Q13490 (BIRC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Baculoviral IAP repeat-containing protein 2
EC=6.3.2.-

Alternative name(s):
C-IAP1
IAP homolog B
Inhibitor of apoptosis protein 2
Short name=IAP-2
Short name=hIAP-2
Short name=hIAP2
RING finger protein 48
TNFR2-TRAF-signaling complex protein 2

Gene names

Name:	BIRC2
Synonyms:	API1, IAP2, MIHB, RNF48

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	618 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. Ref.8 Ref.9 Ref.14 Ref.17 Ref.19
Enzyme regulation	The CARD domain inhibits the activation of E3 ubiquitin ligase activity by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. The CARD domain-mediated autoinhibition of the E3 ubiquitin-protein ligase activity suppresses cell proliferation and migration. USP19 regulates the stability of BIRC2/c-IAP1 by preventing its ubiquitination. Ref.18 Ref.23
Subunit structure	Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19. Ref.8 Ref.17 Ref.18 Ref.19 Ref.22
Subcellular location	Cytoplasm. Nucleus. Note: Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells. Ref.8 Ref.17
Tissue specificity	Present in many fetal and adult tissues. Mainly expressed in adult skeletal muscle, thymus, testis, ovary, and pancreas, low or absent in brain and peripheral blood leukocytes.
Domain	The BIR domains mediate nuclear localization. Ref.23 The CARD domain is necessary to stabilize the protein and inhibit the activation of E3 ubiquitin-protein ligase activity of BIRC2/c-IAP1 by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. Ref.23
Post-translational modification	Auto-ubiquitinated and degraded by the proteasome in apoptotic cells.
Sequence similarities	Belongs to the IAP family. Contains 3 BIR repeats. Contains 1 CARD domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NIK/NF-kappaB cascade Traceable author statement Ref.15. Source: UniProtKB cell surface receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome necroptosis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 21525013. Source: UniProtKB placenta development Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 11907583. Source: UniProtKB protein polyubiquitination Inferred from direct assay PubMed 11907583. Source: UniProtKB regulation of RIG-I signaling pathway Traceable author statement Ref.13. Source: UniProtKB regulation of cell cycle Inferred from direct assay Ref.8. Source: UniProtKB regulation of cell differentiation Traceable author statement Ref.10. Source: UniProtKB regulation of cell proliferation Traceable author statement Ref.10. Source: UniProtKB regulation of cysteine-type endopeptidase activity Traceable author statement Ref.15. Source: UniProtKB regulation of inflammatory response Traceable author statement Ref.16. Source: UniProtKB regulation of innate immune response Traceable author statement Ref.16. Source: UniProtKB regulation of nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement Ref.13. Source: UniProtKB regulation of toll-like receptor signaling pathway Traceable author statement Ref.13. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CD40 receptor complex Inferred from sequence or structural similarity. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL nucleus Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	transcription coactivator activity Inferred from mutant phenotype Ref.17. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay PubMed 11907583. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.22PubMed 20447407. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP7	P55210	2	EBI-514538,EBI-523958
DIABLO	Q9NR28	4	EBI-514538,EBI-517508
RIPK1	Q13546	3	EBI-514538,EBI-358507
RIPK2	O43353	3	EBI-514538,EBI-358522
RIPK3	Q9Y572	3	EBI-514538,EBI-298250
RIPK4	P57078	3	EBI-514538,EBI-4422308
TNFRSF12A	Q9NP84	2	EBI-514538,EBI-2851995
TRAF2	Q12933	8	EBI-514538,EBI-355744

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13490-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13490-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 618

618

Baculoviral IAP repeat-containing protein 2

PRO_0000122347

Regions

Repeat

46 – 113

68

BIR 1

Repeat

184 – 250

67

BIR 2

Repeat

269 – 336

68

BIR 3

Domain

453 – 543

91

CARD

Zinc finger

571 – 606

36

RING-type

Sites

Metal binding

306

1

Zinc

Metal binding

309

1

Zinc

Metal binding

326

1

Zinc

Metal binding

333

1

Zinc

Natural variations

Alternative sequence

1 – 49

49

Missing in isoform 2.

VSP_045314

Natural variant

453

1

M → I.
Corresponds to variant rs34749508 [ dbSNP | Ensembl ].

VAR_049535

Natural variant

453

1

M → V. Ref.4

VAR_025016

Natural variant

506

1

A → V. Ref.4
Corresponds to variant rs34510872 [ dbSNP | Ensembl ].

VAR_025017

Natural variant

549

1

P → S. Ref.4
Corresponds to variant rs35494784 [ dbSNP | Ensembl ].

VAR_025018

Experimental info

Sequence conflict

157

1

S → P in AAC50372. Ref.2

Sequence conflict

308

1

C → G in AAC50372. Ref.2

Sequence conflict

414

1

Q → L in AAC50372. Ref.2

Sequence conflict

514

1

L → W in AAC50372. Ref.2

Secondary structure

1

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618

Helix Strand Turn

Details...

Helix

43 – 51

9

Helix

52 – 55

4

Helix

64 – 69

6

Beta strand

72 – 74

3

Beta strand

81 – 83

3

Turn

84 – 86

3

Helix

99 – 106

8

Helix

111 – 117

7

Helix

264 – 266

3

Helix

269 – 274

6

Turn

275 – 278

4

Beta strand

279 – 282

4

Beta strand

283 – 285

3

Helix

287 – 292

6

Beta strand

295 – 297

3

Beta strand

304 – 306

3

Turn

307 – 309

3

Beta strand

312 – 314

3

Helix

322 – 329

8

Helix

334 – 340

7

Helix

342 – 348

7

Helix

355 – 361

7

Helix

389 – 391

3

Helix

394 – 401

8

Helix

406 – 420

15

Helix

427 – 450

24

Turn

451 – 453

3

Helix

456 – 463

8

Helix

465 – 471

7

Helix

476 – 484

9

Beta strand

485 – 487

3

Helix

490 – 497

8

Helix

502 – 516

15

Helix

518 – 531

14

Helix

533 – 540

8

Helix

553 – 555

3

Helix

558 – 566

9

Turn

572 – 574

3

Beta strand

575 – 578

4

Beta strand

581 – 584

4

Beta strand

589 – 591

3

Turn

593 – 595

3

Helix

596 – 598

3

Turn

603 – 605

3

Beta strand

611 – 614

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: C1778D328063586D	FASTA	618	69,900
	10 20 30 40 50 60 MHKTASQRLF PGPSYQNIKS IMEDSTILSD WTNSNKQKMK YDFSCELYRM STYSTFPAGV 70 80 90 100 110 120 PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKLGDSPI QKHKQLYPSC SFIQNLVSAS 130 140 150 160 170 180 LGSTSKNTSP MRNSFAHSLS PTLEHSSLFS GSYSSLSPNP LNSRAVEDIS SSRTNPYSYA 190 200 210 220 230 240 MSTEEARFLT YHMWPLTFLS PSELARAGFY YIGPGDRVAC FACGGKLSNW EPKDDAMSEH 250 260 270 280 290 300 RRHFPNCPFL ENSLETLRFS ISNLSMQTHA ARMRTFMYWP SSVPVQPEQL ASAGFYYVGR 310 320 330 340 350 360 NDDVKCFCCD GGLRCWESGD DPWVEHAKWF PRCEFLIRMK GQEFVDEIQG RYPHLLEQLL 370 380 390 400 410 420 STSDTTGEEN ADPPIIHFGP GESSSEDAVM MNTPVVKSAL EMGFNRDLVK QTVQSKILTT 430 440 450 460 470 480 GENYKTVNDI VSALLNAEDE KREEEKEKQA EEMASDDLSL IRKNRMALFQ QLTCVLPILD 490 500 510 520 530 540 NLLKANVINK QEHDIIKQKT QIPLQARELI DTILVKGNAA ANIFKNCLKE IDSTLYKNLF 550 560 570 580 590 600 VDKNMKYIPT EDVSGLSLEE QLRRLQEERT CKVCMDKEVS VVFIPCGHLV VCQECAPSLR 610 KCPICRGIIK GTVRTFLS
	Isoform 2 [UniParc]. Checksum: B678A4C2069F0A22	FASTA	569	64,098
	10 20 30 40 50 60 MSTYSTFPAG VPVSERSLAR AGFYYTGVND KVKCFCCGLM LDNWKLGDSP IQKHKQLYPS 70 80 90 100 110 120 CSFIQNLVSA SLGSTSKNTS PMRNSFAHSL SPTLEHSSLF SGSYSSLSPN PLNSRAVEDI 130 140 150 160 170 180 SSSRTNPYSY AMSTEEARFL TYHMWPLTFL SPSELARAGF YYIGPGDRVA CFACGGKLSN 190 200 210 220 230 240 WEPKDDAMSE HRRHFPNCPF LENSLETLRF SISNLSMQTH AARMRTFMYW PSSVPVQPEQ 250 260 270 280 290 300 LASAGFYYVG RNDDVKCFCC DGGLRCWESG DDPWVEHAKW FPRCEFLIRM KGQEFVDEIQ 310 320 330 340 350 360 GRYPHLLEQL LSTSDTTGEE NADPPIIHFG PGESSSEDAV MMNTPVVKSA LEMGFNRDLV 370 380 390 400 410 420 KQTVQSKILT TGENYKTVND IVSALLNAED EKREEEKEKQ AEEMASDDLS LIRKNRMALF 430 440 450 460 470 480 QQLTCVLPIL DNLLKANVIN KQEHDIIKQK TQIPLQAREL IDTILVKGNA AANIFKNCLK 490 500 510 520 530 540 EIDSTLYKNL FVDKNMKYIP TEDVSGLSLE EQLRRLQEER TCKVCMDKEV SVVFIPCGHL 550 560 VVCQECAPSL RKCPICRGII KGTVRTFLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins." Rothe M., Pan M.-G., Henzel W.J., Ayres T.M., Goeddel D.V. Cell 83:1243-1252(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes." Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G., Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G. Nature 379:349-353(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[3]	"Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors." Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L. Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal liver.
[4]	NIEHS SNPs program Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-453; VAL-506 AND SER-549.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Thymus.
[6]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis and Uterus.
[8]	"cIAP1 Localizes to the nuclear compartment and modulates the cell cycle." Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C. Cancer Res. 65:210-218(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BIRC5/SURVIVIN.
[9]	"c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1." Xu L., Zhu J., Hu X., Zhu H., Kim H.T., LaBaer J., Goldberg A., Yuan J. Mol. Cell 28:914-922(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE UBIQUITINATION OF MXD1/MAD1.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[13]	"To fight or die - inhibitor of apoptosis proteins at the crossroad of innate immunity and death." Lopez J., Meier P. Curr. Opin. Cell Biol. 22:872-881(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[14]	"Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases." Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J., Ditzel M., Meier P. Mol. Cell 40:810-822(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION PATHWAY.
[15]	"IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer." Gyrd-Hansen M., Meier P. Nat. Rev. Cancer 10:561-574(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[16]	"Inhibitor of apoptosis (IAP) proteins in regulation of inflammation and innate immunity." Damgaard R.B., Gyrd-Hansen M. Discov. Med. 11:221-231(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[17]	"Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1 transcription factor-mediated control of cyclin transcription." Cartier J., Berthelet J., Marivin A., Gemble S., Edmond V., Plenchette S., Lagrange B., Hammann A., Dupoux A., Delva L., Eymin B., Solary E., Dubrez L. J. Biol. Chem. 286:26406-26417(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH E2F1 AND TRAF2, SUBCELLULAR LOCATION.
[18]	"The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2." Mei Y., Hahn A.A., Hu S., Yang X. J. Biol. Chem. 286:35380-35387(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH USP19.
[19]	"cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)." Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J., Gevaert K., Declercq W., Vandenabeele P. PLoS ONE 6:E22356-E22356(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE UBIQUITINATION OF RIPK1; RIPK2; RIPK3 AND RIPK4, INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4.
[20]	"IAPs: guardians of RIPK1." Darding M., Meier P. Cell Death Differ. 19:58-66(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[21]	"Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat." Hinds M.G., Norton R.S., Vaux D.L., Day C.L. Nat. Struct. Biol. 6:648-651(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 266-363.
[22]	"The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9." Kulathila R., Vash B., Sage D., Cornell-Kennon S., Wright K., Koehn J., Stams T., Clark K., Price A. Acta Crystallogr. D 65:58-66(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 260-352 IN COMPLEXES WITH ZINC IONS; DIABLO AND CASP9 PEPTIDES, SUBUNIT.
[23]	"CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses cell proliferation and migration." Lopez J., John S.W., Tenev T., Rautureau G.J., Hinds M.G., Francalanci F., Wilson R., Broemer M., Santoro M.M., Day C.L., Meier P. Mol. Cell 42:569-583(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 435-562, DOMAIN CARD, ENZYME REGULATION.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L49431 mRNA. Translation: AAC41942.1.
U45879 mRNA. Translation: AAC50372.1.
U37547 mRNA. Translation: AAC50508.1.
AK303197 mRNA. Translation: BAG64288.1.
AP000942 Genomic DNA. No translation available.
DQ068066 Genomic DNA. Translation: AAY46158.1.
BC016174 mRNA. Translation: AAH16174.1.
BC028578 mRNA. Translation: AAH28578.1.

IPI

IPI00013418.

PIR

S68450.

RefSeq

NP_001157.1. NM_001166.4.
NP_001243092.1. NM_001256163.1.
NP_001243095.1. NM_001256166.1.

UniGene

Hs.696238.
Hs.731943.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QBH	NMR	-	A	266-363	[»]
2L9M	NMR	-	A	435-562	[»]
3D9T	X-ray	1.50	A/B	260-352	[»]
3D9U	X-ray	2.30	A	260-352	[»]
3M1D	X-ray	2.00	A/B	40-119	[»]
3MUP	X-ray	2.60	A/B/C/D	251-363	[»]
3OZ1	X-ray	3.00	A/B/C/D	251-363	[»]
3T6P	X-ray	1.90	A	265-618	[»]
3UW4	X-ray	1.79	A	266-343	[»]
4EB9	X-ray	2.60	A/B/C/D	251-363	[»]
4HY4	X-ray	1.25	A/B	260-352	[»]
4HY5	X-ray	1.75	A/B	260-352	[»]

ProteinModelPortal

Q13490.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13490. 34 interactions.

MINT

MINT-216174.

STRING

9606.ENSP00000227758.

Protein family/group databases

MEROPS

I32.002.

PTM databases

PhosphoSite

Q13490.

Polymorphism databases

DMDM

2497238.

Proteomic databases

PaxDb

Q13490.

PRIDE

Q13490.

Protocols and materials databases

DNASU

329.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000227758; ENSP00000227758; ENSG00000110330.
ENST00000530675; ENSP00000431723; ENSG00000110330.

GeneID

329.

KEGG

hsa:329.

UCSC

uc001pgy.3. human.

Organism-specific databases

CTD

329.

GeneCards

GC11P102252.

HGNC

HGNC:590. BIRC2.

HPA

CAB020661.
HPA005513.

MIM

601712. gene.

neXtProt

NX_Q13490.

PharmGKB

PA25359.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG243347.

HOGENOM

HOG000232059.

HOVERGEN

HBG004848.

InParanoid

Q13490.

KO

K16060.

OMA

TYHMWPL.

OrthoDB

EOG4K3KVW.

PhylomeDB

Q13490.

Enzyme and pathway databases

Pathway_Interaction_DB

nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
caspase_pathway. Caspase cascade in apoptosis.
p75ntrpathway. p75(NTR)-mediated signaling.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q13490.

Bgee

Q13490.

CleanEx

HS_BIRC2.

Genevestigator

Q13490.

GermOnline

ENSG00000110330. Homo sapiens.

Family and domain databases

Gene3D

1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.

InterPro

IPR001370. BIR.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]

Pfam

PF00653. BIR. 3 hits.
PF00619. CARD. 1 hit.
[Graphical view]

SMART

SM00238. BIR. 3 hits.
SM00114. CARD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50209. CARD. 1 hit.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13490.

ChEMBL

CHEMBL5462.

EvolutionaryTrace

Q13490.

GenomeRNAi

329.

NextBio

1355.

PMAP-CutDB

Q13490.

SOURCE

Search...

Entry information

Entry name

BIRC2_HUMAN

Accession

Primary (citable) accession number: Q13490
Secondary accession number(s): B4E026, Q16516, Q4TTG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 137 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.