Q9NVI7 (ATD3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATPase family AAA domain-containing protein 3A

Gene names

Name:

ATAD3A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.12 Ref.16
Subunit structure	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. Ref.12 Ref.13 Ref.15 Ref.16
Subcellular location	Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion matrix › mitochondrion 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. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12
Tissue specificity	Overexpressed in lung adenocarcinomas (at protein level). Ref.1
Induction	Up-regulated by Angiotensin/AGT. Ref.12 Ref.16
Domain	The transmembrane domain and a C-terminal adjacent region contain all information necessary for mitochondrial targeting (Ref.12).
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane Mitochondrion nucleoid
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell growth Inferred from mutant phenotype Ref.1. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial nucleoid Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NVI7-1)

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: Q9NVI7-2)

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

Note: May be the predominant ATAD3A form.

Isoform 3 (identifier: Q9NVI7-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 634	633	ATPase family AAA domain-containing protein 3A		PRO_0000084799
Regions
	Topological domain	2 – 294	293	Mitochondrial intermembrane Potential
	Transmembrane	295 – 312	18	Helical; Potential
	Topological domain	313 – 634	322	Mitochondrial matrix Potential
	Nucleotide binding	400 – 407	8	ATP Potential
	Region	2 – 50	49	Required for interaction with the inner surface of the mitochondrial outer membrane
	Region	338 – 353	16	S100B-binding
	Coiled coil	139 – 267	129	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.6
	Modified residue	539	1	N6-acetyllysine Ref.10
Natural variations
	Alternative sequence	1 – 79	79	Missing in isoform 3.		VSP_044145
	Alternative sequence	95 – 142	48	Missing in isoform 2 and isoform 3.		VSP_015636
	Natural variant	15	1	G → D. Ref.5 Corresponds to variant rs2274435 [ dbSNP | Ensembl ].		VAR_023526
	Natural variant	101	1	S → N. Corresponds to variant rs1619896 [ dbSNP | Ensembl ].		VAR_055468
Experimental info
	Mutagenesis	341	1	V → S: Loss of S100B-binding; when associated with S-345. Ref.13
	Mutagenesis	345	1	L → S: Loss of S100B-binding; when associated with S-341. Ref.13
	Mutagenesis	349 – 350	2	Missing: Decrease in S100B-binding.
	Mutagenesis	406	1	K → E: No effect on homooligomerization. Immediate fragmentation of the mitochondrial network. Ref.12
	Mutagenesis	459	1	D → Q: No effect on homooligomerization. Immediate fragmentation of the mitochondrial network. Ref.12
	Sequence conflict	224	1	R → Q in BAG51625. Ref.2
	Sequence conflict	255	1	I → T in BAC03595. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 47E765629B6F3267	FASTA	634	71,369
	10 20 30 40 50 60 MSWLFGINKG PKGEGAGPPP PLPPAQPGAE GGGDRGLGDR PAPKDKWSNF DPTGLERAAK 70 80 90 100 110 120 AARELEHSRY AKDALNLAQM QEQTLQLEQQ SKLKMRLEAL SLLHTLVWAW SLCRAGAVQT 130 140 150 160 170 180 QERLSGSASP EQVPAGECCA LQEYEAAVEQ LKSEQIRAQA EERRKTLSEE TRQHQARAQY 190 200 210 220 230 240 QDKLARQRYE DQLKQQQLLN EENLRKQEES VQKQEAMRRA TVEREMELRH KNEMLRVEAE 250 260 270 280 290 300 ARARAKAERE NADIIREQIR LKAAEHRQTV LESIRTAGTL FGEGFRAFVT DWDKVTATVA 310 320 330 340 350 360 GLTLLAVGVY SAKNATLVAG RFIEARLGKP SLVRETSRIT VLEALRHPIQ VSRRLLSRPQ 370 380 390 400 410 420 DALEGVVLSP SLEARVRDIA IATRNTKKNR SLYRNILMYG PPGTGKTLFA KKLALHSGMD 430 440 450 460 470 480 YAIMTGGDVA PMGREGVTAM HKLFDWANTS RRGLLLFVDE ADAFLRKRAT EKISEDLRAT 490 500 510 520 530 540 LNAFLYRTGQ HSNKFMLVLA SNQPEQFDWA INDRINEMVH FDLPGQEERE RLVRMYFDKY 550 560 570 580 590 600 VLKPATEGKQ RLKLAQFDYG RKCSEVARLT EGMSGREIAQ LAVSWQATAY ASEDGVLTEA 610 620 630 MMDTRVQDAV QQHQQKMCWL KAEGPGRGDE PSPS
	Isoform 2 [UniParc]. Checksum: 1E83D08AE33D550F	FASTA	586	66,218
	10 20 30 40 50 60 MSWLFGINKG PKGEGAGPPP PLPPAQPGAE GGGDRGLGDR PAPKDKWSNF DPTGLERAAK 70 80 90 100 110 120 AARELEHSRY AKDALNLAQM QEQTLQLEQQ SKLKEYEAAV EQLKSEQIRA QAEERRKTLS 130 140 150 160 170 180 EETRQHQARA QYQDKLARQR YEDQLKQQQL LNEENLRKQE ESVQKQEAMR RATVEREMEL 190 200 210 220 230 240 RHKNEMLRVE AEARARAKAE RENADIIREQ IRLKAAEHRQ TVLESIRTAG TLFGEGFRAF 250 260 270 280 290 300 VTDWDKVTAT VAGLTLLAVG VYSAKNATLV AGRFIEARLG KPSLVRETSR ITVLEALRHP 310 320 330 340 350 360 IQVSRRLLSR PQDALEGVVL SPSLEARVRD IAIATRNTKK NRSLYRNILM YGPPGTGKTL 370 380 390 400 410 420 FAKKLALHSG MDYAIMTGGD VAPMGREGVT AMHKLFDWAN TSRRGLLLFV DEADAFLRKR 430 440 450 460 470 480 ATEKISEDLR ATLNAFLYRT GQHSNKFMLV LASNQPEQFD WAINDRINEM VHFDLPGQEE 490 500 510 520 530 540 RERLVRMYFD KYVLKPATEG KQRLKLAQFD YGRKCSEVAR LTEGMSGREI AQLAVSWQAT 550 560 570 580 AYASEDGVLT EAMMDTRVQD AVQQHQQKMC WLKAEGPGRG DEPSPS
	Isoform 3 [UniParc]. Checksum: 759827DA09CDDC15	FASTA	507	57,948
	10 20 30 40 50 60 MQEQTLQLEQ QSKLKEYEAA VEQLKSEQIR AQAEERRKTL SEETRQHQAR AQYQDKLARQ 70 80 90 100 110 120 RYEDQLKQQQ LLNEENLRKQ EESVQKQEAM RRATVEREME LRHKNEMLRV EAEARARAKA 130 140 150 160 170 180 ERENADIIRE QIRLKAAEHR QTVLESIRTA GTLFGEGFRA FVTDWDKVTA TVAGLTLLAV 190 200 210 220 230 240 GVYSAKNATL VAGRFIEARL GKPSLVRETS RITVLEALRH PIQVSRRLLS RPQDALEGVV 250 260 270 280 290 300 LSPSLEARVR DIAIATRNTK KNRSLYRNIL MYGPPGTGKT LFAKKLALHS GMDYAIMTGG 310 320 330 340 350 360 DVAPMGREGV TAMHKLFDWA NTSRRGLLLF VDEADAFLRK RATEKISEDL RATLNAFLYR 370 380 390 400 410 420 TGQHSNKFML VLASNQPEQF DWAINDRINE MVHFDLPGQE ERERLVRMYF DKYVLKPATE 430 440 450 460 470 480 GKQRLKLAQF DYGRKCSEVA RLTEGMSGRE IAQLAVSWQA TAYASEDGVL TEAMMDTRVQ 490 500 DAVQQHQQKM CWLKAEGPGR GDEPSPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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. , 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 (JUL-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] (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, 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, MASS SPECTROMETRY.
[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]	"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].
[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]	"Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis." He J., Cooper H.M., Reyes A., Di Re M., Sembongi H., Litwin T.R., Gao J., Neuman K.C., Fearnley I.M., Spinazzola A., Walker J.E., Holt I.J. Nucleic Acids Res. 40:6109-6121(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PROTEINS INVOLVED IN MITOCHONDRIAL TRANSLATION; RNA METABOLISM; LIPID METABOLISM; GADD45GIP1 AND FAM210A, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00295992. IPI00643435.
RefSeq	NP_001164006.1. NM_001170535.1. NP_001164007.1. NM_001170536.1. NP_060658.3. NM_018188.3.
UniGene	Hs.23413.
3D structure databases
ProteinModelPortal	Q9NVI7.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33194N.
IntAct	Q9NVI7. 10 interactions.
MINT	MINT-1148423.
STRING	9606.ENSP00000368030.
PTM databases
PhosphoSite	Q9NVI7.
Polymorphism databases
DMDM	84028405.
Proteomic databases
PaxDb	Q9NVI7.
PRIDE	Q9NVI7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378755; ENSP00000368030; ENSG00000197785. ENST00000378756; ENSP00000368031; ENSG00000197785. ENST00000536055; ENSP00000439290; ENSG00000197785.
GeneID	55210.
KEGG	hsa:55210.
UCSC	uc001afz.2. human.
Organism-specific databases
CTD	55210.
GeneCards	GC01P001439.
HGNC	HGNC:25567. ATAD3A.
MIM	612316. gene.
neXtProt	NX_Q9NVI7.
PharmGKB	PA134872099.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1223.
HOGENOM	HOG000231291.
HOVERGEN	HBG058506.
InParanoid	Q9NVI7.
OMA	MMDTRVQ.
PhylomeDB	Q9NVI7.
Gene expression databases
ArrayExpress	Q9NVI7.
Bgee	Q9NVI7.
CleanEx	HS_ATAD3A.
Genevestigator	Q9NVI7.
GermOnline	ENSG00000197785. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR021911. DUF3523. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF12037. DUF3523. 2 hits. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATAD3A. human.
GenomeRNAi	55210.
NextBio	59150.
SOURCE	Search...

Entry information

Entry name

ATD3A_HUMAN

Accession

Primary (citable) accession number: Q9NVI7
Secondary accession number(s): B3KPB3 , D2K8Q1, G3V1I6, Q5SV23, Q8N275, Q96A50

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.