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Protein

N-alpha-acetyltransferase 35, NatC auxiliary subunit

Gene

NAA35

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Involved in regulation of apoptosis and proliferation of smooth muscle cells.1 Publication

GO - Biological processi

  • negative regulation of apoptotic process Source: UniProtKB
  • smooth muscle cell proliferation Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
N-alpha-acetyltransferase 35, NatC auxiliary subunit
Alternative name(s):
Embryonic growth-associated protein homolog
Protein MAK10 homolog
Gene namesi
Name:NAA35
Synonyms:EGAP, MAK10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:24340. NAA35.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • NatC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165585932.

Polymorphism and mutation databases

BioMutaiNAA35.
DMDMi74747795.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725N-alpha-acetyltransferase 35, NatC auxiliary subunitPRO_0000308614Add
BLAST

Proteomic databases

EPDiQ5VZE5.
MaxQBiQ5VZE5.
PaxDbiQ5VZE5.
PRIDEiQ5VZE5.

PTM databases

PhosphoSiteiQ5VZE5.

Expressioni

Gene expression databases

BgeeiQ5VZE5.
CleanExiHS_MAK10.
GenevisibleiQ5VZE5. HS.

Organism-specific databases

HPAiHPA021547.
HPA051586.

Interactioni

Subunit structurei

Component of the N-terminal acetyltransferase C (NatC) complex, which is composed of NAA35, NAA38 and NAA30.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NAA30Q147X32EBI-9106478,EBI-9106461

Protein-protein interaction databases

BioGridi121941. 3 interactions.
IntActiQ5VZE5. 2 interactions.
STRINGi9606.ENSP00000354972.

Structurei

3D structure databases

ProteinModelPortaliQ5VZE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MAK10 family.Curated

Phylogenomic databases

eggNOGiKOG2343. Eukaryota.
ENOG410XS3T. LUCA.
GeneTreeiENSGT00390000002445.
HOGENOMiHOG000068098.
HOVERGENiHBG099871.
InParanoidiQ5VZE5.
OMAiNHQAKDY.
OrthoDBiEOG7J70F3.
PhylomeDBiQ5VZE5.
TreeFamiTF320627.

Family and domain databases

InterProiIPR007244. NatC_AcTrfase_Mak10.
[Graphical view]
PfamiPF04112. Mak10. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VZE5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVMKASVDDD DSGWELSMPE KMEKSNTNWV DITQDFEEAC RELKLGELLH
60 70 80 90 100
DKLFGLFEAM SAIEMMDPKM DAGMIGNQVN RKVLNFEQAI KDGTIKIKDL
110 120 130 140 150
TLPELIGIMD TCFCCLITWL EGHSLAQTVF TCLYIHNPDF IEDPAMKAFA
160 170 180 190 200
LGILKICDIA REKVNKAAVF EEEDFQSMTY GFKMANSVTD LRVTGMLKDV
210 220 230 240 250
EDDMQRRVKS TRSRQGEERD PEVELEHQQC LAVFSRVKFT RVLLTVLIAF
260 270 280 290 300
TKKETSAVAE AQKLMVQAAD LLSAIHNSLH HGIQAQNDTT KGDHPIMMGF
310 320 330 340 350
EPLVNQRLLP PTFPRYAKII KREEMVNYFA RLIDRIKTVC EVVNLTNLHC
360 370 380 390 400
ILDFFCEFSE QSPCVLSRSL LQTTFLVDNK KVFGTHLMQD MVKDALRSFV
410 420 430 440 450
SPPVLSPKCY LYNNHQAKDC IDSFVTHCVR PFCSLIQIHG HNRARQRDKL
460 470 480 490 500
GHILEEFATL QDEAEKVDAA LHTMLLKQEP QRQHLACLGT WVLYHNLRIM
510 520 530 540 550
IQYLLSGFEL ELYSMHEYYY IYWYLSEFLY AWLMSTLSRA DGSQMAEERI
560 570 580 590 600
MEEQQKGRSS KKTKKKKKVR PLSREITMSQ AYQNMCAGMF KTMVAFDMDG
610 620 630 640 650
KVRKPKFELD SEQVRYEHRF APFNSVMTPP PVHYLQFKEM SDLNKYSPPP
660 670 680 690 700
QSPELYVAAS KHFQQAKMIL ENIPNPDHEV NRILKVAKPN FVVMKLLAGG
710 720
HKKESKVPPE FDFSAHKYFP VVKLV
Length:725
Mass (Da):83,639
Last modified:December 7, 2004 - v1
Checksum:iA5612BA0CE1BAE3F
GO
Isoform 2 (identifier: Q5VZE5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-294: DH → GL
     295-725: Missing.

Note: No experimental confirmation available.
Show »
Length:294
Mass (Da):33,165
Checksum:iD50F844F5309E00B
GO

Sequence cautioni

The sequence BAB15097.1 differs from that shown. Reason: Frameshift at position 518. Curated
The sequence BAB15435.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291Q → R in BAB15097 (PubMed:14702039).Curated
Sequence conflicti487 – 4871C → W in BAB15097 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei293 – 2942DH → GL in isoform 2. 1 PublicationVSP_056098
Alternative sequencei295 – 725431Missing in isoform 2. 1 PublicationVSP_056099Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025266 mRNA. Translation: BAB15097.1. Frameshift.
AK026296 mRNA. Translation: BAB15435.1. Different initiation.
AK056059 mRNA. Translation: BAG51612.1.
AL161447, AL161453, AL353743 Genomic DNA. Translation: CAH73155.1.
AL353743, AL161447, AL161453 Genomic DNA. Translation: CAI12659.1.
AL161453, AL161447, AL353743 Genomic DNA. Translation: CAI16313.1.
CH471089 Genomic DNA. Translation: EAW62702.1.
CH471089 Genomic DNA. Translation: EAW62703.1.
BC117427 mRNA. Translation: AAI17428.1.
BC117429 mRNA. Translation: AAI17430.1.
CCDSiCCDS6673.1. [Q5VZE5-1]
RefSeqiNP_078911.3. NM_024635.3. [Q5VZE5-1]
XP_005252183.1. XM_005252126.2. [Q5VZE5-1]
XP_005252184.1. XM_005252127.2. [Q5VZE5-1]
XP_011517204.1. XM_011518902.1. [Q5VZE5-1]
UniGeneiHs.436098.

Genome annotation databases

EnsembliENST00000361671; ENSP00000354972; ENSG00000135040. [Q5VZE5-1]
ENST00000376040; ENSP00000365208; ENSG00000135040. [Q5VZE5-2]
GeneIDi60560.
KEGGihsa:60560.
UCSCiuc004aoi.5. human. [Q5VZE5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025266 mRNA. Translation: BAB15097.1. Frameshift.
AK026296 mRNA. Translation: BAB15435.1. Different initiation.
AK056059 mRNA. Translation: BAG51612.1.
AL161447, AL161453, AL353743 Genomic DNA. Translation: CAH73155.1.
AL353743, AL161447, AL161453 Genomic DNA. Translation: CAI12659.1.
AL161453, AL161447, AL353743 Genomic DNA. Translation: CAI16313.1.
CH471089 Genomic DNA. Translation: EAW62702.1.
CH471089 Genomic DNA. Translation: EAW62703.1.
BC117427 mRNA. Translation: AAI17428.1.
BC117429 mRNA. Translation: AAI17430.1.
CCDSiCCDS6673.1. [Q5VZE5-1]
RefSeqiNP_078911.3. NM_024635.3. [Q5VZE5-1]
XP_005252183.1. XM_005252126.2. [Q5VZE5-1]
XP_005252184.1. XM_005252127.2. [Q5VZE5-1]
XP_011517204.1. XM_011518902.1. [Q5VZE5-1]
UniGeneiHs.436098.

3D structure databases

ProteinModelPortaliQ5VZE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121941. 3 interactions.
IntActiQ5VZE5. 2 interactions.
STRINGi9606.ENSP00000354972.

PTM databases

PhosphoSiteiQ5VZE5.

Polymorphism and mutation databases

BioMutaiNAA35.
DMDMi74747795.

Proteomic databases

EPDiQ5VZE5.
MaxQBiQ5VZE5.
PaxDbiQ5VZE5.
PRIDEiQ5VZE5.

Protocols and materials databases

DNASUi60560.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361671; ENSP00000354972; ENSG00000135040. [Q5VZE5-1]
ENST00000376040; ENSP00000365208; ENSG00000135040. [Q5VZE5-2]
GeneIDi60560.
KEGGihsa:60560.
UCSCiuc004aoi.5. human. [Q5VZE5-1]

Organism-specific databases

CTDi60560.
GeneCardsiNAA35.
HGNCiHGNC:24340. NAA35.
HPAiHPA021547.
HPA051586.
neXtProtiNX_Q5VZE5.
PharmGKBiPA165585932.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2343. Eukaryota.
ENOG410XS3T. LUCA.
GeneTreeiENSGT00390000002445.
HOGENOMiHOG000068098.
HOVERGENiHBG099871.
InParanoidiQ5VZE5.
OMAiNHQAKDY.
OrthoDBiEOG7J70F3.
PhylomeDBiQ5VZE5.
TreeFamiTF320627.

Miscellaneous databases

ChiTaRSiNAA35. human.
GenomeRNAii60560.
NextBioi65445.
PROiQ5VZE5.

Gene expression databases

BgeeiQ5VZE5.
CleanExiHS_MAK10.
GenevisibleiQ5VZE5. HS.

Family and domain databases

InterProiIPR007244. NatC_AcTrfase_Mak10.
[Graphical view]
PfamiPF04112. Mak10. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Colon and Small intestine.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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.
  5. "Embryonic growth-associated protein is one subunit of a novel N-terminal acetyltransferase complex essential for embryonic vascular development."
    Wenzlau J.M., Garl P.J., Simpson P., Stenmark K.R., West J., Artinger K.B., Nemenoff R.A., Weiser-Evans M.C.M.
    Circ. Res. 98:846-855(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  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. "Knockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization."
    Starheim K.K., Gromyko D., Evjenth R., Ryningen A., Varhaug J.E., Lillehaug J.R., Arnesen T.
    Mol. Cell. Biol. 29:3569-3581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, IDENTIFICATION IN NATC COMPLEX, SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNAA35_HUMAN
AccessioniPrimary (citable) accession number: Q5VZE5
Secondary accession number(s): Q5VZE6, Q9H631, Q9H703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: December 7, 2004
Last modified: March 16, 2016
This is version 98 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.