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Protein

Breast cancer type 2 susceptibility protein homolog

Gene

Brca2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and DSS1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability, independently of its known role in homologous recombination (By similarity).By similarity

GO - Molecular functioni

  • gamma-tubulin binding Source: GO_Central
  • single-stranded DNA binding Source: RGD

GO - Biological processi

  • centrosome duplication Source: GO_Central
  • chromosome organization Source: GO_Central
  • DNA recombination Source: RGD
  • double-strand break repair via homologous recombination Source: UniProtKB
  • homologous chromosome orientation involved in meiotic metaphase I plate congression Source: RGD
  • mammary gland development Source: RGD
  • multicellular organism growth Source: RGD
  • regulation of cell proliferation Source: GO_Central
  • regulation of transcription, DNA-templated Source: GO_Central
  • response to estradiol Source: RGD
  • response to nutrient Source: RGD
  • spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer type 2 susceptibility protein homolog
Alternative name(s):
Fanconi anemia group D1 protein homolog
Gene namesi
Name:Brca2
Synonyms:Fancd1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2219. Brca2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000649861 – 3343Breast cancer type 2 susceptibility protein homologAdd BLAST3343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei70PhosphoserineBy similarity1
Modified residuei475PhosphoserineBy similarity1
Modified residuei736PhosphoserineBy similarity1
Modified residuei2063PhosphoserineBy similarity1
Modified residuei3222Phosphoserine; by CDK1 and CDK2By similarity1
Modified residuei3250PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3222 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding (By similarity).By similarity
Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO35923.
PRIDEiO35923.

Expressioni

Tissue specificityi

Highest expression in testis. Also expressed in spleen, skeletal muscle, thymus, mammary gland, heart, ovary, prostate, liver, lung, kidney and brain.

Interactioni

Subunit structurei

Monomer and dimer. Interacts with RAD51; regulates RAD51 recruitment and function at sites of DNA repair. Interacts with DSS1, WDR16, USP11, DMC1, ROCK2 and NPM1. Interacts with both nonubiquitinated and monoubiquitinated FANCD2; this complex also includes XRCC3 and phosphorylated FANCG. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with BRCA1 only in the presence of PALB2 which serves as the bridging protein. Interacts with POLH; the interaction is direct. Interacts with the TREX-2 complex subunits PCID2 and DSS1 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001475.

Structurei

Secondary structure

13343
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni2407 – 2409Combined sources3
Helixi2410 – 2428Combined sources19
Turni2441 – 2443Combined sources3
Beta strandi2444 – 2446Combined sources3
Helixi2453 – 2457Combined sources5
Beta strandi2467 – 2469Combined sources3
Helixi2470 – 2473Combined sources4
Helixi2479 – 2481Combined sources3
Turni2484 – 2489Combined sources6
Helixi2494 – 2498Combined sources5
Turni2500 – 2502Combined sources3
Beta strandi2503 – 2505Combined sources3
Beta strandi2509 – 2511Combined sources3
Helixi2512 – 2514Combined sources3
Beta strandi2515 – 2517Combined sources3
Helixi2527 – 2535Combined sources9
Helixi2542 – 2544Combined sources3
Helixi2547 – 2567Combined sources21
Turni2569 – 2571Combined sources3
Turni2573 – 2575Combined sources3
Beta strandi2576 – 2578Combined sources3
Helixi2579 – 2593Combined sources15
Helixi2601 – 2606Combined sources6
Beta strandi2615 – 2622Combined sources8
Beta strandi2649 – 2652Combined sources4
Beta strandi2657 – 2660Combined sources4
Helixi2664 – 2671Combined sources8
Beta strandi2680 – 2684Combined sources5
Beta strandi2687 – 2690Combined sources4
Helixi2697 – 2699Combined sources3
Beta strandi2705 – 2707Combined sources3
Turni2710 – 2712Combined sources3
Beta strandi2713 – 2715Combined sources3
Beta strandi2718 – 2720Combined sources3
Beta strandi2722 – 2724Combined sources3
Beta strandi2746 – 2748Combined sources3
Beta strandi2759 – 2763Combined sources5
Beta strandi2765 – 2772Combined sources8
Helixi2774 – 2782Combined sources9
Beta strandi2895 – 2903Combined sources9
Beta strandi2905 – 2909Combined sources5
Beta strandi2913 – 2919Combined sources7
Turni2922 – 2927Combined sources6
Beta strandi2934 – 2938Combined sources5
Beta strandi2962 – 2965Combined sources4
Helixi2970 – 2973Combined sources4
Turni2974 – 2976Combined sources3
Helixi2985 – 2989Combined sources5
Helixi2996 – 2998Combined sources3
Beta strandi2999 – 3005Combined sources7
Beta strandi3008 – 3010Combined sources3
Beta strandi3013 – 3015Combined sources3
Beta strandi3018 – 3022Combined sources5
Beta strandi3028 – 3035Combined sources8
Beta strandi3046 – 3054Combined sources9
Beta strandi3064 – 3076Combined sources13
Helixi3080 – 3097Combined sources18
Helixi3101 – 3110Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IYJX-ray3.40B/D2335-3151[»]
ProteinModelPortaliO35923.
SMRiO35923.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati984 – 1018BRCA2 1Add BLAST35
Repeati1197 – 1231BRCA2 2Add BLAST35
Repeati1405 – 1439BRCA2 3Add BLAST35
Repeati1503 – 1537BRCA2 4Add BLAST35
Repeati1645 – 1669BRCA2 5Add BLAST25
Repeati1828 – 1845BRCA2 6Add BLAST18
Repeati1939 – 1973BRCA2 7Add BLAST35
Repeati2019 – 2053BRCA2 8Add BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 40Interaction with PALB2By similarityAdd BLAST40
Regioni622 – 982Interaction with NPM1By similarityAdd BLAST361
Regioni2313 – 2475Interaction with FANCD2By similarityAdd BLAST163
Regioni2411 – 2762Interaction with SHFM1/DSS1By similarityAdd BLAST352

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2612 – 2628Nuclear export signal; masked by interaction with SHFM1/DSS1By similarityAdd BLAST17

Sequence similaritiesi

Contains 8 BRCA2 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4751. Eukaryota.
ENOG410Y06W. LUCA.
HOGENOMiHOG000139693.
HOVERGENiHBG050731.
InParanoidiO35923.
PhylomeDBiO35923.

Family and domain databases

InterProiIPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower_dom.
[Graphical view]
PANTHERiPTHR11289. PTHR11289. 2 hits.
PfamiPF09169. BRCA-2_helical. 1 hit.
PF09103. BRCA-2_OB1. 1 hit.
PF09104. BRCA-2_OB3. 1 hit.
PF00634. BRCA2. 7 hits.
PF09121. Tower. 1 hit.
[Graphical view]
PIRSFiPIRSF002397. BRCA2. 1 hit.
SMARTiSM01341. Tower. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEiPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVEYKRRPT FWEIFKARCS TADLGPISLN WFEELFSEAP PYNTEHPEES
60 70 80 90 100
EYKPQGHEPQ LFKTPQRNPS YHQFASTPIM FKEQSQTLPL DQSPFKELGN
110 120 130 140 150
VVANSKRKHH SKKKARKDPV VDVASLPLKA CPSESPCTPR CTQVAPQRRK
160 170 180 190 200
PVVSGSLFYT PKLEETPKHI SESLGVEVDP DMSWTSSLAT PPTLSSTVLI
210 220 230 240 250
ARDEEAHRNA FPADSPASLK SYFSNHNESL KKNDRFIPSV SDSENKSQQE
260 270 280 290 300
AFSQGLEKML GDSSSKINRF RDCLRKPIPN VLEDGETAVD TSGEDSFSLC
310 320 330 340 350
FPKRRTRNLQ KTRMGKMKKK IFSETRTDGL SEEARGQADD KNSFALEIEP
360 370 380 390 400
RDSEPLDPSV TNQKPLYSQS GDISSEAGQC SDSIWSQPDP SGLNGTQTRK
410 420 430 440 450
IPLLHISFHK QSILEDFIDM KKEGTGSITF PHISSLPEPE KMFSEETLVD
460 470 480 490 500
KEHEGQHLES LEDSISGKQM VSGTSQTACL SPSIRKSIVK MREPLEETLD
510 520 530 540 550
TVFSDSMTSS AFTEELDASA GGLEIHTACS QREDSLCPSS VDTGSWPTTL
560 570 580 590 600
TDTSATVKNA GLITTLKNKR RKFIYSVSDD ASHQGKKLQT QRQSELTNLS
610 620 630 640 650
APFEASAFEV PFPFTNVDSG IPDSSIKRSN LPNDPEEPSL SLTNSFVTAA
660 670 680 690 700
SKEISYIHAL ISQDLNDKEA ILSEEKPQPY TALEADFLSC LPERSCENDQ
710 720 730 740 750
KSPKVSDRKE KVLVSACRPS GRLAAAVQLS SISFDSQENP LGSHNVTSTL
760 770 780 790 800
KLTPSPKTPL SKPVVVSRGK MCKMPEKLQC KSCKDNIELS KNIPLGVNEM
810 820 830 840 850
CVLSENSETP ELLPPLEYIT EVSSSVKSQF NQNTKIAVVQ KDQKDSTFIS
860 870 880 890 900
EVTVHMNSEE LFPEKENNFA FQVTNESNKP NIGSTVEFQE EDLSHAKGHS
910 920 930 940 950
LKNSPMTVDR DLDDEQAGQV LITEDSDSLA VVHDCTKKSR NTIEQHQKGT
960 970 980 990 1000
ADKDFKSNSS LYLKSDGNND YLDKWSEFLD PLMNHKLGGS FRTASNKEIK
1010 1020 1030 1040 1050
LSEDNVKKSK MFFKDIEEQY PTSLDCIDTV STLQLANKKR LSEPHTFDLK
1060 1070 1080 1090 1100
SGTTVSTQCH SQSSVSHEDT HTAPQMLSSK QDFHSSHNLT PSQKAEITEL
1110 1120 1130 1140 1150
STILEESGSQ FEFTQFKNPS HIAQNNTSAV LGNQMAVVRT ASEEWKDVDL
1160 1170 1180 1190 1200
HLPLNPSSVG QIDHNKKFEC LVGVKQSSSH LLEDTCNQNT SCFLPIKEME
1210 1220 1230 1240 1250
FGGFCSALGT KLSVSNEALR KAMKLFSDIE NISEEPSTKV GPRGFSSCAH
1260 1270 1280 1290 1300
HDSVASVFKI KKQNTDKSFD EKSSKCQVTV QNNKEMTTCI LVDENPENYV
1310 1320 1330 1340 1350
KNIKQDNNYT GSQRNAYKLE NSDVSKSSTS GTVYINKGDS DLPFAAEKGN
1360 1370 1380 1390 1400
KYPESCTQYV REENAQIKES VSDLTCLEVM KAEETCHMKS SDKEQLPSDK
1410 1420 1430 1440 1450
MEQNMKEFNI SFQTASGKNI RVSKESLNKS VNILDQETED LTVTSDSLNS
1460 1470 1480 1490 1500
KILCGINKDK MHISCHKKSI NIKKVFEEHF PIGTVSQLPA LQQYPEYEIE
1510 1520 1530 1540 1550
SIKEPTLLSF HTASGKKVKI MQESLDKVKN LFDETQYVRK TTNFGHQESK
1560 1570 1580 1590 1600
PLKDREDYKE RLTLAYEKIE VTASKCEEMQ NFVSKQTEML PQQNDHMYRQ
1610 1620 1630 1640 1650
TENLTSNGSS PKVHGNIENK IEKNPRICCI CQSSYFVTED SALACYTGDS
1660 1670 1680 1690 1700
RKTCVGESSL SKGKKWLREQ SDKLGTRNTI EIQCVKEHTE DFAGNALYEH
1710 1720 1730 1740 1750
SLVIIRTEID TSHVSENQAS TLFSDPNVCH SYLSHSSFCH HDDMHNDSGY
1760 1770 1780 1790 1800
FLKDKIDSDV QPDMKNTEGN AIFPKISATK EIKLHPQTVN EECVQKLETN
1810 1820 1830 1840 1850
ASPYANKNIA IDSAMLDLRN CKVGSPVFIT THSQETVRMK EIFTDNCSKI
1860 1870 1880 1890 1900
VEQNRESKPD TCQTSCHKAL DNSEDFICPS SSGDVCINSP MAIFYPQSEQ
1910 1920 1930 1940 1950
ILQHNQSVSG LKKAATPPVS LETWDTCKSI RGSPQEVHPS RTYGFFSTAS
1960 1970 1980 1990 2000
GKAVQVSDAS LEKARQVFSE IDGDAKQLAS MVSLEGNEKS HHSVKRESSV
2010 2020 2030 2040 2050
VHNTHGVLSL RKTLPGNVSS FVFSGFSTAG GKLVTVSESA LHKVKGMLEE
2060 2070 2080 2090 2100
FDLIRTEHTL QHSPTPEDVS KIPPQPCLES RTPEYSVSSK LQKTYNDKSR
2110 2120 2130 2140 2150
SPSNYKESGS SGNTQSLEVS PQLSQMERKQ ETQSVLGTKV SQRKTNILEK
2160 2170 2180 2190 2200
KQNLPQNIKI ESNKMETFSD VSMKTNVGEY YSKEPENYFE TEAVEIAKAF
2210 2220 2230 2240 2250
MEDDELTDSE QTHAKCSLFA CPQNEALLNS RTRKRGGMAG VAVGQPPIKR
2260 2270 2280 2290 2300
SLLNEFDRII ESKGKSLTPS KSTPDGTIKD RRLFTHHMSL EPVTCGPFCS
2310 2320 2330 2340 2350
SKERQETQSP HVTSPAQGLQ SKEHPSRHSA VGKSSSNPTV SALRSERTRH
2360 2370 2380 2390 2400
SVSDKSTKVF VPPFKVKSRF HRDEHFDSKN VNLEGKNQKS ADGVSEDGND
2410 2420 2430 2440 2450
SDFPQFNKDL MSSLQNARDL QDIRIKNKER HHLCPQPGSL YLTKSSTLPR
2460 2470 2480 2490 2500
ISLQAAVGDS VPSACSPKQL YMYGVSKACI SVNSKNAEYF QFAIEDHFGK
2510 2520 2530 2540 2550
EALCAGKGFR LADGGWLIPS DDGKAGKEEF YRALCDTPGV DPKLISSVWV
2560 2570 2580 2590 2600
SNHYRWIVWK LAAMEFAFPK EFANRCLNPE RVLLQLKYRY DVEIDNSSRS
2610 2620 2630 2640 2650
ALKKILERDD TAAKTLVLCV SDIISLSTNV SETSGSKASS EDSNKVDTIE
2660 2670 2680 2690 2700
LTDGWYAVKA QLDPPLLALV KSGRLTVGQK IITQGAELVG SPDACAPLEA
2710 2720 2730 2740 2750
PDSLRLKISA NSTRPARWHS KLGFFHDPRP FPLPLSSLFS DGGNVGCVDV
2760 2770 2780 2790 2800
IVQRVYPLQW VEKTVSGSYI FRNEREEEKE ALRFAEAQQK KLEALFTKVH
2810 2820 2830 2840 2850
TELKEHEEDI AQRRVLSRAL TRQQVHALQD GAELYAAVQD ASDPEHLETC
2860 2870 2880 2890 2900
FSEEQLRALN NYRQMLSDKK QARIQSEFRK ALEAAEKEEG LSRDVSTVWK
2910 2920 2930 2940 2950
LRVTSYKKRE KSALLSIWRP SSDLPSLLTE GQRYRIYHLS VSKSKNKFEW
2960 2970 2980 2990 3000
PSIQLTATKR TQYQQLPVSS ETLLQLYQPR ELLPFSKLSD PAFQPPCSEV
3010 3020 3030 3040 3050
DVVGVVVSVV KPIGLAPLVY LSDECLHLLV VKFGIDLNED IKPRVLIAAS
3060 3070 3080 3090 3100
NLQWRPESTS RVPTLFAGNF SVFSASPKEA HFQERVTNMK HAIENIDTFY
3110 3120 3130 3140 3150
KEAEKKLIQV LKGDSPKWST PNKDPTREPY PASTCSASDL ASGGQLPRSS
3160 3170 3180 3190 3200
PTDQQSYRSP LSCCTPTGKS TPLAHSAWMA AKSCSGENEI EDPKTCRKKR
3210 3220 3230 3240 3250
ALDLLSRLPL PPPLSPVCTF VSPAAQKAFQ PPRSCGTKYP TPLKKEGPSS
3260 3270 3280 3290 3300
PWSRAPFQKA SGVSLLDCDS VADEELALLS TQALVPHSVG GSEQVFPSDS
3310 3320 3330 3340
TRTEGPSAST EARPANRSKR ESLRDCRDDS DGKLAAETVP DYS
Length:3,343
Mass (Da):372,216
Last modified:January 1, 1998 - v1
Checksum:i653DB110D2302A8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89653 mRNA. Translation: AAB71378.1.
PIRiT42207.
UniGeneiRn.103225.

Genome annotation databases

UCSCiRGD:2219. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89653 mRNA. Translation: AAB71378.1.
PIRiT42207.
UniGeneiRn.103225.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IYJX-ray3.40B/D2335-3151[»]
ProteinModelPortaliO35923.
SMRiO35923.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001475.

Proteomic databases

PaxDbiO35923.
PRIDEiO35923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2219. rat.

Organism-specific databases

RGDi2219. Brca2.

Phylogenomic databases

eggNOGiKOG4751. Eukaryota.
ENOG410Y06W. LUCA.
HOGENOMiHOG000139693.
HOVERGENiHBG050731.
InParanoidiO35923.
PhylomeDBiO35923.

Miscellaneous databases

EvolutionaryTraceiO35923.
PROiO35923.

Family and domain databases

InterProiIPR015525. BRCA2.
IPR015252. BRCA2_hlx.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower_dom.
[Graphical view]
PANTHERiPTHR11289. PTHR11289. 2 hits.
PfamiPF09169. BRCA-2_helical. 1 hit.
PF09103. BRCA-2_OB1. 1 hit.
PF09104. BRCA-2_OB3. 1 hit.
PF00634. BRCA2. 7 hits.
PF09121. Tower. 1 hit.
[Graphical view]
PIRSFiPIRSF002397. BRCA2. 1 hit.
SMARTiSM01341. Tower. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 4 hits.
SSF81872. SSF81872. 1 hit.
PROSITEiPS50138. BRCA2_REPEAT. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBRCA2_RAT
AccessioniPrimary (citable) accession number: O35923
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 128 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.