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Q9UKD2

- MRT4_HUMAN

UniProt

Q9UKD2 - MRT4_HUMAN

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Protein

mRNA turnover protein 4 homolog

Gene
MRTO4, C1orf33, MRT4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in mRNA turnover and ribosome assembly By similarity.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. ribosome biogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA turnover protein 4 homolog
Gene namesi
Name:MRTO4
Synonyms:C1orf33, MRT4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18477. MRTO4.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nuclear membrane Source: HPA
  2. nucleolus Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162396216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239mRNA turnover protein 4 homologPRO_0000154816Add
BLAST

Proteomic databases

MaxQBiQ9UKD2.
PaxDbiQ9UKD2.
PeptideAtlasiQ9UKD2.
PRIDEiQ9UKD2.

2D gel databases

SWISS-2DPAGEQ9UKD2.

PTM databases

PhosphoSiteiQ9UKD2.

Expressioni

Gene expression databases

BgeeiQ9UKD2.
CleanExiHS_MRTO4.
GenevestigatoriQ9UKD2.

Organism-specific databases

HPAiHPA026438.
HPA026446.

Interactioni

Protein-protein interaction databases

BioGridi119337. 27 interactions.
IntActiQ9UKD2. 5 interactions.
MINTiMINT-4727757.
STRINGi9606.ENSP00000364320.

Structurei

3D structure databases

ProteinModelPortaliQ9UKD2.
SMRiQ9UKD2. Positions 5-218.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0244.
HOGENOMiHOG000177263.
HOVERGENiHBG052510.
InParanoidiQ9UKD2.
KOiK14815.
OMAiDCMTISE.
OrthoDBiEOG70GMGM.
PhylomeDBiQ9UKD2.
TreeFamiTF300111.

Family and domain databases

InterProiIPR001790. Ribosomal_L10/acidic_P0.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UKD2-1 [UniParc]FASTAAdd to Basket

« Hide

MPKSKRDKKV SLTKTAKKGL ELKQNLIEEL RKCVDTYKYL FIFSVANMRN    50
SKLKDIRNAW KHSRMFFGKN KVMMVALGRS PSDEYKDNLH QVSKRLRGEV 100
GLLFTNRTKE EVNEWFTKYT EMDYARAGNK AAFTVSLDPG PLEQFPHSME 150
PQLRQLGLPT ALKRGVVTLL SDYEVCKEGD VLTPEQARVL KLFGYEMAEF 200
KVTIKYMWDS QSGRFQQMGD DLPESASEST EESDSEDDD 239
Length:239
Mass (Da):27,560
Last modified:August 16, 2004 - v2
Checksum:iF1BFF6E566FF942F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951R → T in AAD52608. 1 Publication
Sequence conflicti235 – 2351S → L in BAB55205. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF173378 mRNA. Translation: AAD52608.1.
AY303790 mRNA. Translation: AAP68821.1.
AK024227 mRNA. Translation: BAG51275.1.
AK027569 mRNA. Translation: BAB55205.1.
AL035413 Genomic DNA. Translation: CAI22233.1.
CH471134 Genomic DNA. Translation: EAW94873.1.
BC003013 mRNA. Translation: AAH03013.1.
BC006504 mRNA. Translation: AAH06504.1.
CCDSiCCDS191.1.
RefSeqiNP_057267.2. NM_016183.3.
UniGeneiHs.463797.

Genome annotation databases

EnsembliENST00000330263; ENSP00000364320; ENSG00000053372.
GeneIDi51154.
KEGGihsa:51154.
UCSCiuc001bbs.3. human.

Polymorphism databases

DMDMi51316541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF173378 mRNA. Translation: AAD52608.1 .
AY303790 mRNA. Translation: AAP68821.1 .
AK024227 mRNA. Translation: BAG51275.1 .
AK027569 mRNA. Translation: BAB55205.1 .
AL035413 Genomic DNA. Translation: CAI22233.1 .
CH471134 Genomic DNA. Translation: EAW94873.1 .
BC003013 mRNA. Translation: AAH03013.1 .
BC006504 mRNA. Translation: AAH06504.1 .
CCDSi CCDS191.1.
RefSeqi NP_057267.2. NM_016183.3.
UniGenei Hs.463797.

3D structure databases

ProteinModelPortali Q9UKD2.
SMRi Q9UKD2. Positions 5-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119337. 27 interactions.
IntActi Q9UKD2. 5 interactions.
MINTi MINT-4727757.
STRINGi 9606.ENSP00000364320.

PTM databases

PhosphoSitei Q9UKD2.

Polymorphism databases

DMDMi 51316541.

2D gel databases

SWISS-2DPAGE Q9UKD2.

Proteomic databases

MaxQBi Q9UKD2.
PaxDbi Q9UKD2.
PeptideAtlasi Q9UKD2.
PRIDEi Q9UKD2.

Protocols and materials databases

DNASUi 51154.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330263 ; ENSP00000364320 ; ENSG00000053372 .
GeneIDi 51154.
KEGGi hsa:51154.
UCSCi uc001bbs.3. human.

Organism-specific databases

CTDi 51154.
GeneCardsi GC01P019578.
HGNCi HGNC:18477. MRTO4.
HPAi HPA026438.
HPA026446.
neXtProti NX_Q9UKD2.
PharmGKBi PA162396216.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0244.
HOGENOMi HOG000177263.
HOVERGENi HBG052510.
InParanoidi Q9UKD2.
KOi K14815.
OMAi DCMTISE.
OrthoDBi EOG70GMGM.
PhylomeDBi Q9UKD2.
TreeFami TF300111.

Miscellaneous databases

ChiTaRSi MRTO4. human.
GenomeRNAii 51154.
NextBioi 54049.
PROi Q9UKD2.

Gene expression databases

Bgeei Q9UKD2.
CleanExi HS_MRTO4.
Genevestigatori Q9UKD2.

Family and domain databases

InterProi IPR001790. Ribosomal_L10/acidic_P0.
[Graphical view ]
Pfami PF00466. Ribosomal_L10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Ge H.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Zou S.W., Miao S.Y., Zhang X.D., Qiao Y., Wang L.F.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "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].
  4. "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].
  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].
    Tissue: Lung.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMRT4_HUMAN
AccessioniPrimary (citable) accession number: Q9UKD2
Secondary accession number(s): B3KNB3
, Q5TG55, Q96SS6, Q9BPV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: September 3, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi