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Protein

BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3

Gene

KCTD10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity).By similarity

Pathwayi: protein 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

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3
Short name:
hBACURD3
Alternative name(s):
BTB/POZ domain-containing protein KCTD10
Potassium channel tetramerization domain-containing protein 10
Gene namesi
Name:KCTD10
Synonyms:ULR061
ORF Names:MSTP028
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:23236. KCTD10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134938409.

Polymorphism and mutation databases

BioMutaiKCTD10.
DMDMi74733570.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3PRO_0000247421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H3F6.
MaxQBiQ9H3F6.
PaxDbiQ9H3F6.
PRIDEiQ9H3F6.

PTM databases

iPTMnetiQ9H3F6.
PhosphoSiteiQ9H3F6.

Expressioni

Gene expression databases

BgeeiQ9H3F6.
CleanExiHS_KCTD10.
ExpressionAtlasiQ9H3F6. baseline and differential.
GenevisibleiQ9H3F6. HS.

Organism-specific databases

HPAiHPA014273.

Interactioni

Subunit structurei

Component of the BCR(BACURD3) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD10/BACURD3 and RBX1. Interacts with DNA polymerase delta subunit 2/POLD2 (By similarity). Interacts with PCNA.By similarity1 Publication

Protein-protein interaction databases

BioGridi123803. 51 interactions.
IntActiQ9H3F6. 20 interactions.
STRINGi9606.ENSP00000228495.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 386Combined sources
Beta strandi41 – 466Combined sources
Helixi47 – 504Combined sources
Beta strandi52 – 554Combined sources
Helixi56 – 616Combined sources
Beta strandi75 – 773Combined sources
Helixi84 – 9310Combined sources
Helixi102 – 11413Combined sources
Helixi118 – 12710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FTAX-ray2.64A/B/C/D26-135[»]
ProteinModelPortaliQ9H3F6.
SMRiQ9H3F6. Positions 34-120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 10069BTBPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi239 – 2457PCNA-bindingBy similarity

Sequence similaritiesi

Belongs to the BACURD family.Curated
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2716. Eukaryota.
ENOG410XQYZ. LUCA.
GeneTreeiENSGT00530000063071.
HOGENOMiHOG000294088.
HOVERGENiHBG052219.
InParanoidiQ9H3F6.
KOiK15074.
OMAiQGLADEC.
OrthoDBiEOG7PS1G1.
PhylomeDBiQ9H3F6.
TreeFamiTF315649.

Family and domain databases

InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
[Graphical view]
PfamiPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H3F6-1) [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
MEEMSGESVV SSAVPAAATR TTSFKGTSPS SKYVKLNVGG ALYYTTMQTL
60 70 80 90 100
TKQDTMLKAM FSGRMEVLTD SEGWILIDRC GKHFGTILNY LRDGAVPLPE
110 120 130 140 150
SRREIEELLA EAKYYLVQGL VEECQAALQN KDTYEPFCKV PVITSSKEEQ
160 170 180 190 200
KLIATSNKPA VKLLYNRSNN KYSYTSNSDD NMLKNIELFD KLSLRFNGRV
210 220 230 240 250
LFIKDVIGDE ICCWSFYGQG RKIAEVCCTS IVYATEKKQT KVEFPEARIY
260 270 280 290 300
EETLNILLYE AQDGRGPDNA LLEATGGAAG RSHHLDEDEE RERIERVRRI
310
HIKRPDDRAH LHQ
Length:313
Mass (Da):35,432
Last modified:March 1, 2001 - v1
Checksum:i199AF07A30D5BCA6
GO
Isoform 2 (identifier: Q9H3F6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-198: Missing.

Note: No experimental confirmation available.
Show »
Length:290
Mass (Da):32,779
Checksum:i44691C6FBB800C1D
GO
Isoform 3 (identifier: Q9H3F6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-158: Missing.
     159-175: PAVKLLYNRSNNKYSYT → MMAVFTSLWSPYQMLFC

Note: No experimental confirmation available.
Show »
Length:155
Mass (Da):17,985
Checksum:i1CD49234B8678D7C
GO

Sequence cautioni

The sequence BAB55188.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD92595.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → V in BAB55188 (PubMed:14702039).Curated
Sequence conflicti68 – 681L → P in AAT09002 (Ref. 3) Curated
Sequence conflicti170 – 1701N → T in BAD96268 (Ref. 6) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 158158Missing in isoform 3. 1 PublicationVSP_019978Add
BLAST
Alternative sequencei159 – 17517PAVKL…KYSYT → MMAVFTSLWSPYQMLFC in isoform 3. 1 PublicationVSP_019979Add
BLAST
Alternative sequencei176 – 19823Missing in isoform 2. 1 PublicationVSP_019980Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY205299 mRNA. Translation: AAO47716.1.
AF113208 mRNA. Translation: AAG39279.1.
AY597809 mRNA. Translation: AAT09002.1.
AK027543 mRNA. Translation: BAB55188.1. Different initiation.
AB209358 mRNA. Translation: BAD92595.1. Different initiation.
AK222548 mRNA. Translation: BAD96268.1.
AC007570 Genomic DNA. No translation available.
BC040062 mRNA. Translation: AAH40062.1.
CCDSiCCDS9128.1. [Q9H3F6-1]
RefSeqiNP_001304324.1. NM_001317395.1.
NP_001304328.1. NM_001317399.1. [Q9H3F6-2]
NP_114160.1. NM_031954.4. [Q9H3F6-1]
UniGeneiHs.524731.

Genome annotation databases

EnsembliENST00000228495; ENSP00000228495; ENSG00000110906. [Q9H3F6-1]
GeneIDi83892.
KEGGihsa:83892.
UCSCiuc001toi.2. human. [Q9H3F6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY205299 mRNA. Translation: AAO47716.1.
AF113208 mRNA. Translation: AAG39279.1.
AY597809 mRNA. Translation: AAT09002.1.
AK027543 mRNA. Translation: BAB55188.1. Different initiation.
AB209358 mRNA. Translation: BAD92595.1. Different initiation.
AK222548 mRNA. Translation: BAD96268.1.
AC007570 Genomic DNA. No translation available.
BC040062 mRNA. Translation: AAH40062.1.
CCDSiCCDS9128.1. [Q9H3F6-1]
RefSeqiNP_001304324.1. NM_001317395.1.
NP_001304328.1. NM_001317399.1. [Q9H3F6-2]
NP_114160.1. NM_031954.4. [Q9H3F6-1]
UniGeneiHs.524731.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FTAX-ray2.64A/B/C/D26-135[»]
ProteinModelPortaliQ9H3F6.
SMRiQ9H3F6. Positions 34-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123803. 51 interactions.
IntActiQ9H3F6. 20 interactions.
STRINGi9606.ENSP00000228495.

PTM databases

iPTMnetiQ9H3F6.
PhosphoSiteiQ9H3F6.

Polymorphism and mutation databases

BioMutaiKCTD10.
DMDMi74733570.

Proteomic databases

EPDiQ9H3F6.
MaxQBiQ9H3F6.
PaxDbiQ9H3F6.
PRIDEiQ9H3F6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228495; ENSP00000228495; ENSG00000110906. [Q9H3F6-1]
GeneIDi83892.
KEGGihsa:83892.
UCSCiuc001toi.2. human. [Q9H3F6-1]

Organism-specific databases

CTDi83892.
GeneCardsiKCTD10.
HGNCiHGNC:23236. KCTD10.
HPAiHPA014273.
MIMi613421. gene.
neXtProtiNX_Q9H3F6.
PharmGKBiPA134938409.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2716. Eukaryota.
ENOG410XQYZ. LUCA.
GeneTreeiENSGT00530000063071.
HOGENOMiHOG000294088.
HOVERGENiHBG052219.
InParanoidiQ9H3F6.
KOiK15074.
OMAiQGLADEC.
OrthoDBiEOG7PS1G1.
PhylomeDBiQ9H3F6.
TreeFamiTF315649.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiKCTD10. human.
GenomeRNAii83892.
NextBioi72983.
PROiQ9H3F6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3F6.
CleanExiHS_KCