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Q9P2N7

- KLH13_HUMAN

UniProt

Q9P2N7 - KLH13_HUMAN

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Protein
Kelch-like protein 13
Gene
KLHL13, BKLHD2, KIAA1309
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134959204.

PTM / Processingi

Molecule processing

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 BTB (POZ) domain.
Contains 6 Kelch repeats.

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.

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.
VSP_037530Add
BLAST
Alternative sequencei1 – 3333MPLKW…SPAYI → MDHLHRGELVAAILRNR in isoform 3.
VSP_037531Add
BLAST
Alternative sequencei1 – 3333MPLKW…SPAYI → MLRFISHLYCCSSKEDCSED DKCILSR in isoform 4.
VSP_037532Add
BLAST
Alternative sequencei1 – 3333MPLKW…SPAYI → MMRVQTLREKWAYWRRRQLS LKQADFKDIFKKSTSG in isoform 5.
VSP_037533Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141K → R in BAG54189. 1 Publication
Sequence conflicti20 – 201L → P in BAG54189. 1 Publication
Sequence conflicti352 – 3521Q → R in BAG54189. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 114 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

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