Skip Header

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

Aurora kinase A-interacting protein

Gene

Aurkaip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May act as a negative regulator of Aurora-A kinase, by down-regulation through proteasome-dependent degradation.

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
Aurora kinase A-interacting protein
Short name:
AURKA-interacting protein
Alternative name(s):
28S ribosomal protein S38, mitochondrial
Short name:
MRP-S38
Gene namesi
Name:Aurkaip1
Synonyms:Aip, Akip, Mrps38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913327. Aurkaip1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 200200Aurora kinase A-interacting proteinPRO_0000064537Add
BLAST

Proteomic databases

MaxQBiQ9DCJ7.
PaxDbiQ9DCJ7.
PRIDEiQ9DCJ7.

PTM databases

iPTMnetiQ9DCJ7.
PhosphoSiteiQ9DCJ7.

Expressioni

Tissue specificityi

Ubiquitously expressed and especially highly expressed in heart, skeletal muscle and testis.

Gene expression databases

CleanExiMM_AIP.
MM_AURKAIP1.
ExpressionAtlasiQ9DCJ7. baseline and differential.
GenevisibleiQ9DCJ7. MM.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins (By similarity). Interacts with Aurora-A.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000081114.

Structurei

3D structure databases

ProteinModelPortaliQ9DCJ7.
SMRiQ9DCJ7. Positions 129-200.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IY6U. Eukaryota.
ENOG4111QH2. LUCA.
GeneTreeiENSGT00390000012802.
HOGENOMiHOG000004845.
HOVERGENiHBG010333.
InParanoidiQ9DCJ7.
KOiK16830.
OMAiPQIQCKN.
TreeFamiTF332330.

Family and domain databases

InterProiIPR013177. DUF1713.
[Graphical view]
PfamiPF08213. DUF1713. 1 hit.
[Graphical view]
SMARTiSM01155. DUF1713. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DCJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLARLTSRL ARTVVPWAGF SRSCPGSGVI GSYAFRPLYS LQPASPSRAA
60 70 80 90 100
SLPGKRTQSE LEEFLVPRKM AISPLESWLT AQYLLPRRNV EVPVTLAPSQ
110 120 130 140 150
FYECPPRQGE EEAQQGVREA WDATPVQCKN VLKIRRRKMN HHKYRKLVKR
160 170 180 190 200
TRFLRRKVRE GRLKKKQIKF EKDLKRIWLK AGLKEAPENW QTPKIYLKNK
Length:200
Mass (Da):23,300
Last modified:October 3, 2012 - v2
Checksum:iFA26D360169CC160
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751K → R in BAB22317 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002737 mRNA. Translation: BAB22317.1.
AK003442 mRNA. Translation: BAB22792.1.
AK144719 mRNA. Translation: BAE26030.1.
AK166049 mRNA. Translation: BAE38543.1.
AL670236 Genomic DNA. Translation: CAM18389.1.
CCDSiCCDS19043.1.
RefSeqiNP_079614.1. NM_025338.4.
XP_006539158.1. XM_006539095.2.
UniGeneiMm.28999.

Genome annotation databases

EnsembliENSMUST00000084097; ENSMUSP00000081114; ENSMUSG00000065990.
ENSMUST00000105591; ENSMUSP00000101216; ENSMUSG00000065990.
ENSMUST00000105592; ENSMUSP00000101217; ENSMUSG00000065990.
GeneIDi66077.
KEGGimmu:66077.
UCSCiuc008wey.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002737 mRNA. Translation: BAB22317.1.
AK003442 mRNA. Translation: BAB22792.1.
AK144719 mRNA. Translation: BAE26030.1.
AK166049 mRNA. Translation: BAE38543.1.
AL670236 Genomic DNA. Translation: CAM18389.1.
CCDSiCCDS19043.1.
RefSeqiNP_079614.1. NM_025338.4.
XP_006539158.1. XM_006539095.2.
UniGeneiMm.28999.

3D structure databases

ProteinModelPortaliQ9DCJ7.
SMRiQ9DCJ7. Positions 129-200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000081114.

PTM databases

iPTMnetiQ9DCJ7.
PhosphoSiteiQ9DCJ7.

Proteomic databases

MaxQBiQ9DCJ7.
PaxDbiQ9DCJ7.
PRIDEiQ9DCJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084097; ENSMUSP00000081114; ENSMUSG00000065990.
ENSMUST00000105591; ENSMUSP00000101216; ENSMUSG00000065990.
ENSMUST00000105592; ENSMUSP00000101217; ENSMUSG00000065990.
GeneIDi66077.
KEGGimmu:66077.
UCSCiuc008wey.2. mouse.

Organism-specific databases

CTDi54998.
MGIiMGI:1913327. Aurkaip1.

Phylogenomic databases

eggNOGiENOG410IY6U. Eukaryota.
ENOG4111QH2. LUCA.
GeneTreeiENSGT00390000012802.
HOGENOMiHOG000004845.
HOVERGENiHBG010333.
InParanoidiQ9DCJ7.
KOiK16830.
OMAiPQIQCKN.
TreeFamiTF332330.

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Miscellaneous databases

PROiQ9DCJ7.
SOURCEiSearch...

Gene expression databases

CleanExiMM_AIP.
MM_AURKAIP1.
ExpressionAtlasiQ9DCJ7. baseline and differential.
GenevisibleiQ9DCJ7. MM.

Family and domain databases

InterProiIPR013177. DUF1713.
[Graphical view]
PfamiPF08213. DUF1713. 1 hit.
[Graphical view]
SMARTiSM01155. DUF1713. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    Tissue: Kidney and Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiAKIP_MOUSE
AccessioniPrimary (citable) accession number: Q9DCJ7
Secondary accession number(s): Q9D1J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 87 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

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.