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Protein

F-box/WD repeat-containing protein 1A

Gene

BTRC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22'. SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (PubMed:25704143, PubMed:25503564). SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2. May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase. Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF. Required for proteolytic processing of GLI3.18 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Biological rhythms, Host-virus interaction, Ubl conjugation pathway, Wnt signaling pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000155347-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1170546. Prolactin receptor signaling.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-400253. Circadian Clock.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9Y297.
SIGNORiQ9Y297.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box/WD repeat-containing protein 1A
Alternative name(s):
E3RSIkappaB
Epididymis tissue protein Li 2a
F-box and WD repeats protein beta-TrCP
pIkappaBalpha-E3 receptor subunit
Gene namesi
Name:BTRC
Synonyms:BTRCP, FBW1A, FBXW1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1144. BTRC.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi8945.
MalaCardsiBTRC.
OpenTargetsiENSG00000166167.
Orphaneti2440. Split hand-split foot malformation.
PharmGKBiPA25465.

Polymorphism and mutation databases

BioMutaiBTRC.
DMDMi13124271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000509801 – 605F-box/WD repeat-containing protein 1AAdd BLAST605

Proteomic databases

EPDiQ9Y297.
PaxDbiQ9Y297.
PeptideAtlasiQ9Y297.
PRIDEiQ9Y297.

PTM databases

iPTMnetiQ9Y297.
PhosphoSitePlusiQ9Y297.

Expressioni

Tissue specificityi

Expressed in epididymis (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000166167.
CleanExiHS_BTRC.
ExpressionAtlasiQ9Y297. baseline and differential.
GenevisibleiQ9Y297. HS.

Organism-specific databases

HPAiCAB032986.
HPA031156.

Interactioni

Subunit structurei

Homodimer. Self-associates. Component of the SCF(BTRC) complex formed of CUL1, SKP1, RBX1 and a BTRC dimer. Direct interaction with SKP1 occurs via the F-box domain. Interacts with phosphorylated ubiquitination substrates SMAD3 and SMAD4. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, NFKBIB, NFKBIE, NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A, DLG1, FBXO5 and SNAI1; the interaction requires the phosphorylation of the 2 serine residues in the substrate destruction motif D-S-G-X(2,3,4)-S. Binds UBQLN1. Interacts with CDC34 and UBE2R2. Interacts with FBXW11. Interacts with CUL4A and DDB1. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with phosphorylated NKBIA and RELA; RELA interacts directly with NFKBIA. Interacts with HIV-1 Vpu. Interacts with the phosphorylated form of GLI3. Interacts with CLU. Interacts with PER1 (phosphorylated), PER2 (phosphorylated) and PER3. Interacts with phosphorylated ubiquitination substrate CEP68 (PubMed:25704143, PubMed:25503564). Interacts with ZC3H12A; the interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (By similarity).By similarity25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMER1Q5JTC65EBI-307461,EBI-6169747
ATF4P188489EBI-307461,EBI-492498
ATF4Q96AQ33EBI-307461,EBI-740263
CTNNB1P352226EBI-307461,EBI-491549
CUL1Q136165EBI-307461,EBI-359390
DLG1Q129592EBI-307461,EBI-357481
Dlg1Q626963EBI-307461,EBI-389325From a different organism.
GLI2P100704EBI-307461,EBI-10821567
MAP2K1Q027503EBI-307461,EBI-492564
MDM2Q009879EBI-307461,EBI-389668
NEDD8Q158432EBI-307461,EBI-716247
NFE2Q166213EBI-307461,EBI-726369
RASSF5Q8WWW03EBI-307461,EBI-367390
SKP1P632086EBI-307461,EBI-307486
SNAI1O958632EBI-307461,EBI-1045459
TACC1O754103EBI-307461,EBI-624237
TRIM9Q9C0264EBI-307461,EBI-720828
WEE1P302912EBI-307461,EBI-914695
ZC3H12AQ5D1E83EBI-307461,EBI-747793

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi114457. 378 interactors.
DIPiDIP-31607N.
IntActiQ9Y297. 72 interactors.
MINTiMINT-108636.
STRINGi9606.ENSP00000359206.

Structurei

Secondary structure

1605
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi129 – 141Combined sources13
Helixi146 – 158Combined sources13
Helixi162 – 172Combined sources11
Helixi173 – 175Combined sources3
Helixi180 – 183Combined sources4
Helixi185 – 187Combined sources3
Helixi190 – 197Combined sources8
Helixi202 – 211Combined sources10
Helixi213 – 221Combined sources9
Helixi224 – 233Combined sources10
Helixi237 – 244Combined sources8
Beta strandi245 – 247Combined sources3
Helixi248 – 251Combined sources4
Helixi266 – 285Combined sources20
Turni286 – 288Combined sources3
Beta strandi306 – 310Combined sources5
Beta strandi313 – 323Combined sources11
Beta strandi325 – 332Combined sources8
Beta strandi335 – 339Combined sources5
Beta strandi346 – 350Combined sources5
Beta strandi353 – 360Combined sources8
Beta strandi365 – 372Combined sources8
Beta strandi375 – 379Combined sources5
Beta strandi386 – 390Combined sources5
Beta strandi395 – 400Combined sources6
Beta strandi405 – 409Combined sources5
Beta strandi411 – 414Combined sources4
Beta strandi417 – 422Combined sources6
Beta strandi429 – 435Combined sources7
Beta strandi438 – 443Combined sources6
Beta strandi446 – 452Combined sources7
Turni453 – 455Combined sources3
Beta strandi458 – 463Combined sources6
Beta strandi469 – 475Combined sources7
Beta strandi478 – 483Combined sources6
Beta strandi488 – 492Combined sources5
Turni493 – 495Combined sources3
Beta strandi498 – 502Combined sources5
Beta strandi509 – 513Combined sources5
Beta strandi516 – 523Combined sources8
Beta strandi528 – 532Combined sources5
Helixi533 – 536Combined sources4
Turni543 – 546Combined sources4
Beta strandi547 – 551Combined sources5
Beta strandi561 – 563Combined sources3
Beta strandi568 – 570Combined sources3
Beta strandi573 – 580Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P22X-ray2.95A175-605[»]
2P64X-ray2.50A/B128-177[»]
ProteinModelPortaliQ9Y297.
SMRiQ9Y297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y297.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini190 – 228F-boxPROSITE-ProRule annotationAdd BLAST39
Repeati301 – 338WD 1Add BLAST38
Repeati341 – 378WD 2Add BLAST38
Repeati381 – 418WD 3Add BLAST38
Repeati424 – 461WD 4Add BLAST38
Repeati464 – 503WD 5Add BLAST40
Repeati505 – 541WD 6Add BLAST37
Repeati553 – 590WD 7Add BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni128 – 177Homodimerization domain DAdd BLAST50
Regioni190 – 228Required for down-regulation of SNAI1Add BLAST39

Domaini

The N-terminal D domain mediates homodimerization.1 Publication

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0281. Eukaryota.
ENOG410XTA8. LUCA.
GeneTreeiENSGT00760000119106.
HOGENOMiHOG000006638.
HOVERGENiHBG002521.
InParanoidiQ9Y297.
KOiK03362.
OMAiWIQYLFK.
OrthoDBiEOG091G0437.
PhylomeDBiQ9Y297.
TreeFamiTF105679.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR021977. Beta-TrCP_D.
IPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12125. Beta-TrCP_D. 1 hit.
PF12937. F-box-like. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM01028. Beta-TrCP_D. 1 hit.
SM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 6 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y297-1) [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
MDPAEAVLQE KALKFMCSMP RSLWLGCSSL ADSMPSLRCL YNPGTGALTA
60 70 80 90 100
FQNSSEREDC NNGEPPRKII PEKNSLRQTY NSCARLCLNQ ETVCLASTAM
110 120 130 140 150
KTENCVAKTK LANGTSSMIV PKQRKLSASY EKEKELCVKY FEQWSESDQV
160 170 180 190 200
EFVEHLISQM CHYQHGHINS YLKPMLQRDF ITALPARGLD HIAENILSYL
210 220 230 240 250
DAKSLCAAEL VCKEWYRVTS DGMLWKKLIE RMVRTDSLWR GLAERRGWGQ
260 270 280 290 300
YLFKNKPPDG NAPPNSFYRA LYPKIIQDIE TIESNWRCGR HSLQRIHCRS
310 320 330 340 350
ETSKGVYCLQ YDDQKIVSGL RDNTIKIWDK NTLECKRILT GHTGSVLCLQ
360 370 380 390 400
YDERVIITGS SDSTVRVWDV NTGEMLNTLI HHCEAVLHLR FNNGMMVTCS
410 420 430 440 450
KDRSIAVWDM ASPTDITLRR VLVGHRAAVN VVDFDDKYIV SASGDRTIKV
460 470 480 490 500
WNTSTCEFVR TLNGHKRGIA CLQYRDRLVV SGSSDNTIRL WDIECGACLR
510 520 530 540 550
VLEGHEELVR CIRFDNKRIV SGAYDGKIKV WDLVAALDPR APAGTLCLRT
560 570 580 590 600
LVEHSGRVFR LQFDEFQIVS SSHDDTILIW DFLNDPAAQA EPPRSPSRTY

TYISR
Length:605
Mass (Da):68,867
Last modified:November 1, 1999 - v1
Checksum:i4C67F3B7E400FD37
GO
Isoform 2 (identifier: Q9Y297-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     17-52: Missing.

Show »
Length:569
Mass (Da):65,049
Checksum:i6E7C4FBE7BB520BA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022027543A → S.Corresponds to variant rs4151060dbSNPEnsembl.1
Natural variantiVAR_020119592P → H.Corresponds to variant rs2270439dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00676417 – 52Missing in isoform 2. 2 PublicationsAdd BLAST36

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF101784 mRNA. Translation: AAD08702.1.
Y14153 mRNA. Translation: CAA74572.1.
AF129530 mRNA. Translation: AAF04464.1.
GU727631 mRNA. Translation: ADU87633.1.
AK313353 mRNA. Translation: BAG36155.1.
AL133387, AL445463, AL627424 Genomic DNA. Translation: CAH70019.1.
AL133387, AL445463, AL627424 Genomic DNA. Translation: CAH70020.1.
AL445463, AL133387, AL627424 Genomic DNA. Translation: CAI12963.1.
AL445463, AL133387, AL627424 Genomic DNA. Translation: CAI12964.1.
AL627424, AL133387, AL445463 Genomic DNA. Translation: CAI41042.1.
AL627424, AL133387, AL445463 Genomic DNA. Translation: CAI41043.1.
CH471066 Genomic DNA. Translation: EAW49772.1.
CH471066 Genomic DNA. Translation: EAW49774.1.
BC027994 mRNA. Translation: AAH27994.1.
CCDSiCCDS7511.1. [Q9Y297-2]
CCDS7512.1. [Q9Y297-1]
RefSeqiNP_003930.1. NM_003939.4. [Q9Y297-2]
NP_378663.1. NM_033637.3. [Q9Y297-1]
UniGeneiHs.643802.

Genome annotation databases

EnsembliENST00000370187; ENSP00000359206; ENSG00000166167. [Q9Y297-1]
ENST00000408038; ENSP00000385339; ENSG00000166167. [Q9Y297-2]
GeneIDi8945.
KEGGihsa:8945.
UCSCiuc001kta.5. human. [Q9Y297-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF101784 mRNA. Translation: AAD08702.1.
Y14153 mRNA. Translation: CAA74572.1.
AF129530 mRNA. Translation: AAF04464.1.
GU727631 mRNA. Translation: ADU87633.1.
AK313353 mRNA. Translation: BAG36155.1.
AL133387, AL445463, AL627424 Genomic DNA. Translation: CAH70019.1.
AL133387, AL445463, AL627424 Genomic DNA. Translation: CAH70020.1.
AL445463, AL133387, AL627424 Genomic DNA. Translation: CAI12963.1.
AL445463, AL133387, AL627424 Genomic DNA. Translation: CAI12964.1.
AL627424, AL133387, AL445463 Genomic DNA. Translation: CAI41042.1.
AL627424, AL133387, AL445463 Genomic DNA. Translation: CAI41043.1.
CH471066 Genomic DNA. Translation: EAW49772.1.
CH471066 Genomic DNA. Translation: EAW49774.1.
BC027994 mRNA. Translation: AAH27994.1.
CCDSiCCDS7511.1. [Q9Y297-2]
CCDS7512.1. [Q9Y297-1]
RefSeqiNP_003930.1. NM_003939.4. [Q9Y297-2]
NP_378663.1. NM_033637.3. [Q9Y297-1]
UniGeneiHs.643802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P22X-ray2.95A175-605[»]
2P64X-ray2.50A/B128-177[»]
ProteinModelPortaliQ9Y297.
SMRiQ9Y297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114457. 378 interactors.
DIPiDIP-31607N.
IntActiQ9Y297. 72 interactors.
MINTiMINT-108636.
STRINGi9606.ENSP00000359206.

PTM databases

iPTMnetiQ9Y297.
PhosphoSitePlusiQ9Y297.

Polymorphism and mutation databases

BioMutaiBTRC.
DMDMi13124271.

Proteomic databases

EPDiQ9Y297.
PaxDbiQ9Y297.
PeptideAtlasiQ9Y297.
PRIDEiQ9Y297.

Protocols and materials databases

DNASUi8945.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370187; ENSP00000359206; ENSG00000166167. [Q9Y297-1]
ENST00000408038; ENSP00000385339; ENSG00000166167. [Q9Y297-2]
GeneIDi8945.
KEGGihsa:8945.
UCSCiuc001kta.5. human. [Q9Y297-1]

Organism-specific databases

CTDi8945.
DisGeNETi8945.
GeneCardsiBTRC.
HGNCiHGNC:1144. BTRC.
HPAiCAB032986.
HPA031156.
MalaCardsiBTRC.
MIMi603482. gene.
neXtProtiNX_Q9Y297.
OpenTargetsiENSG00000166167.
Orphaneti2440. Split hand-split foot malformation.
PharmGKBiPA25465.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0281. Eukaryota.
ENOG410XTA8. LUCA.
GeneTreeiENSGT00760000119106.
HOGENOMiHOG000006638.
HOVERGENiHBG002521.
InParanoidiQ9Y297.
KOiK03362.
OMAiWIQYLFK.
OrthoDBiEOG091G0437.
PhylomeDBiQ9Y297.
TreeFamiTF105679.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000155347-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1170546. Prolactin receptor signaling.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-400253. Circadian Clock.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9Y297.
SIGNORiQ9Y297.

Miscellaneous databases

ChiTaRSiBTRC. human.
EvolutionaryTraceiQ9Y297.
GeneWikiiBTRC_(gene).
GenomeRNAii8945.
PROiQ9Y297.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166167.
CleanExiHS_BTRC.
ExpressionAtlasiQ9Y297. baseline and differential.
GenevisibleiQ9Y297. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR021977. Beta-TrCP_D.
IPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12125. Beta-TrCP_D. 1 hit.
PF12937. F-box-like. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM01028. Beta-TrCP_D. 1 hit.
SM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 6 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFBW1A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y297
Secondary accession number(s): B5MD49
, Q5W141, Q5W142, Q9Y213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 176 of the entry and version 1 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.