Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O60888

- CUTA_HUMAN

UniProt

O60888 - CUTA_HUMAN

Protein

Protein CutA

Gene

CUTA

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

    May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein localization Source: UniProtKB
    2. response to metal ion Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein CutA
    Alternative name(s):
    Acetylcholinesterase-associated protein
    Brain acetylcholinesterase putative membrane anchor
    Gene namesi
    Name:CUTA
    Synonyms:ACHAP, C6orf82
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21101. CUTA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134928220.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 179147Protein CutAPRO_0000006379Add
    BLAST

    Post-translational modificationi

    O-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiO60888.
    PaxDbiO60888.
    PRIDEiO60888.

    PTM databases

    PhosphoSiteiO60888.

    Expressioni

    Tissue specificityi

    Ubiquitous. Widely expressed in brain.1 Publication

    Gene expression databases

    ArrayExpressiO60888.
    BgeeiO60888.
    CleanExiHS_CUTA.
    GenevestigatoriO60888.

    Organism-specific databases

    HPAiCAB016787.

    Interactioni

    Subunit structurei

    Homotrimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NR4A1P227362EBI-1051556,EBI-721550

    Protein-protein interaction databases

    BioGridi119628. 7 interactions.
    IntActiO60888. 7 interactions.

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi67 – 7711
    Helixi78 – 9013
    Beta strandi95 – 10915
    Beta strandi112 – 12615
    Helixi127 – 1293
    Helixi130 – 14011
    Beta strandi142 – 1454
    Beta strandi148 – 1536
    Helixi158 – 1669

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XK8X-ray2.70A/B/C/D/E/F44-179[»]
    2ZFHX-ray2.05A/B/C/D/E/F1-179[»]
    ProteinModelPortaliO60888.
    SMRiO60888. Positions 61-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60888.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni168 – 1769O-glycosylated at one site

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 374Poly-Leu

    Sequence similaritiesi

    Belongs to the CutA family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1324.
    HOVERGENiHBG051265.
    KOiK03926.
    OMAiPVEQGNS.
    PhylomeDBiO60888.
    TreeFamiTF313269.

    Family and domain databases

    InterProiIPR004323. Ion_tolerance_CutA.
    IPR011322. N-reg_PII-like_a/b.
    [Graphical view]
    PANTHERiPTHR23419. PTHR23419. 1 hit.
    PfamiPF03091. CutA1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54913. SSF54913. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: O60888-1) [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

    MSGGRAPAVL LGGVASLLLS FVWMPALLPV ASRLLLLPRV LLTMASGSPP    50
    TQPSPASDSG SGYVPGSVSA AFVTCPNEKV AKEIARAVVE KRLAACVNLI 100
    PQITSIYEWK GKIEEDSEVL MMIKTQSSLV PALTDFVRSV HPYEVAEVIA 150
    LPVEQGNFPY LQWVRQVTES VSDSITVLP 179

    Note: No experimental confirmation available.

    Length:179
    Mass (Da):19,116
    Last modified:March 29, 2005 - v2
    Checksum:iB8EBD7F8C069862A
    GO
    Isoform A (identifier: O60888-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: MSGGRAPAVLLGGV → MIGSGLAGSGGAGGPSSTVTWCALFSNHVAATQ

    Note: No experimental confirmation available.

    Show »
    Length:198
    Mass (Da):20,925
    Checksum:i6FF4D190577FBA1A
    GO
    Isoform C (identifier: O60888-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Show »
    Length:156
    Mass (Da):16,833
    Checksum:i9438E6E87D96F3EF
    GO

    Sequence cautioni

    The sequence AAF61220.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform C. 3 PublicationsVSP_013226Add
    BLAST
    Alternative sequencei1 – 1414MSGGR…LLGGV → MIGSGLAGSGGAGGPSSTVT WCALFSNHVAATQ in isoform A. CuratedVSP_013225Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230924 mRNA. Translation: AAF61220.1. Different initiation.
    AF106943 mRNA. Translation: AAD21026.1.
    AL050332 Genomic DNA. Translation: CAB63779.1.
    AL021366 Genomic DNA. Translation: CAA16160.1.
    AL662799 Genomic DNA. Translation: CAI18273.2.
    AL662799 Genomic DNA. Translation: CAM25571.1.
    BX088650 Genomic DNA. Translation: CAM26302.1.
    BX088650 Genomic DNA. Translation: CAM26303.1.
    BC005890 mRNA. Translation: AAH05890.1.
    BC107751 mRNA. Translation: AAI07752.1.
    CCDSiCCDS34432.1. [O60888-2]
    CCDS34433.1. [O60888-1]
    CCDS4779.1. [O60888-3]
    RefSeqiNP_001014433.1. NM_001014433.2. [O60888-2]
    NP_001014837.1. NM_001014837.1. [O60888-3]
    NP_001014838.1. NM_001014838.1. [O60888-3]
    NP_001014840.1. NM_001014840.1. [O60888-1]
    NP_057005.1. NM_015921.2. [O60888-3]
    XP_006715171.1. XM_006715108.1. [O60888-1]
    XP_006726159.1. XM_006726096.1. [O60888-1]
    UniGeneiHs.520070.

    Genome annotation databases

    EnsembliENST00000374496; ENSP00000363620; ENSG00000112514. [O60888-3]
    ENST00000374500; ENSP00000363624; ENSG00000112514. [O60888-2]
    ENST00000435267; ENSP00000391509; ENSG00000226492. [O60888-2]
    ENST00000440279; ENSP00000403268; ENSG00000112514. [O60888-3]
    ENST00000440930; ENSP00000400114; ENSG00000226492. [O60888-1]
    ENST00000487148; ENSP00000432744; ENSG00000226492. [O60888-3]
    ENST00000488034; ENSP00000417544; ENSG00000112514. [O60888-1]
    ENST00000607266; ENSP00000475963; ENSG00000112514. [O60888-3]
    GeneIDi51596.
    KEGGihsa:51596.
    UCSCiuc003oej.1. human. [O60888-1]
    uc003oen.1. human. [O60888-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230924 mRNA. Translation: AAF61220.1 . Different initiation.
    AF106943 mRNA. Translation: AAD21026.1 .
    AL050332 Genomic DNA. Translation: CAB63779.1 .
    AL021366 Genomic DNA. Translation: CAA16160.1 .
    AL662799 Genomic DNA. Translation: CAI18273.2 .
    AL662799 Genomic DNA. Translation: CAM25571.1 .
    BX088650 Genomic DNA. Translation: CAM26302.1 .
    BX088650 Genomic DNA. Translation: CAM26303.1 .
    BC005890 mRNA. Translation: AAH05890.1 .
    BC107751 mRNA. Translation: AAI07752.1 .
    CCDSi CCDS34432.1. [O60888-2 ]
    CCDS34433.1. [O60888-1 ]
    CCDS4779.1. [O60888-3 ]
    RefSeqi NP_001014433.1. NM_001014433.2. [O60888-2 ]
    NP_001014837.1. NM_001014837.1. [O60888-3 ]
    NP_001014838.1. NM_001014838.1. [O60888-3 ]
    NP_001014840.1. NM_001014840.1. [O60888-1 ]
    NP_057005.1. NM_015921.2. [O60888-3 ]
    XP_006715171.1. XM_006715108.1. [O60888-1 ]
    XP_006726159.1. XM_006726096.1. [O60888-1 ]
    UniGenei Hs.520070.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XK8 X-ray 2.70 A/B/C/D/E/F 44-179 [» ]
    2ZFH X-ray 2.05 A/B/C/D/E/F 1-179 [» ]
    ProteinModelPortali O60888.
    SMRi O60888. Positions 61-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119628. 7 interactions.
    IntActi O60888. 7 interactions.

    PTM databases

    PhosphoSitei O60888.

    Proteomic databases

    MaxQBi O60888.
    PaxDbi O60888.
    PRIDEi O60888.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374496 ; ENSP00000363620 ; ENSG00000112514 . [O60888-3 ]
    ENST00000374500 ; ENSP00000363624 ; ENSG00000112514 . [O60888-2 ]
    ENST00000435267 ; ENSP00000391509 ; ENSG00000226492 . [O60888-2 ]
    ENST00000440279 ; ENSP00000403268 ; ENSG00000112514 . [O60888-3 ]
    ENST00000440930 ; ENSP00000400114 ; ENSG00000226492 . [O60888-1 ]
    ENST00000487148 ; ENSP00000432744 ; ENSG00000226492 . [O60888-3 ]
    ENST00000488034 ; ENSP00000417544 ; ENSG00000112514 . [O60888-1 ]
    ENST00000607266 ; ENSP00000475963 ; ENSG00000112514 . [O60888-3 ]
    GeneIDi 51596.
    KEGGi hsa:51596.
    UCSCi uc003oej.1. human. [O60888-1 ]
    uc003oen.1. human. [O60888-2 ]

    Organism-specific databases

    CTDi 51596.
    GeneCardsi GC06M033384.
    GC06Mo33523.
    HGNCi HGNC:21101. CUTA.
    HPAi CAB016787.
    neXtProti NX_O60888.
    PharmGKBi PA134928220.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1324.
    HOVERGENi HBG051265.
    KOi K03926.
    OMAi PVEQGNS.
    PhylomeDBi O60888.
    TreeFami TF313269.

    Miscellaneous databases

    ChiTaRSi CUTA. human.
    EvolutionaryTracei O60888.
    GenomeRNAii 51596.
    NextBioi 55447.
    PROi O60888.

    Gene expression databases

    ArrayExpressi O60888.
    Bgeei O60888.
    CleanExi HS_CUTA.
    Genevestigatori O60888.

    Family and domain databases

    InterProi IPR004323. Ion_tolerance_CutA.
    IPR011322. N-reg_PII-like_a/b.
    [Graphical view ]
    PANTHERi PTHR23419. PTHR23419. 1 hit.
    Pfami PF03091. CutA1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54913. SSF54913. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Hydrophobic protein that copurifies with human brain acetylcholinesterase: amino acid sequence, genomic organization, and chromosomal localization."
      Navaratnam D.S., Fernando F.S., Priddle J.D., Giles K., Clegg S.M., Pappin D.J.C., Craig I., Smith A.D.
      J. Neurochem. 74:2146-2153(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), PROTEIN SEQUENCE OF 70-74 AND 84-178, TISSUE SPECIFICITY, PUTATIVE FUNCTION.
    2. "Cloning and isolating human CUTA cDNA."
      Luo W.Q., Chen J.H., Huan X.W., Zhou Y., Yuan J.G., Qiang B.Q.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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 C).
      Tissue: Placenta.
    5. "Two distinct proteins are associated with tetrameric acetylcholinesterase on the cell surface."
      Perrier A.L., Cousin X., Boschetti N., Haas R., Chatel J.-M., Bon S., Roberts W.L., Pickett S.R., Massoulie J., Rosenberry T.L., Krejci E.
      J. Biol. Chem. 275:34260-34265(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS A; B AND C).
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Divalent cation tolerant protein CUTA from Homo sapiens O60888."
      Southeast collaboratory for structural genomics (SECSG)
      Submitted (SEP-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 44-179.

    Entry informationi

    Entry nameiCUTA_HUMAN
    AccessioniPrimary (citable) accession number: O60888
    Secondary accession number(s): A2AB26
    , A2BEL4, Q3B784, Q5JXM9, Q5SU05, Q9NYQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3