK YMLKANLIKE AEEMCSKFTR EGTSAVENLN 

       490        500        510        520        530        540 
EMQCMWFQTE CAQAYKAMNK FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD 

       550        560        570        580        590        600 
LLKLEDVLRQ HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR 

       610        620        630        640        650        660 
RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV ETPLEEAIKF 

       670        680        690        700        710        720 
LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA IDSSHPWLHE CMIRLFNTAV 

       730        740        750        760        770        780 
CESKDLSDTV RTVLKQEMNR LFGATNPKNF NETFLKRNSD SLPHRLSAAK MVYYLDPSSQ 

       790        800        810        820        830        840 
KRAIELATTL DESLTNRNLQ TCMEVLEALY DGSLGDCKEA AEIYRANCHK LFPYALAFMP 

       850        860 
PGYEEDMKIT VNGDSSAEAE ELANEI 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 6C66BCE4B7377BB6
Show »

FASTA52661,602

References

« Hide 'large scale' references
[1]"Serological identification and expression analysis of gastric cancer-associated genes."
Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.
Br. J. Cancer 86:1824-1830(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Gastric adenocarcinoma.
[2]"Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex."
Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M., Towler D.A.
J. Biol. Chem. 277:37280-37291(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH XRCC6 AND XRCC5, FUNCTION.
Tissue: Heart and Osteoblast.
[3]"NATH, a novel gene overexpressed in papillary thyroid carcinomas."
Fluge O., Bruland O., Akslen L.A., Varhaug J.E., Lillehaug J.R.
Oncogene 21:5056-5068(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Thyroid carcinoma.
[4]"Cloning and analysis of a novel gene encoding N-terminal acetyltransferase subunit."
He Y.G., Xie Y.F., Chen Y., Qian W., Lai J.H., Tan D.Y.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:353-357(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"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] (ISOFORM 2).
Tissue: Ovary.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORM 1).
Tissue: Brain and Lymph.
[9]"Suppressed expression of tubedown-1 in retinal neovascularization of proliferative diabetic retinopathy."
Gendron R.L., Good W.V., Adams L.C., Paradis H.
Invest. Ophthalmol. Vis. Sci. 42:3000-3007(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]"Identification and characterization of the human ARD1-NATH protein acetyltransferase complex."
Arnesen T., Anderson D., Baldersheim C., Lanotte M., Varhaug J.E., Lillehaug J.R.
Biochem. J. 386:433-443(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NAA10.
[11]"Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferase."
Arnesen T., Betts M.J., Pendino F., Liberles D.A., Anderson D., Caro J., Kong X., Varhaug J.E., Lillehaug J.R.
BMC Biochem. 7:13-13(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAA11.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex."
Arnesen T., Anderson D., Torsvik J., Halseth H.B., Varhaug J.E., Lillehaug J.R.
Gene 371:291-295(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAA50.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substrates."
Polevoda B., Arnesen T., Sherman F.
BMC Proc. 3:S2-S2(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399 AND SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262; LYS-735 AND LYS-756, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation."
Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.
Mol. Cell. Biol. 30:1898-1909(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HYPK, SUBUNIT.
[20]"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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY039242 mRNA. Translation: AAK68661.1.
AY112670 mRNA. Translation: AAM48746.1.
AJ314788 mRNA. Translation: CAC43228.1.
AF327722 mRNA. Translation: AAK15707.1.
AK023402 mRNA. Translation: BAB14562.1.
AC097376 Genomic DNA. Translation: AAY40950.1.
CH471056 Genomic DNA. Translation: EAX05119.1.
BC039818 mRNA. Translation: AAH39818.1. Sequence problems.
BC093928 mRNA. Translation: AAH93928.1.
BC104806 mRNA. Translation: AAI04807.1.
CCDSCCDS43270.1. [Q9BXJ9-1]
RefSeqNP_476516.1. NM_057175.3. [Q9BXJ9-1]
UniGeneHs.745047.

3D structure databases

ProteinModelPortalQ9BXJ9.
SMRQ9BXJ9. Positions 1-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123146. 20 interactions.
IntActQ9BXJ9. 6 interactions.
STRING9606.ENSP00000296543.

PTM databases

PhosphoSiteQ9BXJ9.

Polymorphism databases

DMDM57012969.

Proteomic databases

MaxQBQ9BXJ9.
PaxDbQ9BXJ9.
PRIDEQ9BXJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296543; ENSP00000296543; ENSG00000164134. [Q9BXJ9-1]
GeneID80155.
KEGGhsa:80155.
UCSCuc003ihu.1. human. [Q9BXJ9-1]

Organism-specific databases

CTD80155.
GeneCardsGC04P140222.
HGNCHGNC:30782. NAA15.
HPAHPA023589.
HPA050661.
MIM608000. gene.
neXtProtNX_Q9BXJ9.
PharmGKBPA165664293.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000191711.
HOVERGENHBG052576.
InParanoidQ9BXJ9.
KOK00670.
OMAYDSLPHR.
OrthoDBEOG747PKD.
PhylomeDBQ9BXJ9.
TreeFamTF106301.

Enzyme and pathway databases

BRENDA2.3.1.88. 2681.

Gene expression databases

ArrayExpressQ9BXJ9.
BgeeQ9BXJ9.
CleanExHS_NARG1.
GenevestigatorQ9BXJ9.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR021183. NatA_aux_su.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF12569. NARP1. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PIRSFPIRSF000422. N-terminal-AcTrfase-A_aux_su. 1 hit.
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

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ChiTaRSNAA15. human.
GeneWikiNARG1.
GenomeRNAi80155.
NextBio70453.
PROQ9BXJ9.
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Entry information

Entry nameNAA15_HUMAN
AccessionPrimary (citable) accession number: Q9BXJ9
Secondary accession number(s): D3DNY6 expand/collapse secondary AC list , Q52LG9, Q8IWH4, Q8NEV2, Q9H8P6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 125 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

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM