Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q4LE39

- ARI4B_HUMAN

UniProt

Q4LE39 - ARI4B_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    2. protein binding Source: IntAct

    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

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_200856. NoRC negatively regulates rRNA expression.

    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-SubCell
    2. nucleus Source: UniProtKB-SubCell

    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.
    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. 12 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.
    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

    MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE     50
    VQDDHIKGPL KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT 100
    LRRSSLCLKG ERHFAESETL DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP 150
    EEESSSSSSD EDEDDRKQID ELLGKVVCVD YISLDKKKAL WFPALVVCPD 200
    CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK PDAVLKQAFE 250
    QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE 300
    EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL 350
    GGFDNIESGA VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA 400
    NIEFQMALPE KVVNKQCKEC ENVKEIKVKE ENETEIKEIK MEEERNIIPR 450
    EEKPIEDEIE RKENIKPSLG SKKNLLESIP THSDQEKEVN IKKPEDNENL 500
    DDKDDDTTRV DESLNIKVEA EEEKAKSGDE TNKEEDEDDE EAEEEEEEEE 550
    EEEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG 600
    EVLYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD 650
    KDEKYSPKNC KLRRLSKPPF QTNPSPEMVS KLDLTDAKNS DTAHIKSIEI 700
    TSILNGLQAS ESSAEDSEQE DERGAQDMDN NGKEESKIDH LTNNRNDLIS 750
    KEEQNSSSLL EENKVHADLV ISKPVSKSPE RLRKDIEVLS EDTDYEEDEV 800
    TKKRKDVKKD TTDKSSKPQI KRGKRRYCNT EECLKTGSPG KKEEKAKNKE 850
    SLCMENSSNS SSDEDEEETK AKMTPTKKYN GLEEKRKSLR TTGFYSGFSE 900
    VAEKRIKLLN NSDERLQNSR AKDRKDVWSS IQGQWPKKTL KELFSDSDTE 950
    AAASPPHPAP EEGVAEESLQ TVAEEESCSP SVELEKPPPV NVDSKPIEEK 1000
    TVEVNDRKAE FPSSGSNSVL NTPPTTPESP SSVTVTEGSR QQSSVTVSEP 1050
    LAPNQEEVRS IKSETDSTIE VDSVAGELQD LQSEGNSSPA GFDASVSSSS 1100
    SNQPEPEHPE KACTGQKRVK DAQGGGSSSK KQKRSHKATV VNNKKKGKGT 1150
    NSSDSEELSA GESITKSQPV KSVSTGMKSH STKSPARTQS PGKCGKNGDK 1200
    DPDLKEPSNR LPKVYKWSFQ MSDLENMTSA ERITILQEKL QEIRKHYLSL 1250
    KSEVASIDRR RKRLKKKERE SAATSSSSSS PSSSSITAAV MLTLAEPSMS 1300
    SASQNGMSVE CR 1312
    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.
    The sequence AAF23433.3 differs from that shown. Reason: Frameshift at positions 1287 and 1311.
    The sequence BAB14428.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE06114.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI13751.1 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 12 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 GC01M235296.
    HGNCi HGNC:15550. ARID4B.
    HPAi HPA027333.
    MIMi 609696. gene.
    neXtProti NX_Q4LE39.
    PharmGKBi PA134940494.
    GenAtlasi Search...

    Phylogenomic databases

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

    Enzyme and pathway databases

    Reactomei REACT_200856. NoRC negatively regulates rRNA expression.

    Miscellaneous databases

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

    Gene expression databases

    Bgeei Q4LE39.
    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

    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: October 1, 2014
    This is version 90 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