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Q9UFC0

- LRWD1_HUMAN

UniProt

Q9UFC0 - LRWD1_HUMAN

Protein

Leucine-rich repeat and WD repeat-containing protein 1

Gene

LRWD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (25 Oct 2004)
      Previous versions | rss
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    Functioni

    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.5 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. methylated histone binding Source: UniProtKB
    3. methyl-CpG binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. chromatin organization Source: UniProtKB
    3. DNA replication initiation Source: UniProtKB
    4. establishment of protein localization to chromatin Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    DNA replication

    Enzyme and pathway databases

    SignaLinkiQ9UFC0.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:LRWD1
    Synonyms:CENP33, ORCA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21769. LRWD1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule organizing center Source: UniProtKB-SubCell
    3. nuclear origin of replication recognition complex Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. pericentric heterochromatin Source: UniProtKB
    6. telomeric heterochromatin Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162394694.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 647647Leucine-rich repeat and WD repeat-containing protein 1PRO_0000310994Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei212 – 2121Phosphoserine4 Publications
    Modified residuei243 – 2431Phosphoserine4 Publications
    Modified residuei251 – 2511Phosphoserine1 Publication
    Modified residuei259 – 2591Phosphoserine3 Publications

    Post-translational modificationi

    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.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UFC0.
    PaxDbiQ9UFC0.
    PeptideAtlasiQ9UFC0.
    PRIDEiQ9UFC0.

    PTM databases

    PhosphoSiteiQ9UFC0.

    Expressioni

    Tissue specificityi

    Testis-specific. Drastically down-regulated in testis from patients with Sertoli cell-only syndrome (SCOS).1 Publication

    Developmental stagei

    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 (PubMed:22935713).2 Publications

    Gene expression databases

    ArrayExpressiQ9UFC0.
    BgeeiQ9UFC0.
    CleanExiHS_LRWD1.
    GenevestigatoriQ9UFC0.

    Organism-specific databases

    HPAiHPA021320.
    HPA029916.

    Interactioni

    Subunit structurei

    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.5 Publications

    Protein-protein interaction databases

    BioGridi128790. 9 interactions.
    IntActiQ9UFC0. 5 interactions.
    MINTiMINT-7944578.
    STRINGi9606.ENSP00000292616.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UFC0.
    SMRiQ9UFC0. Positions 3-179, 377-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati22 – 4322LRR 1Add
    BLAST
    Repeati48 – 6922LRR 2Add
    BLAST
    Repeati70 – 9122LRR 3Add
    BLAST
    Repeati92 – 11322LRR 4Add
    BLAST
    Repeati390 – 43041WD 1Add
    BLAST
    Repeati441 – 48040WD 2Add
    BLAST
    Repeati495 – 53440WD 3Add
    BLAST
    Repeati551 – 59040WD 4Add
    BLAST
    Repeati615 – 64733WD 5Add
    BLAST

