Protein detail

RAPH1

Ras-associated and pleckstrin homology domains-containing protein 1 (RAPH1) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein) (Lamellipodin) (Proline-rich EVH1 ligand 2) (PREL-2) (Protein RMO1)

Entry name RAPH1	UniProt ID Q70E73	EVMP confidence score 0.40
Supporting publications (n) 5	Transmembrane count	Protein classification Predicted intracellular proteins

Basic Information

Protein Names

Protein Class

Predicted intracellular proteins

Protein Function

Predicted intracellular proteins

Ensembl

ENSG00000173166

Entrez Gene Symbol

RAPH1

Gene Synonym (3)

ALS2CR18ALS2CR9KIAA1681

Gene Description

Ras association (RalGDS/AF-6) and pleckstrin homology domains 1

Chromosome

Position

203394345-203535335

Supporting publications (n)

EVMP confidence score

0.40

Fluorescence & Localization

Tissue SpecificprostateCell SpecificAdipocytesSecretome LocationIntracellular and membraneSecretome FunctionReceptor

Function & Pathway

Protein Function

Predicted intracellular proteins

Cellular Component (6)

Molecular Function

GO:0005515 protein binding

Mediation Categories

Other mediation

Relations & Evidence16

Enzyme-Mediated Modification (4)

4 records.

Substrate Gene Symbol	Enzyme Gene Symbol	Enzyme UniProt ID	Residue Type	Residue Offset	Modification	Database	References
RAPH1	ABL1	P00519	Y	426	phosphorylation	dbPTMPhosphoSiteSIGNOR	SIGNOR:20417104 dbPTM:20417104
RAPH1	ABL1	P00519	Y	456	phosphorylation	dbPTMPhosphoSiteSIGNOR	SIGNOR:20417104 dbPTM:20417104
RAPH1	ABL1	P00519	Y	1,226	phosphorylation	dbPTMPhosphoSiteSIGNOR	SIGNOR:20417104 dbPTM:20417104
RAPH1	ABL1	P00519	Y	513	phosphorylation	PhosphoSiteSIGNOR	SIGNOR:20417104

Ligand-Receptor Signaling (6)

6 records.

Category	Parent	Database
intracellular	intracellular	ComPPI
intracellular	intracellular	GO_Intercell
intracellular	intracellular	UniProt_location
intracellular	intracellular	OmniPath
plasma_membrane	plasma_membrane	UniProt_location
plasma_membrane	plasma_membrane	OmniPath

Regulatory Interaction Network (4)

4 records.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Database	References
ABL1	P00519	RAPH1	Q70E73	Yes	Yes	iPTMnetSIGNORProtMapperdbPTMSIGNOR_ProtMapperSPIKESPIKE_LC	ProtMapper:20417104 SPIKE:20417104 SIGNOR:20417104 SPIKE_LC:20841568 dbPTM:20417104 SPIKE:20841568 SPIKE_LC:20417104
RAPH1	Q70E73	EVL	Q9UI08	Yes	Yes	SIGNOR	SIGNOR:20417104
RAPH1	Q70E73	ENAH	Q8N8S7	Yes	Yes	SIGNOR	SIGNOR:20417104
RAPH1	Q70E73	VASP	P50552	Yes	Yes	SIGNORBioGRID	SIGNOR:20417104 BioGRID:15469845

Protein Complex Composition (1)

1 record.

Component Name	Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs	References
	RAPH1	Q70E73	2	PDB	PDB:4gn1PDB:4gmv

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential Ultracentrifugation	Mass spectrometryMass spectrometry [MALDI TOF]	1	40326690

Sequence, Structure & Domains

Sequences

Length

1,250

Mass

135,256

Sequence

MEQLSDEEIDHGAEEDSDKEDQDLDKMFGAWLGELDKLTQSLDSDKPMEPVKRSPLRQETNMANFSYRFSIYNLNEALNQGETVDLDALMADLCSIEQELSSIGSGNSKRQITETKATQKLPVSRHTLKHGTLKGLSSSSNRIAKPSHASYSLDDVTAQLEQASLSMDEAAQQSVLEDTKPLVTNQHRRTASAGTVSDAEVHSISNSSHSSITSAASSMDSLDIDKVTRPQELDLTHQGQPITEEEQAAKLKAEKIRVALEKIKEAQVKKLVIRVHMSDDSSKTMMVDERQTVRQVLDNLMDKSHCGYSLDWSLVETVSELQMERIFEDHENLVENLLNWTRDSQNKLIFMERIEKYALFKNPQNYLLGKKETAEMADRNKEVLLEECFCGSSVTVPEIEGVLWLKDDGKKSWKKRYFLLRASGIYYVPKGKAKVSRDLVCFLQLDHVNVYYGQDYRNKYKAPTDYCLVLKHPQIQKKSQYIKYLCCDDVRTLHQWVNGIRIAKYGKQLYMNYQEALKRTESAYDWTSLSSSSIKSGSSSSSIPESQSNHSNQSDSGVSDTQPAGHVRSQSIVSSVFSEAWKRGTQLEESSKARMESMNRPYTSLVPPLSPQPKIVTPYTASQPSPPLPPPPPPPPPPPPPPPPPPPPLPSQSAPSAGSAAPMFVKYSTITRLQNASQHSGALFKPPTPPVMQSQSVKPQILVPPNGVVPPPPPPPPPPTPGSAMAQLKPAPCAPSLPQFSAPPPPLKIHQVQHITQVAPPTPPPPPPIPAPLPPQAPPKPLVTIPAPTSTKTVAPVVTQAAPPTPTPPVPPAKKQPAFPASYIPPSPPTPPVPVPPPTLPKQQSFCAKPPPSPLSPVPSVVKQIASQFPPPPTPPAMESQPLKPVPANVAPQSPPAVKAKPKWQPSSIPVPSPDFPPPPPESSLVFPPPPPSPVPAPPPPPPPTASPTPDKSGSPGKKTSKTSSPGGKKPPPTPQRNSSIKSSSGAEHPEPKRPSVDSLVSKFTPPAESGSPSKETLPPPAAPPKPGKLNLSGVNLPGVLQQGCVSAKAPVLSGRGKDSVVEFPSPPSDSDFPPPPPETELPLPPIEIPAVFSGNTSPKVAVVNPQPQQWSKMSVKKAPPPTRPKRNDSTRLTQAEISEQPTMATVVPQVPTSPKSSLSVQPGFLADLNRTLQRKSITRHGSLSSRMSRAEPTATMDDMALPPPPPELLSDQQKAGYGGSHISGYATLRRGPPPAPPKRDQNTKLSRDW

Alternative Products

Event=Alternative splicing; Named isoforms=9; Name=RMO1-RAPH1; Synonyms=Lamellipodin, RAPH1; IsoId=Q70E73-10; Sequence=Displayed; Name=RMO1; IsoId=Q70E73-2; Sequence=VSP_035788, VSP_035789; Name=RMO1a; IsoId=Q70E73-3; Sequence=VSP_035784, VSP_035788, VSP_035789; Name=RMO1b; IsoId=Q70E73-4; Sequence=VSP_035786, VSP_035788, VSP_035789; Name=RMO1c; IsoId=Q70E73-5; Sequence=VSP_035787; Name=RMO1ab; Synonyms=Lamellipodin-S, Lpd-S; IsoId=Q70E73-6; Sequence=VSP_035785, VSP_035788, VSP_035789; Name=RMO1ac; IsoId=Q70E73-7; Sequence=VSP_035784, VSP_035787; Name=RMO1bc; IsoId=Q70E73-8; Sequence=VSP_035786, VSP_035787; Name=RMO1abc; IsoId=Q70E73-9; Sequence=VSP_035785, VSP_035787

Alternative Sequence

244; E -> EHAISLRCSSKQAKRHIDFTEEQAELTP (in isoform RMO1a and isoform RMO1ac); 244; E -> EHAISLRCSSKQAKRHIDFTEEQAELTPHSYLDRETSLLLRNIAGKPSHLLTK (in isoform RMO1ab and isoform RMO1abc); 244; E -> EHSYLDRETSLLLRNIAGKPSHLLTK (in isoform RMO1b and isoform RMO1bc); 593..1250; Missing (in isoform RMO1c, isoform RMO1ac, isoform RMO1bc and isoform RMO1abc); 593..597; ARMES -> VTASF (in isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab); 598..1250; Missing (in isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab)

3D Structural Models

Helix

255..264; 293..304; 319..321; 333..337; 354..356; 358..361; 363..365; 378..389; 436..438; 445..447; 456..459; 490..505; 507..516

Beta Strand

270..276; 282..288; 312..318; 323..326; 348..352; 390..393; 400..406; 413..421; 424..427; 429..433; 440..443; 449..455; 463..465; 467..471; 483..486

3D Structure

X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias

1..23; Acidic residues; 202..217; Low complexity; 535..551; Low complexity; 552..570; Polar residues; 588..597; Basic and acidic residues; 624..650; Pro residues; 651..662; Low complexity; 707..721; Pro residues; 760..781; Pro residues; 791..802; Low complexity; 803..814; Pro residues; 823..840; Pro residues; 909..947; Pro residues; 948..968; Low complexity; 976..986; Polar residues; 1018..1027; Pro residues; 1065..1088; Pro residues; 1131..1144; Polar residues; 1151..1161; Polar residues; 1238..1250; Basic and acidic residues

Domain (FT)

269..355; Ras-associating; 396..505; PH

Region

1..26; Disordered; 179..217; Disordered; 535..570; Disordered; 588..663; Disordered; 675..1036; Disordered; 1050..1162; Disordered; 1176..1250; Disordered

Protein Families

MRL family

Sequence Similarities

Belongs to the MRL family.

Clinical Relevance

Antibody (2)

HPA016744 HPA020027

Interaction Protein

ENSG00000108518

Interaction Count

Interaction Dataset

biogrid_opencell

Supporting Publications5

PMID	Title	Related sentences
30451371	Extracellular Vesicles from Neurosurgical Aspirates Identifies Chaperonin Containing TCP1 Subunit 6A as a Potential Glioblastoma Biomarker with Prognostic Significance.	No related sentences available
31320591	Exosomes regulate neurogenesis and circuit assembly.	No related sentences available
38731868	The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer.	No related sentences available
40098346	Toward Identification of Markers for Brain-Derived Extracellular Vesicles in Cerebrospinal Fluid: A Large-Scale, Unbiased Analysis Using Proximity Extension Assays.	No related sentences available
41216884	Extracellular Vesicles From Multiple Sclerosis White Matter Exhibit Synaptic, Mitochondrial, Complement and Ageing-Related Pathway Dysregulation.	No related sentences available