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Protein

FAST kinase domain-containing protein 2, mitochondrial

Gene

Fastkd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Plays an important role in assembly of the mitochondrial large ribosomal subunit.By similarity

GO - Molecular functioni

GO - Biological processi

  • cellular respiration Source: UniProtKB
  • mitochondrial large ribosomal subunit assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
FAST kinase domain-containing protein 2, mitochondrial
Gene namesi
Name:Fastkd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1922869. Fastkd2.

Subcellular locationi

  • Mitochondrion matrixmitochondrion nucleoid By similarity

  • Note: Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids.By similarity

GO - Cellular componenti

  • mitochondrial nucleoid Source: UniProtKB
  • mitochondrion Source: MGI
  • ribonucleoprotein granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Mitochondrion nucleoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 689FAST kinase domain-containing protein 2, mitochondrialPRO_0000050784
Transit peptidei1 – ?MitochondrionCurated

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei126 – 1261PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ922E6.
MaxQBiQ922E6.
PaxDbiQ922E6.
PeptideAtlasiQ922E6.
PRIDEiQ922E6.

PTM databases

iPTMnetiQ922E6.
PhosphoSiteiQ922E6.

Expressioni

Tissue specificityi

Expression detected in spleen, testis, colon, heart, smooth muscle, kidney, brain, lung, liver, brown and white adipose tissue with highest expression in testis, heart and smooth muscle.1 Publication

Gene expression databases

BgeeiQ922E6.
CleanExiMM_FASTKD2.
GenevisibleiQ922E6. MM.

Interactioni

Subunit structurei

Monomer. Found in a complex with GRSF1, DDX28, DHX30 and FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027103.

Structurei

3D structure databases

ProteinModelPortaliQ922E6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini617 – 67458RAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the FAST kinase family.Curated
Contains 1 RAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IH1K. Eukaryota.
ENOG410ZQHV. LUCA.
GeneTreeiENSGT00510000048773.
HOGENOMiHOG000112491.
HOVERGENiHBG081516.
InParanoidiQ922E6.
KOiK18190.
OMAiFDIWKLK.
OrthoDBiEOG7TBC2C.
PhylomeDBiQ922E6.
TreeFamiTF352875.

Family and domain databases

InterProiIPR010622. FAST_Leu-rich.
IPR013584. RAP.
[Graphical view]
PfamiPF06743. FAST_1. 1 hit.
PF08373. RAP. 1 hit.
[Graphical view]
SMARTiSM00952. RAP. 1 hit.
[Graphical view]
PROSITEiPS51286. RAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q922E6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSKARSLLW TIRRFSTLLP RSRALRIDPL GTCRPEVIHS KWNPRNHRLN
60 70 80 90 100
VFDEGLQPSV RYLFQDIFIS KSVDGCIQTK GISHSAVFKP DRLLCPRRLS
110 120 130 140 150
FDAKHSFVSD GTSDHDLKKI NFHHTSSEDV FTKKVRPTPV NYKKLAQECN
160 170 180 190 200
SLSDVLDTFS KAPTFPGSNY FLAMWIIAKR ISEDKRRFER QLMFSHPAFN
210 220 230 240 250
QLCEQMMREA KIMHYDHLLF SLNAIVKLGI PQNTLMVQTL LRTIQERINE
260 270 280 290 300
CDERCLSILS TALVSMEPCM NVNALRAGLR ILVDQQVWNI KHVFTLQTVM
310 320 330 340 350
KCIGKDAPSA LKKKLEMKAL KELGRFSILN SQHMFEVLAA MDLRSVVLLN
360 370 380 390 400
ECSKVVIDNV HGCPFKVLIS ILQSCRDLRY QNEDLFKSIA EYVATTFDIW
410 420 430 440 450
KLKQVIFFLL LFETLGFRPP GLMDKLMEKV VQEPGSLNVK NIVSILHVYS
460 470 480 490 500
SLNHVHKIHN REFLEALASA LTGCLHHISS ESLLNAVHSF CMMNYFPLAP
510 520 530 540 550
INQLIKENII NELLTSGDTE KNIHKLHVLN TCLKLDESTY KSVHIPLPQL
560 570 580 590 600
PLSASQPNEK LAEVLSRLLE GEGRFSRNVP LPHNYHIDFE IRMDTNRTQV
610 620 630 640 650
FSFSDVDASS ATNMQRVAVL CVPKSVYCLN SCHPRGLMAM KIRHLNVMGF
660 670 680
HVILIHNWEL KKLKMEDAVT FVRKKIYSDE VLPTADTTV
Length:689
Mass (Da):78,948
Last modified:March 1, 2004 - v2
Checksum:i290D866BC4AAD659
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551G → V in BAE32254 (PubMed:16141072).Curated
Sequence conflicti172 – 1732LA → FS in BAE38740 (PubMed:16141072).Curated
Sequence conflicti361 – 3611H → N in BAE38740 (PubMed:16141072).Curated
Sequence conflicti554 – 5541A → V in BAE28423 (PubMed:16141072).Curated
Sequence conflicti593 – 5931M → V in BAE32254 (PubMed:16141072).Curated
Sequence conflicti606 – 6061V → I in BAE38740 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013125 mRNA. Translation: BAC25392.1.
AK084971 mRNA. Translation: BAC39325.1.
AK148224 mRNA. Translation: BAE28423.1.
AK153916 mRNA. Translation: BAE32254.1.
AK166378 mRNA. Translation: BAE38740.1.
BC008271 mRNA. Translation: AAH08271.2.
BC057208 mRNA. Translation: AAH57208.1.
BC080813 mRNA. Translation: AAH80813.1.
CCDSiCCDS15001.1.
RefSeqiNP_766010.1. NM_172422.3.
UniGeneiMm.30965.

