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O60888 (CUTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Protein CutA
Alternative name(s):
Acetylcholinesterase-associated protein
Brain acetylcholinesterase putative membrane anchor
Gene names
Name:CUTA
Synonyms:ACHAP, C6orf82
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homotrimer.

Tissue specificity

Ubiquitous. Widely expressed in brain. Ref.1

Post-translational modification

O-glycosylated. Ref.7

Sequence similarities

Belongs to the CutA family.

Sequence caution

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

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NR4A1P227362EBI-1051556,EBI-721550

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: O60888-1)

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.
Note: No experimental confirmation available.
Isoform A (identifier: O60888-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MSGGRAPAVLLGGV → MIGSGLAGSGGAGGPSSTVTWCALFSNHVAATQ
Note: No experimental confirmation available.
Isoform C (identifier: O60888-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 179147Protein CutA
PRO_0000006379

Regions

Region168 – 1769O-glycosylated at one site
Compositional bias34 – 374Poly-Leu

Natural variations

Alternative sequence1 – 2323Missing in isoform C.
VSP_013226
Alternative sequence1 – 1414MSGGR…LLGGV → MIGSGLAGSGGAGGPSSTVT WCALFSNHVAATQ in isoform A.
VSP_013225

Secondary structure

................ 179
Helix Strand Turn

Details...

Sequences

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

Last modified March 29, 2005. Version 2.
Checksum: B8EBD7F8C069862A

FASTA17919,116
        10         20         30         40         50         60 
MSGGRAPAVL LGGVASLLLS FVWMPALLPV ASRLLLLPRV LLTMASGSPP TQPSPASDSG 

        70         80         90        100        110        120 
SGYVPGSVSA AFVTCPNEKV AKEIARAVVE KRLAACVNLI PQITSIYEWK GKIEEDSEVL 

       130        140        150        160        170 
MMIKTQSSLV PALTDFVRSV HPYEVAEVIA LPVEQGNFPY LQWVRQVTES VSDSITVLP 

« Hide

Isoform A [UniParc].

Checksum: 6FF4D190577FBA1A
Show »

FASTA19820,925
Isoform C [UniParc].

Checksum: 9438E6E87D96F3EF
Show »

FASTA15616,833

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001014433.1. NM_001014433.2.
NP_001014837.1. NM_001014837.1.
NP_001014838.1. NM_001014838.1.
NP_001014840.1. NM_001014840.1.
NP_057005.1. NM_015921.2.
UniGeneHs.520070.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XK8X-ray2.70A/B/C/D/E/F44-179[»]
2ZFHX-ray2.05A/B/C/D/E/F1-179[»]
ProteinModelPortalO60888.
SMRO60888. Positions 61-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119628. 7 interactions.
IntActO60888. 7 interactions.

PTM databases

PhosphoSiteO60888.

Proteomic databases

PaxDbO60888.
PRIDEO60888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374496; 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]
GeneID51596.
KEGGhsa:51596.
UCSCuc003oej.1. human. [O60888-1]
uc003oen.1. human. [O60888-2]

Organism-specific databases

CTD51596.
GeneCardsGC06M033384.
GC06Mo33523.
HGNCHGNC:21101. CUTA.
HPACAB016787.
neXtProtNX_O60888.
PharmGKBPA134928220.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1324.
HOVERGENHBG051265.
KOK03926.
OMAPVEQGNS.
PhylomeDBO60888.
TreeFamTF313269.

Gene expression databases

ArrayExpressO60888.
BgeeO60888.
CleanExHS_CUTA.
GenevestigatorO60888.

Family and domain databases

InterProIPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]
PANTHERPTHR23419. PTHR23419. 1 hit.
PfamPF03091. CutA1. 1 hit.
[Graphical view]
SUPFAMSSF54913. SSF54913. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCUTA. human.
EvolutionaryTraceO60888.
GenomeRNAi51596.
NextBio55447.
PROO60888.

Entry information

Entry nameCUTA_HUMAN
AccessionPrimary (citable) accession number: O60888
Secondary accession number(s): A2AB26 expand/collapse secondary AC list , A2BEL4, Q3B784, Q5JXM9, Q5SU05, Q9NYQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 114 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM