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Protein

ATPase family AAA domain-containing protein 2B

Gene

ATAD2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi441 – 4488ATPSequence analysis

GO - Molecular functioni

  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: GO_Central
  • lysine-acetylated histone binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase family AAA domain-containing protein 2B
Gene namesi
Name:ATAD2B
Synonyms:KIAA1240
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:29230. ATAD2B.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162377039.

Chemistry

ChEMBLiCHEMBL2176775.

Polymorphism and mutation databases

BioMutaiATAD2B.
DMDMi296439432.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14581458ATPase family AAA domain-containing protein 2BPRO_0000050789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei939 – 9391PhosphoserineCombined sources
Modified residuei1338 – 13381PhosphoserineCombined sources
Modified residuei1347 – 13471PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ULI0.
MaxQBiQ9ULI0.
PaxDbiQ9ULI0.
PRIDEiQ9ULI0.

PTM databases

iPTMnetiQ9ULI0.
PhosphoSiteiQ9ULI0.

Expressioni

Gene expression databases

BgeeiQ9ULI0.
CleanExiHS_ATAD2B.
ExpressionAtlasiQ9ULI0. baseline and differential.
GenevisibleiQ9ULI0. HS.

Organism-specific databases

HPAiHPA034555.

Interactioni

Subunit structurei

Binds acetylated lysine residues in histone H1.4, H2A, H2B, H3 and H4 (in vitro).1 Publication

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119961. 1 interaction.
STRINGi9606.ENSP00000238789.

Structurei

Secondary structure

1
1458
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi952 – 97524Combined sources
Helixi978 – 9803Combined sources
Turni989 – 9913Combined sources
Helixi995 – 9984Combined sources
Helixi1005 – 10139Combined sources
Helixi1020 – 103718Combined sources
Beta strandi1040 – 10423Combined sources
Helixi1043 – 106624Combined sources
Helixi1069 – 108315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKWNMR-A958-1080[»]
3LXJX-ray2.33A/B/C/D952-1086[»]
ProteinModelPortaliQ9ULI0.
SMRiQ9ULI0. Positions 952-1085.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ULI0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini975 – 104571BromoPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili943 – 97432Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi257 – 2626Poly-Glu
Compositional biasi1247 – 12504Poly-Ser

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain, Coiled coil

Phylogenomic databases

eggNOGiKOG0730. Eukaryota.
KOG0732. Eukaryota.
COG0464. LUCA.
HOGENOMiHOG000034119.
HOVERGENiHBG080873.
InParanoidiQ9ULI0.
PhylomeDBiQ9ULI0.
TreeFamiTF314783.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00382. AAA. 1 hit.
SM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEiPS00674. AAA. 1 hit.
PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULI0-1) [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

        10         20         30         40         50
MVNTRKSSLR LLGSKSPGPG PGPGAGAEPG ATGGSSHFIS SRTRSSKTRA
60 70 80 90 100
ASCPAAKAGG SGGAGVTLDE ARKVEVDGSL SDSHVSPPAK RTLKQPDSVC
110 120 130 140 150
KDKSKSRSTG QREEWNLSTG QARLTSQPGA TLPNGHSGLS LRSHPLRGEK
160 170 180 190 200
KGDGDLSCIN GDMEVRKSCR SRKNRFESVN QSLLFDQLVN STAEAVLQEM
210 220 230 240 250
DNINIRQNRR SGEVERLRMW TDTEFENMDM YSRVKRRRKS LRRNSYGIQN
260 270 280 290 300
HHEVSTEGEE EESQEEDGDI EVEEAEGEEN DRPYNLRQRK TVDRYQAPPI
310 320 330 340 350
VPAHQKKREN TLFDIHRSPA RRSHIRRKKH AIHSSDTTSS DEERFERRKS
360 370 380 390 400
KSMARARNRC LPMNFRAEDL ASGILRERVK VGASLADVDP MNIDKSVRFD
410 420 430 440 450
SIGGLSHHIH ALKEMVVFPL LYPEIFEKFK IQPPRGCLFY GPPGTGKTLV
460 470 480 490 500
ARALANECSQ GDKKVAFFMR KGADCLSKWV GESERQLRLL FDQAYLMRPS
510 520 530 540 550
IIFFDEIDGL APVRSSRQDQ IHSSIVSTLL ALMDGLDNRG EIVVIGATNR
560 570 580 590 600
LDSIDPALRR PGRFDREFLF NLPDQKARKH ILQIHTRDWN PKLSDAFLGE
610 620 630 640 650
LAEKCVGYCG ADIKALCTEA ALIALRRRYP QIYASSHKLQ LDVSSIVLSA
660 670 680 690 700
QDFYHAMQNI VPASQRAVMS SGHALSPIIR PLLERSFNNI LAVLQKVFPH
710 720 730 740 750
AEISQSDKKE DIETLILEDS EDENALSIFE TNCHSGSPKK QSSSAAIHKP
760 770 780 790 800
YLHFTMSPYH QPTSYRPRLL LSGERGSGQT SHLAPALLHT LERFSVHRLD
810 820 830 840 850
LPALYSVSAK TPEESCAQIF REARRTVPSI VYMPHIGDWW EAVSETVRAT
860 870 880 890 900
FLTLLQDIPS FSPIFLLSTS ETMYSELPEE VKCIFRIQYE EVLYIQRPIE
910 920 930 940 950
EDRRKFFQEL ILNQASMAPP RRKHAALCAM EVLPLALPSP PRQLSESEKS
960 970 980 990 1000
RMEDQEENTL RELRLFLRDV TKRLATDKRF NIFSKPVDIE EVSDYLEVIK
1010 1020 1030 1040 1050
EPMDLSTVIT KIDKHNYLTA KDFLKDIDLI CSNALEYNPD KDPGDKIIRH
1060 1070 1080 1090 1100
RACTLKDTAH AIIAAELDPE FNKLCEEIKE ARIKRGLSVT SEQINPHSTG
1110 1120 1130 1140 1150
ARKTETRVEE AFRHKQRNPM DVWHNSANKC AFRVRRKSRR RSQWGKGIIK
1160 1170 1180 1190 1200
KRKVNNLKKD EEDTKFADYE NHTEDRKLLE NGEFEVSTDC HEENGEETGD
1210 1220 1230 1240 1250
LSMTNDESSC DIMDLDQGQR LNNGAGTKEN FASTEEESSN ESLLVNSSSS
1260 1270 1280 1290 1300
LNPEQTSRKE TFLKGNCLNG EASTDSFEGI PVLECQNGKL EVVSFCDSGD
1310 1320 1330 1340 1350
KCSSEQKILL EDQSKEKPET STENHGDDLE KLEALECSNN EKLEPGSDVE
1360 1370 1380 1390 1400
VKDAELDKEG ASKVKKYRKL ILEQAKTTSL ELVPEEPSEP VPPLIVDRER
1410 1420 1430 1440 1450
LKKLLDLLVD KSNNLAVDQL ERLYSLLSQC IYRHRKDYDK SQLVEEMERT

VHMFETFL
Length:1,458
Mass (Da):164,914
Last modified:May 18, 2010 - v3
Checksum:iCE7480D7EEBE6F9C
GO
Isoform 2 (identifier: Q9ULI0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     988-992: Missing.

Show »
Length:1,453
Mass (Da):164,328
Checksum:i826AB705C4CB3A49
GO

Sequence cautioni

The sequence BAD18469.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071Q → R in BAC04429 (PubMed:14702039).Curated
Sequence conflicti291 – 2911T → A in BAC04429 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181S → P.
Corresponds to variant rs10210982 [ dbSNP | Ensembl ].
VAR_055467

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei988 – 9925Missing in isoform 2. 1 PublicationVSP_023276

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009242 Genomic DNA. No translation available.
AC066692 Genomic DNA. No translation available.
AC079924 Genomic DNA. No translation available.
AK094821 mRNA. Translation: BAC04429.1.
AK131301 mRNA. Translation: BAD18469.1. Different initiation.
AB033066 mRNA. Translation: BAA86554.1.
CCDSiCCDS46227.1. [Q9ULI0-1]
RefSeqiNP_001229267.2. NM_001242338.2.
NP_060022.2. NM_017552.3.
UniGeneiHs.467862.

Genome annotation databases

EnsembliENST00000238789; ENSP00000238789; ENSG00000119778.
GeneIDi54454.
KEGGihsa:54454.
UCSCiuc002rek.5. human. [Q9ULI0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009242 Genomic DNA. No translation available.
AC066692 Genomic DNA. No translation available.
AC079924 Genomic DNA. No translation available.
AK094821 mRNA. Translation: BAC04429.1.
AK131301 mRNA. Translation: BAD18469.1. Different initiation.
AB033066 mRNA. Translation: BAA86554.1.
CCDSiCCDS46227.1. [Q9ULI0-1]
RefSeqiNP_001229267.2. NM_001242338.2.
NP_060022.2. NM_017552.3.
UniGeneiHs.467862.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKWNMR-A958-1080[»]
3LXJX-ray2.33A/B/C/D952-1086[»]
ProteinModelPortaliQ9ULI0.
SMRiQ9ULI0. Positions 952-1085.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119961. 1 interaction.
STRINGi9606.ENSP00000238789.

Chemistry

ChEMBLiCHEMBL2176775.

PTM databases

iPTMnetiQ9ULI0.
PhosphoSiteiQ9ULI0.

Polymorphism and mutation databases

BioMutaiATAD2B.
DMDMi296439432.

Proteomic databases

EPDiQ9ULI0.
MaxQBiQ9ULI0.
PaxDbiQ9ULI0.
PRIDEiQ9ULI0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238789; ENSP00000238789; ENSG00000119778.
GeneIDi54454.
KEGGihsa:54454.
UCSCiuc002rek.5. human. [Q9ULI0-1]

Organism-specific databases

CTDi54454.
GeneCardsiATAD2B.
HGNCiHGNC:29230. ATAD2B.
HPAiHPA034555.
MIMi615347. gene.
neXtProtiNX_Q9ULI0.
PharmGKBiPA162377039.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0730. Eukaryota.
KOG0732. Eukaryota.
COG0464. LUCA.
HOGENOMiHOG000034119.
HOVERGENiHBG080873.
InParanoidiQ9ULI0.
PhylomeDBiQ9ULI0.
TreeFamiTF314783.

Miscellaneous databases

ChiTaRSiATAD2B. human.
EvolutionaryTraceiQ9ULI0.
GenomeRNAii54454.
NextBioi56685.
PROiQ9ULI0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULI0.
CleanExiHS_ATAD2B.
ExpressionAtlasiQ9ULI0. baseline and differential.
GenevisibleiQ9ULI0. HS.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00382. AAA. 1 hit.
SM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 3 hits.
PROSITEiPS00674. AAA. 1 hit.
PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 1-1076 (ISOFORM 1).
    Tissue: Brain.
  3. "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] OF 721-1458 (ISOFORM 2).
    Tissue: Brain.
  4. "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].
  5. "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-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-16; SER-79; SER-86; SER-1338 AND SER-1347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Nascent chromatin capture proteomics determines chromatin dynamics during DNA replication and identifies unknown fork components."
    Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K., de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.
    Nat. Cell Biol. 16:281-293(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Solution structure of the bromodomain of human protein KIAA1240."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 958-1080.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 952-1086, SUBUNIT.

Entry informationi

Entry nameiATD2B_HUMAN
AccessioniPrimary (citable) accession number: Q9ULI0
Secondary accession number(s): B9ZVQ5, Q6ZNA6, Q8N9E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 18, 2010
Last modified: March 16, 2016
This is version 117 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.