Protein detail

STALP

AMSH-like protease (AMSH-LP) (EC 3.4.19.-) (STAM-binding protein-like 1)

Entry name
STALP
UniProt ID
EVMP confidence score
0.38
Supporting publications (n)
1
Transmembrane count
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
AMSH-like protease (AMSH-LP) (EC 3.4.19.-) (STAM-binding protein-like 1)
Protein Class (3)
EnzymesMetabolic proteinsPredicted intracellular proteins
Protein Function (3)
  • Peptidases:Metallopeptidases
  • Enzymes
  • Predicted intracellular proteins
Entrez Gene Symbol
Gene Synonym (6)
ALMalphaAMSH-FPAMSH-LPbA399O19.2FLJ31524KIAA1373
Gene Description
STAM binding protein like 1
Chromosome
10
Position
88879734-88975153
Supporting publications (n)
1
EVMP confidence score
0.38
Fluorescence & Localization1
Cell SpecificNeutrophils
Function & Pathway5
Relations & Evidence6

Ligand-Receptor Signaling (4)

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Protein Complex Composition (1)

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
CLTCL1PICALMSTAMBPL1P53675Q13492Q96FJ00:0:0hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Polymer PrecipitationWestern blotting138731868
Sequence, Structure & Domains14

Sequences

Length
436
Mass
49,783
Sequence
MDQPFTVNSLKKLAAMPDHTDVSLSPEERVRALSKLGCNITISEDITPRRYFRSGVEMERMASVYLEEGNLENAFVLYNKFITLFVEKLPNHRDYQQCAVPEKQDIMKKLKEIAFPRTDELKNDLLKKYNVEYQEYLQSKNKYKAEILKKLEHQRLIEAERKRIAQMRQQQLESEQFLFFEDQLKKQELARGQMRSQQTSGLSEQIDGSALSCFSTHQNNSLLNVFADQPNKSDATNYASHSPPVNRALTPAATLSAVQNLVVEGLRCVVLPEDLCHKFLQLAESNTVRGIETCGILCGKLTHNEFTITHVIVPKQSAGPDYCDMENVEELFNVQDQHDLLTLGWIHTHPTQTAFLSSVDLHTHCSYQLMLPEAIAIVCSPKHKDTGIFRLTNAGMLEVSACKKKGFHPHTKEPRLFSICKHVLVKDIKIIVLDLR
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q96FJ0-1; Sequence=Displayed; Name=2; IsoId=Q96FJ0-2; Sequence=VSP_014648
Alternative Sequence
420..436; CKHVLVKDIKIIVLDLR -> QKFLSGIISGTALEMEPLKIGYGPNGFPLLGISRSSSPSEQL (in isoform 2)

3D Structural Models

Turn
288..290
Helix
275..287; 328..338; 358..370; 381..383; 393..401
Beta Strand
269..272; 294..302; 305..313; 316..319; 322..325; 341..348; 350..352; 375..380; 385..391; 416..419; 421..426; 431..434
3D Structure
X-ray crystallography (3)

Domain & Motif Annotations

Motif
347..360; JAMM motif
Domain (CC)
The JAMM motif is essential for the protease activity.
Domain (FT)
269..397; MPN
Protein Families
Peptidase M67C family
Sequence Similarities
Belongs to the peptidase M67C family.
Clinical Relevance4
Antibody
Interaction Protein (2)
ENSG00000105982ENSG00000221867
Interaction Count
2
Interaction Dataset (2)
intact_biogridintact_biogrid_bioplex
Supporting Publications1
PMIDTitleAbstract
40689422Defining the Ovarian Cancer Precancerous Landscape through Modeling Fallopian Tube Epithelium Reprogramming Driven by Extracellular Vesicles.No abstract available