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)

P29374

- ARI4A_HUMAN

UniProt

P29374 - ARI4A_HUMAN

Protein

AT-rich interactive domain-containing protein 4A

Gene

ARID4A

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 132 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Interacts with the viral protein-binding domain of the retinoblastoma protein.

    GO - Molecular functioni

    1. DNA binding Source: GDB
    2. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. erythrocyte development Source: Ensembl
    2. histone H3-K4 trimethylation Source: Ensembl
    3. histone H3-K9 trimethylation Source: Ensembl
    4. histone H4-K20 trimethylation Source: Ensembl
    5. negative regulation of transcription, DNA-templated Source: GDB
    6. regulation of gene expression by genetic imprinting Source: Ensembl
    7. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AT-rich interactive domain-containing protein 4A
    Short name:
    ARID domain-containing protein 4A
    Alternative name(s):
    Retinoblastoma-binding protein 1
    Short name:
    RBBP-1
    Gene namesi
    Name:ARID4A
    Synonyms:RBBP1, RBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9885. ARID4A.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: GDB
    2. transcriptional repressor complex Source: GDB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34249.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12571257AT-rich interactive domain-containing protein 4APRO_0000200580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei538 – 5381Phosphoserine1 Publication
    Modified residuei542 – 5421Phosphoserine1 Publication
    Modified residuei676 – 6761Phosphoserine1 Publication
    Modified residuei1109 – 11091Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP29374.
    PaxDbiP29374.
    PRIDEiP29374.

    PTM databases

    PhosphoSiteiP29374.

    Expressioni

    Gene expression databases

    ArrayExpressiP29374.
    BgeeiP29374.
    CleanExiHS_ARID4A.
    HS_RBP1.
    GenevestigatoriP29374.

    Organism-specific databases

    HPAiHPA048899.

    Interactioni

    Subunit structurei

    Interacts with BRMS1. Identified in mSin3A corepressor complexes together with SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1, HDAC1 and HDAC2.1 Publication

    Protein-protein interaction databases

    BioGridi111861. 24 interactions.
    DIPiDIP-463N.
    IntActiP29374. 4 interactions.
    MINTiMINT-150005.
    STRINGi9606.ENSP00000347602.

    Structurei

    Secondary structure

    1
    1257
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Beta strandi15 – 206
    Beta strandi23 – 4220
    Turni43 – 453
    Beta strandi48 – 525
    Turni53 – 553
    Beta strandi56 – 583
    Beta strandi65 – 695
    Beta strandi75 – 9319
    Beta strandi98 – 1025
    Helixi103 – 1053
    Beta strandi112 – 1143
    Beta strandi177 – 1826
    Beta strandi190 – 1967
    Beta strandi211 – 2188
    Beta strandi221 – 2244
    Turni226 – 2283
    Helixi239 – 2446
    Helixi246 – 25611
    Turni262 – 2643
    Helixi269 – 2724
    Beta strandi578 – 5858
    Beta strandi588 – 60215
    Beta strandi605 – 6128
    Beta strandi621 – 6244
    Helixi625 – 6273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LCCNMR-A568-635[»]
    2MAMNMR-A4-121[»]
    2YRVNMR-A170-273[»]
    ProteinModelPortaliP29374.
    SMRiP29374. Positions 4-121, 170-277, 306-397, 568-635.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29374.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini309 – 40193ARIDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni951 – 96414Retinoblastoma protein bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ARID domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG248805.
    HOGENOMiHOG000015398.
    HOVERGENiHBG058247.
    InParanoidiP29374.
    OMAiISPSCND.
    OrthoDBiEOG7PVWNP.
    PhylomeDBiP29374.
    TreeFamiTF106427.

    Family and domain databases

    Gene3Di1.10.150.60. 1 hit.
    InterProiIPR001606. ARID/BRIGHT_DNA-bd.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR012603. RBB1NT.
    IPR002999. Tudor.
    IPR025995. Tudor-knot.
    [Graphical view]
    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. 1 hit.
    [Graphical view]
    SUPFAMiSSF46774. SSF46774. 1 hit.
    SSF54160. SSF54160. 1 hit.
    PROSITEiPS51011. ARID. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform I (identifier: P29374-1) [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

    MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL     50
    VQDDQVKGPL RVGAIVETRT SDGSFQEAII SKLTDASWYT VVFDDGDERT 100
    LRRTSLCLKG ERHFAESETL DQLPLTNPEH FGTPVIAKKT NRGRRSSLPV 150
    TEDEKEEESS EEEDEDKRRL NDELLGKVVS VVSATERTEW YPALVISPSC 200
    NDDITVKKDQ CLVRSFIDSK FYSIARKDIK EVDILNLPES ELSTKPGLQK 250
    ASIFLKTRVV PDNWKMDISE ILESSSSDDE DGPAEENDEE KEKEAKKTEE 300
    EVPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV 350
    YHQGGCDNID SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC 400
    RSANIQFRTV HHHEPKVKEE KKDLEESMEE ALKLDQEMPL TEVKSEPEEN 450
    IDSNSESERE EIELKSPRGR RRIARDVNSI KKEIEEEKTE DKLKDNDTEN 500
    KDVDDDYETA EKKENELLLG RKNTPKQKEK KIKKQEDSDK DSDEEEEKSQ 550
    EREETESKCD SEGEEDEEDM EPCLTGTKVK VKYGRGKTQK IYEASIKSTE 600
    IDDGEVLYLV HYYGWNVRYD EWVKADRIIW PLDKGGPKKK QKKKAKNKED 650
    SEKDEKRDEE RQKSKRGRPP LKSTLSSNMP YGLSKTANSE GKSDSCSSDS 700
    ETEDALEKNL INEELSLKDE LEKNENLNDD KLDEENPKIS AHILKENDRT 750
    QMQPLETLKL EVGENEQIVQ IFGNKMEKTE EVKKEAEKSP KGKGRRSKTK 800
    DLSLEIIKIS SFGQNEAGSE PHIEAHSLEL SSLDNKNFSS ATEDEIDQCV 850
    KEKKLKRKIL GQSSPEKKIR IENGMEMTNT VSQERTSDCI GSEGMKNLNF 900
    EQHFERENEG MPSLIAESNQ CIQQLTSERF DSPAEETVNI PLKEDEDAMP 950
    LIGPETLVCH EVDLDDLDEK DKTSIEDVAV ESSESNSLVS IPPALPPVVQ 1000
    HNFSVASPLT LSQDESRSVK SESDITIEVD SIAEESQEGL CERESANGFE 1050
    TNVASGTCSI IVQERESREK GQKRPSDGNS GLMAKKQKRT PKRTSAAAKN 1100
    EKNGTGQSSD SEDLPVLDNS SKCTPVKHLN VSKPQKLARS PARISPHIKD 1150
    GEKDKHREKH PNSSPRTYKW SFQLNELDNM NSTERISFLQ EKLQEIRKYY 1200
    MSLKSEVATI DRRRKRLKKK DREVSHAGAS MSSASSDTGM SPSSSSPPQN 1250
    VLAVECR 1257
    Length:1,257
    Mass (Da):142,752
    Last modified:September 23, 2008 - v3
    Checksum:i5B3F6A5AFB7588CF
    GO
    Isoform II (identifier: P29374-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1121-1174: Missing.

    Show »
    Length:1,203
    Mass (Da):136,495
    Checksum:iB2A06AA7071AAAE2
    GO
    Isoform III (identifier: P29374-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1106-1174: Missing.
         1175-1175: N → D

    Show »
    Length:1,188
    Mass (Da):134,951
    Checksum:i0576FA849F761B54
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3851V → L in AAB28543. (PubMed:8414517)Curated
    Sequence conflicti618 – 6181R → S in AAB28543. (PubMed:8414517)Curated
    Sequence conflicti653 – 6531K → V in AAB25833. (PubMed:8455946)Curated
    Sequence conflicti653 – 6531K → V in AAB25834. (PubMed:8455946)Curated
    Sequence conflicti653 – 6531K → V in AAB25835. (PubMed:8455946)Curated
    Sequence conflicti1178 – 11781D → S no nucleotide entry (PubMed:1857421)Curated
    Sequence conflicti1196 – 12016IRKYYM → SENIICL no nucleotide entry (PubMed:1857421)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti412 – 4121H → P.
    Corresponds to variant rs34982206 [ dbSNP | Ensembl ].
    VAR_031566
    Natural varianti724 – 7241N → S.
    Corresponds to variant rs2230098 [ dbSNP | Ensembl ].
    VAR_031567
    Natural varianti779 – 7791T → A.1 Publication
    Corresponds to variant rs1051858 [ dbSNP | Ensembl ].
    VAR_031568

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1106 – 117469Missing in isoform III. 1 PublicationVSP_004371Add
    BLAST
    Alternative sequencei1121 – 117454Missing in isoform II. 1 PublicationVSP_004373Add
    BLAST
    Alternative sequencei1175 – 11751N → D in isoform III. 1 PublicationVSP_004372

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S66427 mRNA. Translation: AAB28543.1.
    AL132989 Genomic DNA. No translation available.
    AL139021 Genomic DNA. No translation available.
    S57153 mRNA. Translation: AAB25833.1.
    S57160 mRNA. Translation: AAB25834.1.
    S57162 mRNA. Translation: AAB25835.2.
    CCDSiCCDS45114.1. [P29374-2]
    CCDS9732.1. [P29374-1]
    CCDS9733.1. [P29374-3]
    PIRiI58383.
    RefSeqiNP_002883.3. NM_002892.3. [P29374-1]
    NP_075376.2. NM_023000.2. [P29374-2]
    NP_075377.2. NM_023001.2. [P29374-3]
    UniGeneiHs.161000.

    Genome annotation databases

    EnsembliENST00000348476; ENSP00000344556; ENSG00000032219. [P29374-3]
    ENST00000355431; ENSP00000347602; ENSG00000032219. [P29374-1]
    ENST00000395168; ENSP00000378597; ENSG00000032219. [P29374-2]
    ENST00000431317; ENSP00000397368; ENSG00000032219. [P29374-3]
    GeneIDi5926.
    KEGGihsa:5926.
    UCSCiuc001xdo.3. human. [P29374-2]
    uc001xdp.3. human. [P29374-1]
    uc001xdq.3. human. [P29374-3]

    Polymorphism databases

    DMDMi206729929.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S66427 mRNA. Translation: AAB28543.1 .
    AL132989 Genomic DNA. No translation available.
    AL139021 Genomic DNA. No translation available.
    S57153 mRNA. Translation: AAB25833.1 .
    S57160 mRNA. Translation: AAB25834.1 .
    S57162 mRNA. Translation: AAB25835.2 .
    CCDSi CCDS45114.1. [P29374-2 ]
    CCDS9732.1. [P29374-1 ]
    CCDS9733.1. [P29374-3 ]
    PIRi I58383.
    RefSeqi NP_002883.3. NM_002892.3. [P29374-1 ]
    NP_075376.2. NM_023000.2. [P29374-2 ]
    NP_075377.2. NM_023001.2. [P29374-3 ]
    UniGenei Hs.161000.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LCC NMR - A 568-635 [» ]
    2MAM NMR - A 4-121 [» ]
    2YRV NMR - A 170-273 [» ]
    ProteinModelPortali P29374.
    SMRi P29374. Positions 4-121, 170-277, 306-397, 568-635.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111861. 24 interactions.
    DIPi DIP-463N.
    IntActi P29374. 4 interactions.
    MINTi MINT-150005.
    STRINGi 9606.ENSP00000347602.

    PTM databases

    PhosphoSitei P29374.

    Polymorphism databases

    DMDMi 206729929.

    Proteomic databases

    MaxQBi P29374.
    PaxDbi P29374.
    PRIDEi P29374.

    Protocols and materials databases

    DNASUi 5926.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348476 ; ENSP00000344556 ; ENSG00000032219 . [P29374-3 ]
    ENST00000355431 ; ENSP00000347602 ; ENSG00000032219 . [P29374-1 ]
    ENST00000395168 ; ENSP00000378597 ; ENSG00000032219 . [P29374-2 ]
    ENST00000431317 ; ENSP00000397368 ; ENSG00000032219 . [P29374-3 ]
    GeneIDi 5926.
    KEGGi hsa:5926.
    UCSCi uc001xdo.3. human. [P29374-2 ]
    uc001xdp.3. human. [P29374-1 ]
    uc001xdq.3. human. [P29374-3 ]

    Organism-specific databases

    CTDi 5926.
    GeneCardsi GC14P058766.
    H-InvDB HIX0037655.
    HGNCi HGNC:9885. ARID4A.
    HPAi HPA048899.
    MIMi 180201. gene.
    neXtProti NX_P29374.
    PharmGKBi PA34249.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248805.
    HOGENOMi HOG000015398.
    HOVERGENi HBG058247.
    InParanoidi P29374.
    OMAi ISPSCND.
    OrthoDBi EOG7PVWNP.
    PhylomeDBi P29374.
    TreeFami TF106427.

    Miscellaneous databases

    ChiTaRSi ARID4A. human.
    EvolutionaryTracei P29374.
    GeneWikii ARID4A.
    GenomeRNAii 5926.
    NextBioi 23080.
    PROi P29374.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29374.
    Bgeei P29374.
    CleanExi HS_ARID4A.
    HS_RBP1.
    Genevestigatori P29374.

    Family and domain databases

    Gene3Di 1.10.150.60. 1 hit.
    InterProi IPR001606. ARID/BRIGHT_DNA-bd.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR012603. RBB1NT.
    IPR002999. Tudor.
    IPR025995. Tudor-knot.
    [Graphical view ]
    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. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46774. SSF46774. 1 hit.
    SSF54160. SSF54160. 1 hit.
    PROSITEi PS51011. ARID. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the retinoblastoma binding proteins RBP1 and RBP2."
      Fattaey A.R., Helin K., Dembski M.S., Dyson N., Harlow E., Vuocolo G.A., Hanobik M.G., Haskell K.M., Oliff A., Defeo-Jones D., Jones R.E.
      Oncogene 8:3149-3156(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), VARIANT ALA-779.
    2. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Alternative splicing of the RBP1 gene clusters in an internal exon that encodes potential phosphorylation sites."
      Otterson G.A., Kratzke R.A., Lin A.Y., Johnston P.G., Kaye F.J.
      Oncogene 8:949-957(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 338-1257 (ISOFORMS I; II AND III), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    4. "Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product."
      Defeo-Jones D., Huang P.S., Jones R.E., Haskell K.M., Vuocolo G.A., Hanobik M.G., Huber H.E., Oliff A.
      Nature 352:251-254(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 855-1203 (ISOFORM I).
    5. "Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription."
      Meehan W.J., Samant R.S., Hopper J.E., Carrozza M.J., Shevde L.A., Workman J.L., Eckert K.A., Verderame M.F., Welch D.R.
      J. Biol. Chem. 279:1562-1569(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH WITH SIN3A; SIN3B; HDAC1; HDAC2; SAP30; BRMS1; RBBP4 AND RBBP7.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-676 AND SER-1109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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-538 AND SER-542, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the RBB1NT domain of human RB(Retinoblastoma)-binding protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 170-277.

    Entry informationi

    Entry nameiARI4A_HUMAN
    AccessioniPrimary (citable) accession number: P29374
    Secondary accession number(s): Q15991, Q15992, Q15993
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 132 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 14
      Human chromosome 14: 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

    External Data

    Dasty 3