Genome annotation databases

EnsembliENSMUST00000027103; ENSMUSP00000027103; ENSMUSG00000025962.
GeneIDi75619.
KEGGimmu:75619.
UCSCiuc007bgl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013125 mRNA. Translation: BAC25392.1.
AK084971 mRNA. Translation: BAC39325.1.
AK148224 mRNA. Translation: BAE28423.1.
AK153916 mRNA. Translation: BAE32254.1.
AK166378 mRNA. Translation: BAE38740.1.
BC008271 mRNA. Translation: AAH08271.2.
BC057208 mRNA. Translation: AAH57208.1.
BC080813 mRNA. Translation: AAH80813.1.
CCDSiCCDS15001.1.
RefSeqiNP_766010.1. NM_172422.3.
UniGeneiMm.30965.

3D structure databases

ProteinModelPortaliQ922E6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027103.

PTM databases

iPTMnetiQ922E6.
PhosphoSiteiQ922E6.

Proteomic databases

EPDiQ922E6.
MaxQBiQ922E6.
PaxDbiQ922E6.
PeptideAtlasiQ922E6.
PRIDEiQ922E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027103; ENSMUSP00000027103; ENSMUSG00000025962.
GeneIDi75619.
KEGGimmu:75619.
UCSCiuc007bgl.2. mouse.

Organism-specific databases

CTDi22868.
MGIiMGI:1922869. Fastkd2.

Phylogenomic databases

eggNOGiENOG410IH1K. Eukaryota.
ENOG410ZQHV. LUCA.
GeneTreeiENSGT00510000048773.
HOGENOMiHOG000112491.
HOVERGENiHBG081516.
InParanoidiQ922E6.
KOiK18190.
OMAiFDIWKLK.
OrthoDBiEOG7TBC2C.
PhylomeDBiQ922E6.
TreeFamiTF352875.

Miscellaneous databases

PROiQ922E6.
SOURCEiSearch...

Gene expression databases

BgeeiQ922E6.
CleanExiMM_FASTKD2.
GenevisibleiQ922E6. MM.

Family and domain databases

InterProiIPR010622. FAST_Leu-rich.
IPR013584. RAP.
[Graphical view]
PfamiPF06743. FAST_1. 1 hit.
PF08373. RAP. 1 hit.
[Graphical view]
SMARTiSM00952. RAP. 1 hit.
[Graphical view]
PROSITEiPS51286. RAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo, Fetal lung, Mammary gland and Thymus.
  2. "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].
    Strain: FVB/N and NMRI.
    Tissue: Embryo and Mammary tumor.
  3. "Fast kinase domain-containing protein 3 is a mitochondrial protein essential for cellular respiration."
    Simarro M., Gimenez-Cassina A., Kedersha N., Lazaro J.B., Adelmant G.O., Marto J.A., Rhee K., Tisdale S., Danial N., Benarafa C., Orduna A., Anderson P.
    Biochem. Biophys. Res. Commun. 401:440-446(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiFAKD2_MOUSE
AccessioniPrimary (citable) accession number: Q922E6
Secondary accession number(s): Q3TLQ2
, Q3U526, Q3UFY6, Q8BT79, Q8C3T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: March 1, 2004
Last modified: July 6, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.