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Q9UFC0 (LRWD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat and WD repeat-containing protein 1
Alternative name(s):
Centromere protein 33
Short name=CENP-33
Origin recognition complex-associated protein
Short name=ORC-associated protein
Short name=ORCA
Gene names
Name:LRWD1
Synonyms:CENP33, ORCA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability. Ref.12 Ref.13 Ref.14 Ref.18 Ref.19

Subunit structure

Integral component of the ORC complex. Directly interacts with CDT1, GMNN and ORC2. Interacts with ORC2 only when non-ubiquitinated; this interaction prevents LRWD1 ubiquitination and degradation. Some of these interactions are regulated in a cell-cycle dependent manner. Interaction with ORC1 occurs predominantly during G1. Association with phosphorylated ORC1 during mitosis is not efficient. Interaction with CDT1 occurs during G1 phase, as well as during mitosis with phosphorylated CDT1. Interaction with GMNN occurs from G1/S to mitosis. Interaction with ORC2 is observed throughout the cell cycle. The stoichiometry of the ORCA/ORC/CDT1/GMNN complex is 1:1:1:2. Interacts with CUL4A and DDB1; this interaction may lead to ubiquitination. Ref.12 Ref.13 Ref.14 Ref.17 Ref.19

Subcellular location

Nucleus. Chromosomecentromere. Chromosometelomere. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Localizes to heterochromatin during G1 phase. Restricted to centromeres or telomeres as cells progress though S phase. When cells enter mitosis, relocalizes to centromeres. Recruitment to pericentric heterochromatin largely depends on the presence of H3K9me3. Ref.13 Ref.14 Ref.17 Ref.18

Tissue specificity

Testis-specific. Drastically down-regulated in testis from patients with Sertoli cell-only syndrome (SCOS). Ref.7

Developmental stage

Regulated in a cell-cycle dependent manner. Highest expression in G1 phase. Expression decreases during S phase, rises again during G2 and drops during mitosis (at protein level). In contrast to protein levels, transcript levels do not show any significant variation during different stages of the cell cycle (Ref.17). Ref.14 Ref.17

Domain

The entire WD repeat region is required for the interaction with ORC, CDT1 and GMNN, as well as for association with chromatin and for binding to histone H3 and H4 trimethylation marks H3K9me3 and H4K20me3. Ref.14 Ref.18 Ref.19

Post-translational modification

Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination leading to proteasomal degradation. Ubiquitination occurs within the WD repeats at the end of the G1 phase. Ubiquitination may be catalyzed by the CUL4-DDB1 E3 ubiquitin-protein ligase complex and other E3 ligases. Ref.17

Sequence similarities

Belongs to the LRWD1 family.

Contains 4 LRR (leucine-rich) repeats.

Contains 5 WD repeats.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
Telomere
   DomainLeucine-rich repeat
Repeat
WD repeat
   Molecular functionChromatin regulator
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication initiation

Traceable author statement Ref.14. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

establishment of protein localization to chromatin

Inferred from direct assay Ref.14. Source: UniProtKB

   Cellular_componentcentromeric heterochromatin

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear origin of replication recognition complex

Inferred from direct assay Ref.14Ref.13. Source: UniProtKB

nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

telomeric heterochromatin

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from direct assay Ref.14Ref.13. Source: UniProtKB

methyl-CpG binding

Inferred from direct assay Ref.13. Source: UniProtKB

methylated histone binding

Inferred from direct assay Ref.13. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 647647Leucine-rich repeat and WD repeat-containing protein 1
PRO_0000310994

Regions

Repeat22 – 4322LRR 1
Repeat48 – 6922LRR 2
Repeat70 – 9122LRR 3
Repeat92 – 11322LRR 4
Repeat390 – 43041WD 1
Repeat441 – 48040WD 2
Repeat495 – 53440WD 3
Repeat551 – 59040WD 4
Repeat615 – 64733WD 5

Amino acid modifications

Modified residue2121Phosphoserine Ref.6 Ref.11 Ref.15 Ref.16
Modified residue2431Phosphoserine Ref.9 Ref.11 Ref.15 Ref.16
Modified residue2511Phosphoserine Ref.9
Modified residue2591Phosphoserine Ref.8 Ref.9 Ref.11

Experimental info

Sequence conflict6291F → S in BAF83656. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UFC0 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: 59C6ABF57A957D9F

FASTA64770,861
        10         20         30         40         50         60 
MGPLSARLLM QRGRPKSDRL GKIRSLDLSG LELLSEHLDP KLLCRLTQLQ ELDLSNNHLE 

        70         80         90        100        110        120 
TLPDNLGLSH LRVLRCANNQ LGDVTALCQF PKLEELSLEG NPFLTVNDNL KVSFLLPTLR 

       130        140        150        160        170        180 
KVNGKDASST YSQVENLNRE LTSRVTAHWE KFMATLGPEE EAEKAQADFV KSAVRDVRYG 

       190        200        210        220        230        240 
PESLSEFTQW RVRMISEELV AASRTQVQKA NSPEKPPEAG AAHKPRARLA ALKRPDDVPL 

       250        260        270        280        290        300 
SLSPSKRACA SPSAQVEGSP VAGSDGSQPA VKLEPLHFLQ CHSKNNSPQD LETQLWACAF 

       310        320        330        340        350        360 
EPAWEEGATS QTVATCGGEA VCVIDCQTGI VLHKYKAPGE EFFSVAWTAL MVVTQAGHKK 

       370        380        390        400        410        420 
RWSVLAAAGL RGLVRLLHVR AGFCCGVIRA HKKAIATLCF SPAHETHLFT ASYDKRIILW 

       430        440        450        460        470        480 
DIGVPNQDYE FQASQLLTLD TTSIPLRLCP VASCPDARLL AGCEGGCCCW DVRLDQPQKR 

       490        500        510        520        530        540 
RVCEVEFVFS EGSEASGRRV DGLAFVNEDI VASKGSGLGT ICLWSWRQTW GGRGSQSTVA 

       550        560        570        580        590        600 
VVVLARLQWS STELAYFSLS ACPDKGIVLC GDEEGNVWLY DVSNILKQPP LLPAALQAPT 

       610        620        630        640 
QILKWPQPWA LGQVVTKTMV NTVVANASFT YLTALTDSNI VAIWGRM 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Testis.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain and Eye.
[6]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Identification of ten novel genes involved in human spermatogenesis by microarray analysis of testicular tissue."
Lin Y.H., Lin Y.M., Teng Y.N., Hsieh T.Y., Lin Y.S., Kuo P.L.
Fertil. Steril. 86:1650-1658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-243; SER-251 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-212; SER-243 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers."
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.
Cell 142:967-980(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE ORC COMPLEX, FUNCTION.
[13]"Nucleosome-interacting proteins regulated by DNA and histone methylation."
Bartke T., Vermeulen M., Xhemalce B., Robson S.C., Mann M., Kouzarides T.
Cell 143:470-484(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE ORC COMPLEX, FUNCTION.
[14]"A WD-repeat protein stabilizes ORC binding to chromatin."
Shen Z., Sathyan K.M., Geng Y., Zheng R., Chakraborty A., Freeman B., Wang F., Prasanth K.V., Prasanth S.G.
Mol. Cell 40:99-111(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN WD REPEATS, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ORC COMPLEX, DEVELOPMENTAL STAGE.
[15]"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-212 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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-212 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Orc2 protects ORCA from ubiquitin-mediated degradation."
Shen Z., Prasanth S.G.
Cell Cycle 11:3578-3589(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ORC2; CUL4A AND DDB1, SUBCELLULAR LOCATION, UBIQUITINATION, DEVELOPMENTAL STAGE.
[18]"Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing."
Chan K.M., Zhang Z.
J. Biol. Chem. 287:15024-15033(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BINDING TO HISTONE H3 AND H4 TRIMETHYLATION MARKS, SUBCELLULAR LOCATION, DOMAIN.
[19]"Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation."
Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V., Prasanth S.G.
Mol. Cell. Biol. 32:3107-3120(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDT1; GMNN; ORC1 AND ORC2, STOICHIOMETRY OF THE COMPLEX, DOMAIN.
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK290967 mRNA. Translation: BAF83656.1.
AK313771 mRNA. Translation: BAG36509.1.
AL133057 mRNA. Translation: CAB61382.2.
AC093668 Genomic DNA. No translation available.
CH471197 Genomic DNA. Translation: EAW50250.1.
BC009436 mRNA. Translation: AAH09436.1.
BC018769 mRNA. Translation: AAH18769.1.
BC030547 mRNA. Translation: AAH30547.1.
CCDSCCDS34715.1.
PIRT42659.
RefSeqNP_690852.1. NM_152892.1.
UniGeneHs.274135.

3D structure databases

ProteinModelPortalQ9UFC0.
SMRQ9UFC0. Positions 3-179, 377-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128790. 8 interactions.
IntActQ9UFC0. 3 interactions.
MINTMINT-7944578.
STRING9606.ENSP00000292616.

PTM databases

PhosphoSiteQ9UFC0.

Polymorphism databases

DMDM74761931.

Proteomic databases

MaxQBQ9UFC0.
PaxDbQ9UFC0.
PeptideAtlasQ9UFC0.
PRIDEQ9UFC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292616; ENSP00000292616; ENSG00000161036.
GeneID222229.
KEGGhsa:222229.
UCSCuc003uzn.3. human.

Organism-specific databases

CTD222229.
GeneCardsGC07P102105.
HGNCHGNC:21769. LRWD1.
HPAHPA021320.
HPA029916.
MIM615167. gene.
neXtProtNX_Q9UFC0.
PharmGKBPA162394694.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304996.
HOGENOMHOG000113393.
HOVERGENHBG076949.
InParanoidQ9UFC0.
OMALSEFTQW.
OrthoDBEOG7W9RT7.
PhylomeDBQ9UFC0.
TreeFamTF329554.

Enzyme and pathway databases

SignaLinkQ9UFC0.

Gene expression databases

ArrayExpressQ9UFC0.
BgeeQ9UFC0.
CleanExHS_LRWD1.
GenevestigatorQ9UFC0.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF13855. LRR_8. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
SM00320. WD40. 3 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS51450. LRR. 3 hits.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi222229.
NextBio91575.
PROQ9UFC0.
SOURCESearch...

Entry information

Entry nameLRWD1_HUMAN
AccessionPrimary (citable) accession number: Q9UFC0
Secondary accession number(s): A8K4K2 expand/collapse secondary AC list , B2R9G2, Q8N0T9, Q8WV43, Q96GJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 25, 2004
Last modified: July 9, 2014
This is version 112 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM