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Protein

Baculoviral IAP repeat-containing protein 7

Gene

BIRC7

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

Functioni

Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi124 – 1241Zinc
Metal bindingi127 – 1271Zinc
Metal bindingi144 – 1441Zinc
Metal bindingi151 – 1511Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri252 – 28635RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of JUN kinase activity Source: UniProtKB
  • inhibition of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
  • mitotic spindle assembly Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of natural killer cell apoptotic process Source: UniProtKB
  • regulation of signal transduction Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Protease inhibitor, Thiol protease inhibitor

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ96CA5.
SIGNORiQ96CA5.

Protein family/group databases

MEROPSiI32.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 7 (EC:6.3.2.-)
Alternative name(s):
Kidney inhibitor of apoptosis protein
Short name:
KIAP
Livin
Melanoma inhibitor of apoptosis protein
Short name:
ML-IAP
RING finger protein 50
Cleaved into the following chain:
Baculoviral IAP repeat-containing protein 7 30kDa subunit
Short name:
Truncated livin
Short name:
p30-Livin
Short name:
tLivin
Gene namesi
Name:BIRC7
Synonyms:KIAP, LIVIN, MLIAP, RNF50
ORF Names:UNQ5800/PRO19607/PRO21344
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:13702. BIRC7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • nucleus Source: UniProtKB
  • spindle microtubule Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 882EE → AA: No change in SMAC interaction and anti-apoptotic activity. 1 Publication
Mutagenesisi120 – 1201D → A: Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity. 1 Publication
Mutagenesisi124 – 1241C → A: Abolishes inhibition of caspases and anti-apoptotic activity. 1 Publication
Mutagenesisi138 – 1381D → A: Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity. 1 Publication

Organism-specific databases

PharmGKBiPA25364.

Chemistry

ChEMBLiCHEMBL1075127.
GuidetoPHARMACOLOGYi2794.

Polymorphism and mutation databases

BioMutaiBIRC7.
DMDMi21759008.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Baculoviral IAP repeat-containing protein 7PRO_0000122362Add
BLAST
Chaini53 – 298246Baculoviral IAP repeat-containing protein 7 30kDa subunitPRO_0000416092Add
BLAST

Post-translational modificationi

Autoubiquitinated and undergoes proteasome-mediated degradation.
The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei52 – 532Cleavage; by CASP3 and CASP7

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ96CA5.
PaxDbiQ96CA5.
PeptideAtlasiQ96CA5.
PRIDEiQ96CA5.

PTM databases

iPTMnetiQ96CA5.

Miscellaneous databases

PMAP-CutDBQ96CA5.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed at very low levels or not detectable in most adult tissues. Detected in adult heart, placenta, lung, lymph node, spleen and ovary, and in several carcinoma cell lines. Isoform 2 is detected in fetal kidney, heart and spleen, and at lower levels in adult brain, skeletal muscle and peripheral blood leukocytes.

Gene expression databases

BgeeiQ96CA5.
CleanExiHS_BIRC7.
ExpressionAtlasiQ96CA5. baseline and differential.
GenevisibleiQ96CA5. HS.

Organism-specific databases

HPAiCAB037025.
CAB037119.

Interactioni

Subunit structurei

Binds to CASP9. Interaction with DIABLO/SMAC via the BIR domain disrupts binding to CASP9 and apoptotic suppressor activity. Interacts with TAB1. In vitro, interacts with CASP3 and CASP7 via its BIR domain.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-517623,EBI-717810
BIRC2Q134903EBI-517623,EBI-514538
CASP9P552118EBI-517623,EBI-516799
DDX6P261963EBI-517623,EBI-351257
DIABLOQ9NR286EBI-517623,EBI-517508
FAM124BQ9H5Z63EBI-517623,EBI-741626
HTRA2O434642EBI-517623,EBI-517086
PHF1O431893EBI-517623,EBI-530034
POLR1CO151603EBI-517623,EBI-1055079

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122670. 32 interactions.
DIPiDIP-33486N.
IntActiQ96CA5. 14 interactions.
MINTiMINT-147031.
STRINGi9606.ENSP00000217169.

Chemistry

BindingDBiQ96CA5.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi82 – 843Combined sources
Helixi87 – 926Combined sources
Turni93 – 964Combined sources
Turni100 – 1023Combined sources
Helixi105 – 1106Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi122 – 1243Combined sources
Turni125 – 1273Combined sources
Beta strandi130 – 1323Combined sources
Helixi140 – 1478Combined sources
Helixi152 – 1587Combined sources
Helixi160 – 1667Combined sources
Helixi168 – 1714Combined sources
Helixi243 – 2497Combined sources
Turni253 – 2553Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi262 – 2654Combined sources
Turni273 – 2753Combined sources
Helixi276 – 2783Combined sources
Turni283 – 2853Combined sources
Beta strandi291 – 2944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OXNX-ray2.20A/B/C/D/E63-179[»]
1OXQX-ray2.30A/B/C/D/E63-179[»]
1OY7X-ray2.70A/B/C/D/E63-179[»]
1TW6X-ray1.71A/B63-172[»]
2I3HX-ray1.62A/B63-172[»]
2I3IX-ray2.30A/B63-172[»]
3F7GX-ray2.30A/B/C/D/E63-179[»]
3F7HX-ray1.80A/B63-172[»]
3F7IX-ray1.90A/B63-172[»]
3GT9X-ray1.70A/B63-172[»]
3GTAX-ray1.70A/B63-172[»]
3UW5X-ray1.71A/B63-159[»]
4AUQX-ray2.18B/E239-298[»]
ProteinModelPortaliQ96CA5.
SMRiQ96CA5. Positions 71-171, 242-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96CA5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati90 – 15566BIRAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi64 – 696Poly-Glu

Domaini

The RING domain is essential for autoubiquitination.

Sequence similaritiesi

Belongs to the IAP family.Curated
Contains 1 BIR repeat.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri252 – 28635RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG099136.
InParanoidiQ96CA5.
KOiK16061.
OMAiFPSCQFL.
OrthoDBiEOG78H3TF.
PhylomeDBiQ96CA5.
TreeFamiTF105356.

Family and domain databases

Gene3Di1.10.1170.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00653. BIR. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS01282. BIR_REPEAT_1. 1 hit.
PS50143. BIR_REPEAT_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q96CA5-1) [UniParc]FASTAAdd to basket

Also known as: Livin alpha

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.

« Hide

        10         20         30         40         50
MGPKDSAKCL HRGPQPSHWA AGDGPTQERC GPRSLGSPVL GLDTCRAWDH
60 70 80 90 100
VDGQILGQLR PLTEEEEEEG AGATLSRGPA FPGMGSEELR LASFYDWPLT
110 120 130 140 150
AEVPPELLAA AGFFHTGHQD KVRCFFCYGG LQSWKRGDDP WTEHAKWFPS
160 170 180 190 200
CQFLLRSKGR DFVHSVQETH SQLLGSWDPW EEPEDAAPVA PSVPASGYPE
210 220 230 240 250
LPTPRREVQS ESAQEPGGVS PAEAQRAWWV LEPPGARDVE AQLRRLQEER
260 270 280 290
TCKVCLDRAV SIVFVPCGHL VCAECAPGLQ LCPICRAPVR SRVRTFLS
Length:298
Mass (Da):32,798
Last modified:July 11, 2002 - v2
Checksum:iB2EAAEE531BEC101
GO
Isoform 1 (identifier: Q96CA5-2) [UniParc]FASTAAdd to basket

Also known as: Livin beta

The sequence of this isoform differs from the canonical sequence as follows:
     216-233: Missing.

Show »
Length:280
Mass (Da):30,866
Checksum:i630BE9C0737F7952
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti223 – 2231E → Q.1 Publication
Corresponds to variant rs1077019 [ dbSNP | Ensembl ].
VAR_020253

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei216 – 23318Missing in isoform 1. 2 PublicationsVSP_002459Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF301009 mRNA. Translation: AAG37878.1.
AJ309298 Genomic DNA. Translation: CAC37337.1.
AJ309298 Genomic DNA. Translation: CAC37338.1.
AF311388 mRNA. Translation: AAG33622.1.
AY358835 mRNA. Translation: AAQ89194.1.
AY358836 mRNA. Translation: AAQ89195.1.
AL121827 Genomic DNA. No translation available.
BC014475 mRNA. Translation: AAH14475.1.
CCDSiCCDS13512.1. [Q96CA5-2]
CCDS13513.1. [Q96CA5-1]
PIRiJC7568.
RefSeqiNP_071444.1. NM_022161.3. [Q96CA5-2]
NP_647478.1. NM_139317.2. [Q96CA5-1]
UniGeneiHs.256126.

Genome annotation databases

EnsembliENST00000217169; ENSP00000217169; ENSG00000101197. [Q96CA5-1]
ENST00000342412; ENSP00000345213; ENSG00000101197. [Q96CA5-2]
GeneIDi79444.
KEGGihsa:79444.
UCSCiuc002yei.5. human. [Q96CA5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF301009 mRNA. Translation: AAG37878.1.
AJ309298 Genomic DNA. Translation: CAC37337.1.
AJ309298 Genomic DNA. Translation: CAC37338.1.
AF311388 mRNA. Translation: AAG33622.1.
AY358835 mRNA. Translation: AAQ89194.1.
AY358836 mRNA. Translation: AAQ89195.1.
AL121827 Genomic DNA. No translation available.
BC014475 mRNA. Translation: AAH14475.1.
CCDSiCCDS13512.1. [Q96CA5-2]
CCDS13513.1. [Q96CA5-1]
PIRiJC7568.
RefSeqiNP_071444.1. NM_022161.3. [Q96CA5-2]
NP_647478.1. NM_139317.2. [Q96CA5-1]
UniGeneiHs.256126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OXNX-ray2.20A/B/C/D/E63-179[»]
1OXQX-ray2.30A/B/C/D/E63-179[»]
1OY7X-ray2.70A/B/C/D/E63-179[»]
1TW6X-ray1.71A/B63-172[»]
2I3HX-ray1.62A/B63-172[»]
2I3IX-ray2.30A/B63-172[»]
3F7GX-ray2.30A/B/C/D/E63-179[»]
3F7HX-ray1.80A/B63-172[»]
3F7IX-ray1.90A/B63-172[»]
3GT9X-ray1.70A/B63-172[»]
3GTAX-ray1.70A/B63-172[»]
3UW5X-ray1.71A/B63-159[»]
4AUQX-ray2.18B/E239-298[»]
ProteinModelPortaliQ96CA5.
SMRiQ96CA5. Positions 71-171, 242-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122670. 32 interactions.
DIPiDIP-33486N.
IntActiQ96CA5. 14 interactions.
MINTiMINT-147031.
STRINGi9606.ENSP00000217169.

Chemistry

BindingDBiQ96CA5.
ChEMBLiCHEMBL1075127.
GuidetoPHARMACOLOGYi2794.

Protein family/group databases

MEROPSiI32.007.

PTM databases

iPTMnetiQ96CA5.

Polymorphism and mutation databases

BioMutaiBIRC7.
DMDMi21759008.

Proteomic databases

MaxQBiQ96CA5.
PaxDbiQ96CA5.
PeptideAtlasiQ96CA5.
PRIDEiQ96CA5.

Protocols and materials databases

DNASUi79444.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217169; ENSP00000217169; ENSG00000101197. [Q96CA5-1]
ENST00000342412; ENSP00000345213; ENSG00000101197. [Q96CA5-2]
GeneIDi79444.
KEGGihsa:79444.
UCSCiuc002yei.5. human. [Q96CA5-1]

Organism-specific databases

CTDi79444.
GeneCardsiBIRC7.
HGNCiHGNC:13702. BIRC7.
HPAiCAB037025.
CAB037119.
MIMi605737. gene.
neXtProtiNX_Q96CA5.
PharmGKBiPA25364.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG099136.
InParanoidiQ96CA5.
KOiK16061.
OMAiFPSCQFL.
OrthoDBiEOG78H3TF.
PhylomeDBiQ96CA5.
TreeFamiTF105356.

Enzyme and pathway databases

SignaLinkiQ96CA5.
SIGNORiQ96CA5.

Miscellaneous databases

EvolutionaryTraceiQ96CA5.
GeneWikiiBIRC7.
GenomeRNAii79444.
PMAP-CutDBQ96CA5.
PROiQ96CA5.
SOURCEiSearch...

Gene expression databases

BgeeiQ96CA5.
CleanExiHS_BIRC7.
ExpressionAtlasiQ96CA5. baseline and differential.
GenevisibleiQ96CA5. HS.

Family and domain databases

Gene3Di1.10.1170.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00653. BIR. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS01282. BIR_REPEAT_1. 1 hit.
PS50143. BIR_REPEAT_2. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "KIAP, a novel member of the inhibitor of apoptosis protein family."
    Lin J.-H., Deng G., Huang Q., Morser J.
    Biochem. Biophys. Res. Commun. 279:820-831(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fetal kidney.
  2. "Two splicing variants of a new inhibitor of apoptosis gene with different biological properties and tissue distribution pattern."
    Ashhab Y., Alian A., Polliack A., Panet A., Yehuda D.B.
    FEBS Lett. 495:56-60(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
    Tissue: Melanoma.
  3. "Livin, a novel inhibitor of apoptosis protein family member."
    Kasof G.M., Gomes B.C.
    J. Biol. Chem. 276:3238-3246(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2), VARIANT GLN-223.
    Tissue: Skin.
  7. "ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas."
    Vucic D., Stennicke H.R., Pisabarro M.T., Salvesen G.S., Dixit V.M.
    Curr. Biol. 10:1359-1366(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 87-GLU--GLU-88; ASP-120; CYS-124 AND ASP-138.
  8. "SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP)."
    Vucic D., Deshayes K., Ackerly H., Pisabarro M.T., Kadkhodayan S., Fairbrother W.J., Dixit V.M.
    J. Biol. Chem. 277:12275-12279(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAC.
  9. "IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition."
    Sanna M.G., da Silva Correia J., Ducrey O., Lee J., Nomoto K., Schrantz N., Deveraux Q.L., Ulevitch R.J.
    Mol. Cell. Biol. 22:1754-1766(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION OF MAP KINASES.
  10. "Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathway."
    Ma L., Huang Y., Song Z., Feng S., Tian X., Du W., Qiu X., Heese K., Wu M.
    Cell Death Differ. 13:2079-2088(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE UBIQUITINATION OF DIABLO/SMAC, INTERACTION WITH DIABLO/SMAC.
  11. "Subcellular localization determines the delicate balance between the anti- and pro-apoptotic activity of Livin."
    Nachmias B., Lazar I., Elmalech M., Abed-El-Rahaman I., Asshab Y., Mandelboim O., Perlman R., Ben-Yehuda D.
    Apoptosis 12:1129-1142(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION.
  12. Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE.
  13. "Challenge and promise: roles for Livin in progression and therapy of cancer."
    Wang L., Zhang Q., Liu B., Han M., Shan B.
    Mol. Cancer Ther. 7:3661-3669(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  14. "Research progress on Livin protein: an inhibitor of apoptosis."
    Yan B.
    Mol. Cell. Biochem. 357:39-45(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 63-179 IN COMPLEX WITH PHAGE-AND SMAC-DERIVED PEPTIDES, ZINC-BINDING SITES.
  16. "Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP."
    Vucic D., Franklin M.C., Wallweber H.J., Das K., Eckelman B.P., Shin H., Elliott L.O., Kadkhodayan S., Deshayes K., Salvesen G.S., Fairbrother W.J.
    Biochem. J. 385:11-20(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 63-159, ZINC-BINDING SITES.

Entry informationi

Entry nameiBIRC7_HUMAN
AccessioniPrimary (citable) accession number: Q96CA5
Secondary accession number(s): Q9BQV0, Q9H2A8, Q9HAP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: July 6, 2016
This is version 156 of the entry and version 2 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 20
    Human chromosome 20: 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.