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Protein

Proline-rich membrane anchor 1

Gene

PRIMA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required to anchor acetylcholinesterase (ACHE) to the basal lamina of the neuromuscular junction and to the membrane of neuronal synapses in brain. Also able to organize ACHE into tetramers (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Neurotransmitter degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-rich membrane anchor 1
Short name:
PRiMA
Gene namesi
Name:PRIMA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:18319. PRIMA1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 9257ExtracellularSequence analysisAdd
BLAST
Transmembranei93 – 11321HelicalSequence analysisAdd
BLAST
Topological domaini114 – 15340CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38315.

Polymorphism and mutation databases

BioMutaiPRIMA1.
DMDMi37537937.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535By similarityAdd
BLAST
Chaini36 – 153118Proline-rich membrane anchor 1PRO_0000022107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ86XR5.
PeptideAtlasiQ86XR5.
PRIDEiQ86XR5.

PTM databases

iPTMnetiQ86XR5.
PhosphoSiteiQ86XR5.

Expressioni

Inductioni

By RAF1.1 Publication

Gene expression databases

BgeeiQ86XR5.
CleanExiHS_PRIMA1.
ExpressionAtlasiQ86XR5. baseline and differential.
GenevisibleiQ86XR5. HS.

Organism-specific databases

HPAiHPA060047.

Interactioni

Subunit structurei

Interacts with ACHE, probably through disulfide bonds.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000376848.

Structurei

3D structure databases

ProteinModelPortaliQ86XR5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 7015PRADAdd
BLAST

Domaini

The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IZWQ. Eukaryota.
ENOG410YWDZ. LUCA.
GeneTreeiENSGT00390000006240.
HOGENOMiHOG000115697.
HOVERGENiHBG053680.
InParanoidiQ86XR5.
OMAiNATSCPA.
OrthoDBiEOG7X9G8R.
PhylomeDBiQ86XR5.
TreeFamiTF337232.

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: Q86XR5-1) [UniParc]FASTAAdd to basket

Also known as: Variant I

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
MLLRDLVLRR GCCWSSLLLH CALHPLWGFV QVTHGEPQKS CSKVTDSCRH
60 70 80 90 100
VCQCRPPPPL PPPPPPPPPP RLLSAPAPNS TSCPTEESWW SGLVIIIAVC
110 120 130 140 150
CASLVFLTVL VIICYKAIKR KPLRKDENGT SVAEYPMSAS QSNKGVDVNN

AVV
Length:153
Mass (Da):16,689
Last modified:October 3, 2003 - v2
Checksum:i2F82EA50F0F87EC1
GO
Isoform 2 (identifier: Q86XR5-2) [UniParc]FASTAAdd to basket

Also known as: Variant II

The sequence of this isoform differs from the canonical sequence as follows:
     121-124: KPLR → NHAI
     125-153: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:124
Mass (Da):13,636
Checksum:i4E4FF3CE50A0B434
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035980

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei121 – 1244KPLR → NHAI in isoform 2. 1 PublicationVSP_008494
Alternative sequencei125 – 15329Missing in isoform 2. 1 PublicationVSP_008495Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY225516 mRNA. Translation: AAO74853.1.
AY225517 mRNA. Translation: AAO74854.1.
CCDSiCCDS9912.1. [Q86XR5-1]
RefSeqiNP_821092.1. NM_178013.3. [Q86XR5-1]
XP_011534758.1. XM_011536456.1. [Q86XR5-1]
XP_011544946.1. XM_011546644.1. [Q86XR5-1]
UniGeneiHs.432401.

Genome annotation databases

EnsembliENST00000316227; ENSP00000320948; ENSG00000175785. [Q86XR5-2]
ENST00000393140; ENSP00000376848; ENSG00000175785. [Q86XR5-1]
ENST00000393143; ENSP00000376851; ENSG00000175785. [Q86XR5-1]
ENST00000477603; ENSP00000434370; ENSG00000175785. [Q86XR5-2]
ENST00000611347; ENSP00000479082; ENSG00000274089. [Q86XR5-1]
ENST00000617019; ENSP00000479855; ENSG00000274089. [Q86XR5-2]
ENST00000627063; ENSP00000486875; ENSG00000274089. [Q86XR5-2]
ENST00000629961; ENSP00000486953; ENSG00000274089. [Q86XR5-1]
GeneIDi145270.
KEGGihsa:145270.
UCSCiuc001ybw.2. human. [Q86XR5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY225516 mRNA. Translation: AAO74853.1.
AY225517 mRNA. Translation: AAO74854.1.
CCDSiCCDS9912.1. [Q86XR5-1]
RefSeqiNP_821092.1. NM_178013.3. [Q86XR5-1]
XP_011534758.1. XM_011536456.1. [Q86XR5-1]
XP_011544946.1. XM_011546644.1. [Q86XR5-1]
UniGeneiHs.432401.

3D structure databases

ProteinModelPortaliQ86XR5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000376848.

PTM databases

iPTMnetiQ86XR5.
PhosphoSiteiQ86XR5.

Polymorphism and mutation databases

BioMutaiPRIMA1.
DMDMi37537937.

Proteomic databases

PaxDbiQ86XR5.
PeptideAtlasiQ86XR5.
PRIDEiQ86XR5.

Protocols and materials databases

DNASUi145270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316227; ENSP00000320948; ENSG00000175785. [Q86XR5-2]
ENST00000393140; ENSP00000376848; ENSG00000175785. [Q86XR5-1]
ENST00000393143; ENSP00000376851; ENSG00000175785. [Q86XR5-1]
ENST00000477603; ENSP00000434370; ENSG00000175785. [Q86XR5-2]
ENST00000611347; ENSP00000479082; ENSG00000274089. [Q86XR5-1]
ENST00000617019; ENSP00000479855; ENSG00000274089. [Q86XR5-2]
ENST00000627063; ENSP00000486875; ENSG00000274089. [Q86XR5-2]
ENST00000629961; ENSP00000486953; ENSG00000274089. [Q86XR5-1]
GeneIDi145270.
KEGGihsa:145270.
UCSCiuc001ybw.2. human. [Q86XR5-1]

Organism-specific databases

CTDi145270.
GeneCardsiPRIMA1.
H-InvDBHIX0037698.
HGNCiHGNC:18319. PRIMA1.
HPAiHPA060047.
MIMi613851. gene.
neXtProtiNX_Q86XR5.
PharmGKBiPA38315.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZWQ. Eukaryota.
ENOG410YWDZ. LUCA.
GeneTreeiENSGT00390000006240.
HOGENOMiHOG000115697.
HOVERGENiHBG053680.
InParanoidiQ86XR5.
OMAiNATSCPA.
OrthoDBiEOG7X9G8R.
PhylomeDBiQ86XR5.
TreeFamiTF337232.

Miscellaneous databases

ChiTaRSiPRIMA1. human.
GeneWikiiPRIMA1.
GenomeRNAii145270.
PROiQ86XR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ86XR5.
CleanExiHS_PRIMA1.
ExpressionAtlasiQ86XR5. baseline and differential.
GenevisibleiQ86XR5. HS.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PRiMA: the membrane anchor of acetylcholinesterase in the brain."
    Perrier A.L., Massoulie J., Krejci E.
    Neuron 33:275-285(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Transcriptional regulation of proline-rich membrane anchor (PRiMA) of globular form acetylcholinesterase in neuron: an inductive effect of neuron differentiation."
    Xie H.Q., Choi R.C., Leung K.W., Chen V.P., Chu G.K., Tsim K.W.
    Brain Res. 1265:13-23(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  3. "N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase."
    Chan W.K., Chen V.P., Luk W.K., Choi R.C., Tsim K.W.
    Neurosci. Lett. 523:71-75(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-79.
  4. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-22.

Entry informationi

Entry nameiPRIMA_HUMAN
AccessioniPrimary (citable) accession number: Q86XR5
Secondary accession number(s): Q86XR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: July 6, 2016
This is version 102 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

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 one 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.