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Protein

G-rich sequence factor 1

Gene

GRSF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences.2 Publications

GO - Molecular functioni

  • mRNA binding Source: ProtInc
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, tRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-192823. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
G-rich sequence factor 1
Short name:
GRSF-1
Gene namesi
Name:GRSF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:4610. GRSF1.

Subcellular locationi

  • Cytoplasm
  • Mitochondrion matrixmitochondrion nucleoid 1 Publication

  • Note: Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids.1 Publication

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • mitochondrial nucleoid Source: UniProtKB
  • mitochondrion Source: HPA
  • ribonucleoprotein granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Mitochondrion nucleoid

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29003.

Polymorphism and mutation databases

BioMutaiGRSF1.
DMDMi215274142.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 117117MitochondrionSequence analysisAdd
BLAST
Chaini118 – 480363G-rich sequence factor 1PRO_0000081597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei244 – 2441PhosphoserineCombined sources
Modified residuei335 – 3351PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ12849.
MaxQBiQ12849.
PaxDbiQ12849.
PeptideAtlasiQ12849.
PRIDEiQ12849.

PTM databases

iPTMnetiQ12849.
PhosphoSiteiQ12849.

Expressioni

Gene expression databases

BgeeiQ12849.
CleanExiHS_GRSF1.
ExpressionAtlasiQ12849. baseline and differential.
GenevisibleiQ12849. HS.

Organism-specific databases

HPAiHPA036984.
HPA036985.

Interactioni

Subunit structurei

Monomer. Found in a complex with DDX28, DHX30, FASTKD2 and FASTKD5 (PubMed:25683715). Interacts with the mitochondrial RNase P complex subunit TRMT10C/MRPP1.2 Publications

Protein-protein interaction databases

BioGridi109182. 51 interactions.
IntActiQ12849. 3 interactions.
STRINGi9606.ENSP00000254799.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi150 – 1567Combined sources
Helixi163 – 1697Combined sources
Turni170 – 1723Combined sources
Helixi178 – 1814Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi192 – 20211Combined sources
Helixi203 – 2108Combined sources
Turni211 – 2144Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi220 – 2267Combined sources
Helixi230 – 24213Combined sources
Beta strandi402 – 4065Combined sources
Helixi414 – 4218Combined sources
Beta strandi427 – 4348Combined sources
Beta strandi439 – 4468Combined sources
Helixi450 – 4567Combined sources
Helixi457 – 4593Combined sources
Beta strandi470 – 4767Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LMINMR-A140-245[»]
4QU6X-ray1.75A140-245[»]
4QU7X-ray2.50A/B/C/D400-480[»]
ProteinModelPortaliQ12849.
SMRiQ12849. Positions 140-245, 248-347, 400-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 246125RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini250 – 32677RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini401 – 48080RRM 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 11157Ala-richAdd
BLAST

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiENOG410IQ3R. Eukaryota.
ENOG410YEKV. LUCA.
GeneTreeiENSGT00760000119102.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
InParanoidiQ12849.
OrthoDBiEOG7BS4BZ.
PhylomeDBiQ12849.
TreeFamiTF316157.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR033106. GRSF1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR13976:SF42. PTHR13976:SF42. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12849-1) [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
MAGTRWVLGA LLRGCGCNCS SCRRTGAACL PFYSAAGSIP SGVSGRRRLL
60 70 80 90 100
LLLGAAAAAA SQTRGLQTGP VPPGRLAGPP AVATSAAAAA AASYSALRAS
110 120 130 140 150
LLPQSLAAAA AVPTRSYSQE SKTTYLEDLP PPPEYELAPS KLEEEVDDVF
160 170 180 190 200
LIRAQGLPWS CTMEDVLNFF SDCRIRNGEN GIHFLLNRDG KRRGDALIEM
210 220 230 240 250
ESEQDVQKAL EKHRMYMGQR YVEVYEINNE DVDALMKSLQ VKSSPVVNDG
260 270 280 290 300
VVRLRGLPYS CNEKDIVDFF AGLNIVDITF VMDYRGRRKT GEAYVQFEEP
310 320 330 340 350
EMANQALLKH REEIGNRYIE IFPSRRNEVR THVGSYKGKK IASFPTAKYI
360 370 380 390 400
TEPEMVFEEH EVNEDIQPMT AFESEKEIEL PKEVPEKLPE AADFGTTSSL
410 420 430 440 450
HFVHMRGLPF QANAQDIINF FAPLKPVRIT MEYSSSGKAT GEADVHFETH
460 470 480
EDAVAAMLKD RSHVHHRYIE LFLNSCPKGK
Length:480
Mass (Da):53,126
Last modified:November 25, 2008 - v3
Checksum:iE09EE4E70212A70F
GO
Isoform 2 (identifier: Q12849-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-162: Missing.

Note: No experimental confirmation available.
Show »
Length:318
Mass (Da):36,613
Checksum:iF0AB13A4797FFEBD
GO

Sequence cautioni

The sequence AAC95399.1 differs from that shown.Unlikely isoform. Aberrant splice sites.Curated
The sequence AAH40485.1 differs from that shown.Intron retention.Curated
The sequence AAY40942.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAC03513.1 differs from that shown.Unlikely isoform. Aberrant splice sites.Curated
The sequence BAC86863.1 differs from that shown.Unlikely isoform. Aberrant splice sites.Curated
The sequence EAX05634.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641K → E in BAC86863 (PubMed:14702039).Curated
Sequence conflicti365 – 3662DI → VF in AAC95399 (PubMed:8036161).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771D → Y.1 Publication
Corresponds to variant rs17854012 [ dbSNP | Ensembl ].
VAR_047537

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 162162Missing in isoform 2. 1 PublicationVSP_043118Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07231 mRNA. Translation: AAC95399.1. Sequence problems.
AK056891 mRNA. Translation: BAG51822.1.
AK090755 mRNA. Translation: BAC03513.1. Sequence problems.
AK094806 mRNA. Translation: BAG52934.1.
AK095799 mRNA. Translation: BAG53131.1.
AK097055 mRNA. Translation: BAG53414.1.
AK127161 mRNA. Translation: BAC86863.1. Sequence problems.
AC021989 Genomic DNA. Translation: AAY40942.1. Sequence problems.
CH471057 Genomic DNA. Translation: EAX05631.1.
CH471057 Genomic DNA. Translation: EAX05634.1. Sequence problems.
BC040485 mRNA. Translation: AAH40485.1. Sequence problems.
CCDSiCCDS47069.1. [Q12849-1]
CCDS47070.1. [Q12849-5]
PIRiS48081.
RefSeqiNP_001091947.1. NM_001098477.1. [Q12849-5]
NP_002083.3. NM_002092.3.
XP_011530199.1. XM_011531897.1. [Q12849-5]
XP_011530200.1. XM_011531898.1. [Q12849-5]
UniGeneiHs.309763.

Genome annotation databases

EnsembliENST00000254799; ENSP00000254799; ENSG00000132463. [Q12849-1]
ENST00000502323; ENSP00000425430; ENSG00000132463. [Q12849-5]
GeneIDi2926.
KEGGihsa:2926.
UCSCiuc010iia.2. human. [Q12849-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07231 mRNA. Translation: AAC95399.1. Sequence problems.
AK056891 mRNA. Translation: BAG51822.1.
AK090755 mRNA. Translation: BAC03513.1. Sequence problems.
AK094806 mRNA. Translation: BAG52934.1.
AK095799 mRNA. Translation: BAG53131.1.
AK097055 mRNA. Translation: BAG53414.1.
AK127161 mRNA. Translation: BAC86863.1. Sequence problems.
AC021989 Genomic DNA. Translation: AAY40942.1. Sequence problems.
CH471057 Genomic DNA. Translation: EAX05631.1.
CH471057 Genomic DNA. Translation: EAX05634.1. Sequence problems.
BC040485 mRNA. Translation: AAH40485.1. Sequence problems.
CCDSiCCDS47069.1. [Q12849-1]
CCDS47070.1. [Q12849-5]
PIRiS48081.
RefSeqiNP_001091947.1. NM_001098477.1. [Q12849-5]
NP_002083.3. NM_002092.3.
XP_011530199.1. XM_011531897.1. [Q12849-5]
XP_011530200.1. XM_011531898.1. [Q12849-5]
UniGeneiHs.309763.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LMINMR-A140-245[»]
4QU6X-ray1.75A140-245[»]
4QU7X-ray2.50A/B/C/D400-480[»]
ProteinModelPortaliQ12849.
SMRiQ12849. Positions 140-245, 248-347, 400-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109182. 51 interactions.
IntActiQ12849. 3 interactions.
STRINGi9606.ENSP00000254799.

