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Q92600

- RCD1_HUMAN

UniProt

Q92600 - RCD1_HUMAN

Protein

Cell differentiation protein RCD1 homolog

Gene

RQCD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. May play a role in cell differentiation By similarity. Can bind oligonucleotides, such as poly-G, poly-C or poly-T (in vitro), but the physiological relevance of this is not certain. Does not bind poly-A. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors, including RARA, expect ESR1-mediated transcription that is not only slightly increased, if at all.By similarity2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Ensembl
    2. gene expression Source: Reactome
    3. gene silencing by RNA Source: UniProtKB-KW
    4. mRNA metabolic process Source: Reactome
    5. negative regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
    6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    7. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    8. positive regulation of ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    9. regulation of transcription, DNA-templated Source: UniProtKB-KW
    10. regulation of translation Source: UniProtKB-KW
    11. RNA metabolic process Source: Reactome
    12. sex differentiation Source: ProtInc
    13. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

    Enzyme and pathway databases

    ReactomeiREACT_20514. Deadenylation of mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cell differentiation protein RCD1 homolog
    Short name:
    Rcd-1
    Alternative name(s):
    CCR4-NOT transcription complex subunit 9
    Gene namesi
    Name:RQCD1
    Synonyms:CNOT9, RCD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10445. RQCD1.

    Subcellular locationi

    Nucleus By similarity. CytoplasmP-body By similarity
    Note: NANOS2 promotes its localization to P-body.By similarity

    GO - Cellular componenti

    1. CCR4-NOT complex Source: UniProtKB
    2. cytoplasmic mRNA processing body Source: UniProtKB
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi227 – 2271R → E: Loss of DNA binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA34859.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299Cell differentiation protein RCD1 homologPRO_0000327224Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ92600.
    PaxDbiQ92600.
    PRIDEiQ92600.

    PTM databases

    PhosphoSiteiQ92600.

    Expressioni

    Tissue specificityi

    Detected in spleen, thymus, prostate, testis, ovary and intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ92600.
    BgeeiQ92600.
    CleanExiHS_RQCD1.
    GenevestigatoriQ92600.

    Organism-specific databases

    HPAiHPA046622.

    Interactioni

    Subunit structurei

    Homodimer. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. Interacts with MYB, ATF2, RARA, RARB, RARG, RXRA, RXRB and RXRG. Identified in a complex with ATF2 bound to target DNA By similarity. Interacts with NANOS2 By similarity. Directly interacts with ZNF335.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi114573. 18 interactions.
    DIPiDIP-46840N.
    IntActiQ92600. 7 interactions.
    MINTiMINT-1162783.
    STRINGi9606.ENSP00000273064.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 279
    Beta strandi29 – 313
    Helixi32 – 4312
    Turni44 – 485
    Helixi52 – 587
    Beta strandi59 – 613
    Helixi62 – 7110
    Helixi72 – 765
    Turni77 – 804
    Helixi84 – 10219
    Turni104 – 1063
    Helixi107 – 1126
    Helixi115 – 1184
    Helixi120 – 1234
    Helixi130 – 14718
    Helixi152 – 1609
    Helixi164 – 17310
    Helixi176 – 19116
    Helixi193 – 1997
    Helixi203 – 22220
    Helixi226 – 23914
    Helixi243 – 25210
    Helixi255 – 2573
    Turni261 – 2688
    Helixi270 – 28415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FV2X-ray2.20A/B/C/D18-285[»]
    4CRUX-ray1.65B19-285[»]
    4CRVX-ray2.05B19-285[»]
    4CT6X-ray2.10B18-285[»]
    4CT7X-ray1.90B16-285[»]
    ProteinModelPortaliQ92600.
    SMRiQ92600. Positions 18-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92600.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RCD1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5209.
    HOGENOMiHOG000192069.
    HOVERGENiHBG056785.
    InParanoidiQ92600.
    KOiK12606.
    OrthoDBiEOG7M98GN.
    PhylomeDBiQ92600.
    TreeFamiTF105734.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR007216. Rcd1.
    [Graphical view]
    PANTHERiPTHR12262. PTHR12262. 1 hit.
    PfamiPF04078. Rcd1. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92600-1) [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

    MHSLATAAPV PTTLAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP    50
    DLAPMLWHSF GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV 100
    ASHPETRSAF LAAHIPLFLY PFLHTVSKTR PFEYLRLTSL GVIGALVKTD 150
    EQEVINFLLT TEIIPLCLRI MESGSELSKT VATFILQKIL LDDTGLAYIC 200
    QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS DNPRAREALR 250
    QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ 299
    Length:299
    Mass (Da):33,631
    Last modified:February 1, 1997 - v1
    Checksum:iCFA0E108F5E9D8F2
    GO
    Isoform 2 (identifier: Q92600-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-143: I → IVETGFHHVGQADLELPTSSDLPASASQSAGIT

    Note: No experimental confirmation available.

    Show »
    Length:331
    Mass (Da):36,837
    Checksum:iAD81339464CE9A5C
    GO
    Isoform 3 (identifier: Q92600-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         245-258: AREALRQCLPDQLK → FSDLTFCWSSFQRK
         259-299: Missing.

    Show »
    Length:258
    Mass (Da):29,140
    Checksum:iAA7F7A655A9AFD3E
    GO

    Sequence cautioni

    The sequence AAH07102.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti143 – 1431I → T.1 Publication
    Corresponds to variant rs17856204 [ dbSNP | Ensembl ].
    VAR_042429

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei143 – 1431I → IVETGFHHVGQADLELPTSS DLPASASQSAGIT in isoform 2. 1 PublicationVSP_054371
    Alternative sequencei245 – 25814AREAL…PDQLK → FSDLTFCWSSFQRK in isoform 3. 1 PublicationVSP_055744Add
    BLAST
    Alternative sequencei259 – 29941Missing in isoform 3. 1 PublicationVSP_055745Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87957 Genomic DNA. Translation: BAA13508.1.
    AK293281 mRNA. Translation: BAH11481.1.
    AC012510 Genomic DNA. No translation available.
    CH471063 Genomic DNA. Translation: EAW70625.1.
    CH471063 Genomic DNA. Translation: EAW70624.1.
    BC007102 mRNA. Translation: AAH07102.2. Different initiation.
    BC137455 mRNA. Translation: AAI37456.1.
    BC137456 mRNA. Translation: AAI37457.1.
    CCDSiCCDS33379.1. [Q92600-1]
    CCDS63122.1. [Q92600-2]
    RefSeqiNP_001258563.1. NM_001271634.1. [Q92600-2]
    NP_001258564.1. NM_001271635.1.
    NP_005435.1. NM_005444.2. [Q92600-1]
    UniGeneiHs.148767.

    Genome annotation databases

    EnsembliENST00000273064; ENSP00000273064; ENSG00000144580. [Q92600-1]
    ENST00000295701; ENSP00000295701; ENSG00000144580. [Q92600-3]
    ENST00000542068; ENSP00000443687; ENSG00000144580. [Q92600-1]
    GeneIDi9125.
    KEGGihsa:9125.
    UCSCiuc010zkh.3. human. [Q92600-1]

    Polymorphism databases

    DMDMi74716599.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87957 Genomic DNA. Translation: BAA13508.1 .
    AK293281 mRNA. Translation: BAH11481.1 .
    AC012510 Genomic DNA. No translation available.
    CH471063 Genomic DNA. Translation: EAW70625.1 .
    CH471063 Genomic DNA. Translation: EAW70624.1 .
    BC007102 mRNA. Translation: AAH07102.2 . Different initiation.
    BC137455 mRNA. Translation: AAI37456.1 .
    BC137456 mRNA. Translation: AAI37457.1 .
    CCDSi CCDS33379.1. [Q92600-1 ]
    CCDS63122.1. [Q92600-2 ]
    RefSeqi NP_001258563.1. NM_001271634.1. [Q92600-2 ]
    NP_001258564.1. NM_001271635.1.
    NP_005435.1. NM_005444.2. [Q92600-1 ]
    UniGenei Hs.148767.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FV2 X-ray 2.20 A/B/C/D 18-285 [» ]
    4CRU X-ray 1.65 B 19-285 [» ]
    4CRV X-ray 2.05 B 19-285 [» ]
    4CT6 X-ray 2.10 B 18-285 [» ]
    4CT7 X-ray 1.90 B 16-285 [» ]
    ProteinModelPortali Q92600.
    SMRi Q92600. Positions 18-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114573. 18 interactions.
    DIPi DIP-46840N.
    IntActi Q92600. 7 interactions.
    MINTi MINT-1162783.
    STRINGi 9606.ENSP00000273064.

    PTM databases

    PhosphoSitei Q92600.

    Polymorphism databases

    DMDMi 74716599.

    Proteomic databases

    MaxQBi Q92600.
    PaxDbi Q92600.
    PRIDEi Q92600.

    Protocols and materials databases

    DNASUi 9125.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273064 ; ENSP00000273064 ; ENSG00000144580 . [Q92600-1 ]
    ENST00000295701 ; ENSP00000295701 ; ENSG00000144580 . [Q92600-3 ]
    ENST00000542068 ; ENSP00000443687 ; ENSG00000144580 . [Q92600-1 ]
    GeneIDi 9125.
    KEGGi hsa:9125.
    UCSCi uc010zkh.3. human. [Q92600-1 ]

    Organism-specific databases

    CTDi 9125.
    GeneCardsi GC02P219433.
    HGNCi HGNC:10445. RQCD1.
    HPAi HPA046622.
    MIMi 612054. gene.
    neXtProti NX_Q92600.
    PharmGKBi PA34859.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5209.
    HOGENOMi HOG000192069.
    HOVERGENi HBG056785.
    InParanoidi Q92600.
    KOi K12606.
    OrthoDBi EOG7M98GN.
    PhylomeDBi Q92600.
    TreeFami TF105734.

    Enzyme and pathway databases

    Reactomei REACT_20514. Deadenylation of mRNA.

    Miscellaneous databases

    ChiTaRSi RQCD1. human.
    EvolutionaryTracei Q92600.
    GenomeRNAii 9125.
    NextBioi 34205.
    PROi Q92600.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92600.
    Bgeei Q92600.
    CleanExi HS_RQCD1.
    Genevestigatori Q92600.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR007216. Rcd1.
    [Graphical view ]
    PANTHERi PTHR12262. PTHR12262. 1 hit.
    Pfami PF04078. Rcd1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Novel factor highly conserved among eukaryotes controls sexual development in fission yeast."
      Okazaki N., Okazaki K., Watanabe Y., Kato-Hayashi M., Yamamoto M., Okayama H.
      Mol. Cell. Biol. 18:887-895(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Tissue: Foreskin.
    2. "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] (ISOFORM 2).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORMS 1 AND 3), VARIANT THR-143.
      Tissue: Brain.
    6. Bienvenut W.V., Lempens A., Norman J.C.
      Submitted (OCT-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-21; 36-44; 180-188 AND 275-292, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting Factor NIF-1."
      Garapaty S., Mahajan M.A., Samuels H.H.
      J. Biol. Chem. 283:6806-6816(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZNF335.
    8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex."
      Mauxion F., Preve B., Seraphin B.
      RNA Biol. 10:267-276(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CCR4-NOT COMPLEX.
    11. "Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties."
      Garces R.G., Gillon W., Pai E.F.
      Protein Sci. 16:176-188(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-285, DOMAIN, SUBUNIT, FUNCTION, MUTAGENESIS OF ARG-227.

    Entry informationi

    Entry nameiRCD1_HUMAN
    AccessioniPrimary (citable) accession number: Q92600
    Secondary accession number(s): B2RPI0
    , B5MDQ4, B7Z1E5, Q96IX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 119 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3