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Protein

DNA topoisomerase 2-binding protein 1

Gene

TOPBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double-stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR.6 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: ProtInc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA metabolic process Source: ProtInc
  • DNA repair Source: UniProtKB
  • DNA replication Source: Reactome
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • response to ionizing radiation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ92547.
SIGNORiQ92547.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2-binding protein 1
Alternative name(s):
DNA topoisomerase II-beta-binding protein 1
Short name:
TopBP1
DNA topoisomerase II-binding protein 1
Gene namesi
Name:TOPBP1
Synonyms:KIAA0259
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17008. TOPBP1.

Subcellular locationi

  • Nucleus
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
  • Cytoplasmcytoskeletonspindle pole
  • Chromosome

  • Note: Detected on unpaired autosomes in meiotic prophase cells. Detected on X and Y chromosomes during later stages of prophase. Colocalizes with ATR and H2AFX at unsynapsed chromosome cores during prophase (By similarity). Has a uniform nuclear distribution during G phase. Colocalizes with BRCA1 at stalled replication forks during S phase. In mitotic cells it colocalizes with BRCA1 at spindle poles and centrosomes during metaphase and anaphase. Detected in discrete foci together with PML and numerous DNA repair enzymes after DNA damage by alkylating agents, UV or gamma irradiation. Localizes to sites of DNA damage in a H2AX- independent manner.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • centrosome Source: HPA
  • chromosome Source: UniProtKB
  • condensed nuclear chromosome Source: Ensembl
  • cytoplasm Source: HPA
  • Golgi apparatus Source: HPA
  • male germ cell nucleus Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • PML body Source: UniProtKB
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134934073.

Chemistry

ChEMBLiCHEMBL3175.

Polymorphism and mutation databases

BioMutaiTOPBP1.
DMDMi296453012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15221522DNA topoisomerase 2-binding protein 1PRO_0000072631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei298 – 2981PhosphothreonineCombined sources
Modified residuei301 – 3011PhosphoserineCombined sources
Modified residuei779 – 7791PhosphothreonineCombined sources
Modified residuei848 – 8481PhosphothreonineCombined sources
Modified residuei860 – 8601PhosphoserineCombined sources
Modified residuei861 – 8611PhosphothreonineCombined sources
Modified residuei864 – 8641PhosphoserineCombined sources
Modified residuei886 – 8861PhosphoserineCombined sources
Modified residuei888 – 8881PhosphoserineCombined sources
Modified residuei1002 – 10021PhosphoserineCombined sources
Modified residuei1064 – 10641PhosphothreonineCombined sources
Modified residuei1504 – 15041PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine and threonine residues in response to X-ray irradiation.2 Publications
Ubiquitinated and degraded by the proteasome. X-ray irradiation reduces ubiquitination.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ92547.
MaxQBiQ92547.
PaxDbiQ92547.
PeptideAtlasiQ92547.
PRIDEiQ92547.

PTM databases

iPTMnetiQ92547.
PhosphoSiteiQ92547.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, placenta, lung and kidney.1 Publication

Inductioni

Up-regulated during the S phase of the cell cycle. Up-regulated by E2F1 and interferon.1 Publication

Gene expression databases

BgeeiENSG00000163781.
CleanExiHS_TOPBP1.
ExpressionAtlasiQ92547. baseline and differential.
GenevisibleiQ92547. HS.

Organism-specific databases

HPAiCAB022451.
HPA036738.
HPA063020.
HPA064566.

Interactioni

Subunit structurei

Interacts with POLE (PubMed:11395493). Interacts with RAD9A (PubMed:11395493). Interacts with UBR5 (PubMed:11714696). Interacts with E2F1 (PubMed:12697828, PubMed:15075294). Interacts with PML (PubMed:12773567). Interacts with SMARCA2 (PubMed:15075294). Interacts with SMARCA4 (PubMed:15075294). Interacts with RHNO1 (PubMed:21659603). May interact with TOP2B (PubMed:9461304). Interacts with TICRR (PubMed:20080954). Interacts with HELB (PubMed:25933514).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-308302,EBI-308302
AKT1P317492EBI-308302,EBI-296087
CDC45O754196EBI-308302,EBI-374969
E2P031202EBI-308302,EBI-1779322From a different organism.
E2F1Q010943EBI-308302,EBI-448924
ZBTB17Q131052EBI-308302,EBI-372156

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: ProtInc

Protein-protein interaction databases

BioGridi116256. 55 interactions.
DIPiDIP-24263N.
IntActiQ92547. 19 interactions.
MINTiMINT-275958.
STRINGi9606.ENSP00000260810.

Chemistry

BindingDBiQ92547.

Structurei

Secondary structure

1
1522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 155Combined sources
Helixi21 – 3313Combined sources
Helixi36 – 383Combined sources
Beta strandi39 – 435Combined sources
Helixi44 – 474Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 633Combined sources
Helixi66 – 749Combined sources
Beta strandi77 – 793Combined sources
Helixi81 – 899Combined sources
Turni105 – 1084Combined sources
Beta strandi110 – 1156Combined sources
Helixi118 – 13013Combined sources
Beta strandi145 – 1517Combined sources
Helixi154 – 1618Combined sources
Helixi169 – 18012Combined sources
Turni181 – 1833Combined sources
Helixi187 – 1893Combined sources
Helixi192 – 1954Combined sources
Turni199 – 2024Combined sources
Beta strandi204 – 2074Combined sources
Helixi212 – 22413Combined sources
Turni235 – 2373Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi244 – 2463Combined sources
Helixi249 – 2568Combined sources
Beta strandi260 – 2623Combined sources
Helixi264 – 27310Combined sources
Helixi279 – 2813Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi333 – 3353Combined sources
Helixi341 – 3433Combined sources
Helixi349 – 3513Combined sources
Turni356 – 3616Combined sources
Beta strandi363 – 3686Combined sources
Helixi372 – 38312Combined sources
Beta strandi387 – 3915Combined sources
Beta strandi398 – 4036Combined sources
Helixi407 – 4148Combined sources
Beta strandi421 – 4233Combined sources
Helixi424 – 43310Combined sources
Helixi440 – 4423Combined sources
Turni552 – 5554Combined sources
Beta strandi557 – 5604Combined sources
Helixi565 – 57713Combined sources
Beta strandi591 – 5966Combined sources
Beta strandi607 – 6126Combined sources
Helixi613 – 6219Combined sources
Helixi628 – 6303Combined sources
Helixi632 – 6343Combined sources
Turni645 – 6484Combined sources
Beta strandi650 – 6534Combined sources
Helixi658 – 67013Combined sources
Turni685 – 6884Combined sources
Beta strandi693 – 6964Combined sources
Beta strandi698 – 7003Combined sources
Helixi703 – 7108Combined sources
Helixi718 – 72710Combined sources
Helixi733 – 7353Combined sources
Helixi738 – 7403Combined sources
Turni904 – 9074Combined sources
Beta strandi909 – 9124Combined sources
Helixi914 – 9196Combined sources
Helixi920 – 92910Combined sources
Beta strandi933 – 9375Combined sources
Beta strandi943 – 9464Combined sources
Helixi956 – 9638Combined sources
Beta strandi967 – 9693Combined sources
Helixi971 – 98010Combined sources
Helixi986 – 9883Combined sources
Beta strandi1269 – 12746Combined sources
Helixi1277 – 128913Combined sources
Beta strandi1297 – 12993Combined sources
Beta strandi1306 – 13116Combined sources
Helixi1316 – 13238Combined sources
Beta strandi1327 – 13293Combined sources
Helixi1332 – 13409Combined sources
Helixi1347 – 13493Combined sources
Helixi1354 – 13574Combined sources
Helixi1365 – 138521Combined sources
Turni1386 – 13883Combined sources
Turni1393 – 13964Combined sources
Beta strandi1398 – 14025Combined sources
Helixi1405 – 141713Combined sources
Helixi1428 – 14336Combined sources
Beta strandi1435 – 14395Combined sources
Helixi1453 – 14586Combined sources
Beta strandi1462 – 14654Combined sources
Helixi1467 – 14748Combined sources
Helixi1481 – 14844Combined sources
Helixi1487 – 14926Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WF6NMR-A326-444[»]
2XNHX-ray2.80A1-287[»]
2XNKX-ray2.60A/B/C/D1-290[»]
3AL2X-ray2.00A1264-1493[»]
3AL3X-ray2.15A1264-1493[»]
3JVEX-ray1.34A893-996[»]
3OLCX-ray2.40X1-290[»]
3PD7X-ray1.26A/B893-994[»]
3UENX-ray1.90A549-746[»]
3UEOX-ray2.60A/B/C/D549-746[»]
ProteinModelPortaliQ92547.
SMRiQ92547. Positions 7-286, 329-445, 550-744, 901-994, 1266-1493.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92547.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 18989BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini195 – 28490BRCT 2PROSITE-ProRule annotationAdd
BLAST
Domaini354 – 44491BRCT 3PROSITE-ProRule annotationAdd
BLAST
Domaini548 – 63386BRCT 4PROSITE-ProRule annotationAdd
BLAST
Domaini641 – 73898BRCT 5PROSITE-ProRule annotationAdd
BLAST
Domaini900 – 99192BRCT 6PROSITE-ProRule annotationAdd
BLAST
Domaini1259 – 135193BRCT 7PROSITE-ProRule annotationAdd
BLAST
Domaini1389 – 148698BRCT 8PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi852 – 8587Nuclear localization signalSequence analysis
Motifi1517 – 15204Nuclear localization signalSequence analysis

Sequence similaritiesi

Contains 8 BRCT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1929. Eukaryota.
ENOG410XPFH. LUCA.
GeneTreeiENSGT00840000129846.
HOGENOMiHOG000154662.
HOVERGENiHBG067053.
InParanoidiQ92547.
KOiK10728.
OMAiCAQEYKH.
OrthoDBiEOG091G02MY.
PhylomeDBiQ92547.
TreeFamiTF326403.

Family and domain databases

Gene3Di3.40.50.10190. 6 hits.
InterProiIPR001357. BRCT_dom.
IPR016126. Secretoglobin.
IPR026993. Topbp1.
[Graphical view]
PANTHERiPTHR13561:SF32. PTHR13561:SF32. 3 hits.
PfamiPF00533. BRCT. 4 hits.
PF12738. PTCB-BRCT. 2 hits.
[Graphical view]
SMARTiSM00292. BRCT. 7 hits.
[Graphical view]
SUPFAMiSSF48201. SSF48201. 1 hit.
SSF52113. SSF52113. 6 hits.
PROSITEiPS50172. BRCT. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRNDKEPFF VKFLKSSDNS KCFFKALESI KEFQSEEYLQ IITEEEALKI
60 70 80 90 100
KENDRSLYIC DPFSGVVFDH LKKLGCRIVG PQVVIFCMHH QRCVPRAEHP
110 120 130 140 150
VYNMVMSDVT ISCTSLEKEK REEVHKYVQM MGGRVYRDLN VSVTHLIAGE
160 170 180 190 200
VGSKKYLVAA NLKKPILLPS WIKTLWEKSQ EKKITRYTDI NMEDFKCPIF
210 220 230 240 250
LGCIICVTGL CGLDRKEVQQ LTVKHGGQYM GQLKMNECTH LIVQEPKGQK
260 270 280 290 300
YECAKRWNVH CVTTQWFFDS IEKGFCQDES IYKTEPRPEA KTMPNSSTPT
310 320 330 340 350
SQINTIDSRT LSDVSNISNI NASCVSESIC NSLNSKLEPT LENLENLDVS
360 370 380 390 400
AFQAPEDLLD GCRIYLCGFS GRKLDKLRRL INSGGGVRFN QLNEDVTHVI
410 420 430 440 450
VGDYDDELKQ FWNKSAHRPH VVGAKWLLEC FSKGYMLSEE PYIHANYQPV
460 470 480 490 500
EIPVSHKPES KAALLKKKNS SFSKKDFAPS EKHEQADEDL LSQYENGSST
510 520 530 540 550
VVEAKTSEAR PFNDSTHAEP LNDSTHISLQ EENQSSVSHC VPDVSTITEE
560 570 580 590 600
GLFSQKSFLV LGFSNENESN IANIIKENAG KIMSLLSRTV ADYAVVPLLG
610 620 630 640 650
CEVEATVGEV VTNTWLVTCI DYQTLFDPKS NPLFTPVPVM TGMTPLEDCV
660 670 680 690 700
ISFSQCAGAE KESLTFLANL LGASVQEYFV RKSNAKKGMF ASTHLILKER
710 720 730 740 750
GGSKYEAAKK WNLPAVTIAW LLETARTGKR ADESHFLIEN STKEERSLET
760 770 780 790 800
EITNGINLNS DTAEHPGTRL QTHRKTVVTP LDMNRFQSKA FRAVVSQHAR
810 820 830 840 850
QVAASPAVGQ PLQKEPSLHL DTPSKFLSKD KLFKPSFDVK DALAALETPG
860 870 880 890 900
RPSQQKRKPS TPLSEVIVKN LQLALANSSR NAVALSASPQ LKEAQSEKEE
910 920 930 940 950
APKPLHKVVV CVSKKLSKKQ SELNGIAASL GADYRWSFDE TVTHFIYQGR
960 970 980 990 1000
PNDTNREYKS VKERGVHIVS EHWLLDCAQE CKHLPESLYP HTYNPKMSLD
1010 1020 1030 1040 1050
ISAVQDGRLC NSRLLSAVSS TKDDEPDPLI LEENDVDNMA TNNKESAPSN
1060 1070 1080 1090 1100
GSGKNDSKGV LTQTLEMREN FQKQLQEIMS ATSIVKPQGQ RTSLSRSGCN
1110 1120 1130 1140 1150
SASSTPDSTR SARSGRSRVL EALRQSRQTV PDVNTEPSQN EQIIWDDPTA
1160 1170 1180 1190 1200
REERARLASN LQWPSCPTQY SELQVDIQNL EDSPFQKPLH DSEIAKQAVC
1210 1220 1230 1240 1250
DPGNIRVTEA PKHPISEELE TPIKDSHLIP TPQAPSIAFP LANPPVAPHP
1260 1270 1280 1290 1300
REKIITIEET HEELKKQYIF QLSSLNPQER IDYCHLIEKL GGLVIEKQCF
1310 1320 1330 1340 1350
DPTCTHIVVG HPLRNEKYLA SVAAGKWVLH RSYLEACRTA GHFVQEEDYE
1360 1370 1380 1390 1400
WGSSSILDVL TGINVQQRRL ALAAMRWRKK IQQRQESGIV EGAFSGWKVI
1410 1420 1430 1440 1450
LHVDQSREAG FKRLLQSGGA KVLPGHSVPL FKEATHLFSD LNKLKPDDSG
1460 1470 1480 1490 1500
VNIAEAAAQN VYCLRTEYIA DYLMQESPPH VENYCLPEAI SFIQNNKELG
1510 1520
TGLSQKRKAP TEKNKIKRPR VH
Length:1,522
Mass (Da):170,679
Last modified:May 18, 2010 - v3
Checksum:i02C25880EDCD6AC7
GO

Sequence cautioni

The sequence BAA13389 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA34202 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti457 – 4571K → Q in BAA34202 (PubMed:9461304).Curated
Sequence conflicti457 – 4571K → Q in BAA13389 (PubMed:9039502).Curated
Sequence conflicti911 – 9111C → R in BAH13754 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti817 – 8171S → L.
Corresponds to variant rs17301766 [ dbSNP | Ensembl ].
VAR_059733
Natural varianti955 – 9551N → S.
Corresponds to variant rs10935070 [ dbSNP | Ensembl ].
VAR_057007
Natural varianti1042 – 10421N → S.
Corresponds to variant rs10935070 [ dbSNP | Ensembl ].
VAR_059734

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019397 mRNA. Translation: BAA34202.1. Different initiation.
D87448 mRNA. Translation: BAA13389.1. Different initiation.
AK302584 mRNA. Translation: BAH13754.1.
AC016255 Genomic DNA. No translation available.
AC083905 Genomic DNA. No translation available.
CCDSiCCDS46919.1.
RefSeqiNP_008958.2. NM_007027.3.
UniGeneiHs.593379.

Genome annotation databases

EnsembliENST00000260810; ENSP00000260810; ENSG00000163781.
GeneIDi11073.
KEGGihsa:11073.
UCSCiuc003eps.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019397 mRNA. Translation: BAA34202.1. Different initiation.
D87448 mRNA. Translation: BAA13389.1. Different initiation.
AK302584 mRNA. Translation: BAH13754.1.
AC016255 Genomic DNA. No translation available.
AC083905 Genomic DNA. No translation available.
CCDSiCCDS46919.1.
RefSeqiNP_008958.2. NM_007027.3.
UniGeneiHs.593379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WF6NMR-A326-444[»]
2XNHX-ray2.80A1-287[»]
2XNKX-ray2.60A/B/C/D1-290[»]
3AL2X-ray2.00A1264-1493[»]
3AL3X-ray2.15A1264-1493[»]
3JVEX-ray1.34A893-996[»]
3OLCX-ray2.40X1-290[»]
3PD7X-ray1.26A/B893-994[»]
3UENX-ray1.90A549-746[»]
3UEOX-ray2.60A/B/C/D549-746[»]
ProteinModelPortaliQ92547.
SMRiQ92547. Positions 7-286, 329-445, 550-744, 901-994, 1266-1493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116256. 55 interactions.
DIPiDIP-24263N.
IntActiQ92547. 19 interactions.
MINTiMINT-275958.
STRINGi9606.ENSP00000260810.

Chemistry

BindingDBiQ92547.
ChEMBLiCHEMBL3175.

PTM databases

iPTMnetiQ92547.
PhosphoSiteiQ92547.

Polymorphism and mutation databases

BioMutaiTOPBP1.
DMDMi296453012.

Proteomic databases

EPDiQ92547.
MaxQBiQ92547.
PaxDbiQ92547.
PeptideAtlasiQ92547.
PRIDEiQ92547.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260810; ENSP00000260810; ENSG00000163781.
GeneIDi11073.
KEGGihsa:11073.
UCSCiuc003eps.4. human.

Organism-specific databases

CTDi11073.
GeneCardsiTOPBP1.
H-InvDBHIX0003693.
HGNCiHGNC:17008. TOPBP1.
HPAiCAB022451.
HPA036738.
HPA063020.
HPA064566.
MIMi607760. gene.
neXtProtiNX_Q92547.
PharmGKBiPA134934073.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1929. Eukaryota.
ENOG410XPFH. LUCA.
GeneTreeiENSGT00840000129846.
HOGENOMiHOG000154662.
HOVERGENiHBG067053.
InParanoidiQ92547.
KOiK10728.
OMAiCAQEYKH.
OrthoDBiEOG091G02MY.
PhylomeDBiQ92547.
TreeFamiTF326403.

Enzyme and pathway databases

ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ92547.
SIGNORiQ92547.

Miscellaneous databases

ChiTaRSiTOPBP1. human.
EvolutionaryTraceiQ92547.
GeneWikiiTOPBP1.
GenomeRNAii11073.
PROiQ92547.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163781.
CleanExiHS_TOPBP1.
ExpressionAtlasiQ92547. baseline and differential.
GenevisibleiQ92547. HS.

Family and domain databases

Gene3Di3.40.50.10190. 6 hits.
InterProiIPR001357. BRCT_dom.
IPR016126. Secretoglobin.
IPR026993. Topbp1.
[Graphical view]
PANTHERiPTHR13561:SF32. PTHR13561:SF32. 3 hits.
PfamiPF00533. BRCT. 4 hits.
PF12738. PTCB-BRCT. 2 hits.
[Graphical view]
SMARTiSM00292. BRCT. 7 hits.
[Graphical view]
SUPFAMiSSF48201. SSF48201. 1 hit.
SSF52113. SSF52113. 6 hits.
PROSITEiPS50172. BRCT. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOPB1_HUMAN
AccessioniPrimary (citable) accession number: Q92547
Secondary accession number(s): B7Z7W8, Q7LGC1, Q9UEB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 18, 2010
Last modified: September 7, 2016
This is version 155 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.