Q13625 (ASPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TP53BP2
Synonyms:	ASPP2, BBP

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	1128 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.11 Ref.15
Subunit structure	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. Ref.1 Ref.2 Ref.5 Ref.7 Ref.8 Ref.11 Ref.15
Subcellular location	Cytoplasm › perinuclear region. Nucleus. Note: Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42. Ref.8 Ref.15
Tissue specificity	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. Ref.2 Ref.7 Ref.10
Induction	Following DNA damage induced by UV irradiation. Down-regulated by wild-type, but not mutant, p53/TP53. Ref.9
Domain	The ankyrin repeats and the SH3 domain are required for a specific interactions with TP53.
Sequence similarities	Belongs to the ASPP family. Contains 2 ANK repeats. Contains 1 SH3 domain.
Sequence caution	The sequence AAH46150.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH46150.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence AAH58918.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat SH3 domain SH3-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW central nervous system development Inferred from electronic annotation. Source: Compara embryo development ending in birth or egg hatching Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from direct assay Ref.2. Source: UniProtKB negative regulation of cell cycle Traceable author statement PubMed 14729977. Source: UniProtKB response to ionizing radiation Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement PubMed 9748285. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay Ref.15. Source: UniProtKB nucleus Inferred from direct assay Ref.15. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	SH3/SH2 adaptor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	3	EBI-77642,EBI-77613
Irs1	P35569	2	EBI-287091,EBI-400825	From a different organism.
Irs1	P35570	4	EBI-287091,EBI-520230	From a different organism.
RELA	Q04206	6	EBI-287091,EBI-73886

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13625-1)

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: Q13625-2)

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.

Isoform 3 (identifier: Q13625-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1128

1128

Apoptosis-stimulating of p53 protein 2

PRO_0000066964

Regions

Repeat

958 – 990

33

ANK 1

Repeat

991 – 1023

33

ANK 2

Domain

1057 – 1119

63

SH3

Region

332 – 348

17

Interaction with APPBP1

Region

876 – 1128

253

Mediates interaction with APC2

Motif

866 – 875

10

SH3-binding Potential

Compositional bias

132 – 173

42

Gln-rich

Compositional bias

824 – 902

79

Pro-rich

Amino acid modifications

Modified residue

480

1

Phosphoserine Ref.14 Ref.16 Ref.17 Ref.19

Modified residue

556

1

Phosphoserine Ref.14 Ref.17

Modified residue

572

1

Phosphoserine Ref.17

Modified residue

698

1

Phosphoserine Ref.14 Ref.17

Natural variations

Alternative sequence

1 – 123

123

Missing in isoform 2.

VSP_008010

Alternative sequence

1

1

M → MRFGSK in isoform 3.

VSP_043509

Experimental info

Mutagenesis

1098

1

W → K: Loss of interaction with APC2. Ref.8

Secondary structure

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1128

Helix Strand Turn

Details...

Beta strand

2 – 9

8

Beta strand

17 – 22

6

Helix

29 – 34

6

Beta strand

40 – 42

3

Beta strand

44 – 49

6

Beta strand

52 – 56

5

Helix

62 – 69

8

Helix

73 – 75

3

Beta strand

77 – 81

5

Helix

927 – 936

10

Helix

939 – 945

7

Helix

946 – 948

3

Helix

962 – 969

8

Helix

972 – 981

10

Helix

995 – 1001

7

Helix

1005 – 1013

9

Beta strand

1023 – 1025

3

Helix

1029 – 1032

4

Beta strand

1035 – 1037

3

Helix

1043 – 1053

11

Turn

1054 – 1057

4

Helix

1058 – 1060

3

Beta strand

1061 – 1066

6

Beta strand

1083 – 1086

4

Beta strand

1091 – 1093

3

Beta strand

1095 – 1102

8

Beta strand

1105 – 1110

6

Helix

1111 – 1113

3

Beta strand

1114 – 1117

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 15, 2003. Version 2. Checksum: C75D056FBC1DAD75	FASTA	1,128	125,616
	10 20 30 40 50 60 MMPMFLTVYL SNNEQHFTEV PVTPETICRD VVDLCKEPGE SDCHLAEVWC GSERPVADNE 70 80 90 100 110 120 RMFDVLQRFG SQRNEVRFFL RHERPPGRDI VSGPRSQDPS LKRNGVKVPG EYRRKENGVN 130 140 150 160 170 180 SPRMDLTLAE LQEMASRQQQ QIEAQQQLLA TKEQRLKFLK QQDQRQQQQV AEQEKLKRLK 190 200 210 220 230 240 EIAENQEAKL KKVRALKGHV EQKRLSNGKL VEEIEQMNNL FQQKQRELVL AVSKVEELTR 250 260 270 280 290 300 QLEMLKNGRI DSHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV 310 320 330 340 350 360 MDKRVNELRD RLWKKKAALQ QKENLPVSSD GNLPQQAASA PSRVAAVGPY IQSSTMPRMP 370 380 390 400 410 420 SRPELLVKPA LPDGSLVIQA SEGPMKIQTL PNMRSGAASQ TKGSKIHPVG PDWSPSNADL 430 440 450 460 470 480 FPSQGSASVP QSTGNALDQV DDGEVPLREK EKKVRPFSMF DAVDQSNAPP SFGTLRKNQS 490 500 510 520 530 540 SEDILRDAQV ANKNVAKVPP PVPTKPKQIN LPYFGQTNQP PSDIKPDGSS QQLSTVVPSM 550 560 570 580 590 600 GTKPKPAGQQ PRVLLSPSIP SVGQDQTLSP GSKQESPPAA AVRPFTPQPS KDTLLPPFRK 610 620 630 640 650 660 PQTVAASSIY SMYTQQQAPG KNFQQAVQSA LTKTHTRGPH FSSVYGKPVI AAAQNQQQHP 670 680 690 700 710 720 ENIYSNSQGK PGSPEPETEP VSSVQENHEN ERIPRPLSPT KLLPFLSNPY RNQSDADLEA 730 740 750 760 770 780 LRKKLSNAPR PLKKRSSITE PEGPNGPNIQ KLLYQRTTIA AMETISVPSY PSKSASVTAS 790 800 810 820 830 840 SESPVEIQNP YLHVEPEKEV VSLVPESLSP EDVGNASTEN SDMPAPSPGL DYEPEGVPDN 850 860 870 880 890 900 SPNLQNNPEE PNPEAPHVLD VYLEEYPPYP PPPYPSGEPE GPGEDSVSMR PPEITGQVSL 910 920 930 940 950 960 PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD DPSLPNDEGI 970 980 990 1000 1010 1020 TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA SCNNVQVCKF LVESGAAVFA 1030 1040 1050 1060 1070 1080 MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV QEKMGIMNKG VIYALWDYEP QNDDELPMKE 1090 1100 1110 1120 GDCMTIIHRE DEDEIEWWWA RLNDKEGYVP RNLLGLYPRI KPRQRSLA
	Isoform 2 (Bbp) [UniParc]. Checksum: 3DF4FF49EB589F20	FASTA	1,005	111,431
	10 20 30 40 50 60 MDLTLAELQE MASRQQQQIE AQQQLLATKE QRLKFLKQQD QRQQQQVAEQ EKLKRLKEIA 70 80 90 100 110 120 ENQEAKLKKV RALKGHVEQK RLSNGKLVEE IEQMNNLFQQ KQRELVLAVS KVEELTRQLE 130 140 150 160 170 180 MLKNGRIDSH HDNQSAVAEL DRLYKELQLR NKLNQEQNAK LQQQRECLNK RNSEVAVMDK 190 200 210 220 230 240 RVNELRDRLW KKKAALQQKE NLPVSSDGNL PQQAASAPSR VAAVGPYIQS STMPRMPSRP 250 260 270 280 290 300 ELLVKPALPD GSLVIQASEG PMKIQTLPNM RSGAASQTKG SKIHPVGPDW SPSNADLFPS 310 320 330 340 350 360 QGSASVPQST GNALDQVDDG EVPLREKEKK VRPFSMFDAV DQSNAPPSFG TLRKNQSSED 370 380 390 400 410 420 ILRDAQVANK NVAKVPPPVP TKPKQINLPY FGQTNQPPSD IKPDGSSQQL STVVPSMGTK 430 440 450 460 470 480 PKPAGQQPRV LLSPSIPSVG QDQTLSPGSK QESPPAAAVR PFTPQPSKDT LLPPFRKPQT 490 500 510 520 530 540 VAASSIYSMY TQQQAPGKNF QQAVQSALTK THTRGPHFSS VYGKPVIAAA QNQQQHPENI 550 560 570 580 590 600 YSNSQGKPGS PEPETEPVSS VQENHENERI PRPLSPTKLL PFLSNPYRNQ SDADLEALRK 610 620 630 640 650 660 KLSNAPRPLK KRSSITEPEG PNGPNIQKLL YQRTTIAAME TISVPSYPSK SASVTASSES 670 680 690 700 710 720 PVEIQNPYLH VEPEKEVVSL VPESLSPEDV GNASTENSDM PAPSPGLDYE PEGVPDNSPN 730 740 750 760 770 780 LQNNPEEPNP EAPHVLDVYL EEYPPYPPPP YPSGEPEGPG EDSVSMRPPE ITGQVSLPPG 790 800 810 820 830 840 KRTNLRKTGS ERIAHGMRVK FNPLALLLDS SLEGEFDLVQ RIIYEVDDPS LPNDEGITAL 850 860 870 880 890 900 HNAVCAGHTE IVKFLVQFGV NVNAADSDGW TPLHCAASCN NVQVCKFLVE SGAAVFAMTY 910 920 930 940 950 960 SDMQTAADKC EEMEEGYTQC SQFLYGVQEK MGIMNKGVIY ALWDYEPQND DELPMKEGDC 970 980 990 1000 MTIIHREDED EIEWWWARLN DKEGYVPRNL LGLYPRIKPR QRSLA
	Isoform 3 [UniParc]. Checksum: 2458BDF5EC624C2B	FASTA	1,133	126,192
	10 20 30 40 50 60 MRFGSKMPMF LTVYLSNNEQ HFTEVPVTPE TICRDVVDLC KEPGESDCHL AEVWCGSERP 70 80 90 100 110 120 VADNERMFDV LQRFGSQRNE VRFFLRHERP PGRDIVSGPR SQDPSLKRNG VKVPGEYRRK 130 140 150 160 170 180 ENGVNSPRMD LTLAELQEMA SRQQQQIEAQ QQLLATKEQR LKFLKQQDQR QQQQVAEQEK 190 200 210 220 230 240 LKRLKEIAEN QEAKLKKVRA LKGHVEQKRL SNGKLVEEIE QMNNLFQQKQ RELVLAVSKV 250 260 270 280 290 300 EELTRQLEML KNGRIDSHHD NQSAVAELDR LYKELQLRNK LNQEQNAKLQ QQRECLNKRN 310 320 330 340 350 360 SEVAVMDKRV NELRDRLWKK KAALQQKENL PVSSDGNLPQ QAASAPSRVA AVGPYIQSST 370 380 390 400 410 420 MPRMPSRPEL LVKPALPDGS LVIQASEGPM KIQTLPNMRS GAASQTKGSK IHPVGPDWSP 430 440 450 460 470 480 SNADLFPSQG SASVPQSTGN ALDQVDDGEV PLREKEKKVR PFSMFDAVDQ SNAPPSFGTL 490 500 510 520 530 540 RKNQSSEDIL RDAQVANKNV AKVPPPVPTK PKQINLPYFG QTNQPPSDIK PDGSSQQLST 550 560 570 580 590 600 VVPSMGTKPK PAGQQPRVLL SPSIPSVGQD QTLSPGSKQE SPPAAAVRPF TPQPSKDTLL 610 620 630 640 650 660 PPFRKPQTVA ASSIYSMYTQ QQAPGKNFQQ AVQSALTKTH TRGPHFSSVY GKPVIAAAQN 670 680 690 700 710 720 QQQHPENIYS NSQGKPGSPE PETEPVSSVQ ENHENERIPR PLSPTKLLPF LSNPYRNQSD 730 740 750 760 770 780 ADLEALRKKL SNAPRPLKKR SSITEPEGPN GPNIQKLLYQ RTTIAAMETI SVPSYPSKSA 790 800 810 820 830 840 SVTASSESPV EIQNPYLHVE PEKEVVSLVP ESLSPEDVGN ASTENSDMPA PSPGLDYEPE 850 860 870 880 890 900 GVPDNSPNLQ NNPEEPNPEA PHVLDVYLEE YPPYPPPPYP SGEPEGPGED SVSMRPPEIT 910 920 930 940 950 960 GQVSLPPGKR TNLRKTGSER IAHGMRVKFN PLALLLDSSL EGEFDLVQRI IYEVDDPSLP 970 980 990 1000 1010 1020 NDEGITALHN AVCAGHTEIV KFLVQFGVNV NAADSDGWTP LHCAASCNNV QVCKFLVESG 1030 1040 1050 1060 1070 1080 AAVFAMTYSD MQTAADKCEE MEEGYTQCSQ FLYGVQEKMG IMNKGVIYAL WDYEPQNDDE 1090 1100 1110 1120 1130 LPMKEGDCMT IIHREDEDEI EWWWARLNDK EGYVPRNLLG LYPRIKPRQR SLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"ASPP proteins specifically stimulate the apoptotic function of p53." Samuels-Lev Y., O'Connor D.J., Bergamaschi D., Trigiante G., Hsieh J.-K., Zhong S., Campargue I., Naumovski L., Crook T., Lu X. Mol. Cell 8:781-794(2001) [PubMed] [Europe PMC] [Abstract] 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 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.
[5]	"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.
[6]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-556 AND SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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; SER-572 AND SER-698, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY.
[20]	"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.
[21]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U58334 mRNA. Translation: AAC50557.1.
AJ318888 mRNA. Translation: CAC83012.1.
AK294432 mRNA. Translation: BAG57677.1.
BC046150 mRNA. Translation: AAH46150.2. Sequence problems.
BC058918 mRNA. Translation: AAH58918.2. Different initiation.
U09582 mRNA. Translation: AAA21597.1.