PTM databases

iPTMnetiQ12849.
PhosphoSiteiQ12849.

Polymorphism and mutation databases

BioMutaiGRSF1.
DMDMi215274142.

Proteomic databases

EPDiQ12849.
MaxQBiQ12849.
PaxDbiQ12849.
PeptideAtlasiQ12849.
PRIDEiQ12849.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254799; ENSP00000254799; ENSG00000132463. [Q12849-1]
ENST00000502323; ENSP00000425430; ENSG00000132463. [Q12849-5]
GeneIDi2926.
KEGGihsa:2926.
UCSCiuc010iia.2. human. [Q12849-1]

Organism-specific databases

CTDi2926.
GeneCardsiGRSF1.
HGNCiHGNC:4610. GRSF1.
HPAiHPA036984.
HPA036985.
MIMi604851. gene.
neXtProtiNX_Q12849.
PharmGKBiPA29003.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQ3R. Eukaryota.
ENOG410YEKV. LUCA.
GeneTreeiENSGT00760000119102.
HOGENOMiHOG000220896.
HOVERGENiHBG055557.
InParanoidiQ12849.
OrthoDBiEOG7BS4BZ.
PhylomeDBiQ12849.
TreeFamiTF316157.

Enzyme and pathway databases

ReactomeiR-HSA-192823. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiGRSF1. human.
GenomeRNAii2926.
PROiQ12849.
SOURCEiSearch...

Gene expression databases

BgeeiQ12849.
CleanExiHS_GRSF1.
ExpressionAtlasiQ12849. baseline and differential.
GenevisibleiQ12849. HS.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR033106. GRSF1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR13976:SF42. PTHR13976:SF42. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GRSF-1: a poly(A)+ mRNA binding protein which interacts with a conserved G-rich element."
    Qian Z., Wilusz J.
    Nucleic Acids Res. 22:2334-2343(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain, Caudate nucleus, Cerebellum, Prostate and Small intestine.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1), VARIANT TYR-277.
    Tissue: Testis.
  6. Bienvenut W.V., Vousden K.H., Lukashchuk N.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 177-188; 243-253 AND 318-325, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression."
    Antonicka H., Sasarman F., Nishimura T., Paupe V., Shoubridge E.A.
    Cell Metab. 17:386-398(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  13. Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH TRMT10C.
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "Mitochondrial RNA granules are centers for posttranscriptional RNA processing and ribosome biogenesis."
    Antonicka H., Shoubridge E.A.
    Cell Rep. 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH DDX28; DHX30; FASTKD2 AND FASTKD5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGRSF1_HUMAN
AccessioniPrimary (citable) accession number: Q12849
Secondary accession number(s): B3KPW0
, Q4W5S5, Q6ZST3, Q8IWD6, Q8NBD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: July 6, 2016
This is version 144 of the entry and version 3 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

Depletion of GRSF1 by siRNA results in a combined OXPHOS assembly defect, with the prominent loss of complexes I, III, IV, and V. It also leads to altered steady-state levels of mitochondrial rRNAs and mRNAs.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.