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Protein

Roquin-2

Gene

RC3H2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).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. mRNA binding Source: Ensembl
  3. poly(A) RNA binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: FlyBase
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. B cell homeostasis Source: Ensembl
  2. limb development Source: Ensembl
  3. lung alveolus development Source: Ensembl
  4. lymph node development Source: Ensembl
  5. multicellular organism growth Source: Ensembl
  6. positive regulation of NIK/NF-kappaB signaling Source: Ensembl
  7. post-embryonic development Source: Ensembl
  8. posttranscriptional regulation of gene expression Source: Ensembl
  9. protein polyubiquitination Source: FlyBase
  10. spleen development Source: Ensembl
  11. T cell homeostasis Source: Ensembl
  12. T cell proliferation Source: Ensembl
  13. T follicular helper cell differentiation Source: Ensembl
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. nucleoplasm 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-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

BgeeiQ9HBD1.
CleanExiHS_RC3H2.
ExpressionAtlasiQ9HBD1. baseline and differential.
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 9-74, 87-395.
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.
GeneTreeiENSGT00390000004311.
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. AlignAdd to basket

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

        10         20         30         40         50
MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC
60 70 80 90 100
PFDQTAINTD IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK
110 120 130 140 150
CVEDLALYLK PLSGGKGVAS LNQSALSRPM QRKLVTLVNC QLVEEEGRVR
160 170 180 190 200
AMRAARSLGE RTVTELILQH QNPQQLSANL WAAVRARGCQ FLGPAMQEEA
210 220 230 240 250
LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG HVVQLLYRAS
260 270 280 290 300
CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW
310 320 330 340 350
SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL
360 370 380 390 400
RPHLELLANI DPNPDAVSPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH
410 420 430 440 450
ETPQPQPNSK YKTSMCRDLR QQGGCPRGTN CTFAHSQEEL EKYRLRNKKI
460 470 480 490 500
NATVRTFPLL NKVGVNNTVT TTAGNVISVI GSTETTGKIV PSTNGISNAE
510 520 530 540 550
NSVSQLISRS TDSTLRALET VKKVGKVGAN GQNAAGPSAD SVTENKIGSP
560 570 580 590 600
PKTPVSNVAA TSAGPSNVGT ELNSVPQKSS PFLTRVPVYP PHSENIQYFQ
610 620 630 640 650
DPRTQIPFEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA
660 670 680 690 700
SMPYADHYST FSPRDRMNSS PYQPPPPQPY GPVPPVPSGM YAPVYDSRRI
710 720 730 740 750
WRPPMYQRDD IIRSNSLPPM DVMHSSVYQT SLRERYNSLD GYYSVACQPP
760 770 780 790 800
SEPRTTVPLP REPCGHLKTS CEEQIRRKPD QWAQYHTQKA PLVSSTLPVA
810 820 830 840 850
TQSPTPPSPL FSVDFRADFS ESVSGTKFEE DHLSHYSPWS CGTIGSCINA
860 870 880 890 900
IDSEPKDVIA NSNAVLMDLD SGDVKRRVHL FETQRRTKEE DPIIPFSDGP
910 920 930 940 950
IISKWGAISR SSRTGYHTTD PVQATASQGS ATKPISVSDY VPYVNAVDSR
960 970 980 990 1000
WSSYGNEATS SAHYVERDRF IVTDLSGHRK HSSTGDLLSL ELQQAKSNSL
1010 1020 1030 1040 1050
LLQREANALA MQQKWNSLDE GRHLTLNLLS KEIELRNGEL QSDYTEDATD
1060 1070 1080 1090 1100
TKPDRDIELE LSALDTDEPD GQSEPIEEIL DIQLGISSQN DQLLNGMAVE
1110 1120 1130 1140 1150
NGHPVQQHQK EPPKQKKQSL GEDHVILEEQ KTILPVTSCF SQPLPVSISN
1160 1170 1180 1190
ASCLPITTSV SAGNLILKTH VMSEDKNDFL KPVANGKMVN S
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.Curated
The sequence BAB15634.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9HBD1.
SMRiQ9HBD1. Positions 9-74, 87-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9HBD1.

Polymorphism databases

DMDMi73621223.

Proteomic databases

MaxQBiQ9HBD1.
PaxDbiQ9HBD1.
PRIDEiQ9HBD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi54542.
GeneCardsiGC09M125606.
HGNCiHGNC:21461. RC3H2.
HPAiHPA042863.
MIMi615231. gene.
neXtProtiNX_Q9HBD1.
PharmGKBiPA162400905.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG320727.
GeneTreeiENSGT00390000004311.
HOVERGENiHBG080524.
InParanoidiQ9HBD1.
KOiK15690.
OMAiCFSQPLP.
OrthoDBiEOG7QNVKM.
PhylomeDBiQ9HBD1.
TreeFamiTF317698.

Miscellaneous databases

ChiTaRSiRC3H2. human.
GenomeRNAii54542.
NextBioi56985.
PROiQ9HBD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBD1.
CleanExiHS_RC3H2.
ExpressionAtlasiQ9HBD1. baseline and differential.
GenevestigatoriQ9HBD1.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 99 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

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 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.