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Q9NVI7

- ATD3A_HUMAN

UniProt

Q9NVI7 - ATD3A_HUMAN

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Protein
ATPase family AAA domain-containing protein 3A
Gene
ATAD3A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi400 – 4078ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. nucleoside-triphosphatase activity Source: InterPro

GO - Biological processi

  1. cell growth Source: UniProtKB
  2. negative regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase family AAA domain-containing protein 3A
Gene namesi
Name:ATAD3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:25567. ATAD3A.

Subcellular locationi

Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion matrixmitochondrion nucleoid
Note: In the mitochondrial inner membrane, enriched in sites with the potential to form contacts with the outer membrane. The N-terminal domain interacts with the inner surface of the mitochondrial outer membrane and the C-terminal domain localizes in a specific matrix compartment, where it is associated with nucleoids.5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 294293Mitochondrial intermembrane Reviewed prediction
Add
BLAST
Transmembranei295 – 31218Helical; Reviewed prediction
Add
BLAST
Topological domaini313 – 634322Mitochondrial matrix Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-SubCell
  3. mitochondrial nucleoid Source: UniProtKB-SubCell
  4. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion nucleoid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi341 – 3411V → S: Loss of S100B-binding; when associated with S-345. 1 Publication
Mutagenesisi345 – 3451L → S: Loss of S100B-binding; when associated with S-341. 1 Publication
Mutagenesisi349 – 3502Missing: Decrease in S100B-binding.
Mutagenesisi406 – 4061K → E: No effect on homooligomerization. Immediate fragmentation of the mitochondrial network. 1 Publication
Mutagenesisi459 – 4591D → Q: No effect on homooligomerization. Immediate fragmentation of the mitochondrial network. 1 Publication

Organism-specific databases

PharmGKBiPA134872099.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 634633ATPase family AAA domain-containing protein 3A
PRO_0000084799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei539 – 5391N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NVI7.
PaxDbiQ9NVI7.
PRIDEiQ9NVI7.

PTM databases

PhosphoSiteiQ9NVI7.

Expressioni

Tissue specificityi

Overexpressed in lung adenocarcinomas (at protein level).1 Publication

Inductioni

Up-regulated by Angiotensin/AGT.2 Publications

Gene expression databases

ArrayExpressiQ9NVI7.
BgeeiQ9NVI7.
CleanExiHS_ATAD3A.
GenevestigatoriQ9NVI7.

Interactioni

Subunit structurei

Can form homooligomers. Homodimer formation at the N-terminus may be regulated by ATP and is required for the interaction with the inner surface of the mitochondrial outer membrane and correct mitochondrial homeostasis. Interacts with components of the mitochondrial ribosome and with other proteins involved in mitochondrial RNA metabolism. May also interact with protein involved in lipid metabolism, including STARD9. May interact with FAM210A. Interacts with GADD45GIP1. Interacts with S100B in a Ca(+2)- and Zn(+2)-dependent manner; this interaction probably occurs in the cytosol prior to mitochondrial targeting. S100B could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. Interacts with HSP60/HSPD1. Forms heterooligomers with ATAD3B; this interaction may affect ATAD3A activity.4 Publications

Protein-protein interaction databases

BioGridi120506. 33 interactions.
DIPiDIP-33194N.
IntActiQ9NVI7. 16 interactions.
MINTiMINT-1148423.
STRINGi9606.ENSP00000368030.

Structurei

3D structure databases

ProteinModelPortaliQ9NVI7.
SMRiQ9NVI7. Positions 337-629.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5049Required for interaction with the inner surface of the mitochondrial outer membrane
Add
BLAST
Regioni338 – 35316S100B-binding
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili139 – 267129 Reviewed prediction
Add
BLAST

Domaini

The transmembrane domain and a C-terminal adjacent region contain all information necessary for mitochondrial targeting (1 Publication).

Sequence similaritiesi

Belongs to the AAA ATPase family.

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1223.
HOGENOMiHOG000231291.
HOVERGENiHBG058506.
InParanoidiQ9NVI7.
KOiK17681.
OMAiMQEESAI.
OrthoDBiEOG7J9VP8.
PhylomeDBiQ9NVI7.
TreeFamiTF313922.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR021911. DUF3523.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF12037. DUF3523. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NVI7-1) [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

MSWLFGINKG PKGEGAGPPP PLPPAQPGAE GGGDRGLGDR PAPKDKWSNF    50
DPTGLERAAK AARELEHSRY AKDALNLAQM QEQTLQLEQQ SKLKMRLEAL 100
SLLHTLVWAW SLCRAGAVQT QERLSGSASP EQVPAGECCA LQEYEAAVEQ 150
LKSEQIRAQA EERRKTLSEE TRQHQARAQY QDKLARQRYE DQLKQQQLLN 200
EENLRKQEES VQKQEAMRRA TVEREMELRH KNEMLRVEAE ARARAKAERE 250
NADIIREQIR LKAAEHRQTV LESIRTAGTL FGEGFRAFVT DWDKVTATVA 300
GLTLLAVGVY SAKNATLVAG RFIEARLGKP SLVRETSRIT VLEALRHPIQ 350
VSRRLLSRPQ DALEGVVLSP SLEARVRDIA IATRNTKKNR SLYRNILMYG 400
PPGTGKTLFA KKLALHSGMD YAIMTGGDVA PMGREGVTAM HKLFDWANTS 450
RRGLLLFVDE ADAFLRKRAT EKISEDLRAT LNAFLYRTGQ HSNKFMLVLA 500
SNQPEQFDWA INDRINEMVH FDLPGQEERE RLVRMYFDKY VLKPATEGKQ 550
RLKLAQFDYG RKCSEVARLT EGMSGREIAQ LAVSWQATAY ASEDGVLTEA 600
MMDTRVQDAV QQHQQKMCWL KAEGPGRGDE PSPS 634
Length:634
Mass (Da):71,369
Last modified:September 13, 2005 - v2
Checksum:i47E765629B6F3267
GO
Isoform 2 (identifier: Q9NVI7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-142: Missing.

Note: May be the predominant ATAD3A form.

Show »
Length:586
Mass (Da):66,218
Checksum:i1E83D08AE33D550F
GO
Isoform 3 (identifier: Q9NVI7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     95-142: Missing.

Note: No experimental confirmation available.

Show »
Length:507
Mass (Da):57,948
Checksum:i759827DA09CDDC15
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151G → D.1 Publication
Corresponds to variant rs2274435 [ dbSNP | Ensembl ].
VAR_023526
Natural varianti101 – 1011S → N.
Corresponds to variant rs1619896 [ dbSNP | Ensembl ].
VAR_055468

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7979Missing in isoform 3.
VSP_044145Add
BLAST
Alternative sequencei95 – 14248Missing in isoform 2 and isoform 3.
VSP_015636Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241R → Q in BAG51625. 1 Publication
Sequence conflicti255 – 2551I → T in BAC03595. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GU189416 mRNA. Translation: ACZ80514.1.
AK001571 mRNA. Translation: BAA91764.1.
AK056099 mRNA. Translation: BAG51625.1.
AK091144 mRNA. Translation: BAC03595.1.
AL645728 Genomic DNA. Translation: CAI22954.1.
AL645728 Genomic DNA. Translation: CAI22955.1.
CH471183 Genomic DNA. Translation: EAW56187.1.
CH471183 Genomic DNA. Translation: EAW56190.1.
BC007803 mRNA. Translation: AAH07803.1.
BC011814 mRNA. Translation: AAH11814.1.
BC014101 mRNA. Translation: AAH14101.1.
BC033109 mRNA. Translation: AAH33109.1.
BC063607 mRNA. Translation: AAH63607.1.
CCDSiCCDS31.1. [Q9NVI7-1]
CCDS53259.1. [Q9NVI7-2]
CCDS53260.1. [Q9NVI7-3]
RefSeqiNP_001164006.1. NM_001170535.1. [Q9NVI7-2]
NP_001164007.1. NM_001170536.1. [Q9NVI7-3]
NP_060658.3. NM_018188.3. [Q9NVI7-1]
UniGeneiHs.23413.

Genome annotation databases

EnsembliENST00000378755; ENSP00000368030; ENSG00000197785. [Q9NVI7-1]
ENST00000378756; ENSP00000368031; ENSG00000197785. [Q9NVI7-2]
ENST00000536055; ENSP00000439290; ENSG00000197785. [Q9NVI7-3]
GeneIDi55210.
KEGGihsa:55210.
UCSCiuc001afz.2. human. [Q9NVI7-1]
uc001aga.2. human. [Q9NVI7-2]
uc001agb.2. human. [Q9NVI7-3]

Polymorphism databases

DMDMi84028405.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GU189416 mRNA. Translation: ACZ80514.1 .
AK001571 mRNA. Translation: BAA91764.1 .
AK056099 mRNA. Translation: BAG51625.1 .
AK091144 mRNA. Translation: BAC03595.1 .
AL645728 Genomic DNA. Translation: CAI22954.1 .
AL645728 Genomic DNA. Translation: CAI22955.1 .
CH471183 Genomic DNA. Translation: EAW56187.1 .
CH471183 Genomic DNA. Translation: EAW56190.1 .
BC007803 mRNA. Translation: AAH07803.1 .
BC011814 mRNA. Translation: AAH11814.1 .
BC014101 mRNA. Translation: AAH14101.1 .
BC033109 mRNA. Translation: AAH33109.1 .
BC063607 mRNA. Translation: AAH63607.1 .
CCDSi CCDS31.1. [Q9NVI7-1 ]
CCDS53259.1. [Q9NVI7-2 ]
CCDS53260.1. [Q9NVI7-3 ]
RefSeqi NP_001164006.1. NM_001170535.1. [Q9NVI7-2 ]
NP_001164007.1. NM_001170536.1. [Q9NVI7-3 ]
NP_060658.3. NM_018188.3. [Q9NVI7-1 ]
UniGenei Hs.23413.

3D structure databases

ProteinModelPortali Q9NVI7.
SMRi Q9NVI7. Positions 337-629.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120506. 33 interactions.
DIPi DIP-33194N.
IntActi Q9NVI7. 16 interactions.
MINTi MINT-1148423.
STRINGi 9606.ENSP00000368030.

PTM databases

PhosphoSitei Q9NVI7.

Polymorphism databases

DMDMi 84028405.

Proteomic databases

MaxQBi Q9NVI7.
PaxDbi Q9NVI7.
PRIDEi Q9NVI7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378755 ; ENSP00000368030 ; ENSG00000197785 . [Q9NVI7-1 ]
ENST00000378756 ; ENSP00000368031 ; ENSG00000197785 . [Q9NVI7-2 ]
ENST00000536055 ; ENSP00000439290 ; ENSG00000197785 . [Q9NVI7-3 ]
GeneIDi 55210.
KEGGi hsa:55210.
UCSCi uc001afz.2. human. [Q9NVI7-1 ]
uc001aga.2. human. [Q9NVI7-2 ]
uc001agb.2. human. [Q9NVI7-3 ]

Organism-specific databases

CTDi 55210.
GeneCardsi GC01P001439.
HGNCi HGNC:25567. ATAD3A.
MIMi 612316. gene.
neXtProti NX_Q9NVI7.
PharmGKBi PA134872099.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1223.
HOGENOMi HOG000231291.
HOVERGENi HBG058506.
InParanoidi Q9NVI7.
KOi K17681.
OMAi MQEESAI.
OrthoDBi EOG7J9VP8.
PhylomeDBi Q9NVI7.
TreeFami TF313922.

Miscellaneous databases

ChiTaRSi ATAD3A. human.
GenomeRNAii 55210.
NextBioi 59150.
PROi Q9NVI7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NVI7.
Bgeei Q9NVI7.
CleanExi HS_ATAD3A.
Genevestigatori Q9NVI7.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR021911. DUF3523.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
PF12037. DUF3523. 2 hits.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in lung adenocarcinoma cells."
    Fang H.Y., Chang C.L., Hsu S.H., Huang C.Y., Chiang S.F., Chiou S.H., Huang C.H., Hsiao Y.T., Lin T.Y., Chiang I.P., Hsu W.H., Sugano S., Chen C.Y., Lin C.Y., Ko W.J., Chow K.C.
    J. Cell Sci. 123:1171-1180(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Lung adenocarcinoma.
  2. "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; 2 AND 3).
    Tissue: Teratocarcinoma and Tongue.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORM 2), VARIANT ASP-15.
    Tissue: Brain and Skin.
  6. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-9; 250-256; 276-286; 339-346; 443-451; 479-487 AND 606-616 (ISOFORMS 1/2), PROTEIN SEQUENCE OF 93-152 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  7. "The AAA+ protein ATAD3 has displacement loop binding properties and is involved in mitochondrial nucleoid organization."
    He J., Mao C.C., Reyes A., Sembongi H., Di Re M., Granycome C., Clippingdale A.B., Fearnley I.M., Harbour M., Robinson A.J., Reichelt S., Spelbrink J.N., Walker J.E., Holt I.J.
    J. Cell Biol. 176:141-146(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH NUCLEOIDS.
  8. "The layered structure of human mitochondrial DNA nucleoids."
    Bogenhagen D.F., Rousseau D., Burke S.
    J. Biol. Chem. 283:3665-3675(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, ASSOCIATION WITH NUCLEOIDS.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Topological analysis of ATAD3A insertion in purified human mitochondria."
    Hubstenberger A., Merle N., Charton R., Brandolin G., Rousseau D.
    J. Bioenerg. Biomembr. 42:143-150(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
  12. "The AAA+ ATPase ATAD3A controls mitochondrial dynamics at the interface of the inner and outer membranes."
    Gilquin B., Taillebourg E., Cherradi N., Hubstenberger A., Gay O., Merle N., Assard N., Fauvarque M.O., Tomohiro S., Kuge O., Baudier J.
    Mol. Cell. Biol. 30:1984-1996(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMOOLIGOMERIZATION, INDUCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF LYS-406 AND ASP-459.
  13. "The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A."
    Gilquin B., Cannon B.R., Hubstenberger A., Moulouel B., Falk E., Merle N., Assard N., Kieffer S., Rousseau D., Wilder P.T., Weber D.J., Baudier J.
    Mol. Cell. Biol. 30:2724-2736(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100B, MUTAGENESIS OF VAL-341; LEU-345 AND 349-ILE-GLN-350.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-expressed in cancer cells, that functions as dominant negative for the ubiquitous ATAD3A."
    Merle N., Feraud O., Gilquin B., Hubstenberger A., Kieffer-Jacquinot S., Assard N., Bennaceur-Griscelli A., Honnorat J., Baudier J.
    Mitochondrion 12:441-448(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATAD3B AND HSPD1.
  16. Cited for: FUNCTION, INTERACTION WITH PROTEINS INVOLVED IN MITOCHONDRIAL TRANSLATION; RNA METABOLISM; LIPID METABOLISM; GADD45GIP1 AND FAM210A, INDUCTION.

Entry informationi

Entry nameiATD3A_HUMAN
AccessioniPrimary (citable) accession number: Q9NVI7
Secondary accession number(s): B3KPB3
, D2K8Q1, G3V1I6, Q5SV23, Q8N275, Q96A50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: September 3, 2014
This is version 122 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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