SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9HBD1

- RC3H2_HUMAN

UniProt

Q9HBD1 - RC3H2_HUMAN

(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)

Protein
Roquin-2
Gene
RC3H2, MNAB, RNF164
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5441RING-type; degenerate
Add
BLAST
Zinc fingeri410 – 43829C3H1-type
Add
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
Complete GO annotation...

GO - Biological processi

  1. protein polyubiquitination Source: FlyBase
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11911191Roquin-2
PRO_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 By similarity. Interacts with CCR4-NOT deadenylase complex By similarity.

Protein-protein interaction databases

BioGridi120029. 4 interactions.
IntActiQ9HBD1. 6 interactions.
MINTiMINT-3052676.

Structurei

3D structure databases

ProteinModelPortaliQ9HBD1.
SMRiQ9HBD1. Positions 12-59.

Family & Domainsi

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi576 – 704129Pro-rich
Add
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 By similarity. It may also be involved in localization to stress granules By similarity.

Sequence similaritiesi

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 195195Missing in isoform 6.
VSP_015017Add
BLAST
Alternative sequencei195 – 21824AMQEE…LSRKV → GKIGYYLTFFISYWGLRMPI SGAR in isoform 5.
VSP_015018Add
BLAST
Alternative sequencei219 – 1191973Missing in isoform 5.
VSP_015019Add
BLAST
Alternative sequencei443 – 50664YRLRN…SVSQL → CNPRGLYLHCCLLSSVASLG TVHNELYKQQHCDREKISVC AVKRAETCFSSQFFSPLEEP REED in isoform 3.
VSP_015020Add
BLAST
Alternative sequencei454 – 47825VRTFP…GNVIS → EVLKQQGKLFQVQTEFQMQK TVFPS in isoform 2.
VSP_015021Add
BLAST
Alternative sequencei479 – 1191713Missing in isoform 2.
VSP_015022Add
BLAST
Alternative sequencei507 – 1191685Missing in isoform 3.
VSP_015023Add
BLAST
Alternative sequencei1040 – 1191152LQSDY…KMVNS → VKKLNLSASCLMYLFSAAAS WLYHY in isoform 4 and isoform 6.
VSP_015024Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti650 – 6501A → G in BAA91073. 1 Publication

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]
ENST00000373665; ENSP00000362769; ENSG00000056586. [Q9HBD1-2]
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...

Protein-protein interaction databases

BioGridi 120029. 4 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 ]
ENST00000373665 ; ENSP00000362769 ; ENSG00000056586 . [Q9HBD1-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 94 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 (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

Similar proteinsi