Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5TC82

- RC3H1_HUMAN

UniProt

Q5TC82 - RC3H1_HUMAN

Protein

Roquin-1

Gene

RC3H1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF and in many more mRNAs By similarity. Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs By similarity. In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity By similarity. In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression By similarity. Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri14 – 5441RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri413 – 44129C3H1-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. mRNA 3'-UTR binding Source: BHF-UCL
    2. poly(A) RNA binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: BHF-UCL
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cytoplasmic mRNA processing body assembly Source: BHF-UCL
    2. negative regulation of activated T cell proliferation Source: BHF-UCL
    3. negative regulation of B cell proliferation Source: BHF-UCL
    4. negative regulation of germinal center formation Source: BHF-UCL
    5. negative regulation of T-helper cell differentiation Source: BHF-UCL
    6. nuclear-transcribed mRNA catabolic process Source: BHF-UCL
    7. posttranscriptional regulation of gene expression Source: BHF-UCL
    8. protein ubiquitination Source: GOC
    9. regulation of germinal center formation Source: BHF-UCL
    10. regulation of mRNA stability Source: BHF-UCL
    11. regulation of T cell receptor signaling pathway Source: BHF-UCL

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Roquin-1
    Short name:
    Roquin
    Alternative name(s):
    RING finger and C3H zinc finger protein 1
    RING finger and CCCH-type zinc finger domain-containing protein 1
    RING finger protein 198
    Gene namesi
    Name:RC3H1
    Synonyms:KIAA2025, RNF198
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29434. RC3H1.

    Subcellular locationi

    CytoplasmP-body By similarity
    Note: During stress, such as that induced by arsenite, localizes to cytosolic stress granules.By similarity

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: BHF-UCL
    2. cytoplasmic stress granule Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671090.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11331133Roquin-1PRO_0000055965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei535 – 5351Phosphoserine1 Publication
    Modified residuei1110 – 11101PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5TC82.
    PaxDbiQ5TC82.
    PRIDEiQ5TC82.

    PTM databases

    PhosphoSiteiQ5TC82.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at higher level in cerebellum, spleen, ovary and liver.1 Publication

    Gene expression databases

    ArrayExpressiQ5TC82.
    BgeeiQ5TC82.
    CleanExiHS_RC3H1.
    GenevestigatoriQ5TC82.

    Organism-specific databases

    HPAiHPA027428.
    HPA027434.
    HPA027448.

    Interactioni

    Subunit structurei

    Interacts with DDX6 and EDC4. Interacts with CCR4-NOT deadenylase complex.By similarity

    Protein-protein interaction databases

    BioGridi127186. 7 interactions.
    IntActiQ5TC82. 3 interactions.
    MINTiMINT-2809509.
    STRINGi9606.ENSP00000258349.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5TC82.
    SMRiQ5TC82. Positions 12-59.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni181 – 23252ROQAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi533 – 788256Pro-richAdd
    BLAST

    Domaini

    The RING-type zinc finger is required for proper localization to stress granules, but not to P-bodies.By similarity
    The ROQ region is required for CDE RNA-binding. It may also be involved in localization to stress granules.By similarity

    Sequence similaritiesi

    Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri14 – 5441RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri413 – 44129C3H1-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG320727.
    HOVERGENiHBG080524.
    InParanoidiQ5TC82.
    KOiK15690.
    OMAiICTQTFD.
    OrthoDBiEOG7QNVKM.
    PhylomeDBiQ5TC82.
    TreeFamiTF317698.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.1000.10. 1 hit.
    InterProiIPR000571. Znf_CCCH.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00642. zf-CCCH. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS50103. ZF_C3H1. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5TC82-1) [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

    MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC     50
    PFDQTTINTD IELLPVNSAL LQLVGAQVPE QQPITLCSGV EDTKHYEEAK 100
    KCVEELALYL KPLSSARGVG LNSTTQSVLS RPMQRKLVTL VHCQLVEEEG 150
    RIRAMRAARS LGERTVTELI LQHQNPQQLS SNLWAAVRAR GCQFLGPAMQ 200
    EEALKLVLLA LEDGSALSRK VLVLFVVQRL EPRFPQASKT SIGHVVQLLY 250
    RASCFKVTKR DEDSSLMQLK EEFRTYEALR REHDSQIVQI AMEAGLRIAP 300
    DQWSSLLYGD QSHKSHMQSI IDKLQTPASF AQSVQELTIA LQRTGDPANL 350
    NRLRPHLELL ANIDPSPDAP PPTWEQLENG LVAVRTVVHG LVDYIQNHSK 400
    KGADQQQPPQ HSKYKTYMCR DMKQRGGCPR GASCTFAHSQ EELEKFRKMN 450
    KRLVPRRPLS ASLGQLNEVG LPSAAILPDE GAVDLPSRKP PALPNGIVST 500
    GNTVTQLIPR GTDPSYDSSL KPGKIDHLSS SAPGSPPDLL ESVPKSISAL 550
    PVNPHSIPPR GPADLPPMPV TKPLQMVPRG SQLYPAQQTD VYYQDPRGAA 600
    PPFEPAPYQQ GMYYTPPPQC VSRFVRPPPS APEPAPPYLD HYPPYLQERV 650
    VNSQYGTQPQ QYPPIYPSHY DGRRVYPAPS YTREEIFRES PIPIEIPPAA 700
    VPSYVPESRE RYQQIESYYP VAPHPTQIRP SYLREPPYSR LPPPPQPHPS 750
    LDELHRRRKE IMAQLEERKV ISPPPFAPSP TLPPTFHPEE FLDEDLKVAG 800
    KYKGNDYSQY SPWSCDTIGS YIGTKDAKPK DVVAAGSVEM MNVESKGMRD 850
    QRLDLQRRAA ETSDDDLIPF GDRPTVSRFG AISRTSKTIY QGAGPMQAMA 900
    PQGAPTKSIN ISDYSPYGTH GGWGASPYSP HQNIPSQGHF SERERISMSE 950
    VASHGKPLPS AEREQLRLEL QQLNHQISQQ TQLRGLEAVS NRLVLQREAN 1000
    TLAGQSQPPP PPPPKWPGMI SSEQLSLELH QVEREIGKRT RELSMENQCS 1050
    LDMKSKLNTS KQAENGQPEP QNKVPAEDLT LTFSDVPNGS ALTQENISLL 1100
    SNKTSSLNLS EDPEGGGDNN DSQRSGVTPS SAP 1133
    Length:1,133
    Mass (Da):125,736
    Last modified:December 21, 2004 - v1
    Checksum:iE307838DF80A7099
    GO
    Isoform 2 (identifier: Q5TC82-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         988-996: Missing.
         1084-1084: S → SS

    Note: No experimental confirmation available.

    Show »
    Length:1,125
    Mass (Da):124,842
    Checksum:iEFBE5179071DFA94
    GO

    Sequence cautioni

    The sequence BAC04186.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAH70709.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAH70710.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI19417.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI19419.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti986 – 9861L → P in BAC04186. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei988 – 9969Missing in isoform 2. 1 PublicationVSP_015015
    Alternative sequencei1084 – 10841S → SS in isoform 2. 1 PublicationVSP_015016

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK093501 mRNA. Translation: BAC04186.1. Different initiation.
    AK122948 mRNA. Translation: BAG53813.1.
    AL121983, AL136170 Genomic DNA. Translation: CAH70709.1. Different initiation.
    AL121983, AL136170 Genomic DNA. Translation: CAH70710.1. Different initiation.
    AL136170, AL121983 Genomic DNA. Translation: CAI19417.1. Different initiation.
    AL136170, AL121983 Genomic DNA. Translation: CAI19419.1. Different initiation.
    AB095945 mRNA. Translation: BAC23121.1.
    CCDSiCCDS30940.1. [Q5TC82-1]
    RefSeqiNP_742068.1. NM_172071.2. [Q5TC82-1]
    XP_005244976.1. XM_005244919.1. [Q5TC82-2]
    UniGeneiHs.30258.

    Genome annotation databases

    EnsembliENST00000258349; ENSP00000258349; ENSG00000135870. [Q5TC82-1]
    ENST00000367694; ENSP00000356667; ENSG00000135870. [Q5TC82-2]
    ENST00000367696; ENSP00000356669; ENSG00000135870. [Q5TC82-1]
    GeneIDi149041.
    KEGGihsa:149041.
    UCSCiuc001gju.4. human. [Q5TC82-1]
    uc001gjv.3. human. [Q5TC82-2]

    Polymorphism databases

    DMDMi73621450.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK093501 mRNA. Translation: BAC04186.1 . Different initiation.
    AK122948 mRNA. Translation: BAG53813.1 .
    AL121983 , AL136170 Genomic DNA. Translation: CAH70709.1 . Different initiation.
    AL121983 , AL136170 Genomic DNA. Translation: CAH70710.1 . Different initiation.
    AL136170 , AL121983 Genomic DNA. Translation: CAI19417.1 . Different initiation.
    AL136170 , AL121983 Genomic DNA. Translation: CAI19419.1 . Different initiation.
    AB095945 mRNA. Translation: BAC23121.1 .
    CCDSi CCDS30940.1. [Q5TC82-1 ]
    RefSeqi NP_742068.1. NM_172071.2. [Q5TC82-1 ]
    XP_005244976.1. XM_005244919.1. [Q5TC82-2 ]
    UniGenei Hs.30258.

    3D structure databases

    ProteinModelPortali Q5TC82.
    SMRi Q5TC82. Positions 12-59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127186. 7 interactions.
    IntActi Q5TC82. 3 interactions.
    MINTi MINT-2809509.
    STRINGi 9606.ENSP00000258349.

    PTM databases

    PhosphoSitei Q5TC82.

    Polymorphism databases

    DMDMi 73621450.

    Proteomic databases

    MaxQBi Q5TC82.
    PaxDbi Q5TC82.
    PRIDEi Q5TC82.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258349 ; ENSP00000258349 ; ENSG00000135870 . [Q5TC82-1 ]
    ENST00000367694 ; ENSP00000356667 ; ENSG00000135870 . [Q5TC82-2 ]
    ENST00000367696 ; ENSP00000356669 ; ENSG00000135870 . [Q5TC82-1 ]
    GeneIDi 149041.
    KEGGi hsa:149041.
    UCSCi uc001gju.4. human. [Q5TC82-1 ]
    uc001gjv.3. human. [Q5TC82-2 ]

    Organism-specific databases

    CTDi 149041.
    GeneCardsi GC01M173900.
    HGNCi HGNC:29434. RC3H1.
    HPAi HPA027428.
    HPA027434.
    HPA027448.
    MIMi 609424. gene.
    neXtProti NX_Q5TC82.
    PharmGKBi PA142671090.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320727.
    HOVERGENi HBG080524.
    InParanoidi Q5TC82.
    KOi K15690.
    OMAi ICTQTFD.
    OrthoDBi EOG7QNVKM.
    PhylomeDBi Q5TC82.
    TreeFami TF317698.

    Miscellaneous databases

    GenomeRNAii 149041.
    NextBioi 86056.
    PROi Q5TC82.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5TC82.
    Bgeei Q5TC82.
    CleanExi HS_RC3H1.
    Genevestigatori Q5TC82.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.1000.10. 1 hit.
    InterProi IPR000571. Znf_CCCH.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00642. zf-CCCH. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS50103. ZF_C3H1. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-1133 (ISOFORM 1).
      Tissue: Testis.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The nucleotide sequence of a long cDNA clone isolated from human."
      Nagase T., Kikuno R., Ohara O.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-1133 (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Molecular control of Tfh-cell differentiation by Roquin family proteins."
      Heissmeyer V., Vogel K.U.
      Immunol. Rev. 253:273-289(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, MISCELLANEOUS.

    Entry informationi

    Entry nameiRC3H1_HUMAN
    AccessioniPrimary (citable) accession number: Q5TC82
    Secondary accession number(s): B3KVK1
    , Q5W180, Q5W181, Q8IVE6, Q8N9V1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 94 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

    Miscellaneous

    The RING finger is highly conserved among the paralogs and among species, suggesting it may possess E3 ubiquitin ligase activity. A C. elegans homolog, rle-1, is involved in daf-16 ubiquitin-dependent degradation. Although such an activity has not be observed in mammalian cells so far, it is conceivable that RC3H1 may utilize E3 ubiquitin ligase activity in the promotion of mRNA decay (PubMed:23550652).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3