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Q13625

- ASPP2_HUMAN

UniProt

Q13625 - ASPP2_HUMAN

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Protein
Apoptosis-stimulating of p53 protein 2
Gene
TP53BP2, ASPP2, BBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42.3 Publications

GO - Molecular functioni

  1. NF-kappaB binding Source: UniProtKB
  2. SH3/SH2 adaptor activity Source: ProtInc
  3. identical protein binding Source: IntAct
  4. protein binding Source: IntAct

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. central nervous system development Source: Ensembl
  3. embryo development ending in birth or egg hatching Source: Ensembl
  4. heart development Source: Ensembl
  5. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  6. negative regulation of cell cycle Source: UniProtKB
  7. positive regulation of signal transduction Source: GOC
  8. response to ionizing radiation Source: Ensembl
  9. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis-stimulating of p53 protein 2
Alternative name(s):
Bcl2-binding protein
Short name:
Bbp
Renal carcinoma antigen NY-REN-51
Tumor suppressor p53-binding protein 2
Short name:
53BP2
Short name:
p53-binding protein 2
Short name:
p53BP2
Gene namesi
Name:TP53BP2
Synonyms:ASPP2, BBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12000. TP53BP2.

Subcellular locationi

Cytoplasmperinuclear region. Nucleus
Note: Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1098 – 10981W → K: Loss of interaction with APC2. 1 Publication

Organism-specific databases

PharmGKBiPA36681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11281128Apoptosis-stimulating of p53 protein 2
PRO_0000066964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei480 – 4801Phosphoserine4 Publications
Modified residuei556 – 5561Phosphoserine2 Publications
Modified residuei572 – 5721Phosphoserine1 Publication
Modified residuei698 – 6981Phosphoserine By similarity
Modified residuei714 – 7141Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13625.
PaxDbiQ13625.
PRIDEiQ13625.

PTM databases

PhosphoSiteiQ13625.

Expressioni

Tissue specificityi

Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocyte. Reduced expression in breast carcinomas expressing a wild-type TP53 protein. Overexpressed in lung cancer cell lines.3 Publications

Inductioni

Following DNA damage induced by UV irradiation. Down-regulated by wild-type, but not mutant, p53/TP53.1 Publication

Gene expression databases

ArrayExpressiQ13625.
BgeeiQ13625.
CleanExiHS_TP53BP2.
GenevestigatoriQ13625.

Organism-specific databases

HPAiHPA021603.

Interactioni

Subunit structurei

Binds to the central domain of TP53 as well as to BCL2. Interacts with protein phosphatase 1. Interacts with RELA NF-kappa-B subunit. This interaction probably prevents the activation of apoptosis, possibly by preventing its interaction with TP53. Interacts with APC2 and APPBP1. Interacts with DDX42 (via the C-terminus); the interaction is not inhibited by TP53BP2 ubiquitination and is independent of p53/TP53.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-77642,EBI-77642
APC2O959964EBI-77642,EBI-1053045
APPP050673EBI-77642,EBI-77613
BCL2P1041513EBI-77642,EBI-77694
BCL2L1Q07817-14EBI-77642,EBI-287195
BCL2L2Q928432EBI-77642,EBI-707714
EP300Q094722EBI-77642,EBI-447295
Irs1P355692EBI-287091,EBI-400825From a different organism.
Irs1P355704EBI-287091,EBI-520230From a different organism.
PPP1CAP621367EBI-77642,EBI-357253
PPP1CCP368736EBI-77642,EBI-356283
RELAQ042066EBI-287091,EBI-73886
TP53P046372EBI-77642,EBI-366083
YAP1P469366EBI-287091,EBI-7804091From a different organism.
YAP1P469379EBI-287091,EBI-1044059

Protein-protein interaction databases

BioGridi113012. 37 interactions.
DIPiDIP-24266N.
DIP-29587N.
DIP-426N.
IntActiQ13625. 55 interactions.
MINTiMINT-106406.
STRINGi9606.ENSP00000341957.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98
Beta strandi17 – 226
Helixi29 – 346
Beta strandi40 – 423
Beta strandi44 – 496
Beta strandi52 – 565
Helixi62 – 698
Helixi73 – 753
Beta strandi77 – 815
Helixi747 – 76014
Turni761 – 7644
Helixi927 – 93610
Helixi939 – 9457
Helixi946 – 9483
Helixi962 – 9698
Helixi972 – 98110
Helixi995 – 10017
Helixi1005 – 10139
Beta strandi1023 – 10253
Helixi1029 – 10324
Beta strandi1035 – 10373
Helixi1043 – 105311
Turni1054 – 10574
Helixi1058 – 10603
Beta strandi1061 – 10666
Beta strandi1083 – 10864
Beta strandi1091 – 10933
Beta strandi1095 – 11028
Beta strandi1105 – 11106
Helixi1111 – 11133
Beta strandi1114 – 11174

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YCSX-ray2.20B892-1126[»]
2UWQNMR-A1-83[»]
4A63X-ray2.27B/D/F/H/J/L892-1128[»]
4IRVX-ray2.04E/F/G/H726-782[»]
ProteinModelPortaliQ13625.
SMRiQ13625. Positions 1-83, 926-1118.

Miscellaneous databases

EvolutionaryTraceiQ13625.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati958 – 99033ANK 1
Add
BLAST
Repeati991 – 102333ANK 2
Add
BLAST
Domaini1057 – 111963SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni332 – 34817Interaction with APPBP1
Add
BLAST
Regioni876 – 1128253Mediates interaction with APC2
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi866 – 87510SH3-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi132 – 17342Gln-rich
Add
BLAST
Compositional biasi824 – 90279Pro-rich
Add
BLAST

Domaini

The ankyrin repeats and the SH3 domain are required for a specific interactions with TP53.

Sequence similaritiesi

Belongs to the ASPP family.
Contains 2 ANK repeats.
Contains 1 SH3 domain.

Keywords - Domaini

ANK repeat, Repeat, SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG283717.
HOGENOMiHOG000034106.
HOVERGENiHBG050596.
KOiK16823.
OMAiYRNQSDA.
OrthoDBiEOG73FQKX.
PhylomeDBiQ13625.
TreeFamiTF105545.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR01887. SPECTRNALPHA.
SMARTiSM00248. ANK. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13625-1) [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

MMPMFLTVYL SNNEQHFTEV PVTPETICRD VVDLCKEPGE SDCHLAEVWC     50
GSERPVADNE RMFDVLQRFG SQRNEVRFFL RHERPPGRDI VSGPRSQDPS 100
LKRNGVKVPG EYRRKENGVN SPRMDLTLAE LQEMASRQQQ QIEAQQQLLA 150
TKEQRLKFLK QQDQRQQQQV AEQEKLKRLK EIAENQEAKL KKVRALKGHV 200
EQKRLSNGKL VEEIEQMNNL FQQKQRELVL AVSKVEELTR QLEMLKNGRI 250
DSHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV 300
MDKRVNELRD RLWKKKAALQ QKENLPVSSD GNLPQQAASA PSRVAAVGPY 350
IQSSTMPRMP SRPELLVKPA LPDGSLVIQA SEGPMKIQTL PNMRSGAASQ 400
TKGSKIHPVG PDWSPSNADL FPSQGSASVP QSTGNALDQV DDGEVPLREK 450
EKKVRPFSMF DAVDQSNAPP SFGTLRKNQS SEDILRDAQV ANKNVAKVPP 500
PVPTKPKQIN LPYFGQTNQP PSDIKPDGSS QQLSTVVPSM GTKPKPAGQQ 550
PRVLLSPSIP SVGQDQTLSP GSKQESPPAA AVRPFTPQPS KDTLLPPFRK 600
PQTVAASSIY SMYTQQQAPG KNFQQAVQSA LTKTHTRGPH FSSVYGKPVI 650
AAAQNQQQHP ENIYSNSQGK PGSPEPETEP VSSVQENHEN ERIPRPLSPT 700
KLLPFLSNPY RNQSDADLEA LRKKLSNAPR PLKKRSSITE PEGPNGPNIQ 750
KLLYQRTTIA AMETISVPSY PSKSASVTAS SESPVEIQNP YLHVEPEKEV 800
VSLVPESLSP EDVGNASTEN SDMPAPSPGL DYEPEGVPDN SPNLQNNPEE 850
PNPEAPHVLD VYLEEYPPYP PPPYPSGEPE GPGEDSVSMR PPEITGQVSL 900
PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD 950
DPSLPNDEGI TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA 1000
SCNNVQVCKF LVESGAAVFA MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV 1050
QEKMGIMNKG VIYALWDYEP QNDDELPMKE GDCMTIIHRE DEDEIEWWWA 1100
RLNDKEGYVP RNLLGLYPRI KPRQRSLA 1128
Length:1,128
Mass (Da):125,616
Last modified:August 15, 2003 - v2
Checksum:iC75D056FBC1DAD75
GO
Isoform 2 (identifier: Q13625-2) [UniParc]FASTAAdd to Basket

Also known as: Bbp

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.

Note: Due to Alu sequence insertion that creates a shorter but existing form that may have an alternative function.

Show »
Length:1,005
Mass (Da):111,431
Checksum:i3DF4FF49EB589F20
GO
Isoform 3 (identifier: Q13625-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRFGSKM

Note: No experimental confirmation available.

Show »
Length:1,134
Mass (Da):126,323
Checksum:i2C7683F88B171926
GO

Sequence cautioni

The sequence AAH46150.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH46150.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH58918.2 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 123123Missing in isoform 2.
VSP_008010Add
BLAST
Alternative sequencei1 – 11M → MRFGSKM in isoform 3.
VSP_043509

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58334 mRNA. Translation: AAC50557.1.
AJ318888 mRNA. Translation: CAC83012.1.
AK294432 mRNA. Translation: BAG57677.1.
AC096542 Genomic DNA. No translation available.
BC046150 mRNA. Translation: AAH46150.2. Sequence problems.
BC058918 mRNA. Translation: AAH58918.2. Different initiation.
U09582 mRNA. Translation: AAA21597.1.
CCDSiCCDS1538.1. [Q13625-2]
CCDS44319.1. [Q13625-3]
PIRiI38607.
RefSeqiNP_001026855.2. NM_001031685.2. [Q13625-3]
NP_005417.1. NM_005426.2. [Q13625-2]
UniGeneiHs.523968.

Genome annotation databases

EnsembliENST00000343537; ENSP00000341957; ENSG00000143514. [Q13625-3]
ENST00000391878; ENSP00000375750; ENSG00000143514. [Q13625-2]
GeneIDi7159.
KEGGihsa:7159.
UCSCiuc001hod.3. human. [Q13625-1]

Polymorphism databases

DMDMi33860140.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58334 mRNA. Translation: AAC50557.1 .
AJ318888 mRNA. Translation: CAC83012.1 .
AK294432 mRNA. Translation: BAG57677.1 .
AC096542 Genomic DNA. No translation available.
BC046150 mRNA. Translation: AAH46150.2 . Sequence problems.
BC058918 mRNA. Translation: AAH58918.2 . Different initiation.
U09582 mRNA. Translation: AAA21597.1 .
CCDSi CCDS1538.1. [Q13625-2 ]
CCDS44319.1. [Q13625-3 ]
PIRi I38607.
RefSeqi NP_001026855.2. NM_001031685.2. [Q13625-3 ]
NP_005417.1. NM_005426.2. [Q13625-2 ]
UniGenei Hs.523968.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YCS X-ray 2.20 B 892-1126 [» ]
2UWQ NMR - A 1-83 [» ]
4A63 X-ray 2.27 B/D/F/H/J/L 892-1128 [» ]
4IRV X-ray 2.04 E/F/G/H 726-782 [» ]
ProteinModelPortali Q13625.
SMRi Q13625. Positions 1-83, 926-1118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113012. 37 interactions.
DIPi DIP-24266N.
DIP-29587N.
DIP-426N.
IntActi Q13625. 55 interactions.
MINTi MINT-106406.
STRINGi 9606.ENSP00000341957.

PTM databases

PhosphoSitei Q13625.

Polymorphism databases

DMDMi 33860140.

Proteomic databases

MaxQBi Q13625.
PaxDbi Q13625.
PRIDEi Q13625.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343537 ; ENSP00000341957 ; ENSG00000143514 . [Q13625-3 ]
ENST00000391878 ; ENSP00000375750 ; ENSG00000143514 . [Q13625-2 ]
GeneIDi 7159.
KEGGi hsa:7159.
UCSCi uc001hod.3. human. [Q13625-1 ]

Organism-specific databases

CTDi 7159.
GeneCardsi GC01M223967.
HGNCi HGNC:12000. TP53BP2.
HPAi HPA021603.
MIMi 602143. gene.
neXtProti NX_Q13625.
PharmGKBi PA36681.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283717.
HOGENOMi HOG000034106.
HOVERGENi HBG050596.
KOi K16823.
OMAi YRNQSDA.
OrthoDBi EOG73FQKX.
PhylomeDBi Q13625.
TreeFami TF105545.

Miscellaneous databases

ChiTaRSi TP53BP2. human.
EvolutionaryTracei Q13625.
GeneWikii TP53BP2.
GenomeRNAii 7159.
NextBioi 28014.
PROi Q13625.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13625.
Bgeei Q13625.
CleanExi HS_TP53BP2.
Genevestigatori Q13625.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00023. Ank. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR01887. SPECTRNALPHA.
SMARTi SM00248. ANK. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The p53-binding protein 53BP2 also interacts with Bcl2 and impedes cell cycle progression at G2/M."
    Naumovski L., Cleary M.L.
    Mol. Cell. Biol. 16:3884-3892(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH BCL2.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TP53.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Amygdala.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "Two cellular proteins that bind to wild-type but not mutant p53."
    Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.
    Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 600-1128, INTERACTION WITH TP53.
  7. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  8. "NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2."
    Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.
    Oncogene 18:5177-5186(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH RELA.
  9. "APCL, a central nervous system-specific homologue of adenomatous polyposis coli tumor suppressor, binds to p53-binding protein 2 and translocates it to the perinucleus."
    Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.
    Cancer Res. 60:101-105(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APC2, MUTAGENESIS OF TRP-1098, SUBCELLULAR LOCATION.
  10. "Proapoptotic p53-interacting protein 53BP2 is induced by UV irradiation but suppressed by p53."
    Lopez C.D., Ao Y., Rohde L.H., Perez T.D., O'Connor D.J., Lu X., Ford J.M., Naumovski L.
    Mol. Cell. Biol. 20:8018-8025(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "Aberrant overexpression of 53BP2 mRNA in lung cancer cell lines."
    Mori T., Okamoto H., Takahashi N., Ueda R., Okamoto T.
    FEBS Lett. 465:124-128(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis."
    Chen Y., Liu W., Naumovski L., Neve R.L.
    J. Neurochem. 85:801-809(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APPBP1.
  13. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator of apoptosis."
    Uhlmann-Schiffler H., Kiermayer S., Stahl H.
    Oncogene 28:2065-2073(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDX42, SUBCELLULAR LOCATION.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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; SER-556 AND SER-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2."
    Gorina S., Pavletich N.P.
    Science 274:1001-1005(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 892-1128.
  22. "Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold."
    Tidow H., Andreeva A., Rutherford T.J., Fersht A.R.
    J. Mol. Biol. 371:948-958(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-83.

Entry informationi

Entry nameiASPP2_HUMAN
AccessioniPrimary (citable) accession number: Q13625
Secondary accession number(s): B4DG66
, Q12892, Q86X75, Q96KQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 15, 2003
Last modified: July 9, 2014
This is version 154 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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