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Q99942

- RNF5_HUMAN

UniProt

Q99942 - RNF5_HUMAN

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Protein
E3 ubiquitin-protein ligase RNF5
Gene
RNF5, G16, NG2, RMA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has E2-dependent E3 ubiquitin-protein ligase activity. May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4. Mediates ubiquitination of PXN/paxillin and Salmonella type III secreted protein sopA. May be involved in regulation of cell motility and localization of PXN/paxillin. Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N. Mediates the 'Lys-48'-linked polyubiquitination of TMEM173 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurrs in mitochondria after viral transfection and regulates antiviral responses.5 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri27 – 6842RING-type
Add
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: UniProtKB
  4. zinc ion binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. ER-associated misfolded protein catabolic process Source: UniProtKB
  2. cellular protein catabolic process Source: UniProtKB
  3. protein K48-linked ubiquitination Source: UniProtKB
  4. protein K63-linked ubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF5 (EC:6.3.2.-)
Alternative name(s):
Protein G16
RING finger protein 5
Ram1 homolog
Short name:
HsRma1
Gene namesi
Name:RNF5
Synonyms:G16, NG2, RMA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:10068. RNF5.

Subcellular locationi

Membrane; Multi-pass membrane protein. Mitochondrion membrane. Endoplasmic reticulum membrane
Note: Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei118 – 13821Helical; Reviewed prediction
Add
BLAST
Transmembranei160 – 18021Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421C → S: Loss of E3 ubiquitin-protein ligase activity. 1 Publication

Organism-specific databases

PharmGKBiPA34442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 180179E3 ubiquitin-protein ligase RNF5
PRO_0000240393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99942.
PaxDbiQ99942.
PRIDEiQ99942.

PTM databases

PhosphoSiteiQ99942.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ99942.
CleanExiHS_RNF5.
GenevestigatoriQ99942.

Organism-specific databases

HPAiCAB034107.
HPA052125.

Interactioni

Subunit structurei

Interacts with PXN. Interacts with Salmonella typhimurium sopA. Interacts with JKAMP. Interacts with TMEM173; the interaction of endogenous proteins is dependent on viral infection.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CFTRP135693EBI-348482,EBI-349854
PXNP490236EBI-348482,EBI-702209
UBE2D2P628373EBI-348482,EBI-347677
UBE2D3P610773EBI-348482,EBI-348268

Protein-protein interaction databases

BioGridi111975. 33 interactions.
DIPiDIP-29268N.
IntActiQ99942. 22 interactions.
MINTiMINT-1032027.
STRINGi9606.ENSP00000364235.

Structurei

3D structure databases

ProteinModelPortaliQ99942.
SMRiQ99942. Positions 22-71.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG300581.
HOGENOMiHOG000238304.
HOVERGENiHBG054495.
InParanoidiQ99942.
KOiK10666.
OMAiFQSFGDT.
PhylomeDBiQ99942.
TreeFamiTF317334.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99942-1 [UniParc]FASTAAdd to Basket

« Hide

MAAAEEEDGG PEGPNRERGG AGATFECNIC LETAREAVVS VCGHLYCWPC    50
LHQWLETRPE RQECPVCKAG ISREKVVPLY GRGSQKPQDP RLKTPPRPQG 100
QRPAPESRGG FQPFGDTGGF HFSFGVGAFP FGFFTTVFNA HEPFRRGTGV 150
DLGQGHPASS WQDSLFLFLA IFFFFWLLSI 180
Length:180
Mass (Da):19,881
Last modified:May 1, 1997 - v1
Checksum:iE5AFA4DE6DE85942
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221G → S in CAB51286. 1 Publication
Sequence conflicti60 – 601E → D in CAB51286. 1 Publication
Sequence conflicti117 – 1171T → A in CAB51286. 1 Publication
Sequence conflicti148 – 1481T → A in CAB51286. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB056869 mRNA. Translation: BAB39359.1.
AJ243936 mRNA. Translation: CAB51286.1.
AK311859 mRNA. Translation: BAG34800.1.
BT007105 mRNA. Translation: AAP35769.1.
U89336 Genomic DNA. Translation: AAB47492.1.
AL845464 Genomic DNA. Translation: CAI41808.1.
AL662884 Genomic DNA. Translation: CAI18351.1.
AL662830 Genomic DNA. Translation: CAI17532.1.
BX284686 Genomic DNA. Translation: CAM26222.1.
BX927239 Genomic DNA. Translation: CAQ06594.1.
CR812478 Genomic DNA. Translation: CAQ10698.1.
CR933878 Genomic DNA. Translation: CAQ09623.1.
BC004155 mRNA. Translation: AAH04155.1.
BC111392 mRNA. Translation: AAI11393.1.
BC119741 mRNA. Translation: AAI19742.1.
BC119742 mRNA. Translation: AAI19743.1.
BC127651 mRNA. Translation: AAI27652.1.
BC127652 mRNA. Translation: AAI27653.1.
BC148255 mRNA. Translation: AAI48256.1.
CCDSiCCDS4745.1.
RefSeqiNP_008844.1. NM_006913.3.
UniGeneiHs.731774.

Genome annotation databases

EnsembliENST00000375094; ENSP00000364235; ENSG00000204308.
ENST00000413786; ENSP00000387879; ENSG00000225452.
ENST00000432616; ENSP00000413131; ENSG00000183574.
ENST00000445885; ENSP00000401172; ENSG00000227277.
ENST00000449794; ENSP00000415784; ENSG00000223767.
ENST00000453473; ENSP00000415127; ENSG00000228907.
ENST00000456167; ENSP00000388795; ENSG00000228405.
GeneIDi6048.
KEGGihsa:6048.
UCSCiuc003oaj.4. human.

Polymorphism databases

DMDMi74762702.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB056869 mRNA. Translation: BAB39359.1 .
AJ243936 mRNA. Translation: CAB51286.1 .
AK311859 mRNA. Translation: BAG34800.1 .
BT007105 mRNA. Translation: AAP35769.1 .
U89336 Genomic DNA. Translation: AAB47492.1 .
AL845464 Genomic DNA. Translation: CAI41808.1 .
AL662884 Genomic DNA. Translation: CAI18351.1 .
AL662830 Genomic DNA. Translation: CAI17532.1 .
BX284686 Genomic DNA. Translation: CAM26222.1 .
BX927239 Genomic DNA. Translation: CAQ06594.1 .
CR812478 Genomic DNA. Translation: CAQ10698.1 .
CR933878 Genomic DNA. Translation: CAQ09623.1 .
BC004155 mRNA. Translation: AAH04155.1 .
BC111392 mRNA. Translation: AAI11393.1 .
BC119741 mRNA. Translation: AAI19742.1 .
BC119742 mRNA. Translation: AAI19743.1 .
BC127651 mRNA. Translation: AAI27652.1 .
BC127652 mRNA. Translation: AAI27653.1 .
BC148255 mRNA. Translation: AAI48256.1 .
CCDSi CCDS4745.1.
RefSeqi NP_008844.1. NM_006913.3.
UniGenei Hs.731774.

3D structure databases

ProteinModelPortali Q99942.
SMRi Q99942. Positions 22-71.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111975. 33 interactions.
DIPi DIP-29268N.
IntActi Q99942. 22 interactions.
MINTi MINT-1032027.
STRINGi 9606.ENSP00000364235.

PTM databases

PhosphoSitei Q99942.

Polymorphism databases

DMDMi 74762702.

Proteomic databases

MaxQBi Q99942.
PaxDbi Q99942.
PRIDEi Q99942.

Protocols and materials databases

DNASUi 6048.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375094 ; ENSP00000364235 ; ENSG00000204308 .
ENST00000413786 ; ENSP00000387879 ; ENSG00000225452 .
ENST00000432616 ; ENSP00000413131 ; ENSG00000183574 .
ENST00000445885 ; ENSP00000401172 ; ENSG00000227277 .
ENST00000449794 ; ENSP00000415784 ; ENSG00000223767 .
ENST00000453473 ; ENSP00000415127 ; ENSG00000228907 .
ENST00000456167 ; ENSP00000388795 ; ENSG00000228405 .
GeneIDi 6048.
KEGGi hsa:6048.
UCSCi uc003oaj.4. human.

Organism-specific databases

CTDi 6048.
GeneCardsi GC06P032146.
GC06Pi32157.
GC06Pj32094.
GC06Pl32185.
GC06Pm32222.
GC06Pn32103.
GC06Po32153.
H-InvDB HIX0034363.
HGNCi HGNC:10068. RNF5.
HPAi CAB034107.
HPA052125.
MIMi 602677. gene.
neXtProti NX_Q99942.
PharmGKBi PA34442.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300581.
HOGENOMi HOG000238304.
HOVERGENi HBG054495.
InParanoidi Q99942.
KOi K10666.
OMAi FQSFGDT.
PhylomeDBi Q99942.
TreeFami TF317334.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GeneWikii RNF5.
GenomeRNAii 6048.
NextBioi 23565.
PROi Q99942.
SOURCEi Search...

Gene expression databases

Bgeei Q99942.
CleanExi HS_RNF5.
Genevestigatori Q99942.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and mapping of a novel RING-finger gene (RNF5), a human homologue of a putative zinc-finger gene from Caenorhabditis elegans."
    Kyushiki H., Kuga Y., Suzuki M., Takahashi E., Horie M.
    Cytogenet. Cell Genet. 79:114-117(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase."
    Matsuda N., Suzuki T., Tanaka K., Nakano A.
    J. Cell Sci. 114:1949-1957(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-42.
  3. "Characterisation of a novel gene, G16, in the class III region of the human major histocompatibility complex."
    Khanna A., Campbell R.D.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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].
    Tissue: Brain.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: Lung.
  9. "RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization."
    Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.
    Mol. Cell. Biol. 23:5331-5345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PXN.
  10. "Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1."
    Zhang Y., Higashide W., Dai S., Sherman D.M., Zhou D.
    J. Biol. Chem. 280:38682-38688(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA."
    Zhong B., Zhang L., Lei C., Li Y., Mao A.P., Yang Y., Wang Y.Y., Zhang X.L., Shu H.B.
    Immunity 30:397-407(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF TMEM173, INTERACTION WITH TMEM173, SUBCELLULAR LOCATION.
  13. "Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP)."
    Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.
    J. Biol. Chem. 284:12099-12109(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF JKAMP, INTERACTION WITH JKAMP.
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRNF5_HUMAN
AccessioniPrimary (citable) accession number: Q99942
Secondary accession number(s): A2BFI6
, B2R4K3, Q0VDB7, Q9UMQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi