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Q14CX7 (NAA25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 25, NatB auxiliary subunit
Alternative name(s):
Mitochondrial distribution and morphology protein 20
N-terminal acetyltransferase B complex subunit MDM20
Short name=NatB complex subunit MDM20
N-terminal acetyltransferase B complex subunit NAA25
p120
Gene names
Name:NAA25
Synonyms:C12orf30, MDM20, NAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp-Glu. May play a role in normal cell-cycle progression. Ref.5

Subunit structure

Component of the N-terminal acetyltransferase B (NatB) complex which is composed of NAA20 and NAA25.

Subcellular location

Cytoplasm Ref.5.

Sequence similarities

Belongs to the MDM20/NAA25 family.

Contains 4 TPR repeats.

Sequence caution

The sequence BAB14432.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAE46062.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDK2P249411EBI-1048503,EBI-375096

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14CX7-1)

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: Q14CX7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     847-859: TISVILWVSSYCE → VSFCSLPKRHCCS
     860-972: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 972972N-alpha-acetyltransferase 25, NatB auxiliary subunit
PRO_0000294337

Regions

Repeat11 – 4434TPR 1
Repeat45 – 7834TPR 2
Repeat79 – 11234TPR 3
Repeat114 – 14633TPR 4
Compositional bias871 – 8777Poly-Lys

Natural variations

Alternative sequence847 – 85913TISVI…SSYCE → VSFCSLPKRHCCS in isoform 2.
VSP_026629
Alternative sequence860 – 972113Missing in isoform 2.
VSP_026630
Natural variant4261L → F.
Corresponds to variant rs16941860 [ dbSNP | Ensembl ].
VAR_054099
Natural variant7891S → R in a breast cancer sample; somatic mutation. Ref.8
VAR_035872
Natural variant8761K → R.
Corresponds to variant rs12231744 [ dbSNP | Ensembl ].
VAR_033156
Natural variant9151L → I.
Corresponds to variant rs12298022 [ dbSNP | Ensembl ].
VAR_054100

Experimental info

Sequence conflict2021I → T in BAB14432. Ref.4
Sequence conflict4661Y → S in BAB14432. Ref.4
Sequence conflict6721S → T in BAB14432. Ref.4
Sequence conflict8171S → G in CAE46062. Ref.2

Sequences

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

Last modified August 22, 2006. Version 1.
Checksum: 232B8FD14447DDD6

FASTA972112,292
        10         20         30         40         50         60 
MATRGHVQDP NDRRLRPIYD YLDNGNNKMA IQQADKLLKK HKDLHCAKVL KAIGLQRTGK 

        70         80         90        100        110        120 
QEEAFTLAQE VAALEPTDDN SLQALTILYR EMHRPELVTK LYEAAVKKVP NSEEYHSHLF 

       130        140        150        160        170        180 
MAYARVGEYK KMQQAGMALY KIVPKNPYYF WSVMSLIMQS ISAQDENLSK TMFLPLAERM 

       190        200        210        220        230        240 
VEKMVKEDKI EAEAEVELYY MILERLGKYQ EALDVIRGKL GEKLTSEIQS RENKCMAMYK 

       250        260        270        280        290        300 
KLSRWPECNA LSRRLLLKNS DDWQFYLTYF DSVFRLIEEA WSPPAEGEHS LEGEVHYSAE 

       310        320        330        340        350        360 
KAVKFIEDRI TEESKSSRHL RGPHLAKLEL IRRLRSQGCN DEYKLGDPEE LMFQYFKKFG 

       370        380        390        400        410        420 
DKPCCFTDLK VFVDLLPATQ CTKFINQLLG VVPLSTPTED KLALPADIRA LQQHLCVVQL 

       430        440        450        460        470        480 
TRLLGLYHTM DKNQKLSVVR ELMLRYQHGL EFGKTCLKTE LQFSDYYCLL AVHALIDVWR 

       490        500        510        520        530        540 
ETGDETTVWQ ALTLLEEGLT HSPSNAQFKL LLVRIYCMLG AFEPVVDLYS SLDAKHIQHD 

       550        560        570        580        590        600 
TIGYLLTRYA ESLGQYAAAS QSCNFALRFF HSNQKDTSEY IIQAYKYGAF EKIPEFIAFR 

       610        620        630        640        650        660 
NRLNNSLHFA QVRTERMLLD LLLEANISTS LAESIKSMNL RPEEDDIPWE DLRDNRDLNV 

       670        680        690        700        710        720 
FFSWDPKDRD VSEEHKKLSL EEETLWLRIR SLTLRLISGL PSLNHPVEPK NSEKTAENGV 

       730        740        750        760        770        780 
SSRIDILRLL LQQLEATLET GKRFIEKDIQ YPFLGPVPTR MGGFFNSGCS QCQISSFYLV 

       790        800        810        820        830        840 
NDIYELDTSG LEDTMEIQER IENSFKSLLD QLKDVFSKCK GDLLEVKDGN LKTHPTLLEN 

       850        860        870        880        890        900 
LVFFVETISV ILWVSSYCES VLRPYKLNLQ KKKKKKKETS IIMPPVFTSF QDYVTGLQTL 

       910        920        930        940        950        960 
ISNVVDHIKG LETHLIALKL EELILEDTSL SPEERKFSKT VQGKVQSSYL HSLLEMGELL 

       970 
KKRLETTKKL KI 

« Hide

Isoform 2 [UniParc].

Checksum: 5918C0A1EB63A438
Show »

FASTA85999,269

References

« Hide 'large scale' references
[1]"P120 which associates with nascent polypeptide chain."
Hotokezaka H., Wiedmann M.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterine endothelium.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[4]"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] OF 100-972.
[5]"Identification of the human N(alpha)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression."
Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E., Lillehaug J.R.
Biochem. J. 415:325-331(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NAT5, SUBCELLULAR LOCATION.
[6]"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.
[7]"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].
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-789.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB054990 mRNA. Translation: BAC80174.1.
BX641140 mRNA. Translation: CAE46062.1. Different initiation.
BC034357 mRNA. Translation: AAH34357.1.
BC113585 mRNA. Translation: AAI13586.1.
BC113587 mRNA. Translation: AAI13588.1.
AK023151 mRNA. Translation: BAB14432.1. Different initiation.
CCDSCCDS9159.1. [Q14CX7-1]
RefSeqNP_079229.2. NM_024953.3. [Q14CX7-1]
UniGeneHs.530941.

3D structure databases

ProteinModelPortalQ14CX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123072. 7 interactions.
IntActQ14CX7. 2 interactions.
STRING9606.ENSP00000261745.

PTM databases

PhosphoSiteQ14CX7.

Polymorphism databases

DMDM121948761.

Proteomic databases

MaxQBQ14CX7.
PaxDbQ14CX7.
PRIDEQ14CX7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261745; ENSP00000261745; ENSG00000111300. [Q14CX7-1]
GeneID80018.
KEGGhsa:80018.
UCSCuc001ttm.3. human. [Q14CX7-1]

Organism-specific databases

CTD80018.
GeneCardsGC12M112464.
H-InvDBHIX0011004.
HGNCHGNC:25783. NAA25.
HPAHPA039322.
MIM612755. gene.
neXtProtNX_Q14CX7.
PharmGKBPA165513030.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259643.
HOGENOMHOG000060132.
InParanoidQ14CX7.
KOK17973.
OMAQCTKFIN.
OrthoDBEOG75F4CR.
PhylomeDBQ14CX7.
TreeFamTF315103.

Gene expression databases

ArrayExpressQ14CX7.
BgeeQ14CX7.
CleanExHS_C12orf30.
GenevestigatorQ14CX7.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR019183. N-acetylTrfase_B_cplx_non-cat.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF09797. NatB_MDM20. 1 hit.
[Graphical view]
PROSITEPS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNAA25. human.
GenomeRNAi80018.
NextBio70134.
PROQ14CX7.
SOURCESearch...

Entry information

Entry nameNAA25_HUMAN
AccessionPrimary (citable) accession number: Q14CX7
Secondary accession number(s): A0JLU7 expand/collapse secondary AC list , Q6MZH1, Q7Z4N6, Q9H911
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: August 22, 2006
Last modified: July 9, 2014
This is version 79 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 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 12

Human chromosome 12: entries, gene names and cross-references to MIM