Q92547 (TOPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TOPBP1
Synonyms:	KIAA0259

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.12
Subunit structure	Binds E2F1, PML, RAD9A, C12orf32/RHINO, SMARCA2, SMARCA4, POLE and UBR5. May interact with TOP2B. Interacts with TICRR/C15orf42. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.19 Ref.21
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Cytoplasm › cytoskeleton › spindle 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.21
Tissue specificity	Highly expressed in heart, brain, placenta, lung and kidney. Ref.1
Induction	Up-regulated during the S phase of the cell cycle. Up-regulated by E2F1 and interferon. Ref.9
Post-translational modification	Phosphorylated on serine and threonine residues in response to X-ray irradiation. Ref.6 Ref.7 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ubiquitinated and degraded by the proteasome. X-ray irradiation reduces ubiquitination. Ref.7
Sequence similarities	Contains 8 BRCT domains.
Sequence caution	The sequence BAA13389.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA34202.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Chromosome Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Non-traceable author statement Ref.9. Source: UniProtKB response to ionizing radiation Inferred from direct assay Ref.9. Source: UniProtKB
Cellular component	PML body Inferred from direct assay Ref.9. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC45	O75419	6	EBI-308302,EBI-374969

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1522

1522

DNA topoisomerase 2-binding protein 1

PRO_0000072631

Regions

Domain

101 – 189

89

BRCT 1

Domain

195 – 284

90

BRCT 2

Domain

354 – 444

91

BRCT 3

Domain

548 – 633

86

BRCT 4

Domain

641 – 738

98

BRCT 5

Domain

900 – 991

92

BRCT 6

Domain

1259 – 1351

93

BRCT 7

Domain

1389 – 1486

98

BRCT 8

Motif

852 – 858

7

Nuclear localization signal Potential

Motif

1517 – 1520

4

Nuclear localization signal Potential

Amino acid modifications

Modified residue

298

1

Phosphothreonine Ref.14

Modified residue

301

1

Phosphoserine Ref.14

Modified residue

492

1

Phosphoserine Ref.14

Modified residue

581

1

N6-acetyllysine Ref.18

Modified residue

779

1

Phosphothreonine Ref.16

Modified residue

805

1

Phosphoserine Ref.13 Ref.15

Modified residue

848

1

Phosphothreonine Ref.16

Modified residue

860

1

Phosphoserine Ref.16

Modified residue

861

1

Phosphothreonine Ref.16

Modified residue

864

1

Phosphoserine Ref.16

Modified residue

888

1

Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17

Modified residue

1002

1

Phosphoserine Ref.15 Ref.16

Modified residue

1062

1

Phosphothreonine Ref.14

Modified residue

1138

1

Phosphoserine Ref.14

Natural variations

Natural variant

817

1

S → L.
Corresponds to variant rs17301766 [ dbSNP | Ensembl ].

VAR_059733

Natural variant

955

1

N → S.
Corresponds to variant rs10935070 [ dbSNP | Ensembl ].

VAR_057007

Natural variant

1042

1

N → S.
Corresponds to variant rs10935070 [ dbSNP | Ensembl ].

VAR_059734

Experimental info

Sequence conflict

457

1

K → Q in BAA34202. Ref.1

Sequence conflict

457

1

K → Q in BAA13389. Ref.2

Sequence conflict

911

1

C → R in BAH13754. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

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1522

Helix Strand Turn

Details...

Beta strand

333 – 335

3

Helix

341 – 343

3

Helix

349 – 351

3

Turn

356 – 361

6

Beta strand

363 – 368

6

Helix

372 – 383

12

Beta strand

387 – 391

5

Beta strand

398 – 403

6

Helix

407 – 414

8

Beta strand

421 – 423

3

Helix

424 – 433

10

Helix

440 – 442

3

Sequences

	Sequence		Length	Mass (Da)
	Q92547 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 02C25880EDCD6AC7	FASTA	1,522	170,679
	10 20 30 40 50 60 MSRNDKEPFF VKFLKSSDNS KCFFKALESI KEFQSEEYLQ IITEEEALKI KENDRSLYIC 70 80 90 100 110 120 DPFSGVVFDH LKKLGCRIVG PQVVIFCMHH QRCVPRAEHP VYNMVMSDVT ISCTSLEKEK 130 140 150 160 170 180 REEVHKYVQM MGGRVYRDLN VSVTHLIAGE VGSKKYLVAA NLKKPILLPS WIKTLWEKSQ 190 200 210 220 230 240 EKKITRYTDI NMEDFKCPIF LGCIICVTGL CGLDRKEVQQ LTVKHGGQYM GQLKMNECTH 250 260 270 280 290 300 LIVQEPKGQK YECAKRWNVH CVTTQWFFDS IEKGFCQDES IYKTEPRPEA KTMPNSSTPT 310 320 330 340 350 360 SQINTIDSRT LSDVSNISNI NASCVSESIC NSLNSKLEPT LENLENLDVS AFQAPEDLLD 370 380 390 400 410 420 GCRIYLCGFS GRKLDKLRRL INSGGGVRFN QLNEDVTHVI VGDYDDELKQ FWNKSAHRPH 430 440 450 460 470 480 VVGAKWLLEC FSKGYMLSEE PYIHANYQPV EIPVSHKPES KAALLKKKNS SFSKKDFAPS 490 500 510 520 530 540 EKHEQADEDL LSQYENGSST VVEAKTSEAR PFNDSTHAEP LNDSTHISLQ EENQSSVSHC 550 560 570 580 590 600 VPDVSTITEE GLFSQKSFLV LGFSNENESN IANIIKENAG KIMSLLSRTV ADYAVVPLLG 610 620 630 640 650 660 CEVEATVGEV VTNTWLVTCI DYQTLFDPKS NPLFTPVPVM TGMTPLEDCV ISFSQCAGAE 670 680 690 700 710 720 KESLTFLANL LGASVQEYFV RKSNAKKGMF ASTHLILKER GGSKYEAAKK WNLPAVTIAW 730 740 750 760 770 780 LLETARTGKR ADESHFLIEN STKEERSLET EITNGINLNS DTAEHPGTRL QTHRKTVVTP 790 800 810 820 830 840 LDMNRFQSKA FRAVVSQHAR QVAASPAVGQ PLQKEPSLHL DTPSKFLSKD KLFKPSFDVK 850 860 870 880 890 900 DALAALETPG RPSQQKRKPS TPLSEVIVKN LQLALANSSR NAVALSASPQ LKEAQSEKEE 910 920 930 940 950 960 APKPLHKVVV CVSKKLSKKQ SELNGIAASL GADYRWSFDE TVTHFIYQGR PNDTNREYKS 970 980 990 1000 1010 1020 VKERGVHIVS EHWLLDCAQE CKHLPESLYP HTYNPKMSLD ISAVQDGRLC NSRLLSAVSS 1030 1040 1050 1060 1070 1080 TKDDEPDPLI LEENDVDNMA TNNKESAPSN GSGKNDSKGV LTQTLEMREN FQKQLQEIMS 1090 1100 1110 1120 1130 1140 ATSIVKPQGQ RTSLSRSGCN SASSTPDSTR SARSGRSRVL EALRQSRQTV PDVNTEPSQN 1150 1160 1170 1180 1190 1200 EQIIWDDPTA REERARLASN LQWPSCPTQY SELQVDIQNL EDSPFQKPLH DSEIAKQAVC 1210 1220 1230 1240 1250 1260 DPGNIRVTEA PKHPISEELE TPIKDSHLIP TPQAPSIAFP LANPPVAPHP REKIITIEET 1270 1280 1290 1300 1310 1320 HEELKKQYIF QLSSLNPQER IDYCHLIEKL GGLVIEKQCF DPTCTHIVVG HPLRNEKYLA 1330 1340 1350 1360 1370 1380 SVAAGKWVLH RSYLEACRTA GHFVQEEDYE WGSSSILDVL TGINVQQRRL ALAAMRWRKK 1390 1400 1410 1420 1430 1440 IQQRQESGIV EGAFSGWKVI LHVDQSREAG FKRLLQSGGA KVLPGHSVPL FKEATHLFSD 1450 1460 1470 1480 1490 1500 LNKLKPDDSG VNIAEAAAQN VYCLRTEYIA DYLMQESPPH VENYCLPEAI SFIQNNKELG 1510 1520 TGLSQKRKAP TEKNKIKRPR VH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A DNA topoisomerase II binding protein with eight repeating regions similar to DNA repair enzymes and to a cell cycle regulator." Yamane K., Kawabata M., Tsuruo T. Eur. J. Biochem. 250:794-799(1997) [PubMed: 9461304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TOP2B, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[2]	"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed: 9039502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed: 16641997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Conserved BRCT regions of TopBP1 and of the tumor suppressor BRCA1 bind strand breaks and termini of DNA." Yamane K., Tsuruo T. Oncogene 18:5194-5203(1999) [PubMed: 10498869] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"BRCT domain-containing protein TopBP1 functions in DNA replication and damage response." Maekiniemi M., Hillukkala T., Tuusa J., Reini K., Vaara M., Huang D., Pospiech H., Majuri I., Westerling T., Maekelae T.P., Syvaeoja J.E. J. Biol. Chem. 276:30399-30406(2001) [PubMed: 11395493] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH POLE AND RAD9A.
[7]	"Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response." Honda Y., Tojo M., Matsuzaki K., Anan T., Matsumoto M., Ando M., Saya H., Nakao M. J. Biol. Chem. 277:3599-3605(2002) [PubMed: 11714696] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH EDD, UBIQUITINATION, PROTEASOME-MEDIATED DEGRADATION, SUBCELLULAR LOCATION.
[8]	"Regulation of E2F1 by BRCT domain-containing protein TopBP1." Liu K., Lin F.-T., Ruppert J.M., Lin W.-C. Mol. Cell. Biol. 23:3287-3304(2003) [PubMed: 12697828] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH E2F1.
[9]	"PML colocalizes with and stabilizes the DNA damage response protein TopBP1." Xu Z.-X., Timanova-Atanasova A., Zhao R.-X., Chang K.-S. Mol. Cell. Biol. 23:4247-4256(2003) [PubMed: 12773567] [Abstract] Cited for: INDUCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
[10]	"TopBP1 localises to centrosomes in mitosis and to chromosome cores in meiosis." Reini K., Uitto L., Perera D., Moens P.B., Freire R., Syvaeoja J.E. Chromosoma 112:323-330(2004) [PubMed: 15138768] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival." Liu K., Luo Y., Lin F.-T., Lin W.-C. Genes Dev. 18:673-686(2004) [PubMed: 15075294] [Abstract] Cited for: FUNCTION, INTERACTION WITH E2F1; SMARCA2; SMARCA4 AND THE SWI/SNF CHROMATIN REMODELING COMPLEX.
[12]	"TopBP1 activates the ATR-ATRIP complex." Kumagai A., Lee J., Yoo H.Y., Dunphy W.G. Cell 124:943-955(2006) [PubMed: 16530042] [Abstract] Cited for: FUNCTION.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805 AND SER-888, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-298; SER-301; SER-492; THR-1062 AND SER-1138, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805; SER-888 AND SER-1002, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-779; THR-848; SER-860; THR-861; SER-864; SER-888 AND SER-1002, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-581, MASS SPECTROMETRY.
[19]	"A vertebrate gene, ticrr, is an essential checkpoint and replication regulator." Sansam C.L., Cruz N.M., Danielian P.S., Amsterdam A., Lau M.L., Hopkins N., Lees J.A. Genes Dev. 24:183-194(2010) [PubMed: 20080954] [Abstract] Cited for: INTERACTION WITH TICRR.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling." Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J. Science 332:1313-1317(2011) [PubMed: 21659603] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH C12ORF32, IDENTIFICATION BY MASS SPECTROMETRY.
[22]	"The third BRCA1 C-terminus (BRCT) domain of topoisomerase II binding protein." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 327-444.
[23]	"Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIbeta binding protein 1." Leung C.C., Kellogg E., Kuhnert A., Hanel F., Baker D., Glover J.N. Protein Sci. 19:162-167(2010) [PubMed: 19937654] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF 893-996.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00293921.

RefSeq

NP_008958.2. NM_007027.3.

UniGene

Hs.593379.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WF6	NMR	-	A	326-444	[»]
2XNH	X-ray	2.80	A	1-287	[»]
2XNK	X-ray	2.60	A/B/C/D	1-290	[»]
3AL2	X-ray	2.00	A	1264-1493	[»]
3AL3	X-ray	2.15	A	1264-1493	[»]
3JVE	X-ray	1.34	A	893-996	[»]
3OLC	X-ray	2.40	X	1-290	[»]
3PD7	X-ray	1.26	A/B	893-994	[»]

ProteinModelPortal

Q92547.

SMR

Q92547. Positions 7-286, 329-445, 643-738, 901-994, 1266-1493.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24263N.

IntAct

Q92547. 5 interactions.

MINT

MINT-275958.

STRING

Q92547.

PTM databases

PhosphoSite

Q92547.

Polymorphism databases

DMDM

296453012.

Proteomic databases

PRIDE

Q92547.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260810; ENSP00000260810; ENSG00000163781.

GeneID

11073.

KEGG

hsa:11073.

UCSC

uc003eps.1. human.

Organism-specific databases

CTD

11073.

GeneCards

GC03M133319.

H-InvDB

HIX0003693.

HGNC

HGNC:17008. TOPBP1.

HPA

CAB022451.

MIM

607760. gene.

neXtProt

NX_Q92547.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00590000083160.

HOGENOM

HBG715774.

HOVERGEN

HBG067053.

InParanoid

Q92547.

OMA

DKLFKPS.

OrthoDB

EOG4FXR6Q.

PhylomeDB

Q92547.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.

Gene expression databases

ArrayExpress

Q92547.

Bgee

Q92547.

CleanEx

HS_TOPBP1.

Genevestigator

Q92547.

GermOnline

ENSG00000163781. Homo sapiens.

Family and domain databases

InterPro

IPR001357. BRCT.
IPR016126. Secretoglobin.
[Graphical view]

KO

K10728.

Pfam

PF00533. BRCT. 6 hits.
[Graphical view]

SMART

SM00292. BRCT. 7 hits.
[Graphical view]

SUPFAM

SSF52113. BRCT. 6 hits.
SSF48201. Secretoglobin. 1 hit.

PROSITE

PS50172. BRCT. 7 hits.
[Graphical view]

ProtoNet

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Other

NextBio

42094.

SOURCE

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Entry information

Entry name

TOPB1_HUMAN

Accession

Primary (citable) accession number: Q92547
Secondary accession number(s): B7Z7W8, Q7LGC1, Q9UEB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.