IPI

IPI00337588.
IPI00939154.

PIR

I38607.

RefSeq

NP_001026855.2. NM_001031685.2.
NP_005417.1. NM_005426.2.

UniGene

Hs.523968.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YCS	X-ray	2.20	B	892-1128	[»]
2UWQ	NMR	-	A	1-83	[»]
4A63	X-ray	2.27	B/D/F/H/J/L	892-1128	[»]

ProteinModelPortal

Q13625.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24266N.
DIP-29587N.
DIP-426N.

IntAct

Q13625. 23 interactions.

MINT

MINT-106406.

STRING

9606.ENSP00000341957.

PTM databases

PhosphoSite

Q13625.

Polymorphism databases

DMDM

33860140.

Proteomic databases

PaxDb

Q13625.

PRIDE

Q13625.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343537; ENSP00000341957; ENSG00000143514.
ENST00000391878; ENSP00000375750; ENSG00000143514.

GeneID

7159.

KEGG

hsa:7159.

UCSC

uc001hod.3. human.

Organism-specific databases

CTD

7159.

GeneCards

GC01M223967.

HGNC

HGNC:12000. TP53BP2.

HPA

HPA021603.

MIM

602143. gene.

neXtProt

NX_Q13625.

PharmGKB

PA36681.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG283717.

HOGENOM

HOG000034106.

HOVERGEN

HBG050596.

KO

K16823.

OrthoDB

EOG4KH2T7.

Gene expression databases

ArrayExpress

Q13625.

Bgee

Q13625.

CleanEx

HS_TP53BP2.

Genevestigator

Q13625.

GermOnline

ENSG00000143514. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]

Pfam

PF00023. Ank. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR01887. SPECTRNALPHA.

SMART

SM00248. ANK. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TP53BP2. human.

EvolutionaryTrace

Q13625.

GenomeRNAi

7159.

NextBio

28014.

SOURCE

Search...

Entry information

Entry name

ASPP2_HUMAN

Accession

Primary (citable) accession number: Q13625
Secondary accession number(s): B4DG66 , Q12892, Q86X75, Q96KQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	August 15, 2003
Last modified:	May 1, 2013
This is version 140 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.