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Q6ZNA4

- RN111_HUMAN

UniProt

Q6ZNA4 - RN111_HUMAN

Protein

E3 ubiquitin-protein ligase Arkadia

Gene

RNF111

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Acts in the NODAL pathway of mesoderm patterning during embryonic development. Acts downstream AXIN1 as an E3 ubiquitin-protein ligase which promotes the ubiquitination of inhibitory SMADs such as SMAD7, induces their proteasomal degradation and thereby enhances the transcriptional activity of TGF-beta and BMP. Activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Associates with UBE2D2 as an E2 enzyme.4 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri942 – 98342RING-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. SUMO polymer binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: BHF-UCL
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. gene expression Source: Reactome
    2. pattern specification process Source: Ensembl
    3. positive regulation of protein ubiquitination Source: Ensembl
    4. positive regulation of transcription, DNA-templated Source: BHF-UCL
    5. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    6. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
    7. protein polyubiquitination Source: Ensembl
    8. transcription, DNA-templated Source: Reactome
    9. transcription initiation from RNA polymerase II promoter Source: Reactome
    10. transforming growth factor beta receptor signaling pathway Source: Reactome
    11. ubiquitin-dependent SMAD protein catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ6ZNA4.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase Arkadia (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 111
    Gene namesi
    Name:RNF111
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:17384. RNF111.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Upon TGF-beta treatment, translocates from nucleus to cytosol.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleolus Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi382 – 3821V → A: Abolishes SUMO binding. 1 Publication
    Mutagenesisi382 – 3821V → L: Loss of affinity to SUMO1 and SUMO2. 1 Publication
    Mutagenesisi382 – 3821V → Y: No loss of affinity toward SUMO1 and SUMO2. 1 Publication
    Mutagenesisi383 – 3831V → A: Abolishes SUMO binding. 1 Publication
    Mutagenesisi383 – 3831V → I: No loss of affinity toward SUMO1 and SUMO2. 1 Publication
    Mutagenesisi384 – 3841D → A: Abolishes SUMO binding. 1 Publication
    Mutagenesisi384 – 3841D → E: Loss of affinity to SUMO1 and SUMO2. 1 Publication
    Mutagenesisi384 – 3841D → N: Loss of affinity to SUMO1 and SUMO2. 1 Publication
    Mutagenesisi385 – 3851L → A: Abolishes SUMO binding. 1 Publication
    Mutagenesisi385 – 3851L → I: Loss of affinity to SUMO1 and SUMO2. 1 Publication
    Mutagenesisi386 – 3861T → A: Abolishes SUMO binding. 1 Publication
    Mutagenesisi386 – 3861T → S: Loss of affinity to SUMO1 and SUMO2. 1 Publication
    Mutagenesisi386 – 3861T → V: Loss of affinity to SUMO1 and SUMO2. 1 Publication

    Organism-specific databases

    PharmGKBiPA134868772.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 994994E3 ubiquitin-protein ligase ArkadiaPRO_0000280690Add
    BLAST

    Proteomic databases

    MaxQBiQ6ZNA4.
    PaxDbiQ6ZNA4.
    PRIDEiQ6ZNA4.

    PTM databases

    PhosphoSiteiQ6ZNA4.

    Expressioni

    Tissue specificityi

    Broadly expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ6ZNA4.
    BgeeiQ6ZNA4.
    CleanExiHS_RNF111.
    GenevestigatoriQ6ZNA4.

    Organism-specific databases

    HPAiHPA038576.
    HPA038577.

    Interactioni

    Subunit structurei

    Interacts with SMAD6, SMAD7, AXIN1, AXIN2 and SKIL isoform SNON. Part of a complex containing RNF111, AXIN1 and SMAD7. Interacts (via SIM domains) with SUMO1 and SUMO2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXIN1O151692EBI-2129175,EBI-710484

    Protein-protein interaction databases

    BioGridi120146. 45 interactions.
    IntActiQ6ZNA4. 33 interactions.
    MINTiMINT-1187466.
    STRINGi9606.ENSP00000288199.

    Structurei

    Secondary structure

    1
    994
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni943 – 9464
    Beta strandi951 – 9533
    Beta strandi955 – 9573
    Beta strandi963 – 9653
    Helixi966 – 97510
    Turni980 – 9823
    Beta strandi984 – 9863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KIZNMR-A927-994[»]
    ProteinModelPortaliQ6ZNA4.
    SMRiQ6ZNA4. Positions 941-994.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni241 – 404164Interaction with AXIN1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi300 – 3045SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates
    Motifi325 – 3317SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates
    Motifi382 – 3865SUMO interaction motif 3 (SIM); mediates the binding to polysumoylated substrates

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi252 – 464213Ser-richAdd
    BLAST
    Compositional biasi494 – 52330His-richAdd
    BLAST
    Compositional biasi629 – 781153Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri942 – 98342RING-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG291583.
    HOVERGENiHBG093884.
    InParanoidiQ6ZNA4.
    KOiK10635.
    OMAiPCRKRFV.
    OrthoDBiEOG7WHH9N.
    PhylomeDBiQ6ZNA4.
    TreeFamiTF331862.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR029306. RNF111_N.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF15303. RNF111_N. 1 hit.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZNA4-1) [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

    MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP    50
    AGVEMINSKV GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA 100
    GPSYVQNCVK ENQGILGLRQ HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS 150
    DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR SHKWPRTETE SVSGLLMKRP 200
    CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE VLARRKYALL 250
    PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 300
    VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ 350
    GSSSHASRPQ EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA 400
    RMESQATSAS INNSNPSTSE QASDTASAVT SSQPSTVSET SATLTSNSTT 450
    GTSIGDDSRR TTSSAVTETG PPAMPRLPSC CPQHSPCGGS SQNHHALGHP 500
    HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE RPPQVQAPCG 550
    ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 600
    IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY 650
    ASLTRPLHHQ ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA 700
    TSHPVAPPPP THLASTAAPI PQHLPPTHQP ISHHIPATAP PAQRLHPHEV 750
    MQRMEVQRRR MMQHPTRAHE RPPPHPHRMH PNYGHGHHIH VPQTMSSHPR 800
    QAPERSAWEL GIEAGVTAAT YTPGALHPHL AHYHAPPRLH HLQLGALPLM 850
    VPDMAGYPHI RYISSGLDGT SFRGPFRGNF EELIHLEERL GNVNRGASQG 900
    TIERCTYPHK YKKVTTDWFS QRKLHCKQDG EEGTEEDTEE KCTICLSILE 950
    EGEDVRRLPC MHLFHQVCVD QWLITNKKCP ICRVDIEAQL PSES 994
    Length:994
    Mass (Da):108,862
    Last modified:October 5, 2010 - v3
    Checksum:i7E387321E5F61FAB
    GO
    Isoform 2 (identifier: Q6ZNA4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         914-921: Missing.

    Show »
    Length:986
    Mass (Da):107,896
    Checksum:iBD07D5D2C2B6AEB4
    GO
    Isoform 3 (identifier: Q6ZNA4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         766-766: T → TGLFVFCVSR

    Note: No experimental confirmation available.

    Show »
    Length:1,003
    Mass (Da):109,871
    Checksum:i9F0D0B05B5EB39A8
    GO
    Isoform 4 (identifier: Q6ZNA4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         766-766: T → TGLFVFCVSR
         914-921: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:995
    Mass (Da):108,906
    Checksum:iA648717F19CFB655
    GO

    Sequence cautioni

    The sequence AAH10369.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC04531.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD18633.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti165 – 1651H → R in BX647259. (PubMed:17974005)Curated
    Sequence conflicti473 – 4731A → E in CAD98031. (PubMed:17974005)Curated
    Sequence conflicti562 – 5621Missing in AAH60862. (PubMed:16572171)Curated
    Sequence conflicti562 – 5621Missing in AAH20984. (PubMed:16572171)Curated
    Sequence conflicti625 – 6251M → T in BX647259. (PubMed:17974005)Curated
    Sequence conflicti738 – 7381T → I in BX647259. (PubMed:17974005)Curated
    Sequence conflicti809 – 8091E → G in CAD98031. (PubMed:17974005)Curated
    Sequence conflicti931 – 9311E → G in CAD98031. (PubMed:17974005)Curated
    Sequence conflicti938 – 9381T → A in BX647259. (PubMed:17974005)Curated
    Sequence conflicti974 – 9741I → V in BAD18471. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91N → K.3 Publications
    Corresponds to variant rs2899642 [ dbSNP | Ensembl ].
    VAR_031185
    Natural varianti718 – 7181A → T.
    Corresponds to variant rs34086812 [ dbSNP | Ensembl ].
    VAR_057216

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei766 – 7661T → TGLFVFCVSR in isoform 3 and isoform 4. 2 PublicationsVSP_023840
    Alternative sequencei914 – 9218Missing in isoform 2 and isoform 4. 2 PublicationsVSP_023841

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK095327 mRNA. Translation: BAC04531.1. Different initiation.
    AK131304 mRNA. Translation: BAD18471.1.
    AK131488 mRNA. Translation: BAD18633.1. Different initiation.
    AL157474 mRNA. Translation: CAB75669.2.
    BX538130 mRNA. Translation: CAD98031.1.
    BX647259 mRNA. No translation available.
    AC025918 Genomic DNA. No translation available.
    AC090515 Genomic DNA. No translation available.
    AC092757 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77561.1.
    BC010369 mRNA. Translation: AAH10369.1. Different initiation.
    BC020984 mRNA. Translation: AAH20984.1.
    BC060862 mRNA. Translation: AAH60862.1.
    CCDSiCCDS10169.1. [Q6ZNA4-2]
    CCDS58365.1. [Q6ZNA4-4]
    CCDS58366.1. [Q6ZNA4-1]
    PIRiT46904.
    RefSeqiNP_001257457.1. NM_001270528.1. [Q6ZNA4-4]
    NP_001257458.1. NM_001270529.1.
    NP_001257459.1. NM_001270530.1. [Q6ZNA4-1]
    NP_060080.6. NM_017610.7. [Q6ZNA4-2]
    XP_005254536.1. XM_005254479.1. [Q6ZNA4-3]
    XP_006720642.1. XM_006720579.1. [Q6ZNA4-3]
    XP_006720643.1. XM_006720580.1. [Q6ZNA4-3]
    UniGeneiHs.404423.
    Hs.603489.
    Hs.741727.

    Genome annotation databases

    EnsembliENST00000348370; ENSP00000288199; ENSG00000157450. [Q6ZNA4-2]
    ENST00000557998; ENSP00000452732; ENSG00000157450. [Q6ZNA4-1]
    ENST00000559209; ENSP00000453872; ENSG00000157450. [Q6ZNA4-4]
    ENST00000561186; ENSP00000453015; ENSG00000157450. [Q6ZNA4-3]
    GeneIDi54778.
    KEGGihsa:54778.
    UCSCiuc002afs.4. human. [Q6ZNA4-2]
    uc002aft.4. human.
    uc002afv.4. human. [Q6ZNA4-1]
    uc002afw.4. human. [Q6ZNA4-3]

    Polymorphism databases

    DMDMi308153555.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK095327 mRNA. Translation: BAC04531.1 . Different initiation.
    AK131304 mRNA. Translation: BAD18471.1 .
    AK131488 mRNA. Translation: BAD18633.1 . Different initiation.
    AL157474 mRNA. Translation: CAB75669.2 .
    BX538130 mRNA. Translation: CAD98031.1 .
    BX647259 mRNA. No translation available.
    AC025918 Genomic DNA. No translation available.
    AC090515 Genomic DNA. No translation available.
    AC092757 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77561.1 .
    BC010369 mRNA. Translation: AAH10369.1 . Different initiation.
    BC020984 mRNA. Translation: AAH20984.1 .
    BC060862 mRNA. Translation: AAH60862.1 .
    CCDSi CCDS10169.1. [Q6ZNA4-2 ]
    CCDS58365.1. [Q6ZNA4-4 ]
    CCDS58366.1. [Q6ZNA4-1 ]
    PIRi T46904.
    RefSeqi NP_001257457.1. NM_001270528.1. [Q6ZNA4-4 ]
    NP_001257458.1. NM_001270529.1.
    NP_001257459.1. NM_001270530.1. [Q6ZNA4-1 ]
    NP_060080.6. NM_017610.7. [Q6ZNA4-2 ]
    XP_005254536.1. XM_005254479.1. [Q6ZNA4-3 ]
    XP_006720642.1. XM_006720579.1. [Q6ZNA4-3 ]
    XP_006720643.1. XM_006720580.1. [Q6ZNA4-3 ]
    UniGenei Hs.404423.
    Hs.603489.
    Hs.741727.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KIZ NMR - A 927-994 [» ]
    ProteinModelPortali Q6ZNA4.
    SMRi Q6ZNA4. Positions 941-994.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120146. 45 interactions.
    IntActi Q6ZNA4. 33 interactions.
    MINTi MINT-1187466.
    STRINGi 9606.ENSP00000288199.

    PTM databases

    PhosphoSitei Q6ZNA4.

    Polymorphism databases

    DMDMi 308153555.

    Proteomic databases

    MaxQBi Q6ZNA4.
    PaxDbi Q6ZNA4.
    PRIDEi Q6ZNA4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348370 ; ENSP00000288199 ; ENSG00000157450 . [Q6ZNA4-2 ]
    ENST00000557998 ; ENSP00000452732 ; ENSG00000157450 . [Q6ZNA4-1 ]
    ENST00000559209 ; ENSP00000453872 ; ENSG00000157450 . [Q6ZNA4-4 ]
    ENST00000561186 ; ENSP00000453015 ; ENSG00000157450 . [Q6ZNA4-3 ]
    GeneIDi 54778.
    KEGGi hsa:54778.
    UCSCi uc002afs.4. human. [Q6ZNA4-2 ]
    uc002aft.4. human.
    uc002afv.4. human. [Q6ZNA4-1 ]
    uc002afw.4. human. [Q6ZNA4-3 ]

    Organism-specific databases

    CTDi 54778.
    GeneCardsi GC15P059160.
    HGNCi HGNC:17384. RNF111.
    HPAi HPA038576.
    HPA038577.
    MIMi 605840. gene.
    neXtProti NX_Q6ZNA4.
    PharmGKBi PA134868772.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291583.
    HOVERGENi HBG093884.
    InParanoidi Q6ZNA4.
    KOi K10635.
    OMAi PCRKRFV.
    OrthoDBi EOG7WHH9N.
    PhylomeDBi Q6ZNA4.
    TreeFami TF331862.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q6ZNA4.

    Miscellaneous databases

    GeneWikii RNF111.
    GenomeRNAii 54778.
    NextBioi 57437.
    PROi Q6ZNA4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZNA4.
    Bgeei Q6ZNA4.
    CleanExi HS_RNF111.
    Genevestigatori Q6ZNA4.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR029306. RNF111_N.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF15303. RNF111_N. 1 hit.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 3), VARIANT LYS-9.
      Tissue: Thymus and Tongue.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), VARIANT LYS-9.
      Tissue: Amygdala and Endometrium.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 553-994 (ISOFORM 1), VARIANT LYS-9.
      Tissue: Brain, Colon and Placenta.
    6. "Arkadia amplifies TGF-beta superfamily signaling through degradation of Smad7."
      Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A., Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.
      EMBO J. 22:6458-6470(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    7. "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
      Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
      EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXIN1 AND AXIN2, IDENTIFICATION IN COMPLEX WITH AXIN1 AND SMAD7, SUBCELLULAR LOCATION, FUNCTION.
    8. "Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation."
      Levy L., Howell M., Das D., Harkin S., Episkopou V., Hill C.S.
      Mol. Cell. Biol. 27:6068-6083(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKIL, FUNCTION.
    9. "PolySUMO-binding proteins identified through a string search."
      Sun H., Hunter T.
      J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SUMO1 AND SUMO2, MUTAGENESIS OF VAL-382; VAL-383; ASP-384; LEU-385 AND THR-386.
    10. "NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase."
      Chasapis C.T., Kandias N.G., Episkopou V., Bentrop D., Spyroulias G.A.
      Proteins 80:1484-1489(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 927-994, FUNCTION.

    Entry informationi

    Entry nameiRN111_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZNA4
    Secondary accession number(s): C9JUS4
    , H0YN55, Q6P9A4, Q6ZMU2, Q7L428, Q7Z346, Q8N1P9, Q8WUA3, Q9NSR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 107 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 15
      Human chromosome 15: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3