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P61966

- AP1S1_HUMAN

UniProt

P61966 - AP1S1_HUMAN

Protein

AP-1 complex subunit sigma-1A

Gene

AP1S1

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

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

    GO - Molecular functioni

    1. protein transporter activity Source: InterPro

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. intracellular protein transport Source: InterPro
    3. membrane organization Source: Reactome
    4. post-Golgi vesicle-mediated transport Source: Reactome
    5. receptor-mediated endocytosis Source: UniProtKB
    6. regulation of defense response to virus by virus Source: Reactome
    7. response to virus Source: UniProtKB
    8. viral process Source: Reactome

    Keywords - Biological processi

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-1 complex subunit sigma-1A
    Alternative name(s):
    Adaptor protein complex AP-1 subunit sigma-1A
    Adaptor-related protein complex 1 subunit sigma-1A
    Clathrin assembly protein complex 1 sigma-1A small chain
    Clathrin coat assembly protein AP19
    Golgi adaptor HA1/AP1 adaptin sigma-1A subunit
    HA1 19 kDa subunit
    Sigma 1a subunit of AP-1 clathrin
    Sigma-adaptin 1A
    Sigma1A-adaptin
    Gene namesi
    Name:AP1S1
    Synonyms:AP19, CLAPS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:559. AP1S1.

    Subcellular locationi

    Golgi apparatus 1 Publication. Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Membraneclathrin-coated pit 1 Publication
    Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.

    GO - Cellular componenti

    1. AP-1 adaptor complex Source: UniProtKB
    2. coated pit Source: UniProtKB-SubCell
    3. cytoplasmic vesicle membrane Source: Reactome
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi membrane Source: Reactome
    7. lysosomal membrane Source: Reactome
    8. membrane Source: UniProtKB
    9. trans-Golgi network membrane Source: Reactome

    Keywords - Cellular componenti

    Coated pit, Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, enteropathy, deafness, peripheral neuropathy, ichthyosis, and keratoderma (MEDNIK) [MIM:609313]: A disorder characterized by erythematous skin lesions and hyperkeratosis, severe psychomotor retardation, peripheral neuropathy, sensorineural hearing loss, together with elevated very-long-chain fatty acids and severe congenital diarrhea.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Deafness, Ichthyosis, Mental retardation, Neuropathy

    Organism-specific databases

    MIMi609313. phenotype.
    Orphaneti171851. MEDNIK syndrome.
    PharmGKBiPA24850.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 158158AP-1 complex subunit sigma-1APRO_0000193797Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei147 – 1471Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP61966.
    PaxDbiP61966.
    PRIDEiP61966.

    PTM databases

    PhosphoSiteiP61966.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Inductioni

    Up-regulated in response to enterovirus 71 (EV71) infection.1 Publication

    Gene expression databases

    BgeeiP61966.
    CleanExiHS_AP1S1.
    GenevestigatoriP61966.

    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).

    Protein-protein interaction databases

    BioGridi107588. 12 interactions.
    MINTiMINT-5006039.
    STRINGi9606.ENSP00000336666.

    Structurei

    Secondary structure

    1
    158
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98
    Beta strandi14 – 218
    Helixi25 – 4016
    Beta strandi48 – 525
    Beta strandi55 – 628
    Beta strandi65 – 717
    Helixi77 – 9519
    Helixi100 – 1056
    Helixi107 – 11711
    Beta strandi122 – 1243
    Helixi128 – 14619

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4P6ZX-ray3.00S1-158[»]
    ProteinModelPortaliP61966.
    SMRiP61966. Positions 1-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5030.
    HOVERGENiHBG050517.
    InParanoidiP61966.
    KOiK12394.
    OrthoDBiEOG7S7SGC.
    PhylomeDBiP61966.
    TreeFamiTF312921.

    Family and domain databases

    InterProiIPR016635. AP_complex_ssu.
    IPR022775. AP_mu_sigma_su.
    IPR000804. Clathrin_sm-chain_CS.
    IPR011012. Longin-like_dom.
    [Graphical view]
    PANTHERiPTHR11753. PTHR11753. 1 hit.
    PfamiPF01217. Clat_adaptor_s. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015588. AP_complex_sigma. 1 hit.
    SUPFAMiSSF64356. SSF64356. 1 hit.
    PROSITEiPS00989. CLAT_ADAPTOR_S. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61966-1) [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

    MMRFMLLFSR QGKLRLQKWY LATSDKERKK MVRELMQVVL ARKPKMCSFL    50
    EWRDLKVVYK RYASLYFCCA IEGQDNELIT LELIHRYVEL LDKYFGSVCE 100
    LDIIFNFEKA YFILDEFLMG GDVQDTSKKS VLKAIEQADL LQEEDESPRS 150
    VLEEMGLA 158
    Length:158
    Mass (Da):18,733
    Last modified:June 7, 2004 - v1
    Checksum:iE461937790406D8B
    GO
    Isoform 2 (identifier: P61966-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-158: KKSVLKAIEQADLLQEEDESPRSVLEEMGLA → TFPFSH

    Show »
    Length:133
    Mass (Da):16,011
    Checksum:i3FB1FD64446EBFD6
    GO

    Sequence cautioni

    The sequence AAD45829.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei128 – 15831KKSVL…EMGLA → TFPFSH in isoform 2. 2 PublicationsVSP_000171Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015319 mRNA. Translation: BAA33391.1.
    BT006779 mRNA. Translation: AAP35425.1.
    AK312151 mRNA. Translation: BAG35085.1.
    AC004876 Genomic DNA. Translation: AAD45829.1. Different initiation.
    CH471197 Genomic DNA. Translation: EAW50199.1.
    BC003561 mRNA. Translation: AAH03561.1.
    CCDSiCCDS47669.1.
    RefSeqiNP_001274.1. NM_001283.3. [P61966-1]
    UniGeneiHs.489365.

    Genome annotation databases

    EnsembliENST00000337619; ENSP00000336666; ENSG00000106367. [P61966-1]
    ENST00000443943; ENSP00000410780; ENSG00000106367. [P61966-1]
    GeneIDi1174.
    KEGGihsa:1174.
    UCSCiuc003uxv.4. human.

    Polymorphism databases

    DMDMi48428719.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015319 mRNA. Translation: BAA33391.1 .
    BT006779 mRNA. Translation: AAP35425.1 .
    AK312151 mRNA. Translation: BAG35085.1 .
    AC004876 Genomic DNA. Translation: AAD45829.1 . Different initiation.
    CH471197 Genomic DNA. Translation: EAW50199.1 .
    BC003561 mRNA. Translation: AAH03561.1 .
    CCDSi CCDS47669.1.
    RefSeqi NP_001274.1. NM_001283.3. [P61966-1 ]
    UniGenei Hs.489365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4P6Z X-ray 3.00 S 1-158 [» ]
    ProteinModelPortali P61966.
    SMRi P61966. Positions 1-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107588. 12 interactions.
    MINTi MINT-5006039.
    STRINGi 9606.ENSP00000336666.

    PTM databases

    PhosphoSitei P61966.

    Polymorphism databases

    DMDMi 48428719.

    Proteomic databases

    MaxQBi P61966.
    PaxDbi P61966.
    PRIDEi P61966.

    Protocols and materials databases

    DNASUi 1174.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337619 ; ENSP00000336666 ; ENSG00000106367 . [P61966-1 ]
    ENST00000443943 ; ENSP00000410780 ; ENSG00000106367 . [P61966-1 ]
    GeneIDi 1174.
    KEGGi hsa:1174.
    UCSCi uc003uxv.4. human.

    Organism-specific databases

    CTDi 1174.
    GeneCardsi GC07P100797.
    HGNCi HGNC:559. AP1S1.
    MIMi 603531. gene.
    609313. phenotype.
    neXtProti NX_P61966.
    Orphaneti 171851. MEDNIK syndrome.
    PharmGKBi PA24850.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5030.
    HOVERGENi HBG050517.
    InParanoidi P61966.
    KOi K12394.
    OrthoDBi EOG7S7SGC.
    PhylomeDBi P61966.
    TreeFami TF312921.

    Enzyme and pathway databases

    Reactomei REACT_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.

    Miscellaneous databases

    GeneWikii AP1S1.
    GenomeRNAii 1174.
    NextBioi 4850.
    PROi P61966.
    SOURCEi Search...

    Gene expression databases

    Bgeei P61966.
    CleanExi HS_AP1S1.
    Genevestigatori P61966.

    Family and domain databases

    InterProi IPR016635. AP_complex_ssu.
    IPR022775. AP_mu_sigma_su.
    IPR000804. Clathrin_sm-chain_CS.
    IPR011012. Longin-like_dom.
    [Graphical view ]
    PANTHERi PTHR11753. PTHR11753. 1 hit.
    Pfami PF01217. Clat_adaptor_s. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015588. AP_complex_sigma. 1 hit.
    SUPFAMi SSF64356. SSF64356. 1 hit.
    PROSITEi PS00989. CLAT_ADAPTOR_S. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of novel clathrin adaptor-related proteins."
      Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.
      J. Biol. Chem. 273:24693-24700(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "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.
      , 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] (ISOFORM 1).
      Tissue: Caudate nucleus.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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 2).
      Tissue: Placenta.
    7. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
      Leong W.F., Chow V.T.
      Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Disruption of AP1S1, causing a novel neurocutaneous syndrome, perturbs development of the skin and spinal cord."
      Montpetit A., Cote S., Brustein E., Drouin C.A., Lapointe L., Boudreau M., Meloche C., Drouin R., Hudson T.J., Drapeau P., Cossette P.
      PLoS Genet. 4:E1000296-E1000296(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MEDNIK.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAP1S1_HUMAN
    AccessioniPrimary (citable) accession number: P61966
    Secondary accession number(s): B2R5D8
    , P82267, Q00382, Q53YA7, Q9BTN4, Q9UDW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3