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UniProtKB - Q01831 (XPC_HUMAN)

Entry version 199 (13 Nov 2019)
Sequence version 4 (18 May 2010)
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Protein

DNA repair protein complementing XP-C cells

Gene

XPC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex (PubMed:10734143, PubMed:19609301, PubMed:20649465, PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides (PubMed:10734143, PubMed:19609301, PubMed:20649465). This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity (PubMed:10734143, PubMed:19609301, PubMed:20649465). The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). The orientation of XPC complex binding appears to be crucial for inducing a productive NER (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair (PubMed:9734359, PubMed:10873465, PubMed:12509299, PubMed:12547395, PubMed:19941824, PubMed:20028083, PubMed:20798892). In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts (PubMed:20028083). XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1 (PubMed:20028083).10 Publications
In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT) (PubMed:29973595, PubMed:31527837). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes (PubMed:31527837).2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-5696395 Formation of Incision Complex in GG-NER

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q01831

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA repair protein complementing XP-C cells
Alternative name(s):
Xeroderma pigmentosum group C-complementing protein
p125
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:XPC
Synonyms:XPCC
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:12816 XPC

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		613208 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q01831

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Xeroderma pigmentosum complementation group C (XP-C)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. The skin develops marked freckling and other pigmentation abnormalities.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_005846334P → H in XP-C; severe; does not affect interaction with KAT2A and transcription coactivator activity in absence of DNA damage. 2 PublicationsCorresponds to variant dbSNP:rs74737358EnsemblClinVar.1
Natural variantiVAR_064039690W → S in XP-C; diminishes repair activity and impairs DNA binding. 4 Publications1
Natural variantiVAR_005847697V → VV in XP-C; mild. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi531W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. 1 Publication1
Mutagenesisi542W → A: Slightly diminishes repair activity and sligtly impairs DNA binding. 1 Publication1
Mutagenesisi733F → A: Diminishes repair activity and impairs DNA binding. 2 Publications1
Mutagenesisi754N → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. 1 Publication1
Mutagenesisi755E → K: Reduces nuclear mobility and impairs repair activity. 1 Publication1
Mutagenesisi756F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci. 1 Publication1
Mutagenesisi797F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci; decreases recruitment of TFIIH complex to lesion sites. 1 Publication1
Mutagenesisi799F → A: Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; greatly reduces localization at DNA damaged foci; decreases recruitment of TFIIH complex to lesion sites. 1 Publication1
Mutagenesisi848W → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-851 and A-855. 1 Publication1
Mutagenesisi851L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-855. 1 Publication1
Mutagenesisi855L → A: Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-851. 1 Publication1

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

DisGeNET

More...DisGeNETi		7508

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		XPC

MalaCards human disease database

More...MalaCardsi		XPC
MIMi278720 phenotype

Open Targets

More...OpenTargetsi		ENSG00000154767

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		910 Xeroderma pigmentosum

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37413

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q01831

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		XPC

Domain mapping of disease mutations (DMDM)

More...DMDMi		296453081

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002182932 – 940DNA repair protein complementing XP-C cellsAdd BLAST939

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei94PhosphoserineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Cross-linki161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei169PhosphothreonineCombined sources1
Modified residuei397PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei399PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei460PhosphoserineCombined sources1
Modified residuei876PhosphothreonineCombined sources1
Modified residuei883PhosphoserineCombined sources1
Modified residuei884PhosphoserineCombined sources1
Modified residuei891PhosphoserineCombined sources1
Modified residuei903PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation (PubMed:15882621, PubMed:23751493). Ubiquitinated by RNF11 via 'Lys-63'-linked ubiquitination (PubMed:23751493). Ubiquitination by RNF111 is polysumoylation-dependent and promotes nucleotide excision repair (PubMed:23751493).2 Publications
Sumoylated; sumoylation promotes ubiquitination by RNF111.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q01831

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q01831

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q01831

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q01831

PeptideAtlas

More...PeptideAtlasi		Q01831

PRoteomics IDEntifications database

More...PRIDEi		Q01831

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		19176
20470
58003 [Q01831-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q01831

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q01831

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q01831

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000154767 Expressed in 230 organ(s), highest expression level in left lobe of thyroid gland

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q01831 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q01831 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB009932
HPA035707
HPA069673

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the XPC complex composed of XPC, RAD23B and CETN2 (PubMed:11279143, PubMed:12509233, PubMed:15964821, PubMed:17897675, PubMed:16627479, PubMed:16533048).

Interacts with RAD23A; the interaction is suggesting the existence of a functional equivalent variant XPC complex (PubMed:9372924).

Interacts with TDG; the interaction is demonstrated using the XPC:RAD23B dimer (PubMed:12505994, PubMed:20798892).

Interacts with SMUG1; the interaction is demonstrated using the XPC:RAD23B dimer (PubMed:20798892).

Interacts with DDB2 (PubMed:15882621).

Interacts with CCNH, GTF2H1 and ERCC3 (PubMed:10734143, PubMed:12509233).

Interacts with E2F1 and KAT2A; leading to KAT2A recruitment to promoters and subsequent acetylation of histones (PubMed:29973595, PubMed:31527837).

13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113345, 85 interactors

Database of interacting proteins

More...DIPi		DIP-31225N

Protein interaction database and analysis system

More...IntActi		Q01831, 64 interactors

Molecular INTeraction database

More...MINTi		Q01831

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000285021

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1940
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q01831

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q01831

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni496 – 734Interaction with RAD23BAdd BLAST239
Regioni607 – 766Minimal sensor domain involved in damage recognitionAdd BLAST160
Regioni607 – 741DNA-binding; preference for heteroduplex DNAAdd BLAST135
Regioni767 – 831DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complexAdd BLAST65
Regioni816 – 940Interaction with ERCC2 and GTF2H11 PublicationAdd BLAST125
Regioni847 – 866Interaction with CETN2Add BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi390 – 395Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi30 – 177Glu-rich (acidic)Add BLAST148
Compositional biasi30 – 34Poly-Glu5
Compositional biasi124 – 130Poly-Glu7
Compositional biasi359 – 395Lys-rich (basic)Add BLAST37
Compositional biasi408 – 431Arg/Lys-rich (basic)Add BLAST24
Compositional biasi432 – 461Asp/Glu-rich (acidic)Add BLAST30
Compositional biasi466 – 493Arg/Lys-rich (basic)Add BLAST28
Compositional biasi501 – 507Poly-Ser7

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the XPC family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2179 Eukaryota
COG5535 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000005194

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000124671

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q01831

KEGG Orthology (KO)

More...KOi		K10838

Identification of Orthologs from Complete Genome Data

More...OMAi		EEKWVCV

Database of Orthologous Groups

More...OrthoDBi		750482at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q01831

TreeFam database of animal gene trees

More...TreeFami		TF101242

Family and domain databases

Database of protein disorder

More...DisProti		DP01626

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.70.2460, 1 hit
3.90.260.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR018327 BHD_2
IPR004583 DNA_repair_Rad4
IPR018026 DNA_repair_Rad4_subgr
IPR038765 Papain-like_cys_pep_sf
IPR018325 Rad4/PNGase_transGLS-fold
IPR018326 Rad4_beta-hairpin_dom1
IPR018328 Rad4_beta-hairpin_dom3
IPR042488 Rad4_BHD3_sf
IPR036985 Transglutaminase-like_sf

The PANTHER Classification System

More...PANTHERi		PTHR12135 PTHR12135, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10403 BHD_1, 1 hit
PF10404 BHD_2, 1 hit
PF10405 BHD_3, 1 hit
PF03835 Rad4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01030 BHD_1, 1 hit
SM01031 BHD_2, 1 hit
SM01032 BHD_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54001 SSF54001, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00605 rad4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q01831-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MARKRAAGGE PRGRELRSQK SKAKSKARRE EEEEDAFEDE KPPKKSLLSK 
        60         70         80         90        100
VSQGKRKRGC SHPGGSADGP AKKKVAKVTV KSENLKVIKD EALSDGDDLR 
       110        120        130        140        150
DFPSDLKKAH HLKRGATMNE DSNEEEEESE NDWEEVEELS EPVLGDVRES 
       160        170        180        190        200
TAFSRSLLPV KPVEIEIETP EQAKTRERSE KIKLEFETYL RRAMKRFNKG 
       210        220        230        240        250
VHEDTHKVHL LCLLANGFYR NNICSQPDLH AIGLSIIPAR FTRVLPRDVD 
       260        270        280        290        300
TYYLSNLVKW FIGTFTVNAE LSASEQDNLQ TTLERRFAIY SARDDEELVH 
       310        320        330        340        350
IFLLILRALQ LLTRLVLSLQ PIPLKSATAK GKKPSKERLT ADPGGSSETS 
       360        370        380        390        400
SQVLENHTKP KTSKGTKQEE TFAKGTCRPS AKGKRNKGGR KKRSKPSSSE 
       410        420        430        440        450
EDEGPGDKQE KATQRRPHGR ERRVASRVSY KEESGSDEAG SGSDFELSSG 
       460        470        480        490        500
EASDPSDEDS EPGPPKQRKA PAPQRTKAGS KSASRTHRGS HRKDPSLPAA 
       510        520        530        540        550
SSSSSSSKRG KKMCSDGEKA EKRSIAGIDQ WLEVFCEQEE KWVCVDCVHG 
       560        570        580        590        600
VVGQPLTCYK YATKPMTYVV GIDSDGWVRD VTQRYDPVWM TVTRKCRVDA 
       610        620        630        640        650
EWWAETLRPY QSPFMDREKK EDLEFQAKHM DQPLPTAIGL YKNHPLYALK 
       660        670        680        690        700
RHLLKYEAIY PETAAILGYC RGEAVYSRDC VHTLHSRDTW LKKARVVRLG 
       710        720        730        740        750
EVPYKMVKGF SNRARKARLA EPQLREENDL GLFGYWQTEE YQPPVAVDGK 
       760        770        780        790        800
VPRNEFGNVY LFLPSMMPIG CVQLNLPNLH RVARKLDIDC VQAITGFDFH 
       810        820        830        840        850
GGYSHPVTDG YIVCEEFKDV LLTAWENEQA VIERKEKEKK EKRALGNWKL 
       860        870        880        890        900
LAKGLLIRER LKRRYGPKSE AAAPHTDAGG GLSSDEEEGT SSQAEAARIL 
       910        920        930        940
AASWPQNRED EEKQKLKGGP KKTKREKKAA ASHLFPFEQL
Length:940
Mass (Da):105,953
Last modified:May 18, 2010 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2F8C80D43FAA1256
GO
Isoform 2 (identifier: Q01831-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-172: Missing.

Note: No experimental confirmation available.
Show »
Length:903
Mass (Da):101,847
Checksum:iAF2F96DDCC4DB78E
GO
Isoform 3 (identifier: Q01831-3) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     138-140: ELS → VKR
     141-940: Missing.

Show »
Length:140
Mass (Da):15,712
Checksum:iCA721AA7474B6D20
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EUB5E7EUB5_HUMAN
DNA repair protein-complementing XP...
XPC
168Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti135E → Q in BAG58555 (PubMed:14702039).Curated1
Sequence conflicti489G → E in BAG58555 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01889416L → V1 PublicationCorresponds to variant dbSNP:rs1870134EnsemblClinVar.1
Natural variantiVAR_01889548L → F1 PublicationCorresponds to variant dbSNP:rs2229089EnsemblClinVar.1
Natural variantiVAR_01889686K → R1 PublicationCorresponds to variant dbSNP:rs3731063Ensembl.1
Natural variantiVAR_057475287F → C. Corresponds to variant dbSNP:rs35629274EnsemblClinVar.1
Natural variantiVAR_018897314R → Q1 PublicationCorresponds to variant dbSNP:rs3731126Ensembl.1
Natural variantiVAR_005846334P → H in XP-C; severe; does not affect interaction with KAT2A and transcription coactivator activity in absence of DNA damage. 2 PublicationsCorresponds to variant dbSNP:rs74737358EnsemblClinVar.1
Natural variantiVAR_018898492R → H1 PublicationCorresponds to variant dbSNP:rs2227999EnsemblClinVar.1
Natural variantiVAR_018899499A → V3 PublicationsCorresponds to variant dbSNP:rs2228000EnsemblClinVar.1
Natural variantiVAR_059963511K → Q. Corresponds to variant dbSNP:rs6413541Ensembl.1
Natural variantiVAR_018900513M → I1 PublicationCorresponds to variant dbSNP:rs3731130EnsemblClinVar.1
Natural variantiVAR_057476514C → S. Corresponds to variant dbSNP:rs3731130EnsemblClinVar.1
Natural variantiVAR_018901632Q → E1 PublicationCorresponds to variant dbSNP:rs3731139Ensembl.1
Natural variantiVAR_018902671R → H1 PublicationCorresponds to variant dbSNP:rs3731140Ensembl.1
Natural variantiVAR_018903689T → M1 PublicationCorresponds to variant dbSNP:rs3731152EnsemblClinVar.1
Natural variantiVAR_064039690W → S in XP-C; diminishes repair activity and impairs DNA binding. 4 Publications1
Natural variantiVAR_005847697V → VV in XP-C; mild. 1 Publication1
Natural variantiVAR_018904928K → Q1 PublicationCorresponds to variant dbSNP:rs3731177EnsemblClinVar.1
Natural variantiVAR_005848939Q → K3 PublicationsCorresponds to variant dbSNP:rs2228001EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_046344136 – 172Missing in isoform 2. 1 PublicationAdd BLAST37
Alternative sequenceiVSP_055890138 – 140ELS → VKR in isoform 3. 1 Publication3
Alternative sequenceiVSP_055891141 – 940Missing in isoform 3. 1 PublicationAdd BLAST800

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D21089 mRNA Translation: BAA04651.1
AF261901
, AF261892, AF261893, AF261894, AF261895, AF261896, AF261897, AF261898, AF261899, AF261900 Genomic DNA Translation: AAF87574.1
KJ535085 mRNA Translation: AHW56724.1
AY131066 Genomic DNA Translation: AAM77801.1
AK295711 mRNA Translation: BAG58555.1
AC093495 Genomic DNA No translation available.
FJ695191 Genomic DNA No translation available.
FJ695192 Genomic DNA No translation available.
BC016620 mRNA Translation: AAH16620.1
AK222844 mRNA Translation: BAD96564.1
X65024 mRNA Translation: CAA46158.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS46763.1 [Q01831-1]

Protein sequence database of the Protein Information Resource

More...PIRi		S44345

NCBI Reference Sequences

More...RefSeqi		NP_004619.3, NM_004628.4 [Q01831-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000285021; ENSP00000285021; ENSG00000154767 [Q01831-1]
ENST00000476581; ENSP00000424548; ENSG00000154767 [Q01831-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7508

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7508

UCSC genome browser

More...UCSCi		uc062gzd.1 human [Q01831-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21089 mRNA Translation: BAA04651.1
AF261901
, AF261892, AF261893, AF261894, AF261895, AF261896, AF261897, AF261898, AF261899, AF261900 Genomic DNA Translation: AAF87574.1
KJ535085 mRNA Translation: AHW56724.1
AY131066 Genomic DNA Translation: AAM77801.1
AK295711 mRNA Translation: BAG58555.1
AC093495 Genomic DNA No translation available.
FJ695191 Genomic DNA No translation available.
FJ695192 Genomic DNA No translation available.
BC016620 mRNA Translation: AAH16620.1
AK222844 mRNA Translation: BAD96564.1
X65024 mRNA Translation: CAA46158.1
CCDSiCCDS46763.1 [Q01831-1]
PIRiS44345
RefSeqiNP_004619.3, NM_004628.4 [Q01831-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A4JNMR-B847-863[»]
2GGMX-ray2.35C/D847-863[»]
2OBHX-ray1.80C/D847-863[»]
2RVBNMR-A109-156[»]
SMRiQ01831
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113345, 85 interactors
DIPiDIP-31225N
IntActiQ01831, 64 interactors
MINTiQ01831
STRINGi9606.ENSP00000285021

PTM databases

iPTMnetiQ01831
PhosphoSitePlusiQ01831
SwissPalmiQ01831

Polymorphism and mutation databases

BioMutaiXPC
DMDMi296453081

Proteomic databases

EPDiQ01831
jPOSTiQ01831
MassIVEiQ01831
PaxDbiQ01831
PeptideAtlasiQ01831
PRIDEiQ01831
ProteomicsDBi19176
20470
58003 [Q01831-1]

Genome annotation databases

EnsembliENST00000285021; ENSP00000285021; ENSG00000154767 [Q01831-1]
ENST00000476581; ENSP00000424548; ENSG00000154767 [Q01831-3]
GeneIDi7508
KEGGihsa:7508
UCSCiuc062gzd.1 human [Q01831-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7508
DisGeNETi7508

GeneCards: human genes, protein and diseases

More...GeneCardsi		XPC
GeneReviewsiXPC
HGNCiHGNC:12816 XPC
HPAiCAB009932
HPA035707
HPA069673
MalaCardsiXPC
MIMi278720 phenotype
613208 gene
neXtProtiNX_Q01831
OpenTargetsiENSG00000154767
Orphaneti910 Xeroderma pigmentosum
PharmGKBiPA37413

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2179 Eukaryota
COG5535 LUCA
GeneTreeiENSGT00390000005194
HOGENOMiHOG000124671
InParanoidiQ01831
KOiK10838
OMAiEEKWVCV
OrthoDBi750482at2759
PhylomeDBiQ01831
TreeFamiTF101242

Enzyme and pathway databases

ReactomeiR-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-5696395 Formation of Incision Complex in GG-NER
SIGNORiQ01831

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		XPC human
EvolutionaryTraceiQ01831

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		XPC_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		7508
PharosiQ01831

Protein Ontology

More...PROi		PR:Q01831

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000154767 Expressed in 230 organ(s), highest expression level in left lobe of thyroid gland
ExpressionAtlasiQ01831 baseline and differential
GenevisibleiQ01831 HS

Family and domain databases

DisProtiDP01626
Gene3Di3.30.70.2460, 1 hit
3.90.260.10, 1 hit
InterProiView protein in InterPro
IPR018327 BHD_2
IPR004583 DNA_repair_Rad4
IPR018026 DNA_repair_Rad4_subgr
IPR038765 Papain-like_cys_pep_sf
IPR018325 Rad4/PNGase_transGLS-fold
IPR018326 Rad4_beta-hairpin_dom1
IPR018328 Rad4_beta-hairpin_dom3
IPR042488 Rad4_BHD3_sf
IPR036985 Transglutaminase-like_sf
PANTHERiPTHR12135 PTHR12135, 1 hit
PfamiView protein in Pfam
PF10403 BHD_1, 1 hit
PF10404 BHD_2, 1 hit
PF10405 BHD_3, 1 hit
PF03835 Rad4, 1 hit
SMARTiView protein in SMART
SM01030 BHD_1, 1 hit
SM01031 BHD_2, 1 hit
SM01032 BHD_3, 1 hit
SUPFAMiSSF54001 SSF54001, 1 hit
TIGRFAMsiTIGR00605 rad4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXPC_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01831
Secondary accession number(s): B4DIP3
, E9PB96, E9PH69, Q53GT7, Q96AX0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 18, 2010
Last modified: November 13, 2019
This is version 199 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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