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Protein

AP-1 complex subunit mu-1

Gene

AP1M1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_121399. MHC class II antigen presentation.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinkiQ9BXS5.

Names & Taxonomyi

Protein namesi
Recommended name:
AP-1 complex subunit mu-1
Alternative name(s):
AP-mu chain family member mu1A
Adaptor protein complex AP-1 subunit mu-1
Adaptor-related protein complex 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 namesi
Name:AP1M1
Synonyms:CLTNM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:13667. AP1M1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24848.

Polymorphism and mutation databases

BioMutaiAP1M1.
DMDMi18202738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 423422AP-1 complex subunit mu-1PRO_0000193770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei152 – 1521PhosphothreonineBy similarity
Modified residuei154 – 1541Phosphothreonine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BXS5.
PaxDbiQ9BXS5.
PeptideAtlasiQ9BXS5.
PRIDEiQ9BXS5.

PTM databases

PhosphoSiteiQ9BXS5.

Expressioni

Gene expression databases

BgeeiQ9BXS5.
CleanExiHS_AP1M1.
ExpressionAtlasiQ9BXS5. baseline and differential.
GenevisibleiQ9BXS5. HS.

Organism-specific databases

HPAiHPA045256.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP57L1Q8IYX8-23EBI-541426,EBI-10181988
DZIP3Q86Y133EBI-541426,EBI-948630
ETV6P412123EBI-541426,EBI-1372759
FAM9BQ8IZU03EBI-541426,EBI-10175124
FXR2P511164EBI-541426,EBI-740459
HOOK2Q96ED93EBI-541426,EBI-743290
IKZF1Q134223EBI-541426,EBI-745305
KRT40Q6A1623EBI-541426,EBI-10171697
KRTAP10-7P604093EBI-541426,EBI-10172290
LDOC1O957513EBI-541426,EBI-740738
LZTS2Q9BRK43EBI-541426,EBI-741037
MTF1Q148723EBI-541426,EBI-747024
PHC2Q8IXK03EBI-541426,EBI-713786
PNMA5Q96PV43EBI-541426,EBI-10171633
RUNDC3AQ59EK94EBI-541426,EBI-747225
SDCCAG3Q96C92-23EBI-541426,EBI-10178036
SSX2IPQ9Y2D83EBI-541426,EBI-2212028
TIFAQ96CG34EBI-541426,EBI-740711
TNIP1Q150253EBI-541426,EBI-357849
ZBTB14O438293EBI-541426,EBI-10176632
ZBTB43O432983EBI-541426,EBI-740718
ZBTB44Q8NCP53EBI-541426,EBI-5658292
ZBTB8AQ96BR94EBI-541426,EBI-742740

Protein-protein interaction databases

BioGridi114421. 55 interactions.
IntActiQ9BXS5. 31 interactions.
MINTiMINT-1456291.
STRINGi9606.ENSP00000388996.

Structurei

3D structure databases

ProteinModelPortaliQ9BXS5.
SMRiQ9BXS5. Positions 2-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 421254MHDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG315786.
GeneTreeiENSGT00530000062779.
HOGENOMiHOG000173247.
HOVERGENiHBG050516.
InParanoidiQ9BXS5.
KOiK12393.
OMAiITQNGEY.
PhylomeDBiQ9BXS5.
TreeFamiTF300393.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR001392. Clathrin_mu.
IPR008968. Clathrin_mu_C.
IPR018240. Clathrin_mu_CS.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PfamiPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF005992. Clathrin_mu. 1 hit.
PRINTSiPR00314. CLATHRINADPT.
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS00990. CLAT_ADAPTOR_M_1. 1 hit.
PS00991. CLAT_ADAPTOR_M_2. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BXS5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSASAVYVLD LKGKVLICRN YRGDVDMSEV EHFMPILMEK EEEGMLSPIL
60 70 80 90 100
AHGGVRFMWI KHNNLYLVAT SKKNACVSLV FSFLYKVVQV FSEYFKELEE
110 120 130 140 150
ESIRDNFVII YELLDELMDF GYPQTTDSKI LQEYITQEGH KLETGAPRPP
160 170 180 190 200
ATVTNAVSWR SEGIKYRKNE VFLDVIESVN LLVSANGNVL RSEIVGSIKM
210 220 230 240 250
RVFLSGMPEL RLGLNDKVLF DNTGRGKSKS VELEDVKFHQ CVRLSRFEND
260 270 280 290 300
RTISFIPPDG EFELMSYRLN THVKPLIWIE SVIEKHSHSR IEYMIKAKSQ
310 320 330 340 350
FKRRSTANNV EIHIPVPNDA DSPKFKTTVG SVKWVPENSE IVWSIKSFPG
360 370 380 390 400
GKEYLMRAHF GLPSVEAEDK EGKPPISVKF EIPYFTTSGI QVRYLKIIEK
410 420
SGYQALPWVR YITQNGDYQL RTQ
Length:423
Mass (Da):48,587
Last modified:January 23, 2007 - v3
Checksum:i64EC5E47EA6F8E98
GO
Isoform 2 (identifier: Q9BXS5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     182-182: L → LGKYPGVGWLGHT

Note: No experimental confirmation available.
Show »
Length:435
Mass (Da):49,840
Checksum:iEEA5A4B9F17D86D9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031R → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036536

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei182 – 1821L → LGKYPGVGWLGHT in isoform 2. 1 PublicationVSP_042542

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290613 mRNA. Translation: AAK28024.1.
DQ059565 mRNA. Translation: AAY54246.1.
AC020911 Genomic DNA. No translation available.
BC017469 mRNA. Translation: AAH17469.1.
CCDSiCCDS12342.1. [Q9BXS5-1]
CCDS46008.1. [Q9BXS5-2]
RefSeqiNP_001123996.1. NM_001130524.1. [Q9BXS5-2]
NP_115882.1. NM_032493.3. [Q9BXS5-1]
UniGeneiHs.71040.

Genome annotation databases

EnsembliENST00000291439; ENSP00000291439; ENSG00000072958. [Q9BXS5-1]
ENST00000444449; ENSP00000388996; ENSG00000072958. [Q9BXS5-2]
GeneIDi8907.
KEGGihsa:8907.
UCSCiuc002ndu.2. human. [Q9BXS5-1]
uc002ndv.2. human. [Q9BXS5-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290613 mRNA. Translation: AAK28024.1.
DQ059565 mRNA. Translation: AAY54246.1.
AC020911 Genomic DNA. No translation available.
BC017469 mRNA. Translation: AAH17469.1.
CCDSiCCDS12342.1. [Q9BXS5-1]
CCDS46008.1. [Q9BXS5-2]
RefSeqiNP_001123996.1. NM_001130524.1. [Q9BXS5-2]
NP_115882.1. NM_032493.3. [Q9BXS5-1]
UniGeneiHs.71040.

3D structure databases

ProteinModelPortaliQ9BXS5.
SMRiQ9BXS5. Positions 2-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114421. 55 interactions.
IntActiQ9BXS5. 31 interactions.
MINTiMINT-1456291.
STRINGi9606.ENSP00000388996.

PTM databases

PhosphoSiteiQ9BXS5.

Polymorphism and mutation databases

BioMutaiAP1M1.
DMDMi18202738.

Proteomic databases

MaxQBiQ9BXS5.
PaxDbiQ9BXS5.
PeptideAtlasiQ9BXS5.
PRIDEiQ9BXS5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291439; ENSP00000291439; ENSG00000072958. [Q9BXS5-1]
ENST00000444449; ENSP00000388996; ENSG00000072958. [Q9BXS5-2]
GeneIDi8907.
KEGGihsa:8907.
UCSCiuc002ndu.2. human. [Q9BXS5-1]
uc002ndv.2. human. [Q9BXS5-2]

Organism-specific databases

CTDi8907.
GeneCardsiGC19P016308.
HGNCiHGNC:13667. AP1M1.
HPAiHPA045256.
MIMi603535. gene.
neXtProtiNX_Q9BXS5.
PharmGKBiPA24848.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG315786.
GeneTreeiENSGT00530000062779.
HOGENOMiHOG000173247.
HOVERGENiHBG050516.
InParanoidiQ9BXS5.
KOiK12393.
OMAiITQNGEY.
PhylomeDBiQ9BXS5.
TreeFamiTF300393.

Enzyme and pathway databases

ReactomeiREACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_121399. MHC class II antigen presentation.
REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinkiQ9BXS5.

Miscellaneous databases

GeneWikiiAP1M1.
GenomeRNAii8907.
NextBioi33467.
PROiQ9BXS5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BXS5.
CleanExiHS_AP1M1.
ExpressionAtlasiQ9BXS5. baseline and differential.
GenevisibleiQ9BXS5. HS.

Family and domain databases

InterProiIPR022775. AP_mu_sigma_su.
IPR001392. Clathrin_mu.
IPR008968. Clathrin_mu_C.
IPR018240. Clathrin_mu_CS.
IPR011012. Longin-like_dom.
IPR028565. MHD.
[Graphical view]
PfamiPF00928. Adap_comp_sub. 1 hit.
PF01217. Clat_adaptor_s. 1 hit.
[Graphical view]
PIRSFiPIRSF005992. Clathrin_mu. 1 hit.
PRINTSiPR00314. CLATHRINADPT.
SUPFAMiSSF49447. SSF49447. 1 hit.
SSF64356. SSF64356. 1 hit.
PROSITEiPS00990. CLAT_ADAPTOR_M_1. 1 hit.
PS00991. CLAT_ADAPTOR_M_2. 1 hit.
PS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-303.
  10. "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.

Entry informationi

Entry nameiAP1M1_HUMAN
AccessioniPrimary (citable) accession number: Q9BXS5
Secondary accession number(s): Q4TTY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.