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Q6ZNA4

- RN111_HUMAN

UniProt

Q6ZNA4 - RN111_HUMAN

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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

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.3 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri942 – 98342RING-type; atypical
Add
BLAST

GO - Molecular functioni

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

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 from RNA polymerase II promoter Source: Reactome
  5. positive regulation of transcription, DNA-templated Source: BHF-UCL
  6. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  7. protein polyubiquitination Source: Ensembl
  8. transcription initiation from RNA polymerase II promoter Source: Reactome
  9. transcription, DNA-templated Source: Reactome
  10. transforming growth factor beta receptor signaling pathway Source: Reactome
  11. ubiquitin-dependent SMAD protein catabolic process Source: Ensembl
Complete GO annotation...

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

GO - Cellular componenti

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

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 Arkadia
PRO_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

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni241 – 404164Interaction with AXIN1
Add
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-rich
Add
BLAST
Compositional biasi494 – 52330His-rich
Add
BLAST
Compositional biasi629 – 781153Pro-rich
Add
BLAST

Sequence similaritiesi

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.

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.
VSP_023840
Alternative sequencei914 – 9218Missing in isoform 2 and isoform 4.
VSP_023841

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651H → R in BX647259. 1 Publication
Sequence conflicti473 – 4731A → E in CAD98031. 1 Publication
Sequence conflicti562 – 5621Missing in AAH60862. 1 Publication
Sequence conflicti562 – 5621Missing in AAH20984. 1 Publication
Sequence conflicti625 – 6251M → T in BX647259. 1 Publication
Sequence conflicti738 – 7381T → I in BX647259. 1 Publication
Sequence conflicti809 – 8091E → G in CAD98031. 1 Publication
Sequence conflicti931 – 9311E → G in CAD98031. 1 Publication
Sequence conflicti938 – 9381T → A in BX647259. 1 Publication
Sequence conflicti974 – 9741I → V in BAD18471. 1 Publication

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]
ENST00000434298; ENSP00000393641; ENSG00000157450. [Q6ZNA4-3]
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...

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 ]
ENST00000434298 ; ENSP00000393641 ; ENSG00000157450 . [Q6ZNA4-3 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 106 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

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