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Q9BXS5 (AP1M1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
AP-1 complex subunit mu-1
Alternative name(s):
AP-mu chain family member mu1A
Adapter-related protein complex 1 subunit mu-1
Adaptor protein complex AP-1 subunit mu-1
Clathrin assembly protein complex 1 mu-1 medium chain 1
Clathrin coat assembly protein AP47
Clathrin coat-associated protein AP47
Golgi adaptor HA1/AP1 adaptin mu-1 subunit
Mu-adaptin 1
Mu1A-adaptin
Gene names
Name:AP1M1
Synonyms:CLTNM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.

Subunit structure

Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Interacts with MARCH11 By similarity. Interacts with HIV-1 Nef. Associates with the AP1(MU)-Nef-MHC-I complex; this complex is required for MHC-I internalization. Ref.9

Subcellular location

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

Post-translational modification

Phosphorylation of membrane-bound AP1M1/AP1M2 increases its affinity for sorting signals By similarity.

Sequence similarities

Belongs to the adaptor complexes medium subunit family.

Contains 1 MHD (mu homology) domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein transport
Transport
   Cellular componentCytoplasmic vesicle
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

endosome to melanosome transport

Inferred from mutant phenotype PubMed 19841138. Source: UniProtKB

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

melanosome organization

Inferred from mutant phenotype PubMed 19841138. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

clathrin adaptor complex

Inferred from electronic annotation. Source: InterPro

clathrin-coated vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lysosomal membrane

Traceable author statement. Source: Reactome

trans-Golgi network membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 14691137. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LDOC1O957513EBI-541426,EBI-740738
MTF1Q148723EBI-541426,EBI-747024

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXS5-1)

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: Q9BXS5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     182-182: L → LGKYPGVGWLGHT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 423422AP-1 complex subunit mu-1
PRO_0000193770

Regions

Domain168 – 421254MHD

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.7
Modified residue1521Phosphothreonine By similarity
Modified residue1541Phosphothreonine By similarity

Natural variations

Alternative sequence1821L → LGKYPGVGWLGHT in isoform 2.
VSP_042542
Natural variant3031R → Q in a breast cancer sample; somatic mutation. Ref.8
VAR_036536

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 64EC5E47EA6F8E98

FASTA42348,587
        10         20         30         40         50         60 
MSASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL AHGGVRFMWI 

        70         80         90        100        110        120 
KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE ESIRDNFVII YELLDELMDF 

       130        140        150        160        170        180 
GYPQTTDSKI LQEYITQEGH KLETGAPRPP ATVTNAVSWR SEGIKYRKNE VFLDVIESVN 

       190        200        210        220        230        240 
LLVSANGNVL RSEIVGSIKM RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ 

       250        260        270        280        290        300 
CVRLSRFEND RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMIKAKSQ 

       310        320        330        340        350        360 
FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG GKEYLMRAHF 

       370        380        390        400        410        420 
GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK SGYQALPWVR YITQNGDYQL 


RTQ 

« Hide

Isoform 2 [UniParc].

Checksum: EEA5A4B9F17D86D9
Show »

FASTA43549,840

References

« Hide 'large scale' references
[1]"Human clathrin-associated protein AP47 mRNA."
Qu X., Zhai Y., Zhang C., Yu Y., Xing G., Wei H., Wu S., Zhou G., He F.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]Zhang H.-T., Burakoff S.J., Jin Y.-J.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: T-cell.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(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] (ISOFORM 1).
Tissue: Uterus.
[5]Bienvenut W.V., Claeys D.
Submitted (JAN-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 41-56; 87-96; 130-160; 202-211; 218-225; 380-393 AND 401-421, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[6]"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].
[7]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-303.
[9]"The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail."
Wonderlich E.R., Williams M., Collins K.L.
J. Biol. Chem. 283:3011-3022(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF290613 mRNA. Translation: AAK28024.1.
DQ059565 mRNA. Translation: AAY54246.1.
AC020911 Genomic DNA. No translation available.
BC017469 mRNA. Translation: AAH17469.1.
CCDSCCDS12342.1. [Q9BXS5-1]
CCDS46008.1. [Q9BXS5-2]
RefSeqNP_001123996.1. NM_001130524.1. [Q9BXS5-2]
NP_115882.1. NM_032493.3. [Q9BXS5-1]
UniGeneHs.71040.

3D structure databases

ProteinModelPortalQ9BXS5.
SMRQ9BXS5. Positions 2-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114421. 26 interactions.
IntActQ9BXS5. 14 interactions.
MINTMINT-1456291.
STRING9606.ENSP00000388996.

PTM databases

PhosphoSiteQ9BXS5.

Polymorphism databases

DMDM18202738.

Proteomic databases

MaxQBQ9BXS5.
PaxDbQ9BXS5.
PeptideAtlasQ9BXS5.
PRIDEQ9BXS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291439; ENSP00000291439; ENSG00000072958. [Q9BXS5-1]
ENST00000444449; ENSP00000388996; ENSG00000072958. [Q9BXS5-2]
GeneID8907.
KEGGhsa:8907.
UCSCuc002ndu.2. human. [Q9BXS5-1]
uc002ndv.2. human. [Q9BXS5-2]

Organism-specific databases

CTD8907.
GeneCardsGC19P016308.
HGNCHGNC:13667. AP1M1.
HPAHPA045256.
MIM603535. gene.
neXtProtNX_Q9BXS5.
PharmGKBPA24848.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315786.
HOGENOMHOG000173247.
HOVERGENHBG050516.
InParanoidQ9BXS5.
KOK12393.
OMAYPWVRYI.
PhylomeDBQ9BXS5.
TreeFamTF300393.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkQ9BXS5.

Gene expression databases

ArrayExpressQ9BXS5.
BgeeQ9BXS5.
CleanExHS_AP1M1.
GenevestigatorQ9BXS5.

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

GeneWikiAP1M1.
GenomeRNAi8907.
NextBio33467.
PROQ9BXS5.
SOURCESearch...

Entry information

Entry nameAP1M1_HUMAN
AccessionPrimary (citable) accession number: Q9BXS5
Secondary accession number(s): Q4TTY5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM