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)

Q9HBD1

- RC3H2_HUMAN

UniProt

Q9HBD1 - RC3H2_HUMAN

Protein

Roquin-2

Gene

RC3H2

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 95 (01 Oct 2014)
      Sequence version 2 (16 Aug 2005)
      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 fingeri410 – 43829C3H1-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: FlyBase
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein polyubiquitination Source: FlyBase

    Keywords - Molecular functioni

    Repressor

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Roquin-2
    Alternative name(s):
    Membrane-associated nucleic acid-binding protein
    RING finger and CCCH-type zinc finger domain-containing protein 2
    RING finger protein 164
    Gene namesi
    Name:RC3H2
    Synonyms:MNAB, RNF164
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:21461. RC3H2.

    Subcellular locationi

    CytoplasmP-body By similarity
    Note: During stress, such as that induced by arsenite, localizes to cytosolic stress granules. Localization to stress granules, but not to P-bodies, depends upon the RING-type zinc finger.1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162400905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11911191Roquin-2PRO_0000055968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei549 – 5491Phosphoserine1 Publication
    Modified residuei808 – 8081Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HBD1.
    PaxDbiQ9HBD1.
    PRIDEiQ9HBD1.

    PTM databases

    PhosphoSiteiQ9HBD1.

    Expressioni

    Tissue specificityi

    Expressed in spleen, testis, ovary and small intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ9HBD1.
    BgeeiQ9HBD1.
    CleanExiHS_RC3H2.
    GenevestigatoriQ9HBD1.

    Organism-specific databases

    HPAiHPA042863.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi120029. 5 interactions.
    IntActiQ9HBD1. 6 interactions.
    MINTiMINT-3052676.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HBD1.
    SMRiQ9HBD1. Positions 12-59.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni178 – 22952ROQAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi576 – 704129Pro-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 fingeri410 – 43829C3H1-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG320727.
    HOVERGENiHBG080524.
    InParanoidiQ9HBD1.
    KOiK15690.
    OMAiCFSQPLP.
    OrthoDBiEOG7QNVKM.
    PhylomeDBiQ9HBD1.
    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.
    SM00356. ZnF_C3H1. 1 hit.
    [Graphical view]
    PROSITEiPS50103. ZF_C3H1. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HBD1-1) [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

    MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC     50
    PFDQTAINTD IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK 100
    CVEDLALYLK PLSGGKGVAS LNQSALSRPM QRKLVTLVNC QLVEEEGRVR 150
    AMRAARSLGE RTVTELILQH QNPQQLSANL WAAVRARGCQ FLGPAMQEEA 200
    LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG HVVQLLYRAS 250
    CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW 300
    SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL 350
    RPHLELLANI DPNPDAVSPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH 400
    ETPQPQPNSK YKTSMCRDLR QQGGCPRGTN CTFAHSQEEL EKYRLRNKKI 450
    NATVRTFPLL NKVGVNNTVT TTAGNVISVI GSTETTGKIV PSTNGISNAE 500
    NSVSQLISRS TDSTLRALET VKKVGKVGAN GQNAAGPSAD SVTENKIGSP 550
    PKTPVSNVAA TSAGPSNVGT ELNSVPQKSS PFLTRVPVYP PHSENIQYFQ 600
    DPRTQIPFEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA 650
    SMPYADHYST FSPRDRMNSS PYQPPPPQPY GPVPPVPSGM YAPVYDSRRI 700
    WRPPMYQRDD IIRSNSLPPM DVMHSSVYQT SLRERYNSLD GYYSVACQPP 750
    SEPRTTVPLP REPCGHLKTS CEEQIRRKPD QWAQYHTQKA PLVSSTLPVA 800
    TQSPTPPSPL FSVDFRADFS ESVSGTKFEE DHLSHYSPWS CGTIGSCINA 850
    IDSEPKDVIA NSNAVLMDLD SGDVKRRVHL FETQRRTKEE DPIIPFSDGP 900
    IISKWGAISR SSRTGYHTTD PVQATASQGS ATKPISVSDY VPYVNAVDSR 950
    WSSYGNEATS SAHYVERDRF IVTDLSGHRK HSSTGDLLSL ELQQAKSNSL 1000
    LLQREANALA MQQKWNSLDE GRHLTLNLLS KEIELRNGEL QSDYTEDATD 1050
    TKPDRDIELE LSALDTDEPD GQSEPIEEIL DIQLGISSQN DQLLNGMAVE 1100
    NGHPVQQHQK EPPKQKKQSL GEDHVILEEQ KTILPVTSCF SQPLPVSISN 1150
    ASCLPITTSV SAGNLILKTH VMSEDKNDFL KPVANGKMVN S 1191
    Length:1,191
    Mass (Da):131,669
    Last modified:August 16, 2005 - v2
    Checksum:i93633D8D83DC7409
    GO
    Isoform 2 (identifier: Q9HBD1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         454-478: VRTFPLLNKVGVNNTVTTTAGNVIS → EVLKQQGKLFQVQTEFQMQKTVFPS
         479-1191: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:478
    Mass (Da):53,877
    Checksum:iD6233E801430829F
    GO
    Isoform 3 (identifier: Q9HBD1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         443-506: YRLRNKKINA...SNAENSVSQL → CNPRGLYLHC...SPLEEPREED
         507-1191: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:506
    Mass (Da):56,853
    Checksum:iF2915DA0B8D0AC9E
    GO
    Isoform 4 (identifier: Q9HBD1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1040-1191: LQSDYTEDAT...PVANGKMVNS → VKKLNLSASCLMYLFSAAASWLYHY

    Show »
    Length:1,064
    Mass (Da):117,917
    Checksum:i090E3F438698A35B
    GO
    Isoform 5 (identifier: Q9HBD1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         195-218: AMQEEALKLVLLALEDGSALSRKV → GKIGYYLTFFISYWGLRMPISGAR
         219-1191: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:218
    Mass (Da):24,282
    Checksum:i91A1FAB4AAE5D91B
    GO
    Isoform 6 (identifier: Q9HBD1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-195: Missing.
         1040-1191: LQSDYTEDAT...PVANGKMVNS → VKKLNLSASCLMYLFSAAASWLYHY

    Note: No experimental confirmation available.

    Show »
    Length:869
    Mass (Da):96,362
    Checksum:i56BCB1D341B35899
    GO

    Sequence cautioni

    The sequence BAA91340.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB15634.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti650 – 6501A → G in BAA91073. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 195195Missing in isoform 6. 1 PublicationVSP_015017Add
    BLAST
    Alternative sequencei195 – 21824AMQEE…LSRKV → GKIGYYLTFFISYWGLRMPI SGAR in isoform 5. 1 PublicationVSP_015018Add
    BLAST
    Alternative sequencei219 – 1191973Missing in isoform 5. 1 PublicationVSP_015019Add
    BLAST
    Alternative sequencei443 – 50664YRLRN…SVSQL → CNPRGLYLHCCLLSSVASLG TVHNELYKQQHCDREKISVC AVKRAETCFSSQFFSPLEEP REED in isoform 3. 1 PublicationVSP_015020Add
    BLAST
    Alternative sequencei454 – 47825VRTFP…GNVIS → EVLKQQGKLFQVQTEFQMQK TVFPS in isoform 2. 1 PublicationVSP_015021Add
    BLAST
    Alternative sequencei479 – 1191713Missing in isoform 2. 1 PublicationVSP_015022Add
    BLAST
    Alternative sequencei507 – 1191685Missing in isoform 3. 1 PublicationVSP_015023Add
    BLAST
    Alternative sequencei1040 – 1191152LQSDY…KMVNS → VKKLNLSASCLMYLFSAAAS WLYHY in isoform 4 and isoform 6. 2 PublicationsVSP_015024Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF255303 mRNA. Translation: AAG00432.1.
    AF255304 mRNA. Translation: AAG00433.1.
    AK000308 mRNA. Translation: BAA91073.1.
    AK000720 mRNA. Translation: BAA91340.1. Different initiation.
    AK027042 mRNA. Translation: BAB15634.1. Different initiation.
    AL833177 mRNA. Translation: CAI46182.1.
    AL834431 mRNA. Translation: CAD39091.1.
    AL359512, AC007066 Genomic DNA. Translation: CAI94964.1.
    CH471090 Genomic DNA. Translation: EAW87547.1.
    BC011688 mRNA. Translation: AAH11688.2.
    BC044642 mRNA. Translation: AAH44642.1.
    CCDSiCCDS43874.1. [Q9HBD1-1]
    CCDS48014.1. [Q9HBD1-4]
    RefSeqiNP_001094058.1. NM_001100588.1. [Q9HBD1-1]
    NP_061323.2. NM_018835.2. [Q9HBD1-4]
    UniGeneiHs.533499.
    Hs.709775.

    Genome annotation databases

    EnsembliENST00000357244; ENSP00000349783; ENSG00000056586. [Q9HBD1-1]
    ENST00000373670; ENSP00000362774; ENSG00000056586. [Q9HBD1-1]
    ENST00000423239; ENSP00000411767; ENSG00000056586. [Q9HBD1-4]
    ENST00000471874; ENSP00000474148; ENSG00000056586. [Q9HBD1-5]
    ENST00000498479; ENSP00000474709; ENSG00000056586. [Q9HBD1-2]
    GeneIDi54542.
    KEGGihsa:54542.
    UCSCiuc004bnd.1. human. [Q9HBD1-1]
    uc004bne.4. human. [Q9HBD1-4]
    uc004bng.1. human. [Q9HBD1-5]
    uc011lzg.2. human. [Q9HBD1-2]

    Polymorphism databases

    DMDMi73621223.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF255303 mRNA. Translation: AAG00432.1 .
    AF255304 mRNA. Translation: AAG00433.1 .
    AK000308 mRNA. Translation: BAA91073.1 .
    AK000720 mRNA. Translation: BAA91340.1 . Different initiation.
    AK027042 mRNA. Translation: BAB15634.1 . Different initiation.
    AL833177 mRNA. Translation: CAI46182.1 .
    AL834431 mRNA. Translation: CAD39091.1 .
    AL359512 , AC007066 Genomic DNA. Translation: CAI94964.1 .
    CH471090 Genomic DNA. Translation: EAW87547.1 .
    BC011688 mRNA. Translation: AAH11688.2 .
    BC044642 mRNA. Translation: AAH44642.1 .
    CCDSi CCDS43874.1. [Q9HBD1-1 ]
    CCDS48014.1. [Q9HBD1-4 ]
    RefSeqi NP_001094058.1. NM_001100588.1. [Q9HBD1-1 ]
    NP_061323.2. NM_018835.2. [Q9HBD1-4 ]
    UniGenei Hs.533499.
    Hs.709775.

    3D structure databases

    ProteinModelPortali Q9HBD1.
    SMRi Q9HBD1. Positions 12-59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120029. 5 interactions.
    IntActi Q9HBD1. 6 interactions.
    MINTi MINT-3052676.

    PTM databases

    PhosphoSitei Q9HBD1.

    Polymorphism databases

    DMDMi 73621223.

    Proteomic databases

    MaxQBi Q9HBD1.
    PaxDbi Q9HBD1.
    PRIDEi Q9HBD1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357244 ; ENSP00000349783 ; ENSG00000056586 . [Q9HBD1-1 ]
    ENST00000373670 ; ENSP00000362774 ; ENSG00000056586 . [Q9HBD1-1 ]
    ENST00000423239 ; ENSP00000411767 ; ENSG00000056586 . [Q9HBD1-4 ]
    ENST00000471874 ; ENSP00000474148 ; ENSG00000056586 . [Q9HBD1-5 ]
    ENST00000498479 ; ENSP00000474709 ; ENSG00000056586 . [Q9HBD1-2 ]
    GeneIDi 54542.
    KEGGi hsa:54542.
    UCSCi uc004bnd.1. human. [Q9HBD1-1 ]
    uc004bne.4. human. [Q9HBD1-4 ]
    uc004bng.1. human. [Q9HBD1-5 ]
    uc011lzg.2. human. [Q9HBD1-2 ]

    Organism-specific databases

    CTDi 54542.
    GeneCardsi GC09M125606.
    HGNCi HGNC:21461. RC3H2.
    HPAi HPA042863.
    MIMi 615231. gene.
    neXtProti NX_Q9HBD1.
    PharmGKBi PA162400905.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320727.
    HOVERGENi HBG080524.
    InParanoidi Q9HBD1.
    KOi K15690.
    OMAi CFSQPLP.
    OrthoDBi EOG7QNVKM.
    PhylomeDBi Q9HBD1.
    TreeFami TF317698.

    Miscellaneous databases

    ChiTaRSi RC3H2. human.
    GenomeRNAii 54542.
    NextBioi 56985.
    PROi Q9HBD1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HBD1.
    Bgeei Q9HBD1.
    CleanExi HS_RC3H2.
    Genevestigatori Q9HBD1.

    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.
    SM00356. ZnF_C3H1. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEIC ACID-BINDING, TISSUE SPECIFICITY.
      Tissue: Monocyte.
    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] (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 509-1191.
      Tissue: Hepatoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1191 (ISOFORM 4).
      Tissue: Lymph node and Melanoma.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-1191 (ISOFORM 5).
      Tissue: Brain and Uterus.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "The ROQUIN family of proteins localizes to stress granules via the ROQ domain and binds target mRNAs."
      Athanasopoulos V., Barker A., Yu D., Tan A.H., Srivastava M., Contreras N., Wang J., Lam K.P., Brown S.H., Goodnow C.C., Dixon N.E., Leedman P.J., Saint R., Vinuesa C.G.
      FEBS J. 277:2109-2127(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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 nameiRC3H2_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBD1
    Secondary accession number(s): Q4VXB1
    , Q5JPD7, Q86ST6, Q8N3D6, Q96F27, Q9H5J2, Q9HBD2, Q9NWN9, Q9NXE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 95 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

    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 RC3H2 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 9
      Human chromosome 9: 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