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Q64362 (AKTIP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AKT-interacting protein
Alternative name(s):
FT1
Fused toes protein
Gene names
Name:Aktip
Synonyms:Fif, Ft1, Fts
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade By similarity.

Subunit structure

Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. May interact directly with HOOK1, HOOK2 and HOOK3. The FHF complex associates with the homotypic vesicular sorting complex (the HOPS complex). Also interacts with AKT1 By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.

Tissue specificity

Ubiquitous. Highest expression in kidney, testis and brain and lowest in spleen and liver. Ref.1

Involvement in disease

Defects in Aktip are a cause of embryonic death in homozygous animals. Death occurs at about 10 days of development. Symptoms include loss of left-right asymmetry, malformation of the developing brain and of the spinal cord, syndactyly and polydactyly. Heterozygous animals are characterized by polydactyly and thymic hyperplasia. Ref.5

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family. FTS subfamily.

Caution

Lacks the conserved Cys residue necessary for ubiquitin-conjugating enzyme E2 activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292AKT-interacting protein
PRO_0000082610

Sequences

Sequence LengthMass (Da)Tools
Q64362 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A5FFC7F9053B1E3B

FASTA29232,942
        10         20         30         40         50         60 
MNPLWSMSAG SVRKRAEGEE KTLAGDVKTS PPRSAPKKQL PSIPKNALPI AKPTSPAPAA 

        70         80         90        100        110        120 
QSTNGTHASY GPFYLEYSLL AEFTLVVKQK LPGVYVQPSY RSALVWFGVI FIRHGLYQDG 

       130        140        150        160        170        180 
VFKFTVYIPD NYPDGDCPRL LFDIPVFHPL VDPTSGELDV KRAFAKWRRN HNHIWQVLMY 

       190        200        210        220        230        240 
ARRVFYKIDT TSPLNPEAAV LYEKDIQLFK SKVVDSVKVC TARLFDQPKI EDPYAISFSP 

       250        260        270        280        290 
WNPSVHDEAR EKMLTQKKPD EQHNKSVHVA GLSWVKPGSV QPFSKEEKTV AT 

« Hide

References

« Hide 'large scale' references
[1]"Ft1, a novel gene related to ubiquitin conjugating enzymes, is deleted in the Fused toes mouse mutation."
Lesche R., Peetz A., van der Hoeven F., Ruether U.
Mamm. Genome 8:879-883(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
[2]"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. expand/collapse author list , 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: Amnion and Visual cortex.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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.
Tissue: Mammary tumor.
[5]"Programmed cell death is affected in the novel mouse mutant Fused toes (Ft)."
van der Hoeven F., Schimmang T., Volkmann A., Mattei M.-G., Kyewski B., Ruether U.
Development 120:2601-2607(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z67963 mRNA. Translation: CAA91902.1.
X71978 mRNA. Translation: CAA50800.1.
AK146459 mRNA. Translation: BAE27187.1.
AK158704 mRNA. Translation: BAE34620.1.
CH466525 Genomic DNA. Translation: EDL11072.1.
CH466525 Genomic DNA. Translation: EDL11073.1.
BC008130 mRNA. Translation: AAH08130.1.
PIRS33513.
RefSeqNP_034371.1. NM_010241.4.
XP_006530733.1. XM_006530670.1.
XP_006530734.1. XM_006530671.1.
XP_006530735.1. XM_006530672.1.
UniGeneMm.324588.

3D structure databases

ProteinModelPortalQ64362.
SMRQ64362. Positions 76-223.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ64362.

Proteomic databases

PaxDbQ64362.
PRIDEQ64362.

Protocols and materials databases

DNASU14339.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109609; ENSMUSP00000105238; ENSMUSG00000031667.
ENSMUST00000120213; ENSMUSP00000112375; ENSMUSG00000031667.
ENSMUST00000120349; ENSMUSP00000113769; ENSMUSG00000031667.
GeneID14339.
KEGGmmu:14339.
UCSCuc009msl.1. mouse.

Organism-specific databases

CTD64400.
MGIMGI:3693832. Aktip.

Phylogenomic databases

eggNOGNOG285076.
GeneTreeENSGT00390000010125.
HOGENOMHOG000033885.
HOVERGENHBG095637.
InParanoidQ3TYE3.
OMASPWNPAV.
PhylomeDBQ64362.
TreeFamTF314386.

Gene expression databases

ArrayExpressQ64362.
BgeeQ64362.
GenevestigatorQ64362.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285777.
PROQ64362.
SOURCESearch...

Entry information

Entry nameAKTIP_MOUSE
AccessionPrimary (citable) accession number: Q64362
Secondary accession number(s): Q3TYE3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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