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Q6PL18 (ATAD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 2

EC=3.6.1.3
Alternative name(s):
AAA nuclear coregulator cancer-associated protein
Short name=ANCCA
Gene names
Name:ATAD2
ORF Names:L16, PRO2000
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be a transcriptional coactivator of the nuclear receptor ESR1 required to induce the expression of a subset of estradiol target genes, such as CCND1, MYC and E2F1. May play a role in the recruitment or occupancy of CREBBP at some ESR1 target gene promoters. May be required for histone hyperacetylation. Involved in the estrogen-induced cell proliferation and cell cycle progression of breast cancer cells. Ref.11

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with ESR1 and NCOA3 and these interactions are enhanced by estradiol. Interacts with acetylated lysine residues on histone H1.4, H2A, H2B and H3 (in vitro). Ref.11 Ref.17

Subcellular location

Nucleus Ref.11.

Tissue specificity

Highly expressed in estrogen receptor positive breast tumors and in osteosarcoma tumors. Ref.6 Ref.8 Ref.10

Induction

Up-regulated in breast, uterus, colon, ovary, and stomach tumors. Induced in breast cancer cells overexpressing NCOA3 or treated with estrogen. Down-regulated in 5-fluorouracil-resistant derivatives of the colon cancer cell line HCT 116. Ref.1 Ref.9 Ref.11

Sequence similarities

Belongs to the AAA ATPase family.

Contains 1 bromo domain.

Sequence caution

The sequence AAF22032.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH10686.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part (676-679).

The sequence AAH19909.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PL18-1)

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: Q6PL18-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-170: Missing.
     551-582: IVSTLLALMDGLDSRGEIVVIGATNRLDSIDP → YGWIGQQRGNCGHWCYEQARFYRSCFTKAWSL
     583-1390: Missing.
Note: No experimental confirmation available. Dubious isoform. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13901390ATPase family AAA domain-containing protein 2
PRO_0000084796

Regions

Domain1001 – 107171Bromo
Nucleotide binding467 – 4748ATP Potential
Coiled coil970 – 99425 Potential
Coiled coil1086 – 111227 Potential
Compositional bias250 – 28536Asp-rich
Compositional bias357 – 36610Poly-Ser

Amino acid modifications

Modified residue1701Phosphoserine Ref.14
Modified residue3271Phosphoserine Ref.15 Ref.16
Modified residue3371Phosphoserine Ref.15
Modified residue7461Phosphoserine Ref.12
Modified residue7511Phosphoserine Ref.12
Modified residue11491Phosphothreonine Ref.12
Modified residue11521Phosphothreonine Ref.12
Modified residue12331Phosphoserine Ref.15
Modified residue13021Phosphoserine Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 170170Missing in isoform 2.
VSP_015633
Alternative sequence551 – 58232IVSTL…DSIDP → YGWIGQQRGNCGHWCYEQAR FYRSCFTKAWSL in isoform 2.
VSP_015634
Alternative sequence583 – 1390808Missing in isoform 2.
VSP_015635
Natural variant12801I → T.
Corresponds to variant rs3758122 [ dbSNP | Ensembl ].
VAR_047625

Experimental info

Mutagenesis4731K → T: Reduces the ability to mediate estradiol-dependent induction of CCND1 and E2F1; when associated with Q-532. Ref.11
Mutagenesis5321E → Q: Reduces the ability to mediate estradiol-dependent induction of CCND1 and E2F1; when associated with T-473. Ref.11

Secondary structure

.................. 1390
Helix Strand Turn

Details...

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: F43B30C77BB0F4BA

FASTA1,390158,554
        10         20         30         40         50         60 
MVVLRSSLEL HNHSAASATG SLDLSSDFLS LEHIGRRRLR SAGAAQKKPA ATTAKAGDGS 

        70         80         90        100        110        120 
SVKEVETYHR TRALRSLRKD AQNSSDSSFE KNVEITEQLA NGRHFTRQLA RQQADKKKEE 

       130        140        150        160        170        180 
HREDKVIPVT RSLRARNIVQ STEHLHEDNG DVEVRRSCRI RSRYSGVNQS MLFDKLITNT 

       190        200        210        220        230        240 
AEAVLQKMDD MKKMRRQRMR ELEDLGVFNE TEESNLNMYT RGKQKDIQRT DEETTDNQEG 

       250        260        270        280        290        300 
SVESSEEGED QEHEDDGEDE DDEDDDDDDD DDDDDDDEDD EDEEDGEEEN QKRYYLRQRK 

       310        320        330        340        350        360 
ATVYYQAPLE KPRHQRKPNI FYSGPASPAR PRYRLSSAGP RSPYCKRMNR RRHAIHSSDS 

       370        380        390        400        410        420 
TSSSSSEDEQ HFERRRKRSR NRAINRCLPL NFRKDELKGI YKDRMKIGAS LADVDPMQLD 

       430        440        450        460        470        480 
SSVRFDSVGG LSNHIAALKE MVVFPLLYPE VFEKFKIQPP RGCLFYGPPG TGKTLVARAL 

       490        500        510        520        530        540 
ANECSQGDKR VAFFMRKGAD CLSKWVGESE RQLRLLFDQA YQMRPSIIFF DEIDGLAPVR 

       550        560        570        580        590        600 
SSRQDQIHSS IVSTLLALMD GLDSRGEIVV IGATNRLDSI DPALRRPGRF DREFLFSLPD 

       610        620        630        640        650        660 
KEARKEILKI HTRDWNPKPL DTFLEELAEN CVGYCGADIK SICAEAALCA LRRRYPQIYT 

       670        680        690        700        710        720 
TSEKLQLDLS SINISAKDFE VAMQKMIPAS QRAVTSPGQA LSTVVKPLLQ NTVDKILEAL 

       730        740        750        760        770        780 
QRVFPHAEFR TNKTLDSDIS CPLLESDLAY SDDDVPSVYE NGLSQKSSHK AKDNFNFLHL 

       790        800        810        820        830        840 
NRNACYQPMS FRPRILIVGE PGFGQGSHLA PAVIHALEKF TVYTLDIPVL FGVSTTSPEE 

       850        860        870        880        890        900 
TCAQVIREAK RTAPSIVYVP HIHVWWEIVG PTLKATFTTL LQNIPSFAPV LLLATSDKPH 

       910        920        930        940        950        960 
SALPEEVQEL FIRDYGEIFN VQLPDKEERT KFFEDLILKQ AAKPPISKKK AVLQALEVLP 

       970        980        990       1000       1010       1020 
VAPPPEPRSL TAEEVKRLEE QEEDTFRELR IFLRNVTHRL AIDKRFRVFT KPVDPDEVPD 

      1030       1040       1050       1060       1070       1080 
YVTVIKQPMD LSSVISKIDL HKYLTVKDYL RDIDLICSNA LEYNPDRDPG DRLIRHRACA 

      1090       1100       1110       1120       1130       1140 
LRDTAYAIIK EELDEDFEQL CEEIQESRKK RGCSSSKYAP SYYHVMPKQN STLVGDKRSD 

      1150       1160       1170       1180       1190       1200 
PEQNEKLKTP STPVACSTPA QLKRKIRKKS NWYLGTIKKR RKISQAKDDS QNAIDHKIES 

      1210       1220       1230       1240       1250       1260 
DTEETQDTSV DHNETGNTGE SSVEENEKQQ NASESKLELR NNSNTCNIEN ELEDSRKTTA 

      1270       1280       1290       1300       1310       1320 
CTELRDKIAC NGDASSSQII HISDENEGKE MCVLRMTRAR RSQVEQQQLI TVEKALAILS 

      1330       1340       1350       1360       1370       1380 
QPTPSLVVDH ERLKNLLKTV VKKSQNYNIF QLENLYAVIS QCIYRHRKDH DKTSLIQKME 

      1390 
QEVENFSCSR 

« Hide

Isoform 2 [UniParc].

