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Protein

ATPase family AAA domain-containing protein 3B

Gene

ATAD3B

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

Functioni

May play a role in a mitochondrial network organization typical for stem cells, characterized by reduced mitochondrial metabolism, low mtDNA copies and fragmentated mitochondrial network. may act by suppressing ATAD3A function, interfering with ATAD3A interaction with matrix nucleoid complexes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi352 – 3598ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase family AAA domain-containing protein 3B
Alternative name(s):
AAA-TOB3
Gene namesi
Name:ATAD3B
Synonyms:KIAA1273, TOB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24007. ATAD3B.

Subcellular locationi

Mitochondrion inner membrane 2 Publications; Peripheral membrane protein 2 Publications
Note: Has been found to co-purify with nucleoids (PubMed:22453275). Since it does not face the mitochondrial matrix, the association with nucleoids could be mediated by ATAD3A.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 246245Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Intramembranei247 – 26418HelicalSequence AnalysisAdd
BLAST
Topological domaini265 – 648384Mitochondrial intermembraneSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134993325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 648647ATPase family AAA domain-containing protein 3BPRO_0000084800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei427 – 4271N6-acetyllysine1 Publication
Modified residuei495 – 4951N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ5T9A4.
PaxDbiQ5T9A4.
PRIDEiQ5T9A4.

PTM databases

PhosphoSiteiQ5T9A4.

Expressioni

Tissue specificityi

Tends to be down-regulated in differentiated cells and re-expressed in pluripotent stem cells or cancer cells (at protein level).2 Publications

Developmental stagei

Expressed in proliferating embryonic stem cells and down-regulated during differentiation.1 Publication

Inductioni

Up-regulated by MYC.1 Publication

Gene expression databases

BgeeiQ5T9A4.
CleanExiHS_ATAD3B.
ExpressionAtlasiQ5T9A4. baseline and differential.
GenevestigatoriQ5T9A4.

Organism-specific databases

HPAiHPA058968.

Interactioni

Subunit structurei

Forms heterooligomers with ATAD3A. Interacts with components of the mitochondrial ribosome, including MRPL11 and MRPS18B, and with other proteins involved in mitochondrial RNA metabolism, possibly via interaction with ATAD3A. Interacts with GADD45GIP1.2 Publications

Protein-protein interaction databases

BioGridi123774. 25 interactions.
IntActiQ5T9A4. 11 interactions.
STRINGi9606.ENSP00000311766.

Structurei

3D structure databases

ProteinModelPortaliQ5T9A4.
SMRiQ5T9A4. Positions 289-571.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili69 – 214146Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 247Poly-Pro

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0465.
GeneTreeiENSGT00730000111059.
HOGENOMiHOG000231291.
HOVERGENiHBG058506.
InParanoidiQ5T9A4.
KOiK17681.
OMAiNAFLYHM.
OrthoDBiEOG7J9VP8.
PhylomeDBiQ5T9A4.
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. 1 hit.
[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. AlignAdd to basket

Isoform 1 (identifier: Q5T9A4-1) [UniParc]FASTAAdd to basket

Also known as: AAA-TOB3l

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
MSWLFGVNKG PKGEGAGPPP PLPPAQPGAE GGGDRGLGDR PAPKDKWSNF
60 70 80 90 100
DPTGLERAAK AARELEHSRY AKEALNLAQM QEQTLQLEQQ SKLKEYEAAV
110 120 130 140 150
EQLKSEQIRA QAEERRKTLS EETRQHQARA QYQDKLARQR YEDQLKQQQL
160 170 180 190 200
LNEENLRKQE ESVQKQEAMR RATVEREMEL RHKNEMLRVE TEARARAKAE
210 220 230 240 250
RENADIIREQ IRLKASEHRQ TVLESIRTAG TLFGEGFRAF VTDRDKVTAT
260 270 280 290 300
VAGLTLLAVG VYSAKNATAV TGRFIEARLG KPSLVRETSR ITVLEALRHP
310 320 330 340 350
IQVSRRLLSR PQDVLEGVVL SPSLEARVRD IAIATRNTKK NRGLYRHILL
360 370 380 390 400
YGPPGTGKTL FAKKLALHSG MDYAIMTGGD VAPMGREGVT AMHKLFDWAN
410 420 430 440 450
TSRRGLLLFM DEADAFLRKR ATEEISKDLR ATLNAFLYHM GQHSNKFMLV
460 470 480 490 500
LASNLPEQFD CAINSRIDVM VHFDLPQQEE RERLVRLHFD NCVLKPATEG
510 520 530 540 550
KRRLKLAQFD YGRKCSEVAR LTEGMSGREI AQLAVSWQAT AYASKDGVLT
560 570 580 590 600
EAMMDACVQD AVQQYRQKMR WLKAEGPGRG VEHPLSGVQG ETLTSWSLAT
610 620 630 640
DPSYPCLAGP CTFRICSWMG TGLCPGPLSP RMSCGGGRPF CPPGHPLL
Length:648
Mass (Da):72,573
Last modified:December 21, 2004 - v1
Checksum:i5133DB55E3415707
GO
Isoform 2 (identifier: Q5T9A4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
     119-128: LSEETRQHQA → MCLCRPLLPQ
     252-284: AGLTLLAVGVYSAKNATAVTGRFIEARLGKPSL → NIFIKQGWQVAERQHVGASWSPRSCPCRLCTAL
     285-648: Missing.

Note: No experimental confirmation available.

Show »
Length:166
Mass (Da):19,508
Checksum:i15325B2EF9B86B13
GO
Isoform 3 (identifier: Q5T9A4-3) [UniParc]FASTAAdd to basket

Also known as: AAA-TOB3s

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.
     47-94: WSNFDPTGLE...LQLEQQSKLK → MQLEALNLLH...VPAGECCALQ

Show »
Length:602
Mass (Da):67,608
Checksum:iC787D0F1D620B06F
GO

Sequence cautioni

The sequence BAA86587.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491Q → R in AAH02542 (PubMed:15489334).Curated
Sequence conflicti149 – 1491Q → R in AAH18701 (PubMed:15489334).Curated
Sequence conflicti153 – 1531E → V in AK128357 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71V → I.
Corresponds to variant rs1240504 [ dbSNP | Ensembl ].
VAR_048120

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 2. 1 PublicationVSP_015637Add
BLAST
Alternative sequencei1 – 4646Missing in isoform 3. 2 PublicationsVSP_015638Add
BLAST
Alternative sequencei47 – 9448WSNFD…QSKLK → MQLEALNLLHTLVWARSLCR AGAVQTQERLSGSASPEQVP AGECCALQ in isoform 3. 2 PublicationsVSP_015639Add
BLAST
Alternative sequencei119 – 12810LSEETRQHQA → MCLCRPLLPQ in isoform 2. 1 PublicationVSP_015640
Alternative sequencei252 – 28433AGLTL…GKPSL → NIFIKQGWQVAERQHVGASW SPRSCPCRLCTAL in isoform 2. 1 PublicationVSP_015641Add
BLAST
Alternative sequencei285 – 648364Missing in isoform 2. 1 PublicationVSP_015642Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033099 mRNA. Translation: BAA86587.1. Different initiation.
AK128357 mRNA. No translation available.
AK290586 mRNA. Translation: BAF83275.1.
AL157945 Genomic DNA. Translation: CAI22068.1.
CH471183 Genomic DNA. Translation: EAW56193.1.
BC002542 mRNA. Translation: AAH02542.1.
BC009938 mRNA. No translation available.
BC018701 mRNA. Translation: AAH18701.1.
CCDSiCCDS30.1. [Q5T9A4-1]
RefSeqiNP_114127.3. NM_031921.4. [Q5T9A4-1]
UniGeneiHs.729021.

