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Protein

p53-induced death domain-containing protein 1

Gene

PIDD1

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

Functioni

Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways.3 Publications

GO - Molecular functioni

  1. death receptor binding Source: ProtInc

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  4. negative regulation of apoptotic process Source: UniProtKB
  5. positive regulation of apoptotic process Source: UniProtKB
  6. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  7. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  8. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

SignaLinkiQ9HB75.

Protein family/group databases

MEROPSiS68.001.

Names & Taxonomyi

Protein namesi
Recommended name:
p53-induced death domain-containing protein 1
Alternative name(s):
Leucine-rich repeat and death domain-containing protein
Gene namesi
Name:PIDD1
Synonyms:LRDD, PIDD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:16491. PIDD1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. Golgi apparatus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 910909p53-induced death domain-containing protein 1PRO_0000245243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei305 – 3051Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9HB75.
PRIDEiQ9HB75.

PTM databases

PhosphoSiteiQ9HB75.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Induced by gamma-irradiation.1 Publication

Gene expression databases

BgeeiQ9HB75.
ExpressionAtlasiQ9HB75. baseline and differential.
GenevestigatoriQ9HB75.

Organism-specific databases

HPAiCAB012647.
HPA055473.

Interactioni

Subunit structurei

Interacts with FADD and MAP-kinase activating death domain/MADD. Forms a complex with IKBKG and with receptor-interacting serine-threonine kinase 1/RIP1. Forms also a complex named PIDDosome with CASP2 and CRADD.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRADDP785608EBI-520427,EBI-520375
MDFIQ997503EBI-520427,EBI-724076
PRKDCP785276EBI-520427,EBI-352053

Protein-protein interaction databases

BioGridi120645. 36 interactions.
IntActiQ9HB75. 12 interactions.
MINTiMINT-1474528.

Structurei

Secondary structure

1
910
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni782 – 7843Combined sources
Helixi789 – 7979Combined sources
Helixi803 – 8097Combined sources
Helixi814 – 82310Combined sources
Turni824 – 8263Combined sources
Helixi828 – 84114Combined sources
Helixi849 – 85911Combined sources
Helixi863 – 87210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OF5X-ray3.20H/I/J/K/L778-883[»]
ProteinModelPortaliQ9HB75.
SMRiQ9HB75. Positions 49-876.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HB75.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati126 – 14722LRR 1Add
BLAST
Repeati149 – 17123LRR 2Add
BLAST
Repeati172 – 19423LRR 3Add
BLAST
Repeati195 – 21622LRR 4Add
BLAST
Repeati218 – 24023LRR 5Add
BLAST
Repeati241 – 26323LRR 6Add
BLAST
Repeati264 – 28522LRR 7Add
BLAST
Domaini315 – 422108ZU5 1PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 45230Peptidase S68Add
BLAST
Domaini453 – 565113ZU5 2PROSITE-ProRule annotationAdd
BLAST
Domaini788 – 87386DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni580 – 716137UPA domainBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation
Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 peptidase S68 domain.Curated
Contains 2 ZU5 domains.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG310879.
GeneTreeiENSGT00780000121839.
HOVERGENiHBG066762.
InParanoidiQ9HB75.
KOiK10130.
OMAiVPHFSWF.
OrthoDBiEOG7BP81T.
PhylomeDBiQ9HB75.
TreeFamiTF331183.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR019502. Peptidase_S68_pidd.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
PF10461. Peptidase_S68. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS51450. LRR. 7 hits.
PS51145. ZU5. 2 hits.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HB75-1) [UniParc]FASTAAdd to basket

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
MAATVEGPEL EAAAAAGDAS EDSDAGSRAL PFLGGNRLSL DLYPGGCQQL
60 70 80 90 100
LHLCVQQPLQ LLQVEFLRLS THEDPQLLEA TLAQLPQSLS CLRSLVLKGG
110 120 130 140 150
QRRDTLGACL RGALTNLPAG LSGLAHLAHL DLSFNSLETL PACVLQMRGL
160 170 180 190 200
GALLLSHNCL SELPEALGAL PALTFLTVTH NRLQTLPPAL GALSTLQRLD
210 220 230 240 250
LSQNLLDTLP PEIGGLGSLL ELNLASNRLQ SLPASLAGLR SLRLLVLHSN
260 270 280 290 300
LLASVPADLA RLPLLTRLDL RDNQLRDLPP ELLDAPFVRL QGNPLGEASP
310 320 330 340 350
DAPSSPVAAL IPEMPRLFLT SDLDSFPVTP QGCSVTLACG VRLQFPAGAT
360 370 380 390 400
ATPITIRYRL LLPEPGLVPL GPHDALLSHV LELQPHGVAF QQDVGLWLLF
410 420 430 440 450
TPPQARRCRE VVVRTRNDNS WGDLETYLEE EAPQRLWAHC QVPHFSWFLV
460 470 480 490 500
VSRPVSNACL VPPEGTLLCS SGHPGVKVIF PPGATEEPRR VSMQVVRMAG
510 520 530 540 550
RELQALLGEP EAAVSPLLCL SQSGPPSFLQ PVTVQLPLPS GITGLSLDRS
560 570 580 590 600
RLHLLYWAPP AATWDDITAQ VVLELTHLYA RFQVTHFSWY WLWYTTKNCV
610 620 630 640 650
GGLARKAWER LRLHRVNLIA LQRRRDPEQV LLQCLPRNKV DATLRRLLER
660 670 680 690 700
YRGPEPSDTV EMFEGEEFFA AFERGIDVDA DRPDCVEGRI CFVFYSHLKN
710 720 730 740 750
VKEVYVTTTL DREAQAVRGQ VSFYRGAVPV RVPEEAEAAR QRKGADALWM
760 770 780 790 800
ATLPIKLPRL RGSEGPRRGA GLSLAPLNLG DAETGFLTQS NLLSVAGRLG
810 820 830 840 850
LDWPAVALHL GVSYREVQRI RHEFRDDLDE QIRHMLFSWA ERQAGQPGAV
860 870 880 890 900
GLLVQALEQS DRQDVAEEVR AVLELGRRKY QDSIRRMGLA PKDPALPGSS
910
APQPPEPAQA
Length:910
Mass (Da):99,712
Last modified:October 17, 2006 - v2
Checksum:i8C98FC64230B57F8
GO
Isoform 2 (identifier: Q9HB75-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     704-720: Missing.

Show »
Length:893
Mass (Da):97,823
Checksum:i426694FB8EC10235
GO
Isoform 3 (identifier: Q9HB75-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.
     579-589: Missing.

Show »
Length:753
Mass (Da):82,971
Checksum:i6BD2B00A12B574DC
GO
Isoform 4 (identifier: Q9HB75-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-313: Missing.

Show »
Length:597
Mass (Da):66,720
Checksum:i2572BA6345C426AA
GO
Isoform 5 (identifier: Q9HB75-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-313: Missing.
     589-589: W → WSVPPSFLSPPPPVCTALLTPSSPR
     759-815: RLRGSEGPRR...VALHLGVSYR → VGLRDSRGAG...GGGLASPWHP
     816-910: Missing.

Show »
Length:526
Mass (Da):58,652
Checksum:iACB01B6B05784BF1
GO
Isoform 6 (identifier: Q9HB75-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-492: Missing.
     589-589: W → WSVPPSFLSPPPPVCTALLTPSSPR
     704-720: Missing.
     759-815: RLRGSEGPRR...VALHLGVSYR → VGLRDSRGAG...GGGLASPWHP
     816-910: Missing.

Show »
Length:330
Mass (Da):37,019
Checksum:i1A8F34F669B0F38A
GO
Isoform 7 (identifier: Q9HB75-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-313: Missing.
     585-621: THFSWYWLWYTTKNCVGGLARKAWERLRLHRVNLIAL → LALVHHQELCGRPGSEGLGAAAAAPCEPHRSAAAPGP
     622-910: Missing.

Show »
Length:308
Mass (Da):33,375
Checksum:i5E814E02D2E0E4CB
GO

Sequence cautioni

The sequence BAD92069.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD92186.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD92766.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAD38708.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti335 – 3351V → A in BAC11272 (PubMed:14702039).Curated
Sequence conflicti421 – 4211W → L in AAP97716 (Ref. 3) Curated
Sequence conflicti492 – 4921S → F in BAC11272 (PubMed:14702039).Curated
Sequence conflicti512 – 5121A → V in CAD38708 (PubMed:17974005).Curated
Sequence conflicti601 – 6011G → E in CAD38708 (PubMed:17974005).Curated
Sequence conflicti895 – 8951A → V in AAF69491 (PubMed:10825539).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti331 – 3311Q → R.7 Publications
Corresponds to variant rs10902221 [ dbSNP | Ensembl ].
VAR_028031

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 492492Missing in isoform 6. 1 PublicationVSP_019664Add
BLAST
Alternative sequencei1 – 313313Missing in isoform 4, isoform 5 and isoform 7. 4 PublicationsVSP_019665Add
BLAST
Alternative sequencei1 – 146146Missing in isoform 3. 1 PublicationVSP_019666Add
BLAST
Alternative sequencei579 – 58911Missing in isoform 3. 1 PublicationVSP_019667Add
BLAST
Alternative sequencei585 – 62137THFSW…NLIAL → LALVHHQELCGRPGSEGLGA AAAAPCEPHRSAAAPGP in isoform 7. 1 PublicationVSP_019668Add
BLAST
Alternative sequencei589 – 5891W → WSVPPSFLSPPPPVCTALLT PSSPR in isoform 5 and isoform 6. 2 PublicationsVSP_019669
Alternative sequencei622 – 910289Missing in isoform 7. 1 PublicationVSP_019670Add
BLAST
Alternative sequencei704 – 72017Missing in isoform 2 and isoform 6. 2 PublicationsVSP_019671Add
BLAST
Alternative sequencei759 – 81557RLRGS…GVSYR → VGLRDSRGAGQDRGPGVTRV TWWSWGWSPGLNALFPSNRD FEGPRGHGGGLASPWHP in isoform 5 and isoform 6. 2 PublicationsVSP_019672Add
BLAST
Alternative sequencei816 – 91095Missing in isoform 5 and isoform 6. 2 PublicationsVSP_019673Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF229178 mRNA. Translation: AAF69491.1.
AF274972 mRNA. Translation: AAG13461.1.
AF465246 mRNA. Translation: AAP97716.1.
AK074893 mRNA. Translation: BAC11272.1.
AB208832 mRNA. Translation: BAD92069.1. Different initiation.
AB208949 mRNA. Translation: BAD92186.1. Different initiation.
AB209529 mRNA. Translation: BAD92766.1. Different initiation.
AL833849 mRNA. Translation: CAD38708.1. Different initiation.
BC014904 mRNA. Translation: AAH14904.1.
CCDSiCCDS44508.1. [Q9HB75-2]
CCDS7716.1. [Q9HB75-1]
RefSeqiNP_665893.2. NM_145886.3. [Q9HB75-1]
NP_665894.2. NM_145887.3. [Q9HB75-2]
UniGeneiHs.592290.

Genome annotation databases

EnsembliENST00000347755; ENSP00000337797; ENSG00000177595. [Q9HB75-1]
ENST00000411829; ENSP00000416801; ENSG00000177595. [Q9HB75-2]
GeneIDi55367.
KEGGihsa:55367.
UCSCiuc001lrk.2. human. [Q9HB75-2]
uc001lrl.1. human. [Q9HB75-3]
uc001lrm.1. human. [Q9HB75-1]
uc001lrp.2. human. [Q9HB75-5]

Polymorphism databases

DMDMi116242715.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF229178 mRNA. Translation: AAF69491.1.
AF274972 mRNA. Translation: AAG13461.1.
AF465246 mRNA. Translation: AAP97716.1.
AK074893 mRNA. Translation: BAC11272.1.
AB208832 mRNA. Translation: BAD92069.1. Different initiation.
AB208949 mRNA. Translation: BAD92186.1. Different initiation.
AB209529 mRNA. Translation: BAD92766.1. Different initiation.
AL833849 mRNA. Translation: CAD38708.1. Different initiation.
BC014904 mRNA. Translation: AAH14904.1.
CCDSiCCDS44508.1. [Q9HB75-2]
CCDS7716.1. [Q9HB75-1]
RefSeqiNP_665893.2. NM_145886.3. [Q9HB75-1]
NP_665894.2. NM_145887.3. [Q9HB75-2]
UniGeneiHs.592290.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OF5X-ray3.20H/I/J/K/L778-883[»]
ProteinModelPortaliQ9HB75.
SMRiQ9HB75. Positions 49-876.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120645. 36 interactions.
IntActiQ9HB75. 12 interactions.
MINTiMINT-1474528.

