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Q5TZA2

- CROCC_HUMAN

UniProt

Q5TZA2 - CROCC_HUMAN

Protein

Rootletin

Gene

CROCC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Major structural component of the ciliary rootlet, a cytoskeletal-like structure in ciliated cells which originates from the basal body at the proximal end of a cilium and extends proximally toward the cell nucleus. Contributes to centrosome cohesion before mitosis.By similarity1 Publication

    GO - Molecular functioni

    1. kinesin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell projection organization Source: UniProtKB-KW
    3. centriole-centriole cohesion Source: UniProtKB
    4. centrosome organization Source: UniProtKB
    5. protein localization Source: UniProtKB
    6. protein localization to organelle Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cilium biogenesis/degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rootletin
    Alternative name(s):
    Ciliary rootlet coiled-coil protein
    Gene namesi
    Name:CROCCImported
    Synonyms:KIAA0445Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:21299. CROCC.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 1 Publication
    Note: In ciliated cells, associated with ciliary rootlets. In non-ciliated cells, localized between, around and at the proximal ends of the centrioles. Dissociates from the centrioles at the onset of mitosis and reassociates with them at anaphase.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. centriole Source: UniProtKB
    3. centrosome Source: UniProtKB
    4. ciliary rootlet Source: UniProtKB
    5. cytoplasm Source: HPA
    6. extracellular vesicular exosome Source: UniProt
    7. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134911945.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20172017RootletinPRO_0000239943Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1460 – 14601Phosphoserine2 Publications
    Modified residuei1660 – 16601Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by NEK2 which may regulate its association with centrosomes.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5TZA2.
    PaxDbiQ5TZA2.
    PRIDEiQ5TZA2.

    PTM databases

    PhosphoSiteiQ5TZA2.

    Expressioni

    Gene expression databases

    BgeeiQ5TZA2.
    CleanExiHS_CROCC.
    GenevestigatoriQ5TZA2.

    Organism-specific databases

    HPAiHPA021191.
    HPA021762.

    Interactioni

    Subunit structurei

    Homopolymer. Interacts with KLC3, NEK2 and the N-terminus of CEP250.1 Publication

    Protein-protein interaction databases

    BioGridi115048. 5 interactions.
    IntActiQ5TZA2. 4 interactions.
    MINTiMINT-2807877.
    STRINGi9606.ENSP00000364691.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5TZA2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili70 – 262193Sequence AnalysisAdd
    BLAST
    Coiled coili318 – 444127Sequence AnalysisAdd
    BLAST
    Coiled coili546 – 1058513Sequence AnalysisAdd
    BLAST
    Coiled coili1091 – 1438348Sequence AnalysisAdd
    BLAST
    Coiled coili1505 – 1704200Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1921 – 199979Gln-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the rootletin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000231187.
    HOVERGENiHBG080162.
    InParanoidiQ5TZA2.
    KOiK16469.
    OMAiYKKRCSE.
    OrthoDBiEOG7W6WJX.
    PhylomeDBiQ5TZA2.
    TreeFamiTF101138.

    Family and domain databases

    InterProiIPR026733. Rootletin.
    [Graphical view]
    PANTHERiPTHR23159:SF11. PTHR23159:SF11. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q5TZA2-1) [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

    MSLGLARAQE VELTLETVIQ TLESSVLCQE KGLGARDLAQ DAQITSLPAL     50
    IREIVTRNLS QPESPVLLPA TEMASLLSLQ EENQLLQQEL SRVEDLLAQS 100
    RAERDELAIK YNAVSERLEQ ALRLEPGELE TQEPRGLVRQ SVELRRQLQE 150
    EQASYRRKLQ AYQEGQQRQA QLVQRLQGKI LQYKKRCSEL EQQLLERSGE 200
    LEQQRLRDTE HSQDLESALI RLEEEQQRSA SLAQVNAMLR EQLDQAGSAN 250
    QALSEDIRKV TNDWTRCRKE LEHREAAWRR EEESFNAYFS NEHSRLLLLW 300
    RQVVGFRRLV SEVKMFTERD LLQLGGELAR TSRAVQEAGL GLSTGLRLAE 350
    SRAEAALEKQ ALLQAQLEEQ LRDKVLREKD LAQQQMQSDL DKADLSARVT 400
    ELGLAVKRLE KQNLEKDQVN KDLTEKLEAL ESLRLQEQAA LETEDGEGLQ 450
    QTLRDLAQAV LSDSESGVQL SGSERTADAS NGSLRGLSGQ RTPSPPRRSS 500
    PGRGRSPRRG PSPACSDSST LALIHSALHK RQLQVQDMRG RYEASQDLLG 550
    TLRKQLSDSE SERRALEEQL QRLRDKTDGA MQAHEDAQRE VQRLRSANEL 600
    LSREKSNLAH SLQVAQQQAE ELRQEREKLQ AAQEELRRQR DRLEEEQEDA 650
    VQDGARVRRE LERSHRQLEQ LEGKRSVLAK ELVEVREALS RATLQRDMLQ 700
    AEKAEVAEAL TKAEAGRVEL ELSMTKLRAE EASLQDSLSK LSALNESLAQ 750
    DKLDLNRLVA QLEEEKSALQ GRQRQAEQEA TVAREEQERL EELRLEQEVA 800
    RQGLEGSLRV AEQAQEALEQ QLPTLRHERS QLQEQLAQLS RQLSGREQEL 850
    EQARREAQRQ VEALERAARE KEALAKEHAG LAVQLVAAER EGRTLSEEAT 900
    RLRLEKEALE GSLFEVQRQL AQLEARREQL EAEGQALLLA KETLTGELAG 950
    LRQQIIATQE KASLDKELMA QKLVQAEREA QASLREQRAA HEEDLQRLQR 1000
    EKEAAWRELE AERAQLQSQL QREQEELLAR LEAEKEELSE EIAALQQERD 1050
    EGLLLAESEK QQALSLKESE KTALSEKLMG TRHSLATISL EMERQKRDAQ 1100
    SRQEQDRSTV NALTSELRDL RAQREEAAAA HAQEVRRLQE QARDLGKQRD 1150
    SCLREAEELR TQLRLLEDAR DGLRRELLEA QRKLRESQEG REVQRQEAGE 1200
    LRRSLGEGAK EREALRRSNE ELRSAVKKAE SERISLKLAN EDKEQKLALL 1250
    EEARTAVGKE AGELRTGLQE VERSRLEARR ELQELRRQMK MLDSENTRLG 1300
    RELAELQGRL ALGERAEKES RRETLGLRQR LLKGEASLEV MRQELQVAQR 1350
    KLQEQEGEFR TRERRLLGSL EEARGTEKQQ LDHARGLELK LEAARAEAAE 1400
    LGLRLSAAEG RAQGLEAELA RVEVQRRAAE AQLGGLRSAL RRGLGLGRAP 1450
    SPAPRPVPGS PARDAPAEGS GEGLNSPSTL ECSPGSQPPS PGPATSPASP 1500
    DLDPEAVRGA LREFLQELRS AQRERDELRT QTSALNRQLA EMEAERDSAT 1550
    SRARQLQKAV AESEEARRSV DGRLSGVQAE LALQEESVRR SERERRATLD 1600
    QVATLERSLQ ATESELRASQ EKISKMKANE TKLEGDKRRL KEVLDASESR 1650
    TVKLELQRRS LEGELQRSRL GLSDREAQAQ ALQDRVDSLQ RQVADSEVKA 1700
    GTLQLTVERL NGALAKVEES EGALRDKVRG LTEALAQSSA SLNSTRDKNL 1750
    HLQKALTACE HDRQVLQERL DAARQALSEA RKQSSSLGEQ VQTLRGEVAD 1800
    LELQRVEAEG QLQQLREVLR QRQEGEAAAL NTVQKLQDER RLLQERLGSL 1850
    QRALAQLEAE KREVERSALR LEKDRVALRR TLDKVEREKL RSHEDTVRLS 1900
    AEKGRLDRTL TGAELELAEA QRQIQQLEAQ VVVLEQSHSP AQLEVDAQQQ 1950
    QLELQQEVER LRSAQAQTER TLEARERAHR QRVRGLEEQV STLKGQLQQE 2000
    LRRSSAPFSP PSGPPEK 2017
    Length:2,017
    Mass (Da):228,523
    Last modified:December 7, 2004 - v1
    Checksum:i9711AC13AD9D7C07
    GO
    Isoform 21 Publication (identifier: Q5TZA2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-697: Missing.
         1984-1990: Missing.

    Show »
    Length:1,313
    Mass (Da):148,256
    Checksum:i00DC42FDE419EED1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71R → G.
    Corresponds to variant rs6586566 [ dbSNP | Ensembl ].
    VAR_061626
    Natural varianti372 – 3721R → Q.
    Corresponds to variant rs57442576 [ dbSNP | Ensembl ].
    VAR_061627
    Natural varianti439 – 4391A → V.
    Corresponds to variant rs4463721 [ dbSNP | Ensembl ].
    VAR_059628
    Natural varianti586 – 5861D → H.
    Corresponds to variant rs9435714 [ dbSNP | Ensembl ].
    VAR_059629
    Natural varianti1097 – 10971R → P.
    Corresponds to variant rs6669627 [ dbSNP | Ensembl ].
    VAR_059630

