Q9NR09 (BIRC6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Baculoviral IAP repeat-containing protein 6
EC=6.3.2.-

Alternative name(s):
BIR repeat-containing ubiquitin-conjugating enzyme
Short name=BRUCE
Ubiquitin-conjugating BIR domain enzyme apollon
Short name=APOLLON

Gene names

Name:	BIRC6
Synonyms:	KIAA1289

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4857 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification. Ref.5 Ref.6 Ref.9
Enzyme regulation	Inhibited by DIABLO/SMAC, HTRA2, CASP3, CASP6, CASP7 and CASP9. Ref.6
Subunit structure	Homodimer. Binds the activated, processed forms of CASP3, CASP6, CASP7 and CASP9. Interacts with RNF41, DIABLO/SMAC, HTRA2, KIF23/MKLP1, USP8/UBPY, BIRC5/survivin, MAP2K1/MEK1, RAB8A/RAB8, RAB11A/RAB11, PLK1, EXOC3/SEC6 and EXOC4/SEC8. Ref.5 Ref.6 Ref.9
Subcellular location	Golgi apparatus › trans-Golgi network membrane. Midbody. Endosome. Cytoplasm › cytoskeleton › spindle pole. Cytoplasm › cytoskeleton › centrosome. Note: Concentrates in a pericentriolar compartment in interphase, moves partially to spindle poles in metaphase, and finally localizes to the spindle midzone and the midbody in telophase and during cytokinesis. Ref.9
Tissue specificity	Expressed in brain cancer cells.
Domain	The BIR domain is essential for its antiapoptotic function and is important for binding to DIABLO/SMAC and CASP9. Ref.6
Post-translational modification	Ubiquitinated. Ubiquitination is mediated by the RNF41 E3 ligase and leads to proteasomal degradation, impairing inhibition of apoptosis. Deubiquitinated by USP8/UBPY. Ref.5 Ref.9
Sequence similarities	In the C-terminal section; belongs to the ubiquitin-conjugating enzyme family. Contains 1 BIR repeat.
Sequence caution	The sequence BAA86603.2 differs from that shown. Reason: Frameshift at position 2047.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton Endosome Golgi apparatus Membrane
Molecular function	Ligase Protease inhibitor Thiol protease inhibitor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW labyrinthine layer development Inferred from electronic annotation. Source: Compara mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Inferred from mutant phenotype Ref.5Ref.6. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara protein phosphorylation Traceable author statement Ref.9. Source: UniProtKB regulation of cell proliferation Traceable author statement Ref.10. Source: UniProtKB regulation of cytokinesis Inferred from mutant phenotype Ref.9. Source: UniProtKB spongiotrophoblast layer development Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Inferred from direct assay Ref.9. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-KW microtubule organizing center Inferred from direct assay Ref.9. Source: UniProtKB midbody Inferred from direct assay Ref.9. Source: UniProtKB spindle pole Inferred from direct assay Ref.9. Source: UniProtKB trans-Golgi network Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase inhibitor activity Inferred from mutant phenotype Ref.6. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXOC4	Q96A65	3	EBI-1765160,EBI-355383
KIF23	Q02241	4	EBI-1765160,EBI-306852
MAP2K1	Q02750	2	EBI-1765160,EBI-492564
PLK1	P53350	3	EBI-1765160,EBI-476768

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 4857

4857

Baculoviral IAP repeat-containing protein 6

PRO_0000122361

Regions

Repeat

284 – 358

75

BIR

Region

4576 – 4704

129

Ubiquitin-conjugating

Compositional bias

30 – 36

7

Poly-Ala

Compositional bias

1660 – 1668

9

Poly-Ala

Sites

Active site

4625

1

Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue

473

1

Phosphoserine By similarity

Modified residue

480

1

Phosphoserine Ref.11 Ref.13 Ref.15

Modified residue

486

1

Phosphoserine By similarity

Modified residue

2953

1

Phosphoserine By similarity

Experimental info

Sequence conflict

1332

1

V → L in AAF75772. Ref.2

Sequence conflict

2319

1

L → F in BAA86603. Ref.3

Sequence conflict

2674

1

T → S in AAF75772. Ref.2

Secondary structure

1

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4857

Helix Strand Turn

Details...

Helix

4524 – 4533

10

Beta strand

4536 – 4540

5

Beta strand

4543 – 4545

3

Beta strand

4551 – 4555

5

Helix

4560 – 4564

5

Helix

4572 – 4588

17

Beta strand

4597 – 4604

8

Beta strand

4608 – 4615

8

Beta strand

4625 – 4631

7

Turn

4634 – 4638

5

Beta strand

4642 – 4645

4

Turn

4649 – 4652

4

Helix

4668 – 4670

3

Helix

4677 – 4679

3

Turn

4683 – 4685

3

Helix

4688 – 4698

11

Helix

4704 – 4707

4

Helix

4711 – 4714

4

Helix

4718 – 4738

21

Helix

4741 – 4745

5

Turn

4749 – 4751

3

Helix

4752 – 4777

26

Helix

4788 – 4810

23

Sequences

	Sequence		Length	Mass (Da)
	Q9NR09 [UniParc]. Last modified November 30, 2010. Version 2. Checksum: 0F5939F9C40F4270	FASTA	4,857	530,255
	10 20 30 40 50 60 MVTGGGAAPP GTVTEPLPSV IVLSAGRKMA AAAAAASGPG CSSAAGAGAA GVSEWLVLRD 70 80 90 100 110 120 GCMHCDADGL HSLSYHPALN AILAVTSRGT IKVIDGTSGA TLQASALSAK PGGQVKCQYI 130 140 150 160 170 180 SAVDKVIFVD DYAVGCRKDL NGILLLDTAL QTPVSKQDDV VQLELPVTEA QQLLSACLEK 190 200 210 220 230 240 VDISSTEGYD LFITQLKDGL KNTSHETAAN HKVAKWATVT FHLPHHVLKS IASAIVNELK 250 260 270 280 290 300 KINQNVAALP VASSVMDRLS YLLPSARPEL GVGPGRSVDR SLMYSEANRR ETFTSWPHVG 310 320 330 340 350 360 YRWAQPDPMA QAGFYHQPAS SGDDRAMCFT CSVCLVCWEP TDEPWSEHER HSPNCPFVKG 370 380 390 400 410 420 EHTQNVPLSV TLATSPAQFP CTDGTDRISC FGSGSCPHFL AAATKRGKIC IWDVSKLMKV 430 440 450 460 470 480 HLKFEINAYD PAIVQQLILS GDPSSGVDSR RPTLAWLEDS SSCSDIPKLE GDSDDLLEDS 490 500 510 520 530 540 DSEEHSRSDS VTGHTSQKEA MEVSLDITAL SILQQPEKLQ WEIVANVLED TVKDLEELGA 550 560 570 580 590 600 NPCLTNSKSE KTKEKHQEQH NIPFPCLLAG GLLTYKSPAT SPISSNSHRS LDGLSRTQGE 610 620 630 640 650 660 SISEQGSTDN ESCTNSELNS PLVRRTLPVL LLYSIKESDE KAGKIFSQMN NIMSKSLHDD 670 680 690 700 710 720 GFTVPQIIEM ELDSQEQLLL QDPPVTYIQQ FADAAANLTS PDSEKWNSVF PKPGTLVQCL 730 740 750 760 770 780 RLPKFAEEEN LCIDSITPCA DGIHLLVGLR TCPVESLSAI NQVEALNNLN KLNSALCNRR 790 800 810 820 830 840 KGELESNLAV VNGANISVIQ HESPADVQTP LIIQPEQRNV SGGYLVLYKM NYATRIVTLE 850 860 870 880 890 900 EEPIKIQHIK DPQDTITSLI LLPPDILDNR EDDCEEPIED MQLTSKNGFE REKTSDISTL 910 920 930 940 950 960 GHLVITTQGG YVKILDLSNF EILAKVEPPK KEGTEEQDTF VSVIYCSGTD RLCACTKGGE 970 980 990 1000 1010 1020 LHFLQIGGTC DDIDEADILV DGSLSKGIEP SSEGSKPLSN PSSPGISGVD LLVDQPFTLE 1030 1040 1050 1060 1070 1080 ILTSLVELTR FETLTPRFSA TVPPCWVEVQ QEQQQRRHPQ HLHQQHHGDA AQHTRTWKLQ 1090 1100 1110 1120 1130 1140 TDSNSWDEHV FELVLPKACM VGHVDFKFVL NSNITNIPQI QVTLLKNKAP GLGKVNALNI 1150 1160 1170 1180 1190 1200 EVEQNGKPSL VDLNEEMQHM DVEESQCLRL CPFLEDHKED ILCGPVWLAS GLDLSGHAGM 1210 1220 1230 1240 1250 1260 LTLTSPKLVK GMAGGKYRSF LIHVKAVNER GTEEICNGGM RPVVRLPSLK HQSNKGYSLA 1270 1280 1290 1300 1310 1320 SLLAKVAAGK EKSSNVKNEN TSGTRKSENL RGCDLLQEVS VTIRRFKKTS ISKERVQRCA 1330 1340 1350 1360 1370 1380 MLQFSEFHEK LVNTLCRKTD DGQITEHAQS LVLDTLCWLA GVHSNGPGSS KEGNENLLSK 1390 1400 1410 1420 1430 1440 TRKFLSDIVR VCFFEAGRSI AHKCARFLAL CISNGKCDPC QPAFGPVLLK ALLDNMSFLP 1450 1460 1470 1480 1490 1500 AATTGGSVYW YFVLLNYVKD EDLAGCSTAC ASLLTAVSRQ LQDRLTPMEA LLQTRYGLYS 1510 1520 1530 1540 1550 1560 SPFDPVLFDL EMSGSSCKNV YNSSIGVQSD EIDLSDVLSG NGKVSSCTAA EGSFTSLTGL 1570 1580 1590 1600 1610 1620 LEVEPLHFTC VSTSDGTRIE RDDAMSSFGV TPAVGGLSSG TVGEASTALS SAAQVALQSL 1630 1640 1650 1660 1670 1680 SHAMASAEQQ LQVLQEKQQQ LLKLQQQKAK LEAKLHQTTA AAAAAASAVG PVHNSVPSNP 1690 1700 1710 1720 1730 1740 VAAPGFFIHP SDVIPPTPKT TPLFMTPPLT PPNEAVSVVI NAELAQLFPG SVIDPPAVNL 1750 1760 1770 1780 1790 1800 AAHNKNSNKS RMNPLGSGLA LAISHASHFL QPPPHQSIII ERMHSGARRF VTLDFGRPIL 1810 1820 1830 1840 1850 1860 LTDVLIPTCG DLASLSIDIW TLGEEVDGRR LVVATDISTH SLILHDLIPP PVCRFMKITV 1870 1880 1890 1900 1910 1920 IGRYGSTNAR AKIPLGFYYG HTYILPWESE LKLMHDPLKG EGESANQPEI DQHLAMMVAL 1930 1940 1950 1960 1970 1980 QEDIQCRYNL ACHRLETLLQ SIDLPPLNSA NNAQYFLRKP DKAVEEDSRV FSAYQDCIQL 1990 2000 2010 2020 2030 2040 QLQLNLAHNA VQRLKVALGA SRKMLSETSN PEDLIQTSST EQLRTIIRYL LDTLLSLLHA 2050 2060 2070 2080 2090 2100 SNGHSVPAVL QSTFHAQACE ELFKHLCISG TPKIRLHTGL LLVQLCGGER WWGQFLSNVL 2110 2120 2130 2140 2150 2160 QELYNSEQLL IFPQDRVFML LSCIGQRSLS NSGVLESLLN LLDNLLSPLQ PQLPMHRRTE 2170 2180 2190 2200 2210 2220 GVLDIPMISW VVMLVSRLLD YVATVEDEAA AAKKPLNGNQ WSFINNNLHT QSLNRSSKGS 2230 2240 2250 2260 2270 2280 SSLDRLYSRK IRKQLVHHKQ QLNLLKAKQK ALVEQMEKEK IQSNKGSSYK LLVEQAKLKQ 2290 2300 2310 2320 2330 2340 ATSKHFKDLI RLRRTAEWSR SNLDTEVTTA KESPEIEPLP FTLAHERCIS VVQKLVLFLL 2350 2360 2370 2380 2390 2400 SMDFTCHADL LLFVCKVLAR IANATRPTIH LCEIVNEPQL ERLLLLLVGT DFNRGDISWG 2410 2420 2430 2440 2450 2460 GAWAQYSLTC MLQDILAGEL LAPVAAEAME EGTVGDDVGA TAGDSDDSLQ QSSVQLLETI 2470 2480 2490 2500 2510 2520 DEPLTHDITG APPLSSLEKD KEIDLELLQD LMEVDIDPLD IDLEKDPLAA KVFKPISSTW 2530 2540 2550 2560 2570 2580 YDYWGADYGT YNYNPYIGGL GIPVAKPPAN TEKNGSQTVS VSVSQALDAR LEVGLEQQAE 2590 2600 2610 2620 2630 2640 LMLKMMSTLE ADSILQALTN TSPTLSQSPT GTDDSLLGGL QAANQTSQLI IQLSSVPMLN 2650 2660 2670 2680 2690 2700 VCFNKLFSML QVHHVQLESL LQLWLTLSLN SSSTGNKENG ADIFLYNANR IPVISLNQAS 2710 2720 2730 2740 2750 2760 ITSFLTVLAW YPNTLLRTWC LVLHSLTLMT NMQLNSGSSS AIGTQESTAH LLVSDPNLIH 2770 2780 2790 2800 2810 2820 VLVKFLSGTS PHGTNQHSPQ VGPTATQAMQ EFLTRLQVHL SSTCPQIFSE FLLKLIHILS 2830 2840 2850 2860 2870 2880 TERGAFQTGQ GPLDAQVKLL EFTLEQNFEV VSVSTISAVI ESVTFLVHHY ITCSDKVMSR 2890 2900 2910 2920 2930 2940 SGSDSSVGAR ACFGGLFANL IRPGDAKAVC GEMTRDQLMF DLLKLVNILV QLPLSGNREY 2950 2960 2970 2980 2990 3000 SARVSVTTNT TDSVSDEEKV SGGKDGNGSS TSVQGSPAYV ADLVLANQQI MSQILSALGL 3010 3020 3030 3040 3050 3060 CNSSAMAMII GASGLHLTKH ENFHGGLDAI SVGDGLFTIL TTLSKKASTV HMMLQPILTY 3070 3080 3090 3100 3110 3120 MACGYMGRQG SLATCQLSEP LLWFILRVLD TSDALKAFHD MGGVQLICNN MVTSTRAIVN 3130 3140 3150 3160 3170 3180 TARSMVSTIM KFLDSGPNKA VDSTLKTRIL ASEPDNAEGI HNFAPLGTIT SSSPTAQPAE 3190 3200 3210 3220 3230 3240 VLLQATPPHR RARSAAWSYI FLPEEAWCDL TIHLPAAVLL KEIHIQPHLA SLATCPSSVS 3250 3260 3270 3280 3290 3300 VEVSADGVNM LPLSTPVVTS GLTYIKIQLV KAEVASAVCL RLHRPRDAST LGLSQIKLLG 3310 3320 3330 3340 3350 3360 LTAFGTTSSA TVNNPFLPSE DQVSKTSIGW LRLLHHCLTH ISDLEGMMAS AAAPTANLLQ 3370 3380 3390 3400 3410 3420 TCAALLMSPY CGMHSPNIEV VLVKIGLQST RIGLKLIDIL LRNCAASGSD PTDLNSPLLF 3430 3440 3450 3460 3470 3480 GRLNGLSSDS TIDILYQLGT TQDPGTKDRI QALLKWVSDS ARVAAMKRSG RMNYMCPNSS 3490 3500 3510 3520 3530 3540 TVEYGLLMPS PSHLHCVAAI LWHSYELLVE YDLPALLDQE LFELLFNWSM SLPCNMVLKK 3550 3560 3570 3580 3590 3600 AVDSLLCSMC HVHPNYFSLL MGWMGITPPP VQCHHRLSMT DDSKKQDLSS SLTDDSKNAQ 3610 3620 3630 3640 3650 3660 APLALTESHL ATLASSSQSP EAIKQLLDSG LPSLLVRSLA SFCFSHISSS ESIAQSIDIS 3670 3680 3690 3700 3710 3720 QDKLRRHHVP QQCNKMPITA DLVAPILRFL TEVGNSHIMK DWLGGSEVNP LWTALLFLLC 3730 3740 3750 3760 3770 3780 HSGSTSGSHN LGAQQTSARS ASLSSAATTG LTTQQRTAIE NATVAFFLQC ISCHPNNQKL 3790 3800 3810 3820 3830 3840 MAQVLCELFQ TSPQRGNLPT SGNISGFIRR LFLQLMLEDE KVTMFLQSPC PLYKGRINAT 3850 3860 3870 3880 3890 3900 SHVIQHPMYG AGHKFRTLHL PVSTTLSDVL DRVSDTPSIT AKLISEQKDD KEKKNHEEKE 3910 3920 3930 3940 3950 3960 KVKAENGFQD NYSVVVASGL KSQSKRAVSA TPPRPPSRRG RTIPDKIGST SGAEAANKII 3970 3980 3990 4000 4010 4020 TVPVFHLFHK LLAGQPLPAE MTLAQLLTLL YDRKLPQGYR SIDLTVKLGS RVITDPSLSK 4030 4040 4050 4060 4070 4080 TDSYKRLHPE KDHGDLLASC PEDEALTPGD ECMDGILDES LLETCPIQSP LQVFAGMGGL 4090 4100 4110 4120 4130 4140 ALIAERLPML YPEVIQQVSA PVVTSTTQEK PKDSDQFEWV TIEQSGELVY EAPETVAAEP 4150 4160 4170 4180 4190 4200 PPIKSAVQTM SPIPAHSLAA FGLFLRLPGY AEVLLKERKH AQCLLRLVLG VTDDGEGSHI 4210 4220 4230 4240 4250 4260 LQSPSANVLP TLPFHVLRSL FSTTPLTTDD GVLLRRMALE IGALHLILVC LSALSHHSPR 4270 4280 4290 4300 4310 4320 VPNSSVNQTE PQVSSSHNPT STEEQQLYWA KGTGFGTGST ASGWDVEQAL TKQRLEEEHV 4330 4340 4350 4360 4370 4380 TCLLQVLASY INPVSSAVNG EAQSSHETRG QNSNALPSVL LELLSQSCLI PAMSSYLRND 4390 4400 4410 4420 4430 4440 SVLDMARHVP LYRALLELLR AIASCAAMVP LLLPLSTENG EEEEEQSECQ TSVGTLLAKM 4450 4460 4470 4480 4490 4500 KTCVDTYTNR LRSKRENVKT GVKPDASDQE PEGLTLLVPD IQKTAEIVYA ATTSLRQANQ 4510 4520 4530 4540 4550 4560 EKKLGEYSKK AAMKPKPLSV LKSLEEKYVA VMKKLQFDTF EMVSEDEDGK LGFKVNYHYM 4570 4580 4590 4600 4610 4620 SQVKNANDAN SAARARRLAQ EAVTLSTSLP LSSSSSVFVR CDEERLDIMK VLITGPADTP 4630 4640 4650 4660 4670 4680 YANGCFEFDV YFPQDYPSSP PLVNLETTGG HSVRFNPNLY NDGKVCLSIL NTWHGRPEEK 4690 4700 4710 4720 4730 4740 WNPQTSSFLQ VLVSVQSLIL VAEPYFNEPG YERSRGTPSG TQSSREYDGN IRQATVKWAM 4750 4760 4770 4780 4790 4800 LEQIRNPSPC FKEVIHKHFY LKRVEIMAQC EEWIADIQQY SSDKRVGRTM SHHAAALKRH 4810 4820 4830 4840 4850 TAQLREELLK LPCPEGLDPD TDDAPEVCRA TTGAEETLMH DQVKPSSSKE LPSDFQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"A human IAP-family gene, apollon, expressed in human brain cancer cells." Chen Z., Naito M., Hori S., Mashima T., Yamori T., Tsuruo T. Biochem. Biophys. Res. Commun. 264:847-854(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-4857. Tissue: Brain.
[3]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2063-4857. Tissue: Brain.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel pathway for triggering apoptosis." Qiu X.B., Markant S.L., Yuan J., Goldberg A.L. EMBO J. 23:800-810(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF41, UBIQUITINATION, FUNCTION.
[6]	"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase." Bartke T., Pohl C., Pyrowolakis G., Jentsch S. Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION, DOMAIN BIR, INTERACTION WITH HTRA2; CASP3; CASP6; CASP7; CASP9 AND DIABLO/SMAC.
[7]	"An Apollon vista of death and destruction." Martin S.J. Nat. Cell Biol. 6:804-806(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"Final stages of cytokinesis and midbody ring formation are controlled by BRUCE." Pohl C., Jentsch S. Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, DEUBIQUITINATION, INTERACTION WITH KIF23/MKLP1; USP8/UBPY; BIRC5/SURVIVIN; MAP2K1/MEK1; RAB8A/RAB8; RAB11A/RAB11; PLK1; EXOC3/SEC6 AND EXOC4/SEC8.
[10]	"IAPs: more than just inhibitors of apoptosis proteins." Dubrez-Daloz L., Dupoux A., Cartier J. Cell Cycle 7:1036-1046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY.
[16]	"Ubc domain of the ubiquitin-protein ligase baculoviral IAP repeat-containing protein 6." Structural genomics consortium (SGC) Submitted (APR-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 4498-4820.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AC079837 Genomic DNA. No translation available.
AL133243 Genomic DNA. No translation available.
AL133245 Genomic DNA. No translation available.
AL133246 Genomic DNA. No translation available.
AF265555 mRNA. Translation: AAF75772.1.
AB033115 mRNA. Translation: BAA86603.2. Frameshift.

IPI

IPI00939720.

RefSeq

NP_057336.3. NM_016252.3.

UniGene

Hs.150107.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CEG	X-ray	2.01	A/B	4498-4820	[»]

ProteinModelPortal

Q9NR09.

SMR

Q9NR09. Positions 4521-4818.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NR09. 13 interactions.

STRING

9606.ENSP00000393596.

Protein family/group databases

MEROPS

I32.006.

PTM databases

PhosphoSite

Q9NR09.

Polymorphism databases

DMDM

12585192.

Proteomic databases

PaxDb

Q9NR09.

PRIDE

Q9NR09.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000421745; ENSP00000393596; ENSG00000115760.

GeneID

57448.

KEGG

hsa:57448.

UCSC

uc010ezu.3. human.

Organism-specific databases

CTD

57448.

GeneCards

GC02P032582.

H-InvDB

HIX0001957.
HIX0030282.

HGNC

HGNC:13516. BIRC6.

MIM

605638. gene.

neXtProt

NX_Q9NR09.

PharmGKB

PA25363.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000168828.

HOVERGEN

HBG050691.

InParanoid

Q9NR09.

KO

K10586.

OMA

FLIHVKA.

OrthoDB

EOG4DJJVH.

Gene expression databases

ArrayExpress

Q9NR09.

Bgee

Q9NR09.

CleanEx

HS_BIRC6.

Genevestigator

Q9NR09.

Family and domain databases

Gene3D

1.10.1170.10. 1 hit.
2.130.10.10. 4 hits.
3.10.110.10. 1 hit.

InterPro

IPR001370. BIR.
IPR022103. DUF3643.
IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]

Pfam

PF00653. BIR. 1 hit.
PF12356. DUF3643. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]

SMART

SM00238. BIR. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS01282. BIR_REPEAT_1. False negative.
PS50143. BIR_REPEAT_2. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

BIRC6. human.

EvolutionaryTrace

Q9NR09.

GenomeRNAi

57448.

NextBio

63594.

SOURCE

Search...

Entry information

Entry name

BIRC6_HUMAN

Accession

Primary (citable) accession number: Q9NR09
Secondary accession number(s): Q9ULD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 116 of the entry and version 2 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.