Protein detail
SHRM2
Protein Shroom2 (Apical-like protein) (Protein APXL)
Entry name SHRM2 | UniProt ID | EVMP confidence score 0.40 |
Supporting publications (n) 3 | Transmembrane count | Protein classification Plasma proteinsPredicted intracellular proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
Protein Names
Protein Shroom2 (Apical-like protein) (Protein APXL)
Protein Class (2)
Plasma proteinsPredicted intracellular proteins
Protein Function
Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym
APXL
Gene Description
Shroom family member 2
Chromosome
X
Position
9786429-9949443
Supporting publications (n)
3
EVMP confidence score
0.40
Fluorescence & Localization
Cell SpecificEsophageal apical cells
Function & Pathway
Protein Function
Predicted intracellular proteins
Cellular Component (9)
Molecular Function (5)
Biological Process (3)
Mediation Categories
Fusion and delivery mediation
Relations & Evidence12
Ligand-Receptor Signaling (9)
9 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath | |||||
| tight_junction | tight_junction | GO_Intercell | Yes | Yes | |||
| tight_junction | tight_junction | OmniPath | Yes | Yes | |||
| plasma_membrane | plasma_membrane | UniProt_location | |||||
| apical_cell_membrane | plasma_membrane | UniProt_location | |||||
| plasma_membrane | plasma_membrane | OmniPath |
Protein Complex Composition (2)
Sequence, Structure & Domains
Sequences
Length
1,616
Mass
176,410
Sequence
MEGAEPRARPERLAEAETRAADGGRLVEVQLSGGAPWGFTLKGGREHGEPLVITKIEEGSKAAAVDKLLAGDEIVGINDIGLSGFRQEAICLVKGSHKTLKLVVKRRSELGWRPHSWHATKFSDSHPELAASPFTSTSGCPSWSGRHHASSSSHDLSSSWEQTNLQRTLDHFSSLGSVDSLDHPSSRLSVAKSNSSIDHLGSHSKRDSAYGSFSTSSSTPDHTLSKADTSSAENILYTVGLWEAPRQGGRQAQAAGDPQGSEEKLSCFPPRVPGDSGKGPRPEYNAEPKLAAPGRSNFGPVWYVPDKKKAPSSPPPPPPPLRSDSFAATKSHEKAQGPVFSEAAAAQHFTALAQAQPRGDRRPELTDRPWRSAHPGSLGKGSGGPGCPQEAHADGSWPPSKDGASSRLQASLSSSDVRFPQSPHSGRHPPLYSDHSPLCADSLGQEPGAASFQNDSPPQVRGLSSCDQKLGSGWQGPRPCVQGDLQAAQLWAGCWPSDTALGALESLPPPTVGQSPRHHLPQPEGPPDARETGRCYPLDKGAEGCSAGAQEPPRASRAEKASQRLAASITWADGESSRICPQETPLLHSLTQEGKRRPESSPEDSATRPPPFDAHVGKPTRRSDRFATTLRNEIQMHRAKLQKSRSTVALTAAGEAEDGTGRWRAGLGGGTQEGPLAGTYKDHLKEAQARVLRATSFKRRDLDPNPGDLYPESLEHRMGDPDTVPHFWEAGLAQPPSSTSGGPHPPRIGGRRRFTAEQKLKSYSEPEKMNEVGLTRGYSPHQHPRTSEDTVGTFADRWKFFEETSKPVPQRPAQKQALHGIPRDKPERPRTAGRTCEGTEPWSRTTSLGDSLNAHSAAEKAGTSDLPRRLGTFAEYQASWKEQRKPLEARSSGRCHSADDILDVSLDPQERPQHVHGRSRSSPSTDHYKQEASVELRRQAGDPGEPREELPSAVRAEEGQSTPRQADAQCREGSPGSQQHPPSQKAPNPPTFSELSHCRGAPELPREGRGRAGTLPRDYRYSEESTPADLGPRAQSPGSPLHARGQDSWPVSSALLSKRPAPQRPPPPKREPRRYRATDGAPADAPVGVLGRPFPTPSPASLDVYVARLSLSHSPSVFSSAQPQDTPKATVCERGSQHVSGDASRPLPEALLPPKQQHLRLQTATMETSRSPSPQFAPQKLTDKPPLLIQDEDSTRIERVMDNNTTVKMVPIKIVHSESQPEKESRQSLACPAEPPALPHGLEKDQIKTLSTSEQFYSRFCLYTRQGAEPEAPHRAQPAEPQPLGTQVPPEKDRCTSPPGLSYMKAKEKTVEDLKSEELAREIVGKDKSLADILDPSVKIKTTMDLMEGIFPKDEHLLEEAQQRRKLLPKIPSPRSTEERKEEPSVPAAVSLATNSTYYSTSAPKAELLIKMKDLQEQQEHEEDSGSDLDHDLSVKKQELIESISRKLQVLREARESLLEDVQANTVLGAEVEAIVKGVCKPSEFDKFRMFIGDLDKVVNLLLSLSGRLARVENALNNLDDGASPGDRQSLLEKQRVLIQQHEDAKELKENLDRRERIVFDILANYLSEESLADYEHFVKMKSALIIEQRELEDKIHLGEEQLKCLLDSLQPERGK
3D Structural Models
Helix
1428..1436; 1438..1479; 1482..1519; 1527..1564; 1569..1604
3D Structure
X-ray crystallography (2)
Domain & Motif Annotations
Compositional Bias
150..159; Low complexity; 186..197; Polar residues; 220..229; Polar residues; 247..259; Low complexity; 312..321; Pro residues; 343..356; Low complexity; 358..370; Basic and acidic residues; 405..415; Low complexity; 754..770; Basic and acidic residues; 821..830; Basic and acidic residues; 842..854; Polar residues; 926..958; Basic and acidic residues; 975..994; Polar residues; 1068..1077; Basic and acidic residues; 1159..1176; Polar residues
Domain (CC)
The ASD1 domain mediates F-actin binding.
Domain (FT)
26..108; PDZ; 684..773; ASD1; 1317..1611; ASD2
Region
128..159; Disordered; 183..229; Disordered; 247..475; Disordered; 502..678; Disordered; 695..790; Disordered; 802..869; Disordered; 881..1100; Disordered; 1115..1184; Disordered; 1268..1302; Disordered; 1363..1389; Disordered
Protein Families
Shroom family
Sequence Similarities
Belongs to the shroom family.
Clinical Relevance
Drugs (50)
SRIF-28BIM 23068BIM 23197[125I]LTT-SRIF-28CORTISTATIN-14SRIF-14MK-4256L-363,301BIM 23050BIM 23052BIM 23454[125I]TYR10-CST14BN-81,674BIM 23056KE 108[111IN,90Y]DOTA-TOCL-796,778[111IN]DOTA-NOCBIM 23627[L-TYR8]CYN 154806VAPREOTIDE[111IN]DOTA-NOC-ATESEGLITIDECST-17OCTREOTIDE ACETATE[111IN,90Y]DOTA-LANPRL-2915[125I]CGP 23996[125I]TYR7-SST3-ODN-8DES-AA5-[D-TRP8]SRIFBIM 23030PASIREOTIDENC 8-12CGP 23996BOC-ATEACQ090[111IN,90Y]DOTA-NOCPRL-2970[D-TYR8]CYN 154806L-362,855[111IN,90Y]DOTA-OCNC 4-28BBN-81,644BIM 23058SST3-ODN-8LANREOTIDE ACETATE[111IN]DOTA-BOC-ATEBIM 23023BIM 23034NOC-ATE
Supporting Publications3
| PMID | Title | Related sentences |
|---|---|---|
| 25755179 | Urinary extracellular vesicles as reservoirs of altered proteins during the pathogenesis of polycystic kidney disease. | No related sentences available |
| 37223008 | Proteomic analysis of urinary extracellular vesicles highlights specific signatures for patients with primary aldosteronism. | No related sentences available |
| 38014595 | Proteome and immune responses of extracellular vesicles derived from macrophages infected with the periodontal pathogen Tannerella forsythia. | No related sentences available |