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Q9P2N7

- KLH13_HUMAN

UniProt

Q9P2N7 - KLH13_HUMAN

Protein

Kelch-like protein 13

Gene

KLHL13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis.3 Publications

    Pathwayi

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. protein ubiquitination Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kelch-like protein 13
    Alternative name(s):
    BTB and kelch domain-containing protein 2
    Gene namesi
    Name:KLHL13
    Synonyms:BKLHD2, KIAA1309
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:22931. KLHL13.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul3-RING ubiquitin ligase complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134959204.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 655655Kelch-like protein 13PRO_0000119115Add
    BLAST

    Proteomic databases

    MaxQBiQ9P2N7.
    PaxDbiQ9P2N7.
    PRIDEiQ9P2N7.

    PTM databases

    PhosphoSiteiQ9P2N7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9P2N7.
    BgeeiQ9P2N7.
    CleanExiHS_KLHL13.
    GenevestigatoriQ9P2N7.

    Organism-specific databases

    HPAiHPA046039.

    Interactioni

    Subunit structurei

    Component of the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL9, KLHL13 and RBX1. Interacts with AURKB.2 Publications

    Protein-protein interaction databases

    BioGridi124688. 21 interactions.
    IntActiQ9P2N7. 13 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P2N7.
    SMRiQ9P2N7. Positions 69-634.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 16170BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini196 – 297102BACKAdd
    BLAST
    Repeati341 – 38949Kelch 1Add
    BLAST
    Repeati390 – 44152Kelch 2Add
    BLAST
    Repeati442 – 48847Kelch 3Add
    BLAST
    Repeati490 – 53546Kelch 4Add
    BLAST
    Repeati537 – 58751Kelch 5Add
    BLAST
    Repeati588 – 63649Kelch 6Add
    BLAST

    Sequence similaritiesi

    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 6 Kelch repeats.Curated

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG293088.
    HOVERGENiHBG106526.
    InParanoidiQ9P2N7.
    KOiK10447.
    OMAiGATRIFT.
    OrthoDBiEOG7VTDMJ.
    PhylomeDBiQ9P2N7.
    TreeFamiTF328485.

    Family and domain databases

    Gene3Di2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProiIPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 5 hits.
    [Graphical view]
    PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTiSM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P2N7-1) [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

    MPLKWKTSSP AIWKFPVPVL KTSRSTPLSP AYISLVEEED QHMKLSLGGS    50
    EMGLSSHLQS SKAGPTRIFT SNTHSSVVLQ GFDQLRLEGL LCDVTLMPGD 100
    TDDAFPVHRV MMASASDYFK AMFTGGMKEQ DLMCIKLHGV SKVGLRKIID 150
    FIYTAKLSLN MDNLQDTLEA ASFLQILPVL DFCKVFLISG VTLDNCVEVG 200
    RIANTYNLTE VDKYVNSFVL KNFPALLSTG EFLKLPFERL AFVLSSNSLK 250
    HCTELELFKA TCRWLRLEEP RMDFAAKLMK NIRFPLMTPQ ELINYVQTVD 300
    FMRTDNTCVN LLLEASNYQM MPYMQPVMQS DRTAIRSDTT HLVTLGGVLR 350
    QQLVVSKELR MYDEKAHEWK SLAPMDAPRY QHGIAVIGNF LYVVGGQSNY 400
    DTKGKTAVDT VFRFDPRYNK WMQVASLNEK RTFFHLSALK GYLYAVGGRN 450
    AAGELPTVEC YNPRTNEWTY VAKMSEPHYG HAGTVYGGVM YISGGITHDT 500
    FQKELMCFDP DTDKWIQKAP MTTVRGLHCM CTVGERLYVI GGNHFRGTSD 550
    YDDVLSCEYY SPILDQWTPI AAMLRGQSDV GVAVFENKIY VVGGYSWNNR 600
    CMVEIVQKYD PDKDEWHKVF DLPESLGGIR ACTLTVFPPE ETTPSPSRES 650
    PLSAP 655
    Length:655
    Mass (Da):73,868
    Last modified:June 16, 2009 - v3
    Checksum:i0916420562F0B093
    GO
    Isoform 2 (identifier: Q9P2N7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: Missing.

    Show »
    Length:613
    Mass (Da):69,090
    Checksum:iDBF234A9F50B1556
    GO
    Isoform 3 (identifier: Q9P2N7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYI → MDHLHRGELVAAILRNR

    Show »
    Length:639
    Mass (Da):72,141
    Checksum:i6EEA9A2DD4455933
    GO
    Isoform 4 (identifier: Q9P2N7-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYI → MLRFISHLYCCSSKEDCSEDDKCILSR

    Show »
    Length:649
    Mass (Da):73,322
    Checksum:i78A8F91FDDA79734
    GO
    Isoform 5 (identifier: Q9P2N7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: MPLKWKTSSPAIWKFPVPVLKTSRSTPLSPAYI → MMRVQTLREKWAYWRRRQLSLKQADFKDIFKKSTSG

    Show »
    Length:658
    Mass (Da):74,630
    Checksum:iF0CA2A42E52E6306
    GO

    Sequence cautioni

    The sequence BAA92547.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC41335.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141K → R in BAG54189. (PubMed:14702039)Curated
    Sequence conflicti20 – 201L → P in BAG54189. (PubMed:14702039)Curated
    Sequence conflicti352 – 3521Q → R in BAG54189. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti223 – 2231F → I Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064725
    Natural varianti261 – 2611T → S.1 Publication
    VAR_069423

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242Missing in isoform 2. 3 PublicationsVSP_037530Add
    BLAST
    Alternative sequencei1 – 3333MPLKW…SPAYI → MDHLHRGELVAAILRNR in isoform 3. 1 PublicationVSP_037531Add
    BLAST
    Alternative sequencei1 – 3333MPLKW…SPAYI → MLRFISHLYCCSSKEDCSED DKCILSR in isoform 4. 1 PublicationVSP_037532Add
    BLAST
    Alternative sequencei1 – 3333MPLKW…SPAYI → MMRVQTLREKWAYWRRRQLS LKQADFKDIFKKSTSG in isoform 5. 1 PublicationVSP_037533Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037730 mRNA. Translation: BAA92547.1. Different initiation.
    AL591986 mRNA. Translation: CAC41335.1. Different initiation.
    AK122724 mRNA. Translation: BAG53690.1.
    AK125356 mRNA. Translation: BAG54189.1.
    AK296324 mRNA. Translation: BAH12315.1.
    AK299257 mRNA. Translation: BAH12978.1.
    AK302713 mRNA. Translation: BAH13788.1.
    AC006968 Genomic DNA. No translation available.
    AC006963 Genomic DNA. Translation: AAF03529.1.
    CH471161 Genomic DNA. Translation: EAW89898.1.
    CH471161 Genomic DNA. Translation: EAW89900.1.
    BC064576 mRNA. Translation: AAH64576.2.
    CCDSiCCDS14571.1. [Q9P2N7-1]
    CCDS55479.1. [Q9P2N7-2]
    CCDS55480.1. [Q9P2N7-5]
    CCDS55481.1. [Q9P2N7-3]
    RefSeqiNP_001161771.1. NM_001168299.1. [Q9P2N7-5]
    NP_001161772.1. NM_001168300.1. [Q9P2N7-4]
    NP_001161773.1. NM_001168301.1. [Q9P2N7-3]
    NP_001161774.1. NM_001168302.1. [Q9P2N7-3]
    NP_001161775.1. NM_001168303.1. [Q9P2N7-2]
    NP_277030.2. NM_033495.3. [Q9P2N7-1]
    UniGeneiHs.348262.

    Genome annotation databases

    EnsembliENST00000262820; ENSP00000262820; ENSG00000003096. [Q9P2N7-1]
    ENST00000371876; ENSP00000360943; ENSG00000003096.
    ENST00000371878; ENSP00000360945; ENSG00000003096.
    ENST00000371882; ENSP00000360949; ENSG00000003096.
    ENST00000447671; ENSP00000412640; ENSG00000003096.
    ENST00000469946; ENSP00000419803; ENSG00000003096.
    ENST00000539496; ENSP00000443191; ENSG00000003096. [Q9P2N7-5]
    ENST00000540167; ENSP00000441029; ENSG00000003096. [Q9P2N7-3]
    ENST00000541812; ENSP00000444450; ENSG00000003096. [Q9P2N7-3]
    ENST00000545703; ENSP00000440707; ENSG00000003096. [Q9P2N7-2]
    GeneIDi90293.
    KEGGihsa:90293.
    UCSCiuc004eqk.3. human. [Q9P2N7-1]
    uc011mto.2. human. [Q9P2N7-4]
    uc011mtp.2. human. [Q9P2N7-5]
    uc011mtq.2. human. [Q9P2N7-3]

    Polymorphism databases

    DMDMi239938883.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037730 mRNA. Translation: BAA92547.1 . Different initiation.
    AL591986 mRNA. Translation: CAC41335.1 . Different initiation.
    AK122724 mRNA. Translation: BAG53690.1 .
    AK125356 mRNA. Translation: BAG54189.1 .
    AK296324 mRNA. Translation: BAH12315.1 .
    AK299257 mRNA. Translation: BAH12978.1 .
    AK302713 mRNA. Translation: BAH13788.1 .
    AC006968 Genomic DNA. No translation available.
    AC006963 Genomic DNA. Translation: AAF03529.1 .
    CH471161 Genomic DNA. Translation: EAW89898.1 .
    CH471161 Genomic DNA. Translation: EAW89900.1 .
    BC064576 mRNA. Translation: AAH64576.2 .
    CCDSi CCDS14571.1. [Q9P2N7-1 ]
    CCDS55479.1. [Q9P2N7-2 ]
    CCDS55480.1. [Q9P2N7-5 ]
    CCDS55481.1. [Q9P2N7-3 ]
    RefSeqi NP_001161771.1. NM_001168299.1. [Q9P2N7-5 ]
    NP_001161772.1. NM_001168300.1. [Q9P2N7-4 ]
    NP_001161773.1. NM_001168301.1. [Q9P2N7-3 ]
    NP_001161774.1. NM_001168302.1. [Q9P2N7-3 ]
    NP_001161775.1. NM_001168303.1. [Q9P2N7-2 ]
    NP_277030.2. NM_033495.3. [Q9P2N7-1 ]
    UniGenei Hs.348262.

    3D structure databases

    ProteinModelPortali Q9P2N7.
    SMRi Q9P2N7. Positions 69-634.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124688. 21 interactions.
    IntActi Q9P2N7. 13 interactions.

    PTM databases

    PhosphoSitei Q9P2N7.

    Polymorphism databases

    DMDMi 239938883.

    Proteomic databases

    MaxQBi Q9P2N7.
    PaxDbi Q9P2N7.
    PRIDEi Q9P2N7.

    Protocols and materials databases

    DNASUi 90293.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262820 ; ENSP00000262820 ; ENSG00000003096 . [Q9P2N7-1 ]
    ENST00000371876 ; ENSP00000360943 ; ENSG00000003096 .
    ENST00000371878 ; ENSP00000360945 ; ENSG00000003096 .
    ENST00000371882 ; ENSP00000360949 ; ENSG00000003096 .
    ENST00000447671 ; ENSP00000412640 ; ENSG00000003096 .
    ENST00000469946 ; ENSP00000419803 ; ENSG00000003096 .
    ENST00000539496 ; ENSP00000443191 ; ENSG00000003096 . [Q9P2N7-5 ]
    ENST00000540167 ; ENSP00000441029 ; ENSG00000003096 . [Q9P2N7-3 ]
    ENST00000541812 ; ENSP00000444450 ; ENSG00000003096 . [Q9P2N7-3 ]
    ENST00000545703 ; ENSP00000440707 ; ENSG00000003096 . [Q9P2N7-2 ]
    GeneIDi 90293.
    KEGGi hsa:90293.
    UCSCi uc004eqk.3. human. [Q9P2N7-1 ]
    uc011mto.2. human. [Q9P2N7-4 ]
    uc011mtp.2. human. [Q9P2N7-5 ]
    uc011mtq.2. human. [Q9P2N7-3 ]

    Organism-specific databases

    CTDi 90293.
    GeneCardsi GC0XM117031.
    H-InvDB HIX0056474.
    HGNCi HGNC:22931. KLHL13.
    HPAi HPA046039.
    MIMi 300655. gene.
    neXtProti NX_Q9P2N7.
    PharmGKBi PA134959204.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293088.
    HOVERGENi HBG106526.
    InParanoidi Q9P2N7.
    KOi K10447.
    OMAi GATRIFT.
    OrthoDBi EOG7VTDMJ.
    PhylomeDBi Q9P2N7.
    TreeFami TF328485.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi KLHL13. human.
    GenomeRNAii 90293.
    NextBioi 76640.
    PROi Q9P2N7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P2N7.
    Bgeei Q9P2N7.
    CleanExi HS_KLHL13.
    Genevestigatori Q9P2N7.

    Family and domain databases

    Gene3Di 2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProi IPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view ]
    Pfami PF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 5 hits.
    [Graphical view ]
    PIRSFi PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTi SM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 6 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. Howell G.R., Huckle E., Ross M.T.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. "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] (ISOFORMS 1; 2; 3; 4 AND 5).
      Tissue: Brain, Testis and Thalamus.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Brain.
    7. "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases."
      Furukawa M., He Y.J., Borchers C., Xiong Y.
      Nat. Cell Biol. 5:1001-1007(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH CUL3.
    8. "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells."
      Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.
      Dev. Cell 12:887-900(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AURKB; CUL3 AND KLHL9.
    9. "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis."
      Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M., Sumara I., Peter M.
      J. Cell Biol. 187:791-800(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: VARIANT ILE-223.
    11. Cited for: VARIANT SER-261.

    Entry informationi

    Entry nameiKLH13_HUMAN
    AccessioniPrimary (citable) accession number: Q9P2N7
    Secondary accession number(s): B3KV78
    , B3KWM7, B7Z3S9, B7Z5P2, B7Z802, D3DWH6, Q6P2E3, Q96QI7, Q9UDN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 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 X
      Human chromosome X: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3