Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NVI7 (ATD3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATPase family AAA domain-containing protein 3A
Gene names
Name:ATAD3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 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. 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 634633ATPase family AAA domain-containing protein 3A
PRO_0000084799

Regions

Topological domain2 – 294293Mitochondrial intermembrane Potential
Transmembrane295 – 31218Helical; Potential
Topological domain313 – 634322Mitochondrial matrix Potential
Nucleotide binding400 – 4078ATP Potential
Region2 – 5049Required for interaction with the inner surface of the mitochondrial outer membrane
Region338 – 35316S100B-binding
Coiled coil139 – 267129 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue5391N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 7979Missing in isoform 3.
VSP_044145
Alternative sequence95 – 14248Missing in isoform 2 and isoform 3.
VSP_015636
Natural variant151G → D. Ref.5
Corresponds to variant rs2274435 [ dbSNP | Ensembl ].
VAR_023526
Natural variant1011S → N.
Corresponds to variant rs1619896 [ dbSNP | Ensembl ].
VAR_055468

Experimental info

Mutagenesis3411V → S: Loss of S100B-binding; when associated with S-345. Ref.13
Mutagenesis3451L → S: Loss of S100B-binding; when associated with S-341. Ref.13
Mutagenesis349 – 3502Missing: Decrease in S100B-binding.
Mutagenesis4061K → E: No effect on homooligomerization. Immediate fragmentation of the mitochondrial network. Ref.12
Mutagenesis4591D → Q: No effect on homooligomerization. Immediate fragmentation of the mitochondrial network. Ref.12
Sequence conflict2241R → Q in BAG51625. Ref.2
Sequence conflict2551I → T in BAC03595. Ref.2

Sequences

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

Last modified September 13, 2005. Version 2.
Checksum: 47E765629B6F3267

FASTA63471,369
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 1E83D08AE33D550F
Show »

FASTA58666,218
Isoform 3 [UniParc].

Checksum: 759827DA09CDDC15
Show »

FASTA50757,948

References

« Hide '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. 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] (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. expand/collapse author list , 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. 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 (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, 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]"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.
CCDSCCDS31.1. [Q9NVI7-1]
CCDS53259.1. [Q9NVI7-2]
CCDS53260.1. [Q9NVI7-3]
RefSeqNP_001164006.1. NM_001170535.1. [Q9NVI7-2]
NP_001164007.1. NM_001170536.1. [Q9NVI7-3]
NP_060658.3. NM_018188.3. [Q9NVI7-1]
UniGeneHs.23413.

3D structure databases

ProteinModelPortalQ9NVI7.
SMRQ9NVI7. Positions 337-629.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120506. 47 interactions.
DIPDIP-33194N.
IntActQ9NVI7. 16 interactions.
MINTMINT-1148423.
STRING9606.ENSP00000368030.

PTM databases

PhosphoSiteQ9NVI7.

Polymorphism databases

DMDM84028405.

Proteomic databases

MaxQBQ9NVI7.
PaxDbQ9NVI7.
PRIDEQ9NVI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378755; ENSP00000368030; ENSG00000197785. [Q9NVI7-1]
ENST00000378756; ENSP00000368031; ENSG00000197785. [Q9NVI7-2]
ENST00000536055; ENSP00000439290; ENSG00000197785. [Q9NVI7-3]
GeneID55210.
KEGGhsa:55210.
UCSCuc001afz.2. human. [Q9NVI7-1]
uc001aga.2. human. [Q9NVI7-2]
uc001agb.2. human. [Q9NVI7-3]

Organism-specific databases

CTD55210.
GeneCardsGC01P001439.
HGNCHGNC:25567. ATAD3A.
MIM612316. gene.
neXtProtNX_Q9NVI7.
PharmGKBPA134872099.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1223.
HOGENOMHOG000231291.
HOVERGENHBG058506.
InParanoidQ9NVI7.
KOK17681.
OMAMQEESAI.
OrthoDBEOG7J9VP8.
PhylomeDBQ9NVI7.
TreeFamTF313922.

Gene expression databases

ArrayExpressQ9NVI7.
BgeeQ9NVI7.
CleanExHS_ATAD3A.
GenevestigatorQ9NVI7.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR021911. DUF3523.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF12037. DUF3523. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATAD3A. human.
GenomeRNAi55210.
NextBio59150.
PROQ9NVI7.
SOURCESearch...

Entry information

Entry nameATD3A_HUMAN
AccessionPrimary (citable) accession number: Q9NVI7
Secondary accession number(s): B3KPB3 expand/collapse secondary AC list , D2K8Q1, G3V1I6, Q5SV23, Q8N275, Q96A50
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 121 of the entry and version 2 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 1

Human chromosome 1: entries, gene names and cross-references to MIM