Protein family/group databases

MEROPSiS68.001.

PTM databases

PhosphoSiteiQ9HB75.

Polymorphism databases

DMDMi116242715.

Proteomic databases

PaxDbiQ9HB75.
PRIDEiQ9HB75.

Protocols and materials databases

DNASUi55367.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000347755; ENSP00000337797; ENSG00000177595. [Q9HB75-1]
ENST00000411829; ENSP00000416801; ENSG00000177595. [Q9HB75-2]
GeneIDi55367.
KEGGihsa:55367.
UCSCiuc001lrk.2. human. [Q9HB75-2]
uc001lrl.1. human. [Q9HB75-3]
uc001lrm.1. human. [Q9HB75-1]
uc001lrp.2. human. [Q9HB75-5]

Organism-specific databases

CTDi55367.
GeneCardsiGC11M000799.
H-InvDBHIX0021767.
HGNCiHGNC:16491. PIDD1.
HPAiCAB012647.
HPA055473.
MIMi605247. gene.
neXtProtiNX_Q9HB75.
PharmGKBiPA30445.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310879.
GeneTreeiENSGT00780000121839.
HOVERGENiHBG066762.
InParanoidiQ9HB75.
KOiK10130.
OMAiVPHFSWF.
OrthoDBiEOG7BP81T.
PhylomeDBiQ9HB75.
TreeFamiTF331183.

Enzyme and pathway databases

SignaLinkiQ9HB75.

Miscellaneous databases

EvolutionaryTraceiQ9HB75.
GeneWikiiLRDD.
GenomeRNAii55367.
NextBioi59757.
PROiQ9HB75.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HB75.
ExpressionAtlasiQ9HB75. baseline and differential.
GenevestigatoriQ9HB75.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR019502. Peptidase_S68_pidd.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 2 hits.
PF10461. Peptidase_S68. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS51450. LRR. 7 hits.
PS51145. ZU5. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LRDD, a novel leucine rich repeat and death domain containing protein."
    Telliez J.-B., Bean K.M., Lin L.-L.
    Biochim. Biophys. Acta 1478:280-288(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH FADD AND MADD, VARIANT ARG-331.
  2. "Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis."
    Lin Y., Ma W., Benchimol S.
    Nat. Genet. 26:122-127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, VARIANT ARG-331.
  3. Zan Q., Guo J.H., Yu L.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT ARG-331.
    Tissue: Brain.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), VARIANT ARG-331.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), VARIANT ARG-331.
    Tissue: Brain and Spleen.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT ARG-331.
    Tissue: Testis.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ARG-331.
    Tissue: Uterus.
  8. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (FEB-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-37; 69-93; 103-111; 183-316; 343-357; 415-435; 454-497; 552-581; 598-605; 613-623; 626-637; 651-740; 743-759; 768-798 AND 826-870, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-299 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  9. "The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress."
    Tinel A., Tschopp J.
    Science 304:843-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH CASP2 AND CRADD.
  10. "PIDD mediates NF-kappaB activation in response to DNA damage."
    Janssens S., Tinel A., Lippens S., Tschopp J.
    Cell 123:1079-1092(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKG AND RIP1, SUBCELLULAR LOCATION.
  11. "Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage."
    Vakifahmetoglu H., Olsson M., Orrenius S., Zhivotovsky B.
    Oncogene 25:5683-5692(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASP2 AND CRADD.

Entry informationi

Entry nameiPIDD1_HUMAN
AccessioniPrimary (citable) accession number: Q9HB75
Secondary accession number(s): Q59FD1
, Q59H10, Q59HC7, Q7Z4P8, Q8NC89, Q8NDL2, Q96C25, Q9NRE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 117 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.