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Protein

E3 ubiquitin-protein ligase Arkadia

Gene

RNF111

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.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. SUMO polymer binding Source: UniProtKB
  3. ubiquitin protein ligase activity Source: BHF-UCL
  4. 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. protein ubiquitination Source: BHF-UCL
  9. transcription, DNA-templated Source: Reactome
  10. transcription initiation from RNA polymerase II promoter Source: Reactome
  11. transforming growth factor beta receptor signaling pathway Source: Reactome
  12. 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

BRENDAi6.3.2.19. 2681.
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 Componenti: 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: HPA
  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 ArkadiaPRO_0000280690Add
BLAST

Proteomic databases

MaxQBiQ6ZNA4.
PaxDbiQ6ZNA4.
PRIDEiQ6ZNA4.

PTM databases

PhosphoSiteiQ6ZNA4.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Gene expression databases

BgeeiQ6ZNA4.
CleanExiHS_RNF111.
ExpressionAtlasiQ6ZNA4. baseline and differential.
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
UBE2V1Q134042EBI-2129175,EBI-1050671

Protein-protein interaction databases

BioGridi120146. 52 interactions.
IntActiQ6ZNA4. 35 interactions.
MINTiMINT-1187466.
STRINGi9606.ENSP00000288199.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00730000110863.
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. AlignAdd to basket

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

        10         20         30         40         50
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP
60 70 80 90 100
AGVEMINSKV GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA
110 120 130 140 150
GPSYVQNCVK ENQGILGLRQ HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS
160 170 180 190 200
DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR SHKWPRTETE SVSGLLMKRP
210 220 230 240 250
CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE VLARRKYALL
260 270 280 290 300
PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV
310 320 330 340 350
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ
360 370 380 390 400
GSSSHASRPQ EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA
410 420 430 440 450
RMESQATSAS INNSNPSTSE QASDTASAVT SSQPSTVSET SATLTSNSTT
460 470 480 490 500
GTSIGDDSRR TTSSAVTETG PPAMPRLPSC CPQHSPCGGS SQNHHALGHP
510 520 530 540 550
HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE RPPQVQAPCG
560 570 580 590 600
ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA
610 620 630 640 650
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY
660 670 680 690 700
ASLTRPLHHQ ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA
710 720 730 740 750
TSHPVAPPPP THLASTAAPI PQHLPPTHQP ISHHIPATAP PAQRLHPHEV
760 770 780 790 800
MQRMEVQRRR MMQHPTRAHE RPPPHPHRMH PNYGHGHHIH VPQTMSSHPR
810 820 830 840 850
QAPERSAWEL GIEAGVTAAT YTPGALHPHL AHYHAPPRLH HLQLGALPLM
860 870 880 890 900
VPDMAGYPHI RYISSGLDGT SFRGPFRGNF EELIHLEERL GNVNRGASQG
910 920 930 940 950
TIERCTYPHK YKKVTTDWFS QRKLHCKQDG EEGTEEDTEE KCTICLSILE
960 970 980 990
EGEDVRRLPC MHLFHQVCVD QWLITNKKCP ICRVDIEAQL PSES
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.Curated
The sequence BAC04531.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD18633.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi120146. 52 interactions.
IntActiQ6ZNA4. 35 interactions.
MINTiMINT-1187466.
STRINGi9606.ENSP00000288199.

PTM databases

PhosphoSiteiQ6ZNA4.

Polymorphism databases

DMDMi308153555.

Proteomic databases

MaxQBiQ6ZNA4.
PaxDbiQ6ZNA4.
PRIDEiQ6ZNA4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi54778.
GeneCardsiGC15P059160.
HGNCiHGNC:17384. RNF111.
HPAiHPA038576.
HPA038577.
MIMi605840. gene.
neXtProtiNX_Q6ZNA4.
PharmGKBiPA134868772.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG291583.
GeneTreeiENSGT00730000110863.
HOVERGENiHBG093884.
InParanoidiQ6ZNA4.
KOiK10635.
OMAiPCRKRFV.
OrthoDBiEOG7WHH9N.
PhylomeDBiQ6ZNA4.
TreeFamiTF331862.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
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.

Miscellaneous databases

ChiTaRSiRNF111. human.
GeneWikiiRNF111.
GenomeRNAii54778.
NextBioi57437.
PROiQ6ZNA4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZNA4.
CleanExiHS_RNF111.
ExpressionAtlasiQ6ZNA4. baseline and differential.
GenevestigatoriQ6ZNA4.

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]
ProtoNetiSearch...

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(2003) [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(2005) [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(2003) [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(2002) [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(2005) [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(2006) [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(2011) [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(2011) [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: April 1, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.