    Domaini

    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 H4K20me3.3 Publications

    Sequence similaritiesi

    Belongs to the LRWD1 family.Curated
    Contains 4 LRR (leucine-rich) repeats.Curated
    Contains 5 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Leucine-rich repeat, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiNOG304996.
    HOGENOMiHOG000113393.
    HOVERGENiHBG076949.
    InParanoidiQ9UFC0.
    OMAiLSEFTQW.
    OrthoDBiEOG7W9RT7.
    PhylomeDBiQ9UFC0.
    TreeFamiTF329554.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR001611. 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]
    PfamiPF13855. LRR_8. 1 hit.
    PF00400. WD40. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00320. WD40. 3 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS51450. LRR. 3 hits.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UFC0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPLSARLLM QRGRPKSDRL GKIRSLDLSG LELLSEHLDP KLLCRLTQLQ    50
    ELDLSNNHLE TLPDNLGLSH LRVLRCANNQ LGDVTALCQF PKLEELSLEG 100
    NPFLTVNDNL KVSFLLPTLR KVNGKDASST YSQVENLNRE LTSRVTAHWE 150
    KFMATLGPEE EAEKAQADFV KSAVRDVRYG PESLSEFTQW RVRMISEELV 200
    AASRTQVQKA NSPEKPPEAG AAHKPRARLA ALKRPDDVPL SLSPSKRACA 250
    SPSAQVEGSP VAGSDGSQPA VKLEPLHFLQ CHSKNNSPQD LETQLWACAF 300
    EPAWEEGATS QTVATCGGEA VCVIDCQTGI VLHKYKAPGE EFFSVAWTAL 350
    MVVTQAGHKK RWSVLAAAGL RGLVRLLHVR AGFCCGVIRA HKKAIATLCF 400
    SPAHETHLFT ASYDKRIILW DIGVPNQDYE FQASQLLTLD TTSIPLRLCP 450
    VASCPDARLL AGCEGGCCCW DVRLDQPQKR RVCEVEFVFS EGSEASGRRV 500
    DGLAFVNEDI VASKGSGLGT ICLWSWRQTW GGRGSQSTVA VVVLARLQWS 550
    STELAYFSLS ACPDKGIVLC GDEEGNVWLY DVSNILKQPP LLPAALQAPT 600
    QILKWPQPWA LGQVVTKTMV NTVVANASFT YLTALTDSNI VAIWGRM 647
    Length:647
    Mass (Da):70,861
    Last modified:October 25, 2004 - v2
    Checksum:i59C6ABF57A957D9F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti629 – 6291F → S in BAF83656. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS34715.1.
    PIRiT42659.
    RefSeqiNP_690852.1. NM_152892.1.
    UniGeneiHs.274135.

    Genome annotation databases

    EnsembliENST00000292616; ENSP00000292616; ENSG00000161036.
    GeneIDi222229.
    KEGGihsa:222229.
    UCSCiuc003uzn.3. human.

    Polymorphism databases

    DMDMi74761931.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS34715.1.
    PIRi T42659.
    RefSeqi NP_690852.1. NM_152892.1.
    UniGenei Hs.274135.

    3D structure databases

    ProteinModelPortali Q9UFC0.
    SMRi Q9UFC0. Positions 3-179, 377-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128790. 9 interactions.
    IntActi Q9UFC0. 5 interactions.
    MINTi MINT-7944578.
    STRINGi 9606.ENSP00000292616.

    PTM databases

    PhosphoSitei Q9UFC0.

    Polymorphism databases

    DMDMi 74761931.

    Proteomic databases

    MaxQBi Q9UFC0.
    PaxDbi Q9UFC0.
    PeptideAtlasi Q9UFC0.
    PRIDEi Q9UFC0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292616 ; ENSP00000292616 ; ENSG00000161036 .
    GeneIDi 222229.
    KEGGi hsa:222229.
    UCSCi uc003uzn.3. human.

    Organism-specific databases

    CTDi 222229.
    GeneCardsi GC07P102105.
    HGNCi HGNC:21769. LRWD1.
    HPAi HPA021320.
    HPA029916.
    MIMi 615167. gene.
    neXtProti NX_Q9UFC0.
    PharmGKBi PA162394694.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG304996.
    HOGENOMi HOG000113393.
    HOVERGENi HBG076949.
    InParanoidi Q9UFC0.
    OMAi LSEFTQW.
    OrthoDBi EOG7W9RT7.
    PhylomeDBi Q9UFC0.
    TreeFami TF329554.

    Enzyme and pathway databases

    SignaLinki Q9UFC0.

    Miscellaneous databases

    GenomeRNAii 222229.
    NextBioi 91575.
    PROi Q9UFC0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UFC0.
    Bgeei Q9UFC0.
    CleanExi HS_LRWD1.
    Genevestigatori Q9UFC0.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR001611. 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 ]
    Pfami PF13855. LRR_8. 1 hit.
    PF00400. WD40. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00320. WD40. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS51450. LRR. 3 hits.
    PS00678. WD_REPEATS_1. 1 hit.
    PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLRWD1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UFC0
    Secondary accession number(s): A8K4K2
    , B2R9G2, Q8N0T9, Q8WV43, Q96GJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3