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 697697Missing in isoform 2. 2 PublicationsVSP_052069Add
    BLAST
    Alternative sequencei1984 – 19907Missing in isoform 2. 2 PublicationsVSP_052070

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ139275 mRNA. Translation: ABA43896.1.
    BX284668, AL049569 Genomic DNA. Translation: CAH70055.1.
    AL049569, BX284668 Genomic DNA. Translation: CAI20363.1.
    AB007914 mRNA. Translation: BAA32290.2.
    AF527734 mRNA. Translation: AAP85633.1.
    BK005505 mRNA. Translation: DAA05505.1.
    CCDSiCCDS30616.1. [Q5TZA2-1]
    RefSeqiNP_055490.4. NM_014675.4.
    UniGeneiHs.309403.

    Genome annotation databases

    EnsembliENST00000375541; ENSP00000364691; ENSG00000058453. [Q5TZA2-1]
    GeneIDi9696.
    KEGGihsa:9696.
    UCSCiuc001azt.2. human. [Q5TZA2-1]
    uc001azu.2. human. [Q5TZA2-2]

    Polymorphism databases

    DMDMi74746681.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ139275 mRNA. Translation: ABA43896.1 .
    BX284668 , AL049569 Genomic DNA. Translation: CAH70055.1 .
    AL049569 , BX284668 Genomic DNA. Translation: CAI20363.1 .
    AB007914 mRNA. Translation: BAA32290.2 .
    AF527734 mRNA. Translation: AAP85633.1 .
    BK005505 mRNA. Translation: DAA05505.1 .
    CCDSi CCDS30616.1. [Q5TZA2-1 ]
    RefSeqi NP_055490.4. NM_014675.4.
    UniGenei Hs.309403.

    3D structure databases

    ProteinModelPortali Q5TZA2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115048. 5 interactions.
    IntActi Q5TZA2. 4 interactions.
    MINTi MINT-2807877.
    STRINGi 9606.ENSP00000364691.

    PTM databases

    PhosphoSitei Q5TZA2.

    Polymorphism databases

    DMDMi 74746681.

    Proteomic databases

    MaxQBi Q5TZA2.
    PaxDbi Q5TZA2.
    PRIDEi Q5TZA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375541 ; ENSP00000364691 ; ENSG00000058453 . [Q5TZA2-1 ]
    GeneIDi 9696.
    KEGGi hsa:9696.
    UCSCi uc001azt.2. human. [Q5TZA2-1 ]
    uc001azu.2. human. [Q5TZA2-2 ]

    Organism-specific databases

    GeneCardsi GC01P017093.
    H-InvDB HIX0000171.
    HIX0000176.
    HGNCi HGNC:21299. CROCC.
    HPAi HPA021191.
    HPA021762.
    MIMi 615776. gene.
    neXtProti NX_Q5TZA2.
    PharmGKBi PA134911945.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000231187.
    HOVERGENi HBG080162.
    InParanoidi Q5TZA2.
    KOi K16469.
    OMAi YKKRCSE.
    OrthoDBi EOG7W6WJX.
    PhylomeDBi Q5TZA2.
    TreeFami TF101138.

    Miscellaneous databases

    ChiTaRSi CROCC. human.
    GeneWikii Rootletin.
    GenomeRNAii 9696.
    NextBioi 36431.
    PROi Q5TZA2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5TZA2.
    CleanExi HS_CROCC.
    Genevestigatori Q5TZA2.

    Family and domain databases

    InterProi IPR026733. Rootletin.
    [Graphical view ]
    PANTHERi PTHR23159:SF11. PTHR23159:SF11. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A centrosomal target of human T-cell leukemia virus type 1 oncoprotein Tax."
      Ching Y.-P., Chan S.-F., Jeang K.-T., Jin D.-Y.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-2017 (ISOFORM 1).
      Tissue: BrainImported.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1572-2017 (ISOFORM 2).
      Tissue: MedulloblastomaImported.
    5. "Proteomic characterization of the human centrosome by protein correlation profiling."
      Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
      Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Lymphoblast.
    6. "Rootletin forms centriole-associated filaments and functions in centrosome cohesion."
      Bahe S., Stierhof Y.-D., Wilkinson C.J., Leiss F., Nigg E.A.
      J. Cell Biol. 171:27-33(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CEP250 AND NEK2, PHOSPHORYLATION.
    7. "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-1460 AND SER-1660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCROCC_HUMAN
    AccessioniPrimary (citable) accession number: Q5TZA2
    Secondary accession number(s): Q2VHY3
    , Q66GT7, Q7Z2L4, Q7Z5D7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 95 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3