Genome annotation databases

EnsembliENST00000308647; ENSP00000311766; ENSG00000160072. [Q5T9A4-1]
GeneIDi83858.
KEGGihsa:83858.
UCSCiuc001afv.3. human. [Q5T9A4-1]
uc001afw.2. human. [Q5T9A4-2]
uc001afx.3. human. [Q5T9A4-3]

Polymorphism databases

DMDMi74745646.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033099 mRNA. Translation: BAA86587.1. Different initiation.
AK128357 mRNA. No translation available.
AK290586 mRNA. Translation: BAF83275.1.
AL157945 Genomic DNA. Translation: CAI22068.1.
CH471183 Genomic DNA. Translation: EAW56193.1.
BC002542 mRNA. Translation: AAH02542.1.
BC009938 mRNA. No translation available.
BC018701 mRNA. Translation: AAH18701.1.
CCDSiCCDS30.1. [Q5T9A4-1]
RefSeqiNP_114127.3. NM_031921.4. [Q5T9A4-1]
UniGeneiHs.729021.

3D structure databases

ProteinModelPortaliQ5T9A4.
SMRiQ5T9A4. Positions 289-571.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123774. 25 interactions.
IntActiQ5T9A4. 11 interactions.
STRINGi9606.ENSP00000311766.

PTM databases

PhosphoSiteiQ5T9A4.

Polymorphism databases

DMDMi74745646.

Proteomic databases

MaxQBiQ5T9A4.
PaxDbiQ5T9A4.
PRIDEiQ5T9A4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308647; ENSP00000311766; ENSG00000160072. [Q5T9A4-1]
GeneIDi83858.
KEGGihsa:83858.
UCSCiuc001afv.3. human. [Q5T9A4-1]
uc001afw.2. human. [Q5T9A4-2]
uc001afx.3. human. [Q5T9A4-3]

Organism-specific databases

CTDi83858.
GeneCardsiGC01P001397.
HGNCiHGNC:24007. ATAD3B.
HPAiHPA058968.
MIMi612317. gene.
neXtProtiNX_Q5T9A4.
PharmGKBiPA134993325.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0465.
GeneTreeiENSGT00730000111059.
HOGENOMiHOG000231291.
HOVERGENiHBG058506.
InParanoidiQ5T9A4.
KOiK17681.
OMAiNAFLYHM.
OrthoDBiEOG7J9VP8.
PhylomeDBiQ5T9A4.
TreeFamiTF313922.

Miscellaneous databases

ChiTaRSiATAD3B. human.
GenomeRNAii83858.
NextBioi72857.
PROiQ5T9A4.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T9A4.
CleanExiHS_ATAD3B.
ExpressionAtlasiQ5T9A4. baseline and differential.
GenevestigatoriQ5T9A4.

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. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  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 AND 2).
    Tissue: Thymus.
  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] (ISOFORMS 1 AND 3).
    Tissue: Leiomyosarcoma and Placenta.
  6. "Molecular characterization of the tumor-associated antigen AAA-TOB3."
    Schaffrik M., Mack B., Matthias C., Rauch J., Gires O.
    Cell. Mol. Life Sci. 63:2162-2174(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ISOFORMS 1 AND 3, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
  7. "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.
  8. "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-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: FUNCTION, INTERACTION WITH ATAD3A, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, TOPOLOGY.
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: INTERACTION WITH PROTEINS INVOLVED IN MITOCHONDRIAL TRANSLATION; RNA METABOLISM; ATAD3A AND GADD45GIP1.

Entry informationi

Entry nameiATD3B_HUMAN
AccessioniPrimary (citable) accession number: Q5T9A4
Secondary accession number(s): A8K3H1
, Q6ZRB5, Q9BUK4, Q9ULE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 21, 2004
Last modified: March 4, 2015
This is version 101 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 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

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 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.