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Protein

Tumor suppressor p53-binding protein 1

Gene

Tp53bp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53-mediated transcriptional activation (By similarity).By similarity1 Publication

GO - Molecular functioni

  • damaged DNA binding Source: MGI
  • histone binding Source: GO_Central
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: MGI
  • RNA polymerase II transcription cofactor activity Source: MGI
  • sequence-specific DNA binding Source: MGI
  • telomeric DNA binding Source: MGI
  • transcription factor binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor suppressor p53-binding protein 1
Short name:
53BP1
Short name:
p53-binding protein 1
Short name:
p53BP1
Gene namesi
Name:Tp53bp1
Synonyms:Trp53bp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1351320. Trp53bp1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosomecentromerekinetochore 1 Publication

  • Note: Associated with kinetochores. Both nuclear and cytoplasmic in some cells. Recruited to sites of DNA damage, such as double stand breaks. H4K20me2 is required for efficient localization to double strand breaks and removal of proteins that have a high affinity for H4K20me2 such as L3MBTL1 and KDM4A is needed (By similarity).By similarity

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • DNA repair complex Source: MGI
  • kinetochore Source: MGI
  • nuclear chromosome, telomeric region Source: MGI
  • nucleus Source: MGI
  • replication fork Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000726441 – 1957Tumor suppressor p53-binding protein 1Add BLAST1957

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25PhosphoserineBy similarity1
Modified residuei63PhosphoserineBy similarity1
Modified residuei68PhosphoserineCombined sources1
Modified residuei104PhosphoserineBy similarity1
Modified residuei163PhosphoserineBy similarity1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei261PhosphoserineCombined sources1
Modified residuei262PhosphoserineCombined sources1
Modified residuei291PhosphoserineBy similarity1
Modified residuei299PhosphothreonineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Modified residuei376PhosphoserineCombined sources1
Modified residuei391PhosphoserineBy similarity1
Modified residuei446PhosphoserineBy similarity1
Modified residuei458PhosphoserineCombined sources1
Modified residuei501PhosphoserineBy similarity1
Modified residuei512PhosphoserineBy similarity1
Modified residuei517PhosphoserineBy similarity1
Modified residuei519PhosphoserineBy similarity1
Modified residuei537PhosphothreonineBy similarity1
Modified residuei542PhosphothreonineBy similarity1
Modified residuei546PhosphoserineCombined sources1
Modified residuei573PhosphoserineBy similarity1
Modified residuei616PhosphoserineBy similarity1
Modified residuei621PhosphoserineCombined sources1
Modified residuei625PhosphoserineCombined sources1
Modified residuei626PhosphoserineCombined sources1
Modified residuei678PhosphoserineBy similarity1
Modified residuei710PhosphoserineCombined sources1
Modified residuei713PhosphoserineCombined sources1
Modified residuei757PhosphoserineBy similarity1
Modified residuei816PhosphoserineCombined sources1
Modified residuei906PhosphothreonineBy similarity1
Cross-linki914Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei959PhosphoserineBy similarity1
Modified residuei1012PhosphoserineBy similarity1
Modified residuei1069PhosphoserineBy similarity1
Modified residuei1090PhosphoserineCombined sources1
Modified residuei1103PhosphoserineCombined sources1
Modified residuei1199PhosphothreonineBy similarity1
Modified residuei1201PhosphoserineBy similarity1
Modified residuei1204PhosphoserineBy similarity1
Modified residuei1302PhosphoserineBy similarity1
Modified residuei1317Omega-N-methylarginineCombined sources1
Modified residuei1327PhosphoserineBy similarity1
Modified residuei1340Omega-N-methylarginineCombined sources1
Modified residuei1347PhosphoserineBy similarity1
Modified residuei1353PhosphoserineBy similarity1
Modified residuei1411PhosphoserineCombined sources1
Modified residuei1415PhosphoserineCombined sources1
Cross-linki1419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1419Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1445PhosphoserineBy similarity1
Modified residuei1447PhosphoserineCombined sources1
Modified residuei1458PhosphoserineCombined sources1
Modified residuei1459PhosphoserineBy similarity1
Cross-linki1548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki1548Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1594PhosphothreonineBy similarity1
Modified residuei1603PhosphoserineBy similarity1
Modified residuei1616PhosphoserineCombined sources1
Modified residuei1620PhosphoserineBy similarity1
Modified residuei1623PhosphothreonineBy similarity1
Modified residuei1633PhosphothreonineBy similarity1
Modified residuei1641PhosphoserineBy similarity1
Modified residuei1658PhosphoserineBy similarity1
Modified residuei1663PhosphoserineBy similarity1
Modified residuei1686PhosphoserineBy similarity1
Modified residuei1744PhosphoserineBy similarity1

Post-translational modificationi

Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding (By similarity).By similarity
Phosphorylated at basal level in the absence of DNA damage. Hyper-phosphorylated in an ATM-dependent manner in response to DNA damage induced by ionizing radiation. Hyper-phosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation. Dephosphorylated by PPP5C (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP70399.
MaxQBiP70399.
PaxDbiP70399.
PeptideAtlasiP70399.
PRIDEiP70399.

PTM databases

iPTMnetiP70399.
PhosphoSitePlusiP70399.

Interactioni

Subunit structurei

May form homooligomers. Interacts with DCLRE1C. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3). Has low affinity for histone H3 that has been dimethylated on 'Lys-79'. Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro). Does not bind unmethylated histone H3. Interacts with MUM1/EXPAND1. Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared (By similarity). Binds to the central domain of p53/TP53. Interacts with IFI202A. Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205144. 30 interactors.
DIPiDIP-31595N.
IntActiP70399. 6 interactors.
MINTiMINT-136714.
STRINGi10090.ENSMUSP00000106278.

Structurei

Secondary structure

11957
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1475 – 1478Combined sources4
Beta strandi1483 – 1493Combined sources11
Turni1496 – 1498Combined sources3
Beta strandi1499 – 1503Combined sources5
Beta strandi1509 – 1513Combined sources5
Turni1514 – 1516Combined sources3
Beta strandi1517 – 1520Combined sources4
Beta strandi1525 – 1533Combined sources9
Turni1535 – 1537Combined sources3
Beta strandi1539 – 1549Combined sources11
Beta strandi1552 – 1559Combined sources8
Beta strandi1562 – 1566Combined sources5
Helixi1568 – 1570Combined sources3
Beta strandi1571 – 1574Combined sources4
Helixi1575 – 1579Combined sources5
Turni1580 – 1584Combined sources5
Beta strandi1585 – 1587Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSFNMR-A1463-1617[»]
ProteinModelPortaliP70399.
SMRiP70399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70399.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1737 – 1833BRCT 1PROSITE-ProRule annotationAdd BLAST97
Domaini1849 – 1949BRCT 2PROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1469 – 1588Tudor-likeBy similarityAdd BLAST120
Regioni1480 – 1508Interaction with dimethylated histone H4By similarityAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1381 – 1388GAR8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi131 – 143Poly-GluAdd BLAST13
Compositional biasi631 – 808Glu-richAdd BLAST178
Compositional biasi1273 – 1315Ser-richAdd BLAST43
Compositional biasi1464 – 1467Poly-Ser4
Compositional biasi1628 – 1631Poly-Ser4
Compositional biasi1745 – 1749Poly-Glu5

Domaini

The Tudor-like region mediates binding to H4K20me2.By similarity

Sequence similaritiesi

Contains 2 BRCT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3548. Eukaryota.
ENOG411075K. LUCA.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiP70399.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
[Graphical view]
PfamiPF09038. 53-BP1_Tudor. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P70399-1) [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
MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEEDAGSHF SVLSRHLPNL
60 70 80 90 100
QMHKENPVLD IVSNPEQSAV EQGDSNSSFN EHLKEKKASD PVESSHLGTS
110 120 130 140 150
GSISQVIERL PQPNRTSSAL AVTVEAASLP EEEKEEEELE EKEGVGANAP
160 170 180 190 200
GADSLAAEDS ASSQLGFGVL ELSQSQDVEE HTVPYDVNQE HLQLVTTNSG
210 220 230 240 250
SSPLSDVDAS TAIKCEEQPT EDIAMIEQPS KDIPVTVQPG KGIHVVEEQN
260 270 280 290 300
LPLVRSEDRP SSPQVSVAAV ETKEQVPARE LLEEGPQVQP SSEPEVSSTQ
310 320 330 340 350
EDLFDQSSKT ASDGCSTPSR EEGGCSPVST PATTLQLLQL SGQKPLVQES
360 370 380 390 400
LSTNSSDLVA PSPDAFRSTP FIVPSSPTEQ GGRKDEPMDM SVIPAGGEPF
410 420 430 440 450
QKLHDDEAME TEKPLLPSQP TVSPQASTPV SRSTPVFTPG SLPIPSQPEF
460 470 480 490 500
SHDIFIPSPS LEEPSDDVKK GGGLHSSSLT VECSKTSESE PKNFTDDLGL
510 520 530 540 550
SMTGDSCKLM LSTSEYSQSS KMESLGSPRT EEDRENTQID DTEPLSPVSN
560 570 580 590 600
SKLPADSENV LVTPSQDDQV EMSQNVDKAK EDETEDRGDC KGREDAVAED
610 620 630 640 650
VCIDLTCDSG SQAVPSPATR SEALSSVLDQ EEAMDTKEHH PEEGFSGSEV
660 670 680 690 700
EEVPETPCGS HREEPKEEAM ESIPLHLSLT ETQSEALCLQ KEAPKEECPE
710 720 730 740 750
AMEVETSVIS IDSPQKLQVL DQELEHKDPD TWEEATSEDS SVVIVDVKEP
760 770 780 790 800
SPRADVSCEP LEEVEKCSDS QSWEGVAPEE EPCAENRLDT PEEKRIECDG
810 820 830 840 850
DSKAETTEKD AVTEDSPQPP LPSVRDEPVR PDQETQQPQV QEKESPVTVD
860 870 880 890 900
AEVADDKQLG PEGACQQLEK APACASQSFC ESSSETPFHF TLPKEGDIIP
910 920 930 940 950
PLTGATPPLI GHLKLEPKRH STPIGISNYP ESTIATSDVT SESMVEINDP
960 970 980 990 1000
LLGNEKGDSE SAPEMDGKLS LKMKLVSPET EASEESLQFS LEKPTTAERK
1010 1020 1030 1040 1050
NGSTAIAEPV ASLQKPVPVF GCIYEAQQEK EAQSEAPPSA PDRANLLHFP
1060 1070 1080 1090 1100
SAQEEDKERP DVTPKLRQSE QPVKPVGPVM DDAAPEDSAS PVSQQRASQE
1110 1120 1130 1140 1150
PFSPAEDVME TDLLEGLAAN QDRPSKMLMD RPTQSNIGIQ TVDHSLCAPE
1160 1170 1180 1190 1200
TVSAATQTVK SVCEQGTSTA EQNSGKQDAT VQTERGSGEK PASAPVDDTE
1210 1220 1230 1240 1250
SLHSQGEEEF EMPQPPHGHV LHRHMRTIRE VRTLVTRVIT DVYYVDGTEV
1260 1270 1280 1290 1300
ERKVTEETEE PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSSHHT
1310 1320 1330 1340 1350
SSGTSLSAIH SSGSSGRGAG PLKGKASGTE AADFALPSSR GGPGKLSPRK
1360 1370 1380 1390 1400
GISQTGAPVC EEDGDAGLGI RQGGKAPVTP RGRGRRGRPP SRTTGTRETV
1410 1420 1430 1440 1450
VSGPLGVEDI SPSMSPDDKS FTRIMPRVPD STKRTDASSS TLRRSDSPEI
1460 1470 1480 1490 1500
PFQAATGSSD GLDSSSSGNS FVGLRVVAKW SSNGYFYSGK ITRDVGAGKY
1510 1520 1530 1540 1550
KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA GVVKGHRKES
1560 1570 1580 1590 1600
GELYYSIEKE GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA
1610 1620 1630 1640 1650
DISLDNLVEG KRKRRSNISS PVTPTAASSS STTPTRKATE SPRASTGVPS
1660 1670 1680 1690 1700
GKRKLPTSEE ERSPAKRGRK SATVKPGTVG AAEFVSPCET GDNIGEPSVL
1710 1720 1730 1740 1750
EEPRGPLPLN KTLFLGYAFL LTMATTSDKL ASRSKLLDGP TGSSEEEEEF
1760 1770 1780 1790 1800
LEIPPFNKQY TECQLRAGAG YILEDFNEAQ CNTAYQCLLI ADQHCRTRKY
1810 1820 1830 1840 1850
FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE EQRILDWQPR
1860 1870 1880 1890 1900
ENPFQNLKVL LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG
1910 1920 1930 1940 1950
VFDVVVTDPS CPASVLKCAE ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY

KHDYVSH
Length:1,957
Mass (Da):211,340
Last modified:January 10, 2006 - v2
Checksum:i0FFA0C26DD526E7B
GO
Isoform 2 (identifier: P70399-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-943: Missing.

Note: No experimental confirmation available.
Show »
Length:1,014
Mass (Da):109,745
Checksum:i52E51794028163EA
GO
Isoform 3 (identifier: P70399-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1100: E → EQRASQE
     1347-1396: Missing.

Note: No experimental confirmation available.
Show »
Length:1,913
Mass (Da):206,958
Checksum:i919C52122DFE5F93
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti141E → EE in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti395A → V in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti421T → A in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti669A → P in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti1064P → L in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti1065K → N in AAH35206 (PubMed:15489334).Curated1
Sequence conflicti1171 – 1172EQ → DE in AAC52876 (PubMed:8910340).Curated2
Sequence conflicti1175G → R in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti1194A → T in AAC52876 (PubMed:8910340).Curated1
Sequence conflicti1259E → G in AAC52876 (PubMed:8910340).Curated1
Sequence conflicti1759Q → H in AAH79906 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0168991 – 943Missing in isoform 2. 1 PublicationAdd BLAST943
Alternative sequenceiVSP_0169001100E → EQRASQE in isoform 3. 1 Publication1
Alternative sequenceiVSP_0169011347 – 1396Missing in isoform 3. 1 PublicationAdd BLAST50

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ414734 mRNA. Translation: CAC94013.1.
BC035206 mRNA. Translation: AAH35206.1.
BC079906 mRNA. Translation: AAH79906.1.
U67885 mRNA. Translation: AAC52876.1.
RefSeqiNP_001277759.1. NM_001290830.1.
NP_038763.3. NM_013735.4.
UniGeneiMm.215389.
Mm.383499.
Mm.481841.

Genome annotation databases

GeneIDi27223.
KEGGimmu:27223.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ414734 mRNA. Translation: CAC94013.1.
BC035206 mRNA. Translation: AAH35206.1.
BC079906 mRNA. Translation: AAH79906.1.
U67885 mRNA. Translation: AAC52876.1.
RefSeqiNP_001277759.1. NM_001290830.1.
NP_038763.3. NM_013735.4.
UniGeneiMm.215389.
Mm.383499.
Mm.481841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSFNMR-A1463-1617[»]
ProteinModelPortaliP70399.
SMRiP70399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205144. 30 interactors.
DIPiDIP-31595N.
IntActiP70399. 6 interactors.
MINTiMINT-136714.
STRINGi10090.ENSMUSP00000106278.

PTM databases

iPTMnetiP70399.
PhosphoSitePlusiP70399.

Proteomic databases

EPDiP70399.
MaxQBiP70399.
PaxDbiP70399.
PeptideAtlasiP70399.
PRIDEiP70399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi27223.
KEGGimmu:27223.

Organism-specific databases

CTDi27223.
MGIiMGI:1351320. Trp53bp1.

Phylogenomic databases

eggNOGiKOG3548. Eukaryota.
ENOG411075K. LUCA.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiP70399.

Miscellaneous databases

EvolutionaryTraceiP70399.
PROiP70399.
SOURCEiSearch...

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
[Graphical view]
PfamiPF09038. 53-BP1_Tudor. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTP53B_MOUSE
AccessioniPrimary (citable) accession number: P70399
Secondary accession number(s): Q68FD0, Q8CI97, Q91YC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 10, 2006
Last modified: November 30, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.