Checksum: 24E5F0638207B64A
Show »

FASTA41247,986

References

« Hide 'large scale' references
[1]"Suppression subtractive hybridization and expression profiling identifies a unique set of genes overexpressed in non-small-cell lung cancer."
Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., Cerveny C., Law C.-L., Wahl A., Carter P.
Oncogene 23:7734-7745(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-1390 (ISOFORM 1).
Tissue: Lymph node and Testis.
[3]"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: Cerebellum, Cervix and Eye.
[4]"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] OF 1-978 (ISOFORM 1).
Tissue: Spleen.
[5]"Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 813-1390.
Tissue: Fetal liver.
[6]"Gene-expression profiles to predict distant metastasis of lymph-node-negative primary breast cancer."
Wang Y., Klijn J.G., Zhang Y., Sieuwerts A.M., Look M.P., Yang F., Talantov D., Timmermans M., Meijer-van Gelder M.E., Yu J., Jatkoe T., Berns E.M.J.J., Atkins D., Foekens J.A.
Lancet 365:671-679(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A consensus prognostic gene expression classifier for ER positive breast cancer."
Teschendorff A.E., Naderi A., Barbosa-Morais N.L., Pinder S.E., Ellis I.O., Aparicio S., Brenton J.D., Caldas C.
Genome Biol. 7:R101.1-R101.13(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Cellular response to 5-fluorouracil (5-FU) in 5-FU-resistant colon cancer cell lines during treatment and recovery."
De Angelis P.M., Svendsrud D.H., Kravik K.L., Stokke T.
Mol. Cancer 5:20-20(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Prognostic significance of drug-regulated genes in high-grade osteosarcoma."
Fellenberg J., Bernd L., Delling G., Witte D., Zahlten-Hinguranage A.
Mod. Pathol. 20:1085-1094(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification."
Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.
Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1 AND NCOA3, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF LYS-473 AND GLU-532.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746; SER-751; THR-1149; THR-1152 AND SER-1302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-1302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-337; SER-1233 AND SER-1302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 981-1108, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY598335 mRNA. Translation: AAT06746.1.
CR749832 mRNA. Translation: CAH18688.1.
AL833653 mRNA. Translation: CAH56229.1.
BC010686 mRNA. Translation: AAH10686.1. Sequence problems.
BC019909 mRNA. Translation: AAH19909.1. Different initiation.
BC113656 mRNA. Translation: AAI13657.1.
AK097133 mRNA. Translation: BAC04959.1.
AF118088 mRNA. Translation: AAF22032.1. Different initiation.
RefSeqNP_054828.2. NM_014109.3.
UniGeneHs.370834.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DAIX-ray1.95A981-1108[»]
ProteinModelPortalQ6PL18.
SMRQ6PL18. Positions 981-1108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118827. 13 interactions.
DIPDIP-46197N.
IntActQ6PL18. 1 interaction.
STRING9606.ENSP00000287394.

Chemistry

ChEMBLCHEMBL2150837.

PTM databases

PhosphoSiteQ6PL18.

Polymorphism databases

DMDM74762365.

Proteomic databases

PaxDbQ6PL18.
PRIDEQ6PL18.

Protocols and materials databases

DNASU29028.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287394; ENSP00000287394; ENSG00000156802. [Q6PL18-1]
GeneID29028.
KEGGhsa:29028.
UCSCuc003yqh.4. human. [Q6PL18-1]

Organism-specific databases

CTD29028.
GeneCardsGC08M124332.
H-InvDBHIX0007764.
HGNCHGNC:30123. ATAD2.
HPACAB056158.
HPA019860.
HPA029424.
MIM611941. gene.
neXtProtNX_Q6PL18.
PharmGKBPA134895566.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOVERGENHBG080873.
InParanoidQ6PL18.
OMAPYCKRMN.
OrthoDBEOG76X5ZF.
PhylomeDBQ6PL18.
TreeFamTF314783.

Gene expression databases

ArrayExpressQ6PL18.
BgeeQ6PL18.
CleanExHS_ATAD2.
GenevestigatorQ6PL18.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
1.25.10.10. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011989. ARM-like.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR001487. Bromodomain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00382. AAA. 1 hit.
SM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEPS00674. AAA. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATAD2. human.
EvolutionaryTraceQ6PL18.
GenomeRNAi29028.
NextBio51959.
PROQ6PL18.
SOURCESearch...

Entry information

Entry nameATAD2_HUMAN
AccessionPrimary (citable) accession number: Q6PL18
Secondary accession number(s): Q14CR1 expand/collapse secondary AC list , Q658P2, Q68CQ0, Q6PJV6, Q8N890, Q9UHS5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 5, 2004
Last modified: March 19, 2014
This is version 98 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 8

Human chromosome 8: entries, gene names and cross-references to MIM