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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:ROR1

Protein Summary

check button Gene summary
Gene name: ROR1
ASpdb.0 ID: 4919
Gene
Gene symbol

ROR1

Gene ID

4919

Gene namereceptor tyrosine kinase like orphan receptor 1
SynonymsNTRKR1|dJ537F10.1
Cytomap

1p31.3

Type of geneprotein-coding
Descriptioninactive tyrosine-protein kinase transmembrane receptor ROR1neurotrophic tyrosine kinase, receptor-related 1
Modification date20240411
UniProtAcc

Q01973


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneROR1

GO:0005886

plasma membrane

27162350

GeneROR1

GO:0043235

receptor complex

23382219



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
Q01973-1Q01973-1_6tu9_A.pdb6TU9X-ray1.94A460749

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
Q01973ROR1Q01973-1Q01973-29373881549Deletionnonenone00
Q01973ROR1Q01973-1Q01973-3937393392393SubstitutionDSGK392393
Q01973ROR1Q01973-1Q01973-3937393394937Deletionnonenone393393

check buttonMultiple sequence alignment of our canonical and alternatively spliced ROR1

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of ROR1
UniProt-idENSGENSTENSP
Q01973-1ENSG00000185483.13ENST00000371079.6ENSP00000360120.1
Q01973-3ENSG00000185483.13ENST00000371080.5ENSP00000360121.1

UniProt-idNM IDNP ID
Q01973-1NM_005012.3NP_005003.2
Q01973-3NM_001083592.1NP_001077061.1

check buttonAmino acid sequences of our canonical and alternatively spliced ROR1
accession_idProtein sequence
Q01973-1MHRPRRRGTRPPLLALLAALLLAARGAAAQETELSVSAELVPTSSWNISSELNKDSYLTLDEPMNNITTSLGQTAELHCKVSGNPPPTIR
WFKNDAPVVQEPRRLSFRSTIYGSRLRIRNLDTTDTGYFQCVATNGKEVVSSTGVLFVKFGPPPTASPGYSDEYEEDGFCQPYRGIACAR
FIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPRDLCRDECEILENVLCQTEYIFARSN
PMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPINKNHKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHTFTALRFPELNGGHS
YCRNPGNQKEAPWCFTLDENFKSDLCDIPACDSKDSKEKNKMEILYILVPSVAIPLAIALLFFFICVCRNNQKSSSAPVQRQPKHVRGQN
VEMSMLNAYKPKSKAKELPLSAVRFMEELGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDYNNPQQWTEFQQEASLMAELHHPNIVCLLG
AVTQEQPVCMLFEYINQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVK
ISDLGLSREIYSADYYRVQSKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCPPR
MYSLMTECWNEIPSRRPRFKDIHVRLRSWEGLSSHTSSTTPSGGNATTQTTSLSASPVSNLSNPRYPNYMFPSQGITPQGQIAGFIGPPI
PQNQRFIPINGYPIPPGYAAFPAAHYQPTGPPRVIQHCPPPKSRSPSSASGSTSTGHVTSLPSSGSNQEANIPLLPHMSIPNHPGGMGIT
Q01973-2MLFEYINQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILIGEQLHVKISDLGLSRE
IYSADYYRVQSKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECW
NEIPSRRPRFKDIHVRLRSWEGLSSHTSSTTPSGGNATTQTTSLSASPVSNLSNPRYPNYMFPSQGITPQGQIAGFIGPPIPQNQRFIPI
NGYPIPPGYAAFPAAHYQPTGPPRVIQHCPPPKSRSPSSASGSTSTGHVTSLPSSGSNQEANIPLLPHMSIPNHPGGMGITVFGNKSQKP
Q01973-3MHRPRRRGTRPPLLALLAALLLAARGAAAQETELSVSAELVPTSSWNISSELNKDSYLTLDEPMNNITTSLGQTAELHCKVSGNPPPTIR
WFKNDAPVVQEPRRLSFRSTIYGSRLRIRNLDTTDTGYFQCVATNGKEVVSSTGVLFVKFGPPPTASPGYSDEYEEDGFCQPYRGIACAR
FIGNRTVYMESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCDETSSVPKPRDLCRDECEILENVLCQTEYIFARSN
PMILMRLKLPNCEDLPQPESPEAANCIRIGIPMADPINKNHKCYNSTGVDYRGTVSVTKSGRQCQPWNSQYPHTHTFTALRFPELNGGHS

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
ROR1 (go to UniProt):Q01973

check buttonRetention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
Q01973Topological domain30406Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=1;End=549
Q01973Topological domain30406Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=392;End=393
Q01973Topological domain30406Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=394;End=937
Q01973Transmembrane407427Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=1;End=549
Q01973Transmembrane407427Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=394;End=937
Q01973Topological domain428937Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=1;End=549
Q01973Topological domain428937Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=394;End=937
Q01973Domain42147Note=Ig-like C2-typeType=Deletion;Start=1;End=549
Q01973Domain165299Note=FZ;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00090Type=Deletion;Start=1;End=549
Q01973Domain312391Note=Kringle;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00121Type=Deletion;Start=1;End=549
Q01973Domain473746Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159Type=Deletion;Start=1;End=549
Q01973Domain473746Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159Type=Deletion;Start=394;End=937
Q01973Region753779Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=937
Q01973Region833890Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=937
Q01973Compositional bias851883Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=937


Gene Isoform Structures and Expression Levels for ROR1

check buttonGene structures of our canonical and alternative spliced genes of ROR1
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.
gene isoform structure of ROR1

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.
3D view using mol* of Q01973-1
3D view using mol* of Q01973-2
3D view using mol* of Q01973-3


pLDDT Score Distribution

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of Q01973-1
all structure
pLDDT distribution across the protein length of Q01973-2
all structure
pLDDT distribution across the protein length of Q01973-3
all structure


Ramachandran Plot of Protein Structures


check button Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.
Ramachandran plot of Q01973-1
all structure
Ramachandran plot of Q01973-3
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
Q01973-11.0494201.0691266.3560.5040.7590.9540.69710.6980.82171,174,175,176,177,178,179,180,181,192,193,195,19
6,199,200,201,203,204,206,207,208,209,210,211,212,
213,214,215,216,217,220,224,266,270,272,273,276,56
1,562,565,566,568,570,571,572,573,619,639,640,641,
642,643,644,645,657,658,684,689,690,691,692,693,69
4,695,696,697,698,814,815,816,817,818,819,820,821,
822
Q01973-20.897580.888179.0460.5170.7541.0130.9230.8611.0721.02621,40,43,134,137,138,139,141,145,163,164,165,166,1
67,273,274,276,279
Q01973-31.184631.26777.5180.330.9361.3336.0250.12548.2814.653206,209,210,214,215,219,223,224,227,260,262,263,26
4,266,267,273,277,279

Protein Structure and Feature Comparision


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)
3D view using mol* of Q01973-1_Q01973-1_6tu9_A.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q01973-1_6tu9_A_Q01973-2.pdb
3D view using mol* of Q01973-1_6tu9_A_Q01973-3.pdb

check button Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)
3D view using mol* of Q01973-1_Q01973-2.pdb
3D view using mol* of Q01973-1_Q01973-3.pdb

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/Q01973-1_vs_Q01973-2.png
all structure<
./stats/secondary_structure/figure/Q01973-1_vs_Q01973-3.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/Q01973-1_vs_Q01973-2.png
all structure<
./stats/relative_asa/Q01973-1_vs_Q01973-3.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to ROR1


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions

Related Diseases to ROR1


check button Previous studies relating to the alternative splicing of ROR1 and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term
ROR18875995Human neural tissues express a truncated Ror1 receptor tyrosine kinase, lacking both extracellular and transmembrane domains.Human heart, lung and kidney express a 6 kb mRNA encoding Ror1, a member of the receptor tyrosine kinase (RTK) family with as yet unknown ligand specificity. We used a Ror1 cDNA probe to screen a cDNA library prepared from the human neuronogenic teratocarcinoma line, NTera2, and cloned a 2373 nucleotide transcript. This transcript contains an open reading frame that encodes a 388 amino acid protein identical with the cytosolic, C-terminal region of ror1 but lacking the ror1 transmembrane and entire extracellular domains. Northern blots demonstrate that mRNA encoding this truncated Ror1 ('t-Rorl') is abundantly expressed in fetal and adult human CNS, in human leukemia, lymphoma cell lines, and in a variety of human cancers derived from neuroectoderm. While previous studies have documented alternative splicing patterns within 5' and 3' regions of mRNAs encoding various RTKs altering their ligand binding specificity or their intracellular signaling, the present report is the first to demonstrate tissue-specific alternative mRNA splicing causing loss of the entire extracellular and transmembrane regions of an RTK.D009423Nervous System Neoplasms
ROR18875995Human neural tissues express a truncated Ror1 receptor tyrosine kinase, lacking both extracellular and transmembrane domains.Human heart, lung and kidney express a 6 kb mRNA encoding Ror1, a member of the receptor tyrosine kinase (RTK) family with as yet unknown ligand specificity. We used a Ror1 cDNA probe to screen a cDNA library prepared from the human neuronogenic teratocarcinoma line, NTera2, and cloned a 2373 nucleotide transcript. This transcript contains an open reading frame that encodes a 388 amino acid protein identical with the cytosolic, C-terminal region of ror1 but lacking the ror1 transmembrane and entire extracellular domains. Northern blots demonstrate that mRNA encoding this truncated Ror1 ('t-Rorl') is abundantly expressed in fetal and adult human CNS, in human leukemia, lymphoma cell lines, and in a variety of human cancers derived from neuroectoderm. While previous studies have documented alternative splicing patterns within 5' and 3' regions of mRNAs encoding various RTKs altering their ligand binding specificity or their intracellular signaling, the present report is the first to demonstrate tissue-specific alternative mRNA splicing causing loss of the entire extracellular and transmembrane regions of an RTK.D018243Teratocarcinoma


Clinically important variants in ROR1


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance