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Q9UFC0

- LRWD1_HUMAN

UniProt

Q9UFC0 - LRWD1_HUMAN

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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

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

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
Complete GO annotation...

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. cytoskeleton Source: UniProtKB-KW
  3. nuclear origin of replication recognition complex Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. pericentric heterochromatin Source: UniProtKB
  6. telomeric heterochromatin Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9UFC0.
CleanExiHS_LRWD1.
ExpressionAtlasiQ9UFC0. baseline and differential.
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. 15 interactions.
IntActiQ9UFC0. 5 interactions.
MINTiMINT-7944578.
STRINGi9606.ENSP00000292616.

Structurei

3D structure databases

ProteinModelPortaliQ9UFC0.
SMRiQ9UFC0. Positions 3-101, 449-474, 499-526.
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.
GeneTreeiENSGT00390000008446.
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

        10         20         30         40         50
MGPLSARLLM QRGRPKSDRL GKIRSLDLSG LELLSEHLDP KLLCRLTQLQ
60 70 80 90 100
ELDLSNNHLE TLPDNLGLSH LRVLRCANNQ LGDVTALCQF PKLEELSLEG
110 120 130 140 150
NPFLTVNDNL KVSFLLPTLR KVNGKDASST YSQVENLNRE LTSRVTAHWE
160 170 180 190 200
KFMATLGPEE EAEKAQADFV KSAVRDVRYG PESLSEFTQW RVRMISEELV
210 220 230 240 250
AASRTQVQKA NSPEKPPEAG AAHKPRARLA ALKRPDDVPL SLSPSKRACA
260 270 280 290 300
SPSAQVEGSP VAGSDGSQPA VKLEPLHFLQ CHSKNNSPQD LETQLWACAF
310 320 330 340 350
EPAWEEGATS QTVATCGGEA VCVIDCQTGI VLHKYKAPGE EFFSVAWTAL
360 370 380 390 400
MVVTQAGHKK RWSVLAAAGL RGLVRLLHVR AGFCCGVIRA HKKAIATLCF
410 420 430 440 450
SPAHETHLFT ASYDKRIILW DIGVPNQDYE FQASQLLTLD TTSIPLRLCP
460 470 480 490 500
VASCPDARLL AGCEGGCCCW DVRLDQPQKR RVCEVEFVFS EGSEASGRRV
510 520 530 540 550
DGLAFVNEDI VASKGSGLGT ICLWSWRQTW GGRGSQSTVA VVVLARLQWS
560 570 580 590 600
STELAYFSLS ACPDKGIVLC GDEEGNVWLY DVSNILKQPP LLPAALQAPT
610 620 630 640
QILKWPQPWA LGQVVTKTMV NTVVANASFT YLTALTDSNI VAIWGRM
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 3-101, 449-474, 499-526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128790. 15 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.
GeneTreei ENSGT00390000008446.
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

Bgeei Q9UFC0.
CleanExi HS_LRWD1.
ExpressionAtlasi Q9UFC0. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 115 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