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Q9Y2T2 (AP3M1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
AP-3 complex subunit mu-1
Alternative name(s):
AP-3 adapter complex mu3A subunit
Adapter-related protein complex 3 subunit mu-1
Mu-adaptin 3A
Mu3A-adaptin
Gene names
Name:AP3M1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.

Subunit structure

Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2). Interacts with AGAP1. AP-3 associates with the BLOC-1 complex By similarity.

Subcellular location

Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex By similarity.

Sequence similarities

Belongs to the adaptor complexes medium subunit family.

Contains 1 MHD (mu homology) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418AP-3 complex subunit mu-1
PRO_0000193781

Regions

Domain176 – 417242MHD

Experimental info

Sequence conflict1601G → V in BAB15614. Ref.2
Sequence conflict2851N → D in BAB15614. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y2T2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 533E189C320C4C48

FASTA41846,939
        10         20         30         40         50         60 
MIHSLFLINC SGDIFLEKHW KSVVSQSVCD YFFEAQEKAA DVENVPPVIS TPHHYLISIY 

        70         80         90        100        110        120 
RDKLFFVSVI QTEVPPLFVI EFLHRVADTF QDYFGECSEA AIKDNVVIVY ELLEEMLDNG 

       130        140        150        160        170        180 
FPLATESNIL KELIKPPTIL RSVVNSITGS SNVGDTLPTG QLSNIPWRRA GVKYTNNEAY 

       190        200        210        220        230        240 
FDVVEEIDAI IDKSGSTVFA EIQGVIDACI KLSGMPDLSL SFMNPRLLDD VSFHPCIRFK 

       250        260        270        280        290        300 
RWESERVLSF IPPDGNFRLI SYRVSSQNLV AIPVYVKHSI SFKENSSCGR FDITIGPKQN 

       310        320        330        340        350        360 
MGKTIEGITV TVHMPKVVLN MNLTPTQGSY TFDPVTKVLT WDVGKITPQK LPSLKGLVNL 

       370        380        390        400        410 
QSGAPKPEEN PSLNIQFKIQ QLAISGLKVN RLDMYGEKYK PFKGVKYVTK AGKFQVRT 

« Hide

References

« Hide 'large scale' references
[1]"Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor."
Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A., Bonifacino J.S.
Mol. Cell 3:11-21(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood and Skin fibroblast.
[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. expand/collapse author list , 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].
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Eye and Prostate.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF092092 mRNA. Translation: AAD20446.1.
AK026983 mRNA. Translation: BAB15614.1.
AL731576 Genomic DNA. Translation: CAI39670.1.
BC026232 mRNA. Translation: AAH26232.1.
BC067127 mRNA. Translation: AAH67127.1.
CCDSCCDS7342.1.
RefSeqNP_036227.1. NM_012095.4.
NP_996895.1. NM_207012.2.
XP_006717826.1. XM_006717763.1.
XP_006717827.1. XM_006717764.1.
UniGeneHs.500104.

3D structure databases

ProteinModelPortalQ9Y2T2.
SMRQ9Y2T2. Positions 4-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117938. 19 interactions.
IntActQ9Y2T2. 4 interactions.
STRING9606.ENSP00000347408.

PTM databases

PhosphoSiteQ9Y2T2.

Polymorphism databases

DMDM13123952.

Proteomic databases

MaxQBQ9Y2T2.
PaxDbQ9Y2T2.
PeptideAtlasQ9Y2T2.
PRIDEQ9Y2T2.

Protocols and materials databases

DNASU26985.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355264; ENSP00000347408; ENSG00000185009.
ENST00000372745; ENSP00000361831; ENSG00000185009.
GeneID26985.
KEGGhsa:26985.
UCSCuc001jwf.3. human.

Organism-specific databases

CTD26985.
GeneCardsGC10M075880.
HGNCHGNC:569. AP3M1.
MIM610366. gene.
neXtProtNX_Q9Y2T2.
PharmGKBPA24860.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298719.
HOGENOMHOG000234366.
HOVERGENHBG104910.
InParanoidQ9Y2T2.
KOK12398.
OMAHMPKAVL.
OrthoDBEOG79KPF6.
PhylomeDBQ9Y2T2.
TreeFamTF315187.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkQ9Y2T2.

Gene expression databases

ArrayExpressQ9Y2T2.
BgeeQ9Y2T2.
CleanExHS_AP3M1.
GenevestigatorQ9Y2T2.

Family and domain databases

InterProIPR022775. AP_mu_sigma_su.
IPR001392. Clathrin_mu.
IPR008968. Clathrin_mu_C.
IPR018240. Clathrin_mu_CS.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PfamPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFPIRSF005992. Clathrin_mu. 1 hit.
PRINTSPR00314. CLATHRINADPT.
SUPFAMSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEPS00990. CLAT_ADAPTOR_M_1. 1 hit.
PS00991. CLAT_ADAPTOR_M_2. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAP3M1. human.
GeneWikiAP3M1.
GenomeRNAi26985.
NextBio49448.
PROQ9Y2T2.
SOURCESearch...

Entry information

Entry nameAP3M1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2T2
Secondary accession number(s): Q5JQ12, Q9H5L2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM