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Protein

E3 ubiquitin-protein ligase RNF149

Gene

RNF149

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri269 – 31042RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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 RNF149 (EC:6.3.2.-)
Alternative name(s):
DNA polymerase-transactivated protein 2
RING finger protein 149
Gene namesi
Name:RNF149
Synonyms:DNAPTP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:23137. RNF149.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei201 – 22121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134895641.

Polymorphism and mutation databases

BioMutaiRNF149.
DMDMi160332298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 400368E3 ubiquitin-protein ligase RNF149PRO_0000261611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Modified residuei345 – 3451PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8NC42.
PaxDbiQ8NC42.
PRIDEiQ8NC42.

PTM databases

iPTMnetiQ8NC42.
PhosphoSiteiQ8NC42.

Expressioni

Gene expression databases

BgeeiQ8NC42.
CleanExiHS_RNF149.
ExpressionAtlasiQ8NC42. baseline and differential.
GenevisibleiQ8NC42. HS.

Organism-specific databases

HPAiHPA011424.

Interactioni

Protein-protein interaction databases

BioGridi129991. 25 interactions.
IntActiQ8NC42. 4 interactions.
MINTiMINT-6489471.
STRINGi9606.ENSP00000295317.

Structurei

3D structure databases

ProteinModelPortaliQ8NC42.
SMRiQ8NC42. Positions 29-191, 267-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 175109PAAdd
BLAST

Domaini

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri269 – 31042RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
HOVERGENiHBG057659.
InParanoidiQ8NC42.
KOiK15704.
OMAiCAPDTRF.
OrthoDBiEOG7W41BX.
PhylomeDBiQ8NC42.
TreeFamiTF317486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8NC42-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWRRREASV GARGVLALAL LALALCVPGA RGRALEWFSA VVNIEYVDPQ
60 70 80 90 100
TNLTVWSVSE SGRFGDSSPK EGAHGLVGVP WAPGGDLEGC APDTRFFVPE
110 120 130 140 150
PGGRGAAPWV ALVARGGCTF KDKVLVAARR NASAVVLYNE ERYGNITLPM
160 170 180 190 200
SHAGTGNIVV IMISYPKGRE ILELVQKGIP VTMTIGVGTR HVQEFISGQS
210 220 230 240 250
VVFVAIAFIT MMIISLAWLI FYYIQRFLYT GSQIGSQSHR KETKKVIGQL
260 270 280 290 300
LLHTVKHGEK GIDVDAENCA VCIENFKVKD IIRILPCKHI FHRICIDPWL
310 320 330 340 350
LDHRTCPMCK LDVIKALGYW GEPGDVQEMP APESPPGRDP AANLSLALPD
360 370 380 390 400
DDGSDDSSPP SASPAESEPQ CDPSFKGDAG ENTALLEAGR SDSRHGGPIS
Length:400
Mass (Da):43,165
Last modified:November 13, 2007 - v2
Checksum:iDC03309E0E17DCDE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035958
Natural varianti9 – 91S → G.2 Publications
Corresponds to variant rs11123868 [ dbSNP | Ensembl ].
VAR_029455
Natural varianti344 – 3441L → F.1 Publication
Corresponds to variant rs17856945 [ dbSNP | Ensembl ].
VAR_029456
Natural varianti356 – 3561D → E.4 Publications
Corresponds to variant rs13151 [ dbSNP | Ensembl ].
VAR_029457

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY450390 mRNA. Translation: AAR21083.1.
AK074985 mRNA. Translation: BAC11334.1.
AK075141 mRNA. Translation: BAC11430.1.
AM392566 mRNA. Translation: CAL37444.1.
AC013722 Genomic DNA. No translation available.
AC073643 Genomic DNA. Translation: AAY14775.1.
BC019355 mRNA. Translation: AAH19355.2.
BC032328 mRNA. Translation: AAH32328.2.
BC045743 mRNA. Translation: AAH45743.1.
CCDSiCCDS2051.1.
RefSeqiNP_775918.2. NM_173647.3.
UniGeneiHs.142074.

Genome annotation databases

EnsembliENST00000295317; ENSP00000295317; ENSG00000163162.
GeneIDi284996.
KEGGihsa:284996.
UCSCiuc002taz.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY450390 mRNA. Translation: AAR21083.1.
AK074985 mRNA. Translation: BAC11334.1.
AK075141 mRNA. Translation: BAC11430.1.
AM392566 mRNA. Translation: CAL37444.1.
AC013722 Genomic DNA. No translation available.
AC073643 Genomic DNA. Translation: AAY14775.1.
BC019355 mRNA. Translation: AAH19355.2.
BC032328 mRNA. Translation: AAH32328.2.
BC045743 mRNA. Translation: AAH45743.1.
CCDSiCCDS2051.1.
RefSeqiNP_775918.2. NM_173647.3.
UniGeneiHs.142074.

3D structure databases

ProteinModelPortaliQ8NC42.
SMRiQ8NC42. Positions 29-191, 267-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129991. 25 interactions.
IntActiQ8NC42. 4 interactions.
MINTiMINT-6489471.
STRINGi9606.ENSP00000295317.

PTM databases

iPTMnetiQ8NC42.
PhosphoSiteiQ8NC42.

Polymorphism and mutation databases

BioMutaiRNF149.
DMDMi160332298.

Proteomic databases

MaxQBiQ8NC42.
PaxDbiQ8NC42.
PRIDEiQ8NC42.

Protocols and materials databases

DNASUi284996.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295317; ENSP00000295317; ENSG00000163162.
GeneIDi284996.
KEGGihsa:284996.
UCSCiuc002taz.3. human.

Organism-specific databases

CTDi284996.
GeneCardsiRNF149.
H-InvDBHIX0023941.
HGNCiHGNC:23137. RNF149.
HPAiHPA011424.
neXtProtiNX_Q8NC42.
PharmGKBiPA134895641.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00760000119057.
HOGENOMiHOG000231432.
HOVERGENiHBG057659.
InParanoidiQ8NC42.
KOiK15704.
OMAiCAPDTRF.
OrthoDBiEOG7W41BX.
PhylomeDBiQ8NC42.
TreeFamiTF317486.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF149. human.
GenomeRNAii284996.
NextBioi95209.
PROiQ8NC42.

Gene expression databases

BgeeiQ8NC42.
CleanExiHS_RNF149.
ExpressionAtlasiQ8NC42. baseline and differential.
GenevisibleiQ8NC42. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003137. PA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02225. PA. 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. "Screening and cloning of the target genes transactivated by hepatitis B virus DNA polymerase using suppression subtractive hybridization (SSH) technique."
    Wang C., Cheng J., Lang Z., Ji D., Yang Y., Zhang L., Wu Y.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-356.
  2. "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], VARIANTS GLY-9 AND GLU-356.
    Tissue: Placenta and Teratocarcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-356.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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], VARIANTS GLY-9; PHE-344 AND GLU-356.
    Tissue: Brain, Cervix and Placenta.
  6. "Ring finger protein 149 is an E3 ubiquitin ligase active on wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF)."
    Hong S.W., Jin D.H., Shin J.S., Moon J.H., Na Y.S., Jung K.A., Kim S.M., Kim J.C., Kim K.P., Hong Y.S., Lee J.L., Choi E.K., Lee J.S., Kim T.W.
    J. Biol. Chem. 287:24017-24025(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-7.

Entry informationi

Entry nameiRN149_HUMAN
AccessioniPrimary (citable) accession number: Q8NC42
Secondary accession number(s): Q53S14
, Q8N5I8, Q8NBY5, Q8WUU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 13, 2007
Last modified: March 16, 2016
This is version 115 of the entry and version 2 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 2
    Human chromosome 2: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.