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O60888

- CUTA_HUMAN

UniProt

O60888 - CUTA_HUMAN

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Protein
Protein CutA
Gene
CUTA, ACHAP, C6orf82
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE).1 Publication

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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134928220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 179147Protein CutA
PRO_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

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.

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.

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.
VSP_013226Add
BLAST
Alternative sequencei1 – 1414MSGGR…LLGGV → MIGSGLAGSGGAGGPSSTVT WCALFSNHVAATQ in isoform A.
VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 117 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

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