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Q4LE39

- ARI4B_HUMAN

UniProt

Q4LE39 - ARI4B_HUMAN

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Protein

AT-rich interactive domain-containing protein 4B

Gene

ARID4B

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

Functioni

Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes.1 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. histone H3-K9 trimethylation Source: Ensembl
  2. histone H4-K20 trimethylation Source: Ensembl
  3. regulation of gene expression by genetic imprinting Source: Ensembl
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_200856. NoRC negatively regulates rRNA expression.
REACT_228222. HDACs deacetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
AT-rich interactive domain-containing protein 4B
Short name:
ARID domain-containing protein 4B
Alternative name(s):
180 kDa Sin3-associated polypeptide
Short name:
Sin3-associated polypeptide p180
Breast cancer-associated antigen BRCAA1
Histone deacetylase complex subunit SAP180
Retinoblastoma-binding protein 1-like 1
Gene namesi
Name:ARID4B
Synonyms:BRCAA1, RBBP1L1, RBP1L1, SAP180
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:15550. ARID4B.

Subcellular locationi

Nucleus PROSITE-ProRule annotation. Cytoplasm 2 Publications
Note: Cytoplasmic in breast cancer cells.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134940494.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13121312AT-rich interactive domain-containing protein 4BPRO_0000282863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761Phosphoserine1 Publication
Modified residuei666 – 6661Phosphoserine1 Publication
Modified residuei675 – 6751Phosphoserine2 Publications
Modified residuei717 – 7171Phosphoserine1 Publication
Modified residuei778 – 7781Phosphoserine2 Publications
Modified residuei790 – 7901Phosphoserine4 Publications
Modified residuei793 – 7931Phosphothreonine4 Publications
Modified residuei1014 – 10141Phosphoserine1 Publication
Modified residuei1026 – 10261Phosphothreonine1 Publication
Modified residuei1150 – 11501Phosphothreonine1 Publication
Modified residuei1152 – 11521Phosphoserine1 Publication
Modified residuei1153 – 11531Phosphoserine1 Publication
Modified residuei1155 – 11551Phosphoserine1 Publication
Modified residuei1159 – 11591Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ4LE39.
PaxDbiQ4LE39.
PRIDEiQ4LE39.

PTM databases

PhosphoSiteiQ4LE39.

Expressioni

Tissue specificityi

Highly expressed in the testis and in breast, lung, colon, pancreatic and ovarian cancers. Expressed at low levels in the thymus, prostate and ovary.3 Publications

Gene expression databases

BgeeiQ4LE39.
ExpressionAtlasiQ4LE39. baseline and differential.
GenevestigatoriQ4LE39.

Organism-specific databases

HPAiHPA027333.

Interactioni

Subunit structurei

Component of a Sin3A corepressor complex consisting of SIN3A, SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ETS1P149212EBI-2680990,EBI-913209

Protein-protein interaction databases

BioGridi119708. 17 interactions.
IntActiQ4LE39. 11 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ4LE39.
SMRiQ4LE39. Positions 5-121, 170-271, 308-394, 564-632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini306 – 39893ARIDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni465 – 4739Antigenic epitope
Regioni1130 – 11378Antigenic epitope

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili728 – 75427Sequence AnalysisAdd
BLAST
Coiled coili1231 – 127040Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi154 – 1596Poly-Ser
Compositional biasi268 – 567300Glu-richAdd
BLAST
Compositional biasi1095 – 11017Poly-Ser
Compositional biasi1271 – 130333Ser-richAdd
BLAST

Domaini

The C-terminus mediates interaction with mSin3A corepressor complex.1 Publication
The N-terminus is involved in transcriptional repression by HDAC-independent mechanisms.1 Publication
The ARID domain is involved in stabilizing the mSin3A corepressor complex on DNA.1 Publication

Sequence similaritiesi

Contains 1 ARID domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG248805.
GeneTreeiENSGT00510000046413.
HOVERGENiHBG058247.
InParanoidiQ4LE39.
OMAiFRLVHKL.
PhylomeDBiQ4LE39.
TreeFamiTF106427.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID/BRIGHT_DNA-bd.
IPR028853. ARID4B.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view]
PANTHERiPTHR13964:SF21. PTHR13964:SF21. 1 hit.
PfamiPF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q4LE39-1) [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
MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE
60 70 80 90 100
VQDDHIKGPL KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT
110 120 130 140 150
LRRSSLCLKG ERHFAESETL DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP
160 170 180 190 200
EEESSSSSSD EDEDDRKQID ELLGKVVCVD YISLDKKKAL WFPALVVCPD
210 220 230 240 250
CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK PDAVLKQAFE
260 270 280 290 300
QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE
310 320 330 340 350
EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL
360 370 380 390 400
GGFDNIESGA VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA
410 420 430 440 450
NIEFQMALPE KVVNKQCKEC ENVKEIKVKE ENETEIKEIK MEEERNIIPR
460 470 480 490 500
EEKPIEDEIE RKENIKPSLG SKKNLLESIP THSDQEKEVN IKKPEDNENL
510 520 530 540 550
DDKDDDTTRV DESLNIKVEA EEEKAKSGDE TNKEEDEDDE EAEEEEEEEE
560 570 580 590 600
EEEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG
610 620 630 640 650
EVLYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD
660 670 680 690 700
KDEKYSPKNC KLRRLSKPPF QTNPSPEMVS KLDLTDAKNS DTAHIKSIEI
710 720 730 740 750
TSILNGLQAS ESSAEDSEQE DERGAQDMDN NGKEESKIDH LTNNRNDLIS
760 770 780 790 800
KEEQNSSSLL EENKVHADLV ISKPVSKSPE RLRKDIEVLS EDTDYEEDEV
810 820 830 840 850
TKKRKDVKKD TTDKSSKPQI KRGKRRYCNT EECLKTGSPG KKEEKAKNKE
860 870 880 890 900
SLCMENSSNS SSDEDEEETK AKMTPTKKYN GLEEKRKSLR TTGFYSGFSE
910 920 930 940 950
VAEKRIKLLN NSDERLQNSR AKDRKDVWSS IQGQWPKKTL KELFSDSDTE
960 970 980 990 1000
AAASPPHPAP EEGVAEESLQ TVAEEESCSP SVELEKPPPV NVDSKPIEEK
1010 1020 1030 1040 1050
TVEVNDRKAE FPSSGSNSVL NTPPTTPESP SSVTVTEGSR QQSSVTVSEP
1060 1070 1080 1090 1100
LAPNQEEVRS IKSETDSTIE VDSVAGELQD LQSEGNSSPA GFDASVSSSS
1110 1120 1130 1140 1150
SNQPEPEHPE KACTGQKRVK DAQGGGSSSK KQKRSHKATV VNNKKKGKGT
1160 1170 1180 1190 1200
NSSDSEELSA GESITKSQPV KSVSTGMKSH STKSPARTQS PGKCGKNGDK
1210 1220 1230 1240 1250
DPDLKEPSNR LPKVYKWSFQ MSDLENMTSA ERITILQEKL QEIRKHYLSL
1260 1270 1280 1290 1300
KSEVASIDRR RKRLKKKERE SAATSSSSSS PSSSSITAAV MLTLAEPSMS
1310
SASQNGMSVE CR
Length:1,312
Mass (Da):147,809
Last modified:April 3, 2007 - v2
Checksum:iE4175FF80F5217EE
GO
Isoform 2 (identifier: Q4LE39-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     529-614: Missing.

Show »
Length:1,226
Mass (Da):137,607
Checksum:i3ADAB4A897403AD9
GO
Isoform 3 (identifier: Q4LE39-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1150-1153: TNSS → SAPH
     1154-1312: Missing.

Show »
Length:1,153
Mass (Da):130,418
Checksum:i9C540DF507EBC220
GO
Isoform 4 (identifier: Q4LE39-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-319: Missing.
     1112-1122: ACTGQKRVKDA → GEKENVYVDLF
     1123-1312: Missing.

Show »
Length:803
Mass (Da):91,140
Checksum:iAC58481D8DE15417
GO

Sequence cautioni

The sequence AAD41239.1 differs from that shown. Reason: Frameshift at positions 859, 869, 1287 and 1311. Curated
The sequence AAF23433.3 differs from that shown. Reason: Frameshift at positions 1287 and 1311. Curated
The sequence BAB14428.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE06114.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI13751.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151D → G in AAO63590. (PubMed:12724404)Curated
Sequence conflicti79 – 791V → A in AAO63590. (PubMed:12724404)Curated
Sequence conflicti330 – 3301R → Q in AAF28341. (PubMed:11481388)Curated
Sequence conflicti330 – 3301R → Q in AAF23433. (PubMed:15247124)Curated
Sequence conflicti400 – 4001A → P in BAA89794. 1 PublicationCurated
Sequence conflicti436 – 4361I → IEFCGR in AAF23433. (PubMed:15247124)Curated
Sequence conflicti437 – 4371K → Q in BAA89794. 1 PublicationCurated
Sequence conflicti559 – 5613DNN → ATI in BAA89794. 1 PublicationCurated
Sequence conflicti568 – 5681C → S in BAA89794. 1 PublicationCurated
Sequence conflicti575 – 5751V → A in BAA89794. 1 PublicationCurated
Sequence conflicti584 – 5841N → H in BAA89794. 1 PublicationCurated
Sequence conflicti605 – 6051L → S in AAF36964. 1 PublicationCurated
Sequence conflicti616 – 6161D → G in AAF36964. 1 PublicationCurated
Sequence conflicti813 – 8131D → G in AAO63590. (PubMed:12724404)Curated
Sequence conflicti915 – 9173RLQ → LP in AAF23433. (PubMed:15247124)Curated
Sequence conflicti940 – 9401L → R in AAF23433. (PubMed:15247124)Curated
Sequence conflicti1000 – 10001K → E in AAF28341. (PubMed:11481388)Curated
Sequence conflicti1000 – 10001K → E in AAF36964. 1 PublicationCurated
Sequence conflicti1001 – 10011T → Q in AAF23433. (PubMed:15247124)Curated
Sequence conflicti1032 – 10321S → P in AAO63590. (PubMed:12724404)Curated
Sequence conflicti1087 – 10871S → N in AAO63590. (PubMed:12724404)Curated
Sequence conflicti1118 – 11181R → G in CAI46047. (PubMed:17974005)Curated
Sequence conflicti1144 – 11441K → T in AAF23433. (PubMed:15247124)Curated
Sequence conflicti1144 – 11441K → T in AAD41239. 1 PublicationCurated
Sequence conflicti1243 – 12442IR → NQ in AAF23433. (PubMed:15247124)Curated
Sequence conflicti1243 – 12442IR → NQ in AAD41239. 1 PublicationCurated
Sequence conflicti1290 – 12901V → A in AAF28341. (PubMed:11481388)Curated
Sequence conflicti1290 – 12901V → A in AAF36964. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 319319Missing in isoform 4. 1 PublicationVSP_024230Add
BLAST
Alternative sequencei529 – 61486Missing in isoform 2. 4 PublicationsVSP_024231Add
BLAST
Alternative sequencei1112 – 112211ACTGQKRVKDA → GEKENVYVDLF in isoform 4. 1 PublicationVSP_024232Add
BLAST
Alternative sequencei1123 – 1312190Missing in isoform 4. 1 PublicationVSP_024233Add
BLAST
Alternative sequencei1150 – 11534TNSS → SAPH in isoform 3. 1 PublicationVSP_024234
Alternative sequencei1154 – 1312159Missing in isoform 3. 1 PublicationVSP_024235Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF214114 mRNA. Translation: AAF28341.2.
AY220790 mRNA. Translation: AAO63590.1.
AF208045 mRNA. Translation: AAF23433.3. Frameshift.
AB030181 mRNA. Translation: BAA89794.1.
AB210032 mRNA. Translation: BAE06114.1. Different initiation.
AL391994, AL133418 Genomic DNA. Translation: CAI13747.2.
AL391994 Genomic DNA. Translation: CAI13749.1.
AL391994, AL133418 Genomic DNA. Translation: CAI13751.1. Sequence problems.
AL133418, AL391994 Genomic DNA. Translation: CAI22961.2.
AL133418, AL391994 Genomic DNA. Translation: CAI22962.1.
BC048959 mRNA. Translation: AAH48959.1. Different termination.
BC062536 mRNA. Translation: AAH62536.1. Different termination.
BC104632 mRNA. Translation: AAI04633.1. Different termination.
BC130418 mRNA. Translation: AAI30419.1.
BX648820 mRNA. Translation: CAI46047.1.
AL133594 mRNA. Translation: CAB63731.1.
AF227899 mRNA. Translation: AAF36964.1.
AF083249 mRNA. Translation: AAD41239.1. Frameshift.
AK023144 mRNA. Translation: BAB14428.1. Different initiation.
CCDSiCCDS31060.1. [Q4LE39-2]
CCDS31061.1. [Q4LE39-1]
PIRiT43497.
RefSeqiNP_001193723.1. NM_001206794.1. [Q4LE39-1]
NP_057458.4. NM_016374.5. [Q4LE39-1]
NP_112739.2. NM_031371.3. [Q4LE39-2]
UniGeneiHs.575782.

Genome annotation databases

EnsembliENST00000264183; ENSP00000264183; ENSG00000054267. [Q4LE39-1]
ENST00000349213; ENSP00000264184; ENSG00000054267. [Q4LE39-2]
ENST00000366603; ENSP00000355562; ENSG00000054267. [Q4LE39-1]
ENST00000421364; ENSP00000394663; ENSG00000054267. [Q4LE39-3]
GeneIDi51742.
KEGGihsa:51742.
UCSCiuc001hwq.3. human. [Q4LE39-1]
uc001hwr.3. human. [Q4LE39-2]
uc001hwt.4. human. [Q4LE39-4]

Polymorphism databases

DMDMi143955276.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF214114 mRNA. Translation: AAF28341.2 .
AY220790 mRNA. Translation: AAO63590.1 .
AF208045 mRNA. Translation: AAF23433.3 . Frameshift.
AB030181 mRNA. Translation: BAA89794.1 .
AB210032 mRNA. Translation: BAE06114.1 . Different initiation.
AL391994 , AL133418 Genomic DNA. Translation: CAI13747.2 .
AL391994 Genomic DNA. Translation: CAI13749.1 .
AL391994 , AL133418 Genomic DNA. Translation: CAI13751.1 . Sequence problems.
AL133418 , AL391994 Genomic DNA. Translation: CAI22961.2 .
AL133418 , AL391994 Genomic DNA. Translation: CAI22962.1 .
BC048959 mRNA. Translation: AAH48959.1 . Different termination.
BC062536 mRNA. Translation: AAH62536.1 . Different termination.
BC104632 mRNA. Translation: AAI04633.1 . Different termination.
BC130418 mRNA. Translation: AAI30419.1 .
BX648820 mRNA. Translation: CAI46047.1 .
AL133594 mRNA. Translation: CAB63731.1 .
AF227899 mRNA. Translation: AAF36964.1 .
AF083249 mRNA. Translation: AAD41239.1 . Frameshift.
AK023144 mRNA. Translation: BAB14428.1 . Different initiation.
CCDSi CCDS31060.1. [Q4LE39-2 ]
CCDS31061.1. [Q4LE39-1 ]
PIRi T43497.
RefSeqi NP_001193723.1. NM_001206794.1. [Q4LE39-1 ]
NP_057458.4. NM_016374.5. [Q4LE39-1 ]
NP_112739.2. NM_031371.3. [Q4LE39-2 ]
UniGenei Hs.575782.

3D structure databases

ProteinModelPortali Q4LE39.
SMRi Q4LE39. Positions 5-121, 170-271, 308-394, 564-632.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119708. 17 interactions.
IntActi Q4LE39. 11 interactions.

PTM databases

PhosphoSitei Q4LE39.

Polymorphism databases

DMDMi 143955276.

Proteomic databases

MaxQBi Q4LE39.
PaxDbi Q4LE39.
PRIDEi Q4LE39.

Protocols and materials databases

DNASUi 51742.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264183 ; ENSP00000264183 ; ENSG00000054267 . [Q4LE39-1 ]
ENST00000349213 ; ENSP00000264184 ; ENSG00000054267 . [Q4LE39-2 ]
ENST00000366603 ; ENSP00000355562 ; ENSG00000054267 . [Q4LE39-1 ]
ENST00000421364 ; ENSP00000394663 ; ENSG00000054267 . [Q4LE39-3 ]
GeneIDi 51742.
KEGGi hsa:51742.
UCSCi uc001hwq.3. human. [Q4LE39-1 ]
uc001hwr.3. human. [Q4LE39-2 ]
uc001hwt.4. human. [Q4LE39-4 ]

Organism-specific databases

CTDi 51742.
GeneCardsi GC01M235298.
HGNCi HGNC:15550. ARID4B.
HPAi HPA027333.
MIMi 609696. gene.
neXtProti NX_Q4LE39.
PharmGKBi PA134940494.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG248805.
GeneTreei ENSGT00510000046413.
HOVERGENi HBG058247.
InParanoidi Q4LE39.
OMAi FRLVHKL.
PhylomeDBi Q4LE39.
TreeFami TF106427.

Enzyme and pathway databases

Reactomei REACT_200856. NoRC negatively regulates rRNA expression.
REACT_228222. HDACs deacetylate histones.

Miscellaneous databases

ChiTaRSi ARID4B. human.
GeneWikii ARID4B.
GenomeRNAii 51742.
NextBioi 55820.
PROi Q4LE39.
SOURCEi Search...

Gene expression databases

Bgeei Q4LE39.
ExpressionAtlasi Q4LE39. baseline and differential.
Genevestigatori Q4LE39.

Family and domain databases

Gene3Di 1.10.150.60. 1 hit.
InterProi IPR001606. ARID/BRIGHT_DNA-bd.
IPR028853. ARID4B.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR012603. RBB1NT.
IPR002999. Tudor.
IPR025995. Tudor-knot.
[Graphical view ]
PANTHERi PTHR13964:SF21. PTHR13964:SF21. 1 hit.
Pfami PF01388. ARID. 1 hit.
PF08169. RBB1NT. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00501. BRIGHT. 1 hit.
SM00298. CHROMO. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view ]
SUPFAMi SSF46774. SSF46774. 1 hit.
SSF54160. SSF54160. 1 hit.
PROSITEi PS51011. ARID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "RBP1L1, a retinoblastoma-binding protein-related gene encoding an antigenic epitope abundantly expressed in human carcinomas and normal testis."
    Cao J.-N., Gao T.-W., Stanbridge E.J., Irie R.
    J. Natl. Cancer Inst. 93:1159-1165(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Identification and characterization of three new components of the mSin3A corepressor complex."
    Fleischer T.C., Yun U.J., Ayer D.E.
    Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DOMAIN, TISSUE SPECIFICITY, IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
  3. "Characterization of BRCAA1 and its novel antigen epitope identification."
    Cui D., Jin G., Gao T.W., Sun T., Tian F., Estrada G.G., Gao H., Sarai A.
    Cancer Epidemiol. Biomarkers Prev. 13:1136-1145(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Rheumatoid arthritis antigenic protein similar to retinoblastoma binding protein 1 (RBP1)."
    Tanaka M.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Synovium.
  5. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
    Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "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].
  7. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-651 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-424.
    Tissue: Hippocampus, Kidney and Lung.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1149 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-1312.
    Tissue: Adipose tissue and Testis.
  9. "Human breast carcinoma-associated antigen isoform I."
    Cao J., Irie R.F., Stanbridge E.J.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 440-1312 (ISOFORM 1).
  10. "Human Rb binding protein homolog gene, partial CDS."
    Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1312.
  11. "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 828-1312.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-675; SER-790; THR-793; THR-1150; SER-1152; SER-1153; SER-1155 AND SER-1159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. "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-790; THR-793; SER-1014 AND THR-1026, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-675; SER-778; SER-790 AND THR-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-276; SER-778; SER-790 AND THR-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARI4B_HUMAN
AccessioniPrimary (citable) accession number: Q4LE39
Secondary accession number(s): A1L465
, Q3MHV4, Q5HY99, Q5T2C2, Q5T2C3, Q5T2C4, Q5T2C5, Q5T2C6, Q6P600, Q86UX1, Q86WR4, Q9H915, Q9NYU3, Q9NZB6, Q9NZG4, Q9P2W4, Q9UF62, Q9Y6E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: November 26, 2014
This is version 92 of the entry and version 2 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3