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Q13625 (ASPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1128 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050673EBI-77642,EBI-77613
Irs1P355692EBI-287091,EBI-400825From a different organism.
Irs1P355704EBI-287091,EBI-520230From a different organism.
RELAQ042066EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11281128Apoptosis-stimulating of p53 protein 2
PRO_0000066964

Regions

Repeat958 – 99033ANK 1
Repeat991 – 102333ANK 2
Domain1057 – 111963SH3
Region332 – 34817Interaction with APPBP1
Region876 – 1128253Mediates interaction with APC2
Motif866 – 87510SH3-binding Potential
Compositional bias132 – 17342Gln-rich
Compositional bias824 – 90279Pro-rich

Amino acid modifications

Modified residue4801Phosphoserine Ref.14 Ref.16 Ref.17 Ref.19
Modified residue5561Phosphoserine Ref.14 Ref.17
Modified residue5721Phosphoserine Ref.17
Modified residue6981Phosphoserine Ref.14 Ref.17

Natural variations

Alternative sequence1 – 123123Missing in isoform 2.
VSP_008010
Alternative sequence11M → MRFGSK in isoform 3.
VSP_043509

Experimental info

Mutagenesis10981W → K: Loss of interaction with APC2. Ref.8

Secondary structure

1 ..................................................... 1128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 15, 2003. Version 2.
Checksum: C75D056FBC1DAD75

FASTA1,128125,616
        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

« Hide

Isoform 2 (Bbp) [UniParc].

Checksum: 3DF4FF49EB589F20
Show »

FASTA1,005111,431
Isoform 3 [UniParc].

Checksum: 2458BDF5EC624C2B
Show »

FASTA1,133126,192

References

« Hide '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. expand/collapse author list , 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.
IPIIPI00337588.
IPI00939154.
PIRI38607.
RefSeqNP_001026855.2. NM_001031685.2.
NP_005417.1. NM_005426.2.
UniGeneHs.523968.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YCSX-ray2.20B892-1128[»]
2UWQNMR-A1-83[»]
4A63X-ray2.27B/D/F/H/J/L892-1128[»]
ProteinModelPortalQ13625.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-24266N.
DIP-29587N.
DIP-426N.
IntActQ13625. 23 interactions.
MINTMINT-106406.
STRING9606.ENSP00000341957.

PTM databases

PhosphoSiteQ13625.

Polymorphism databases

DMDM33860140.

Proteomic databases

PaxDbQ13625.
PRIDEQ13625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343537; ENSP00000341957; ENSG00000143514.
ENST00000391878; ENSP00000375750; ENSG00000143514.
GeneID7159.
KEGGhsa:7159.
UCSCuc001hod.3. human.

Organism-specific databases

CTD7159.
GeneCardsGC01M223967.
HGNCHGNC:12000. TP53BP2.
HPAHPA021603.
MIM602143. gene.
neXtProtNX_Q13625.
PharmGKBPA36681.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283717.
HOGENOMHOG000034106.
HOVERGENHBG050596.
KOK16823.
OrthoDBEOG4KH2T7.

Gene expression databases

ArrayExpressQ13625.
BgeeQ13625.
CleanExHS_TP53BP2.
GenevestigatorQ13625.
GermOnlineENSG00000143514. Homo sapiens.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR01887. SPECTRNALPHA.
SMARTSM00248. ANK. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
SSF50044. SH3. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTP53BP2. human.
EvolutionaryTraceQ13625.
GenomeRNAi7159.
NextBio28014.
SOURCESearch...

Entry information

Entry nameASPP2_HUMAN
AccessionPrimary (citable) accession number: Q13625
Secondary accession number(s): B4DG66 expand/collapse secondary AC list , 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 statusReviewed (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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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