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Q9WU78 (PDC6I_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Programmed cell death 6-interacting protein
Alternative name(s):
ALG-2-interacting protein 1
ALG-2-interacting protein X
E2F1-inducible protein
Eig2
Gene names
Name:Pdcd6ip
Synonyms:Aip1, Alix
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length869 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. May play a role in the regulation of both apoptosis and cell proliferation.

Subunit structure

Interacts with SH3KBP1. Interacts with PDCD6; the interaction is calcium-dependent. Interacts with TSG101 By similarity. Interacts with SGSM3. Self-associates. Interacts with CHMP4A; the interaction is direct. Interacts with CHMP4B; the interaction is direct. Interacts with CHMP4C; the interaction is direct. Interacts with CEP55; the interaction is direct; CEP55 binds PDCD6IP in a 2:1 stoichiometry. Interacts with SH3GL1 and SH3GL2. Interacts with PDGFRB By similarity. Ref.1

Subcellular location

Cytoplasmcytosol By similarity. Melanosome By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Colocalized with CEP55 in the midbody during cytokinesis. Colocalized with CEP55 at centrosomes of non-dividing cells By similarity.

Tissue specificity

Ubiquitously expressed.

Post-translational modification

May be phosphorylated on tyrosine residues by activated PDGFRB By similarity.

Sequence similarities

Contains 1 BRO1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Plcg2Q8CIH57EBI-641897,EBI-617954

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WU78-1)

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.
Isoform 2 (identifier: Q9WU78-2)

Also known as: Alix-SF; Short;

The sequence of this isoform differs from the canonical sequence as follows:
     159-805: Missing.
Note: Does not interact with ALG-2.
Isoform 3 (identifier: Q9WU78-3)

The sequence of this isoform differs from the canonical sequence as follows:
     239-239: K → KYFYFQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 869868Programmed cell death 6-interacting protein
PRO_0000218892

Regions

Domain3 – 392390BRO1
Region176 – 503328Interaction with CHMP4A, CHMP4B and CHMP4C By similarity
Region503 – 869367Self-association By similarity
Region717 – 7204Interaction with TSG101 By similarity
Region798 – 80710Interaction with CEP55 By similarity
Compositional bias717 – 861145Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2151N6-acetyllysine By similarity
Modified residue7301Phosphoserine By similarity
Modified residue7411Phosphothreonine By similarity

Natural variations

Alternative sequence159 – 805647Missing in isoform 2.
VSP_007502
Alternative sequence2391K → KYFYFQ in isoform 3.
VSP_007501

Experimental info

Sequence conflict329 – 3335LDPIG → SGSYR in AAD26813. Ref.2
Sequence conflict5301L → V in CAA06329. Ref.1
Sequence conflict547 – 5482EV → DL in AAD26813. Ref.2
Sequence conflict5951N → T in AAH26823. Ref.6
Sequence conflict6251L → V in AAD26813. Ref.2
Sequence conflict640 – 6412KQ → NE in AAD26813. Ref.2
Sequence conflict8211G → R in AAD26813. Ref.2
Sequence conflict8531P → L in CAA06330. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: BFDC87ACA183C5D4

FASTA86996,024
        10         20         30         40         50         60 
MASFIWVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RSALGRPLDK 

        70         80         90        100        110        120 
HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK 

       130        140        150        160        170        180 
SCVLFNCAAL ASQIAAEQNL DNDEGLKTAA KQYQFASGAF LHIKDTVLSA LSREPTVDIS 

       190        200        210        220        230        240 
PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE 

       250        260        270        280        290        300 
VFPTLAAKQC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKNVASR YDEYVNVKDF 

       310        320        330        340        350        360 
SDKINRALTA AKKDNDFIYH DRVPDLKDLD PIGKATLVKP TPVNVPVSQK FTDLFEKMVP 

       370        380        390        400        410        420 
VSVQQSLAVF SQRKADLVNR SIAQMREATT LANGVLASLN LPAAIEDVSG DTVPQSILTK 

       430        440        450        460        470        480 
STSVVEQGGI QTVDQLIKEL PELLQRNREI LEESLRLLDE EEATDNDLRA KFKDRWQRTP 

       490        500        510        520        530        540 
SNDLYKPLRA EGAKFRAVLD KAVQADGQVK ERYQSHRDTI ALLCKPEPEL NAAIPSANPA 

       550        560        570        580        590        600 
KTMQGSEVVS VLKSLLSNLD EIKKERESLE NDLKSVNFDM TSKFLTALAQ DGVINEEALS 

       610        620        630        640        650        660 
VTELDRIYGG LTSKVQESLK KQEGLLKNIQ VSHQEFSKMK QSNNEANLRE EVLKNLATAY 

       670        680        690        700        710        720 
DNFVELVANL KEGTKFYNEL TEILVRFQNK CSDIVFARKT ERDELLKDLQ QSIAREPSAP 

       730        740        750        760        770        780 
SIPPPAYQSS PAAGHAAAPP TPAPRTMPPA KPQPPARPPP PVLPANRVPP ASAAAAPAGV 

       790        800        810        820        830        840 
GTASAAPPQT PGSAPPPQAQ GPPYPTYPGY PGYCQMPMPM GYNPYAYGQY NMPYPPVYHQ 

       850        860 
SPGQAPYPGP QQPTYPFPQP PQQSYYPQQ 

« Hide

Isoform 2 (Alix-SF) (Short) [UniParc].

Checksum: 35BEBFF783AF1519
Show »

FASTA22224,924
Isoform 3 [UniParc].

Checksum: 4B3AA18F84E39723
Show »

FASTA87496,773

References

« Hide 'large scale' references
[1]"Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptotsis-linked-gene 2 (ALG-2) protein."
Missotten M., Nichols A., Rieger K., Sadoul R.
Cell Death Differ. 6:124-129(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH PDCD6.
Tissue: Brain.
[2]"Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction."
Vito P., Pellegrini L., Guiet C., D'Adamio L.
J. Biol. Chem. 274:1533-1540(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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] (ISOFORMS 1 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Forelimb, Placenta and Thymus.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Mammary gland.
[7]"Rapid analysis of gene expression (RAGE) facilitates universal expression profiling."
Wang A.J., Pierce A., Judson-Kremer K., Gaddis S., Aldaz C.M., Johnson D.G., MacLeod M.C.
Nucleic Acids Res. 27:4609-4618(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 671-869.
Strain: C57BL/6J.
Tissue: Forelimb.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005073 mRNA. Translation: CAA06329.1.
AJ005074 mRNA. Translation: CAA06330.1.
AF119955 mRNA. Translation: AAD26813.1.
AK031256 mRNA. Translation: BAC27323.1.
AK167574 mRNA. Translation: BAE39637.1.
AK169704 mRNA. Translation: BAE41316.1.
CT025751, AC162177, AC167246 Genomic DNA. Translation: CAX15748.1.
CH466621 Genomic DNA. Translation: EDL08950.1.
BC002261 mRNA. Translation: AAH02261.1.
BC026823 mRNA. Translation: AAH26823.1.
AF176514 mRNA. Translation: AAD53115.1.
CCDSCCDS23588.1. [Q9WU78-1]
CCDS52947.1. [Q9WU78-3]
RefSeqNP_001158149.1. NM_001164677.1. [Q9WU78-3]
NP_001158150.1. NM_001164678.1.
NP_035182.2. NM_011052.2. [Q9WU78-1]
UniGeneMm.29816.

3D structure databases

ProteinModelPortalQ9WU78.
SMRQ9WU78. Positions 2-698.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202072. 5 interactions.
DIPDIP-41418N.
IntActQ9WU78. 10 interactions.
MINTMINT-238635.

PTM databases

PhosphoSiteQ9WU78.

2D gel databases

REPRODUCTION-2DPAGEQ9WU78.
UCD-2DPAGEQ9WU78.

Proteomic databases

MaxQBQ9WU78.
PaxDbQ9WU78.
PRIDEQ9WU78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035086; ENSMUSP00000035086; ENSMUSG00000032504. [Q9WU78-1]
ENSMUST00000111861; ENSMUSP00000107492; ENSMUSG00000032504. [Q9WU78-3]
GeneID18571.
KEGGmmu:18571.
UCSCuc009rwn.2. mouse. [Q9WU78-1]

Organism-specific databases

CTD10015.
MGIMGI:1333753. Pdcd6ip.

Phylogenomic databases

eggNOGNOG325528.
GeneTreeENSGT00750000117459.
HOVERGENHBG053533.
KOK12200.
OMAQVKECYQ.
OrthoDBEOG7V49XV.
TreeFamTF323502.

Gene expression databases

ArrayExpressQ9WU78.
BgeeQ9WU78.
CleanExMM_PDCD6IP.
GenevestigatorQ9WU78.

Family and domain databases

Gene3D1.25.40.280. 1 hit.
InterProIPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
[Graphical view]
PfamPF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
[Graphical view]
SMARTSM01041. BRO1. 1 hit.
[Graphical view]
PROSITEPS51180. BRO1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDCD6IP. mouse.
NextBio294408.
PROQ9WU78.
SOURCESearch...

Entry information

Entry namePDC6I_MOUSE
AccessionPrimary (citable) accession number: Q9WU78
Secondary accession number(s): O88695 expand/collapse secondary AC list , O89014, Q3TED2, Q8BSL8, Q8R0H5, Q99LR3, Q9QZN8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 110 of the entry and version 3 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