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Protein

Kelch-like protein 13

Gene

KLHL13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

  • cytokinesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • 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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:22931. KLHL13.

Subcellular locationi

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134959204.

Polymorphism and mutation databases

BioMutaiKLHL13.
DMDMi239938883.

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

BgeeiQ9P2N7.
CleanExiHS_KLHL13.
ExpressionAtlasiQ9P2N7. baseline and differential.
GenevisibleiQ9P2N7. HS.

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.
STRINGi9606.ENSP00000443191.

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.
GeneTreeiENSGT00760000118825.
HOVERGENiHBG106526.
InParanoidiQ9P2N7.
KOiK10447.
OMAiTEVDKYI.
OrthoDBiEOG7VTDMJ.
PhylomeDBiQ9P2N7.
TreeFamiTF328485.

Family and domain databases

Gene3Di2.130.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR015916. Gal_Oxidase_b-propeller.
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. AlignAdd to basket

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

        10         20         30         40         50
MPLKWKTSSP AIWKFPVPVL KTSRSTPLSP AYISLVEEED QHMKLSLGGS
60 70 80 90 100
EMGLSSHLQS SKAGPTRIFT SNTHSSVVLQ GFDQLRLEGL LCDVTLMPGD
110 120 130 140 150
TDDAFPVHRV MMASASDYFK AMFTGGMKEQ DLMCIKLHGV SKVGLRKIID
160 170 180 190 200
FIYTAKLSLN MDNLQDTLEA ASFLQILPVL DFCKVFLISG VTLDNCVEVG
210 220 230 240 250
RIANTYNLTE VDKYVNSFVL KNFPALLSTG EFLKLPFERL AFVLSSNSLK
260 270 280 290 300
HCTELELFKA TCRWLRLEEP RMDFAAKLMK NIRFPLMTPQ ELINYVQTVD
310 320 330 340 350
FMRTDNTCVN LLLEASNYQM MPYMQPVMQS DRTAIRSDTT HLVTLGGVLR
360 370 380 390 400
QQLVVSKELR MYDEKAHEWK SLAPMDAPRY QHGIAVIGNF LYVVGGQSNY
410 420 430 440 450
DTKGKTAVDT VFRFDPRYNK WMQVASLNEK RTFFHLSALK GYLYAVGGRN
460 470 480 490 500
AAGELPTVEC YNPRTNEWTY VAKMSEPHYG HAGTVYGGVM YISGGITHDT
510 520 530 540 550
FQKELMCFDP DTDKWIQKAP MTTVRGLHCM CTVGERLYVI GGNHFRGTSD
560 570 580 590 600
YDDVLSCEYY SPILDQWTPI AAMLRGQSDV GVAVFENKIY VVGGYSWNNR
610 620 630 640 650
CMVEIVQKYD PDKDEWHKVF DLPESLGGIR ACTLTVFPPE ETTPSPSRES

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

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:
EMBLi
GenBanki
DDBJi
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]
XP_011529713.1. XM_011531411.1. [Q9P2N7-1]
UniGeneiHs.348262.

Genome annotation databases

EnsembliENST00000262820; ENSP00000262820; 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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011529713.1. XM_011531411.1. [Q9P2N7-1]
UniGeneiHs.348262.

3D structure databases

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

Protein-protein interaction databases

BioGridi124688. 21 interactions.
IntActiQ9P2N7. 13 interactions.
STRINGi9606.ENSP00000443191.

PTM databases

PhosphoSiteiQ9P2N7.

Polymorphism and mutation databases

BioMutaiKLHL13.
DMDMi239938883.

Proteomic databases

MaxQBiQ9P2N7.
PaxDbiQ9P2N7.
PRIDEiQ9P2N7.

Protocols and materials databases

DNASUi90293.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262820; ENSP00000262820; 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]

Organism-specific databases

CTDi90293.
GeneCardsiGC0XM117031.
H-InvDBHIX0056474.
HGNCiHGNC:22931. KLHL13.
HPAiHPA046039.
MIMi300655. gene.
neXtProtiNX_Q9P2N7.
PharmGKBiPA134959204.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG293088.
GeneTreeiENSGT00760000118825.
HOVERGENiHBG106526.
InParanoidiQ9P2N7.
KOiK10447.
OMAiTEVDKYI.
OrthoDBiEOG7VTDMJ.
PhylomeDBiQ9P2N7.
TreeFamiTF328485.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiKLHL13. human.
GenomeRNAii90293.
NextBioi76640.
PROiQ9P2N7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2N7.
CleanExiHS_KLHL13.
ExpressionAtlasiQ9P2N7. baseline and differential.
GenevisibleiQ9P2N7. HS.

Family and domain databases

Gene3Di2.130.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR015916. Gal_Oxidase_b-propeller.
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]
ProtoNetiSearch...

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: July 22, 2015
This is version 122 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.