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Protein

AT-rich interactive domain-containing protein 5B

Gene

ARID5B

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

Functioni

Transcription coactivator that binds to the 5'-AATA[CT]-3' core sequence and plays a key role in adipogenesis and liver development. Acts by forming a complex with phosphorylated PHF2, which mediates demethylation at Lys-336, leading to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. Required for adipogenesis: regulates triglyceride metabolism in adipocytes by regulating expression of adipogenic genes. Overexpression leads to induction of smooth muscle marker genes, suggesting that it may also act as a regulator of smooth muscle cell differentiation and proliferation. Represses the cytomegalovirus enhancer.1 Publication

GO - Molecular functioni

  • DNA binding Source: GDB
  • histone demethylase activity Source: Reactome
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: NTNU_SB
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-3214842. HDMs demethylate histones.
SignaLinkiQ14865.

Names & Taxonomyi

Protein namesi
Recommended name:
AT-rich interactive domain-containing protein 5B
Short name:
ARID domain-containing protein 5B
Alternative name(s):
MRF1-like protein
Modulator recognition factor 2
Short name:
MRF-2
Gene namesi
Name:ARID5B
Synonyms:DESRT, MRF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:17362. ARID5B.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in ARID5B may be a cause of susceptibility to coronary atherosclerosis in the Japanese population.

Leukemia, acute lymphoblastic (ALL)7 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. ALL is a malignant disease of bone marrow and the most common malignancy diagnosed in children. The malignant cells are lymphoid precursor cells (lymphoblasts) that are arrested in an early stage of development. The lymphoblasts replace the normal marrow elements, resulting in a marked decrease in the production of normal blood cells. Consequently, anemia, thrombocytopenia, and neutropenia occur to varying degrees. The lymphoblasts also proliferate in organs other than the marrow, particularly the liver, spleen, and lymphonodes.
See also OMIM:613065

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi336 – 3361K → A or R: Abolishes methylation and FSK-dependent DNA-binding of the PHF2-ARID5B complex to promoters. 1 Publication

Organism-specific databases

MIMi613065. phenotype.
PharmGKBiPA134943193.

Polymorphism and mutation databases

BioMutaiARID5B.
DMDMi209572763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11881188AT-rich interactive domain-containing protein 5BPRO_0000200581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei336 – 3361N6,N6-dimethyllysine1 Publication
Cross-linki774 – 774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki803 – 803Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1032 – 10321PhosphoserineCombined sources

Post-translational modificationi

Methylation at Lys-336 prevents DNA-binding. Demethylation by PHF2 promotes recruitment of the PHF2-ARID5B complex to promoters.1 Publication

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14865.
MaxQBiQ14865.
PaxDbiQ14865.
PRIDEiQ14865.

PTM databases

iPTMnetiQ14865.
PhosphoSiteiQ14865.

Expressioni

Tissue specificityi

Widely expressed, including in liver (at protein level).1 Publication

Gene expression databases

BgeeiQ14865.
CleanExiHS_ARID5B.
GenevisibleiQ14865. HS.

Organism-specific databases

HPAiHPA015037.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC1Q135475EBI-1210388,EBI-301834

Protein-protein interaction databases

BioGridi123918. 18 interactions.
IntActiQ14865. 14 interactions.
STRINGi9606.ENSP00000279873.

Structurei

Secondary structure

1
1188
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi319 – 33315Combined sources
Turni334 – 3363Combined sources
Helixi339 – 3413Combined sources
Beta strandi345 – 3495Combined sources
Helixi352 – 36110Combined sources
Helixi364 – 3718Combined sources
Helixi374 – 3818Combined sources
Turni388 – 3936Combined sources
Helixi394 – 4018Combined sources
Turni402 – 4054Combined sources
Helixi406 – 4127Combined sources
Beta strandi414 – 4174Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG6NMR-A318-424[»]
2OEHNMR-A318-424[»]
ProteinModelPortaliQ14865.
SMRiQ14865. Positions 318-424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14865.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini318 – 41093ARIDPROSITE-ProRule annotationAdd
BLAST

Domaini

The ARID domain mediates the interaction with DNA.

Sequence similaritiesi

Belongs to the ARID5B family.Curated
Contains 1 ARID domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IQ7B. Eukaryota.
ENOG4110NWK. LUCA.
GeneTreeiENSGT00840000129864.
HOVERGENiHBG102783.
InParanoidiQ14865.
OMAiPVGSSYG.
OrthoDBiEOG7992PR.
PhylomeDBiQ14865.
TreeFamiTF324725.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR030408. ARID5B.
IPR001606. ARID_dom.
[Graphical view]
PANTHERiPTHR13964:SF29. PTHR13964:SF29. 1 hit.
PfamiPF01388. ARID. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14865-1) [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
MEPNSLQWVG SPCGLHGPYI FYKAFQFHLE GKPRILSLGD FFFVRCTPKD
60 70 80 90 100
PICIAELQLL WEERTSRQLL SSSKLYFLPE DTPQGRNSDH GEDEVIAVSE
110 120 130 140 150
KVIVKLEDLV KWVHSDFSKW RCGFHAGPVK TEALGRNGQK EALLKYRQST
160 170 180 190 200
LNSGLNFKDV LKEKADLGED EEETNVIVLS YPQYCRYRSM LKRIQDKPSS
210 220 230 240 250
ILTDQFALAL GGIAVVSRNP QILYCRDTFD HPTLIENESI CDEFAPNLKG
260 270 280 290 300
RPRKKKPCPQ RRDSFSGVKD SNNNSDGKAV AKVKCEARSA LTKPKNNHNC
310 320 330 340 350
KKVSNEEKPK VAIGEECRAD EQAFLVALYK YMKERKTPIE RIPYLGFKQI
360 370 380 390 400
NLWTMFQAAQ KLGGYETITA RRQWKHIYDE LGGNPGSTSA ATCTRRHYER
410 420 430 440 450
LILPYERFIK GEEDKPLPPI KPRKQENSSQ ENENKTKVSG TKRIKHEIPK
460 470 480 490 500
SKKEKENAPK PQDAAEVSSE QEKEQETLIS QKSIPEPLPA ADMKKKIEGY
510 520 530 540 550
QEFSAKPLAS RVDPEKDNET DQGSNSEKVA EEAGEKGPTP PLPSAPLAPE
560 570 580 590 600
KDSALVPGAS KQPLTSPSAL VDSKQESKLC CFTESPESEP QEASFPSFPT
610 620 630 640 650
TQPPLANQNE TEDDKLPAMA DYIANCTVKV DQLGSDDIHN ALKQTPKVLV
660 670 680 690 700
VQSFDMFKDK DLTGPMNENH GLNYTPLLYS RGNPGIMSPL AKKKLLSQVS
710 720 730 740 750
GASLSSSYPY GSPPPLISKK KLIARDDLCS SLSQTHHGQS TDHMAVSRPS
760 770 780 790 800
VIQHVQSFRS KPSEERKTIN DIFKHEKLSR SDPHRCSFSK HHLNPLADSY
810 820 830 840 850
VLKQEIQEGK DKLLEKRALP HSHMPSFLAD FYSSPHLHSL YRHTEHHLHN
860 870 880 890 900
EQTSKYPSRD MYRESENSSF PSHRHQEKLH VNYLTSLHLQ DKKSAAAEAP
910 920 930 940 950
TDDQPTDLSL PKNPHKPTGK VLGLAHSTTG PQESKGISQF QVLGSQSRDC
960 970 980 990 1000
HPKACRVSPM TMSGPKKYPE SLSRSGKPHH VRLENFRKME GMVHPILHRK
1010 1020 1030 1040 1050
MSPQNIGAAR PIKRSLEDLD LVIAGKKARA VSPLDPSKEV SGKEKASEQE
1060 1070 1080 1090 1100
SEGSKAAHGG HSGGGSEGHK LPLSSPIFPG LYSGSLCNSG LNSRLPAGYS
1110 1120 1130 1140 1150
HSLQYLKNQT VLSPLMQPLA FHSLVMQRGI FTSPTNSQQL YRHLAAATPV
1160 1170 1180
GSSYGDLLHN SIYPLAAINP QAAFPSSQLS SVHPSTKL
Length:1,188
Mass (Da):132,375
Last modified:October 14, 2008 - v3
Checksum:i23B7C525B0055330
GO
Isoform 2 (identifier: Q14865-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: Missing.
     244-244: F → M

Show »
Length:945
Mass (Da):104,602
Checksum:iEAD2A25EDB4EF57D
GO
Isoform 3 (identifier: Q14865-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     284-318: KCEARSALTKPKNNHNCKKVSNEEKPKVAIGEECR → RSFTPRYSFRCIFLFLLFLFISLCLCLGGSFQFSI
     319-1188: Missing.

Note: No experimental confirmation available.
Show »
Length:318
Mass (Da):36,282
Checksum:iAFE2D2C2665FE375
GO

Sequence cautioni

The sequence AAH15120.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH36831.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH66345.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI07801.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB15012.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti401 – 4011L → S in AAH15120 (PubMed:15489334).Curated
Sequence conflicti451 – 4511S → N in AAH15120 (PubMed:15489334).Curated
Sequence conflicti827 – 8271F → L in CAE46013 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 243243Missing in isoform 2. 2 PublicationsVSP_009355Add
BLAST
Alternative sequencei244 – 2441F → M in isoform 2. 2 PublicationsVSP_009356
Alternative sequencei284 – 31835KCEAR…GEECR → RSFTPRYSFRCIFLFLLFLF ISLCLCLGGSFQFSI in isoform 3. CuratedVSP_041560Add
BLAST
Alternative sequencei319 – 1188870Missing in isoform 3. CuratedVSP_041561Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL671972 Genomic DNA. Translation: CAH72685.1.
AL671972, AC067742 Genomic DNA. Translation: CAH72686.1.
AK024803 mRNA. Translation: BAB15012.1. Sequence problems.
AK296921 mRNA. Translation: BAG59475.1.
BC015120 mRNA. Translation: AAH15120.1. Sequence problems.
BC036831 mRNA. Translation: AAH36831.1. Different initiation.
BC066345 mRNA. Translation: AAH66345.1. Sequence problems.
BC107800 mRNA. Translation: AAI07801.1. Sequence problems.
M73837 mRNA. Translation: AAA59870.1.
BX537690 mRNA. Translation: CAD97814.1.
BX641020 mRNA. Translation: CAE46013.1.
CCDSiCCDS31208.1. [Q14865-1]
CCDS58082.1. [Q14865-2]
PIRiS27963.
RefSeqiNP_001231567.1. NM_001244638.1. [Q14865-2]
NP_115575.1. NM_032199.2. [Q14865-1]
UniGeneiHs.535297.

Genome annotation databases

EnsembliENST00000279873; ENSP00000279873; ENSG00000150347. [Q14865-1]
ENST00000309334; ENSP00000308862; ENSG00000150347. [Q14865-2]
GeneIDi84159.
KEGGihsa:84159.
UCSCiuc001jlt.3. human. [Q14865-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL671972 Genomic DNA. Translation: CAH72685.1.
AL671972, AC067742 Genomic DNA. Translation: CAH72686.1.
AK024803 mRNA. Translation: BAB15012.1. Sequence problems.
AK296921 mRNA. Translation: BAG59475.1.
BC015120 mRNA. Translation: AAH15120.1. Sequence problems.
BC036831 mRNA. Translation: AAH36831.1. Different initiation.
BC066345 mRNA. Translation: AAH66345.1. Sequence problems.
BC107800 mRNA. Translation: AAI07801.1. Sequence problems.
M73837 mRNA. Translation: AAA59870.1.
BX537690 mRNA. Translation: CAD97814.1.
BX641020 mRNA. Translation: CAE46013.1.
CCDSiCCDS31208.1. [Q14865-1]
CCDS58082.1. [Q14865-2]
PIRiS27963.
RefSeqiNP_001231567.1. NM_001244638.1. [Q14865-2]
NP_115575.1. NM_032199.2. [Q14865-1]
UniGeneiHs.535297.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG6NMR-A318-424[»]
2OEHNMR-A318-424[»]
ProteinModelPortaliQ14865.
SMRiQ14865. Positions 318-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123918. 18 interactions.
IntActiQ14865. 14 interactions.
STRINGi9606.ENSP00000279873.

PTM databases

iPTMnetiQ14865.
PhosphoSiteiQ14865.

Polymorphism and mutation databases

BioMutaiARID5B.
DMDMi209572763.

Proteomic databases

EPDiQ14865.
MaxQBiQ14865.
PaxDbiQ14865.
PRIDEiQ14865.

Protocols and materials databases

DNASUi84159.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279873; ENSP00000279873; ENSG00000150347. [Q14865-1]
ENST00000309334; ENSP00000308862; ENSG00000150347. [Q14865-2]
GeneIDi84159.
KEGGihsa:84159.
UCSCiuc001jlt.3. human. [Q14865-1]

Organism-specific databases

CTDi84159.
GeneCardsiARID5B.
H-InvDBHIX0008854.
HGNCiHGNC:17362. ARID5B.
HPAiHPA015037.
MIMi608538. gene.
613065. phenotype.
neXtProtiNX_Q14865.
PharmGKBiPA134943193.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQ7B. Eukaryota.
ENOG4110NWK. LUCA.
GeneTreeiENSGT00840000129864.
HOVERGENiHBG102783.
InParanoidiQ14865.
OMAiPVGSSYG.
OrthoDBiEOG7992PR.
PhylomeDBiQ14865.
TreeFamiTF324725.

Enzyme and pathway databases

ReactomeiR-HSA-3214842. HDMs demethylate histones.
SignaLinkiQ14865.

Miscellaneous databases

ChiTaRSiARID5B. human.
EvolutionaryTraceiQ14865.
GeneWikiiARID5B.
GenomeRNAii84159.
PROiQ14865.
SOURCEiSearch...

Gene expression databases

BgeeiQ14865.
CleanExiHS_ARID5B.
GenevisibleiQ14865. HS.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR030408. ARID5B.
IPR001606. ARID_dom.
[Graphical view]
PANTHERiPTHR13964:SF29. PTHR13964:SF29. 1 hit.
PfamiPF01388. ARID. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
  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 1-453 (ISOFORM 2).
    Tissue: Smooth muscle and Tongue.
  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] OF 1-450 AND 477-1188 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-453 (ISOFORM 2).
    Tissue: Placenta and Uterus.
  4. "A new family of DNA binding factors contain a member responsive to retinoic acid."
    Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N., Itakura K.
    Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-547.
    Tissue: Foreskin.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-1188.
    Tissue: Colon endothelium and Fetal kidney.
  6. "The novel Mrf-2 DNA-binding domain recognizes a five-base core sequence through major and minor-groove contacts."
    Whitson R.H., Huang T., Itakura K.
    Biochem. Biophys. Res. Commun. 258:326-331(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  7. "DNA-binding properties of ARID family proteins."
    Patsialou A., Wilsker D., Moran E.
    Nucleic Acids Res. 33:66-80(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  8. "Genetic variations of Mrf-2/ARID5B confer risk of coronary atherosclerosis in the Japanese population."
    Wang G., Watanabe M., Imai Y., Hara K., Manabe I., Maemura K., Horikoshi M., Kohro T., Amiya E., Sugiyama T., Fujita T., Kadowaki T., Yamazaki T., Nagai R.
    Int. Heart J. 49:313-327(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN CORONARY ATHEROSCLEROSIS.
  9. Cited for: POSSIBLE INVOLVEMENT IN ALL.
  10. Cited for: POSSIBLE INVOLVEMENT IN ALL.
  11. "Verification of the susceptibility loci on 7p12.2, 10q21.2, and 14q11.2 in precursor B-cell acute lymphoblastic leukemia of childhood."
    Prasad R.B., Hosking F.J., Vijayakrishnan J., Papaemmanuil E., Koehler R., Greaves M., Sheridan E., Gast A., Kinsey S.E., Lightfoot T., Roman E., Taylor M., Pritchard-Jones K., Stanulla M., Schrappe M., Bartram C.R., Houlston R.S., Kumar R., Hemminki K.
    Blood 115:1765-1767(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN ALL.
  12. "Replication analysis confirms the association of ARID5B with childhood B-cell acute lymphoblastic leukemia."
    Healy J., Richer C., Bourgey M., Kritikou E.A., Sinnett D.
    Haematologica 95:1608-1611(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN ALL.
  13. "ARID5B SNP rs10821936 is associated with risk of childhood acute lymphoblastic leukemia in blacks and contributes to racial differences in leukemia incidence."
    Yang W., Trevino L.R., Yang J.J., Scheet P., Pui C.H., Evans W.E., Relling M.V.
    Leukemia 24:894-896(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN ALL.
  14. "Genome-wide association study of childhood acute lymphoblastic leukemia in Korea."
    Han S., Lee K.M., Park S.K., Lee J.E., Ahn H.S., Shin H.Y., Kang H.J., Koo H.H., Seo J.J., Choi J.E., Ahn Y.O., Kang D.
    Leuk. Res. 34:1271-1274(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN ALL.
  15. Cited for: POSSIBLE INVOLVEMENT IN ALL.
  16. "PKA-dependent regulation of the histone lysine demethylase complex PHF2-ARID5B."
    Baba A., Ohtake F., Okuno Y., Yokota K., Okada M., Imai Y., Ni M., Meyer C.A., Igarashi K., Kanno J., Brown M., Kato S.
    Nat. Cell Biol. 13:668-675(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHF2, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, DNA-BINDING, IDENTIFICATION IN THE PHF2-ARID5B COMPLEX, METHYLATION AT LYS-336, MUTAGENESIS OF LYS-336.
  17. "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-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-774 AND LYS-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "A novel DNA-binding motif shares structural homology to DNA replication and repair nucleases and polymerases."
    Yuan Y.-C., Whitson R.H., Liu Q., Itakura K., Chen Y.
    Nat. Struct. Biol. 5:959-964(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 318-417.
  22. "Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA."
    Zhu L., Hu J., Lin D., Whitson R., Itakura K., Chen Y.
    Biochemistry 40:9142-9150(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 318-417 IN COMPLEX WITH DNA.
  23. "Determination of the three-dimensional structure of the Mrf2-DNA complex using paramagnetic spin labeling."
    Cai S., Zhu L., Zhang Z., Chen Y.
    Biochemistry 46:4943-4950(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 318-417 IN COMPLEX WITH DNA.

Entry informationi

Entry nameiARI5B_HUMAN
AccessioniPrimary (citable) accession number: Q14865
Secondary accession number(s): B4DLB3
, Q05DG6, Q32Q59, Q5VST4, Q6NZ42, Q7Z3M4, Q8N421, Q9H786
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: October 14, 2008
Last modified: June 8, 2016
This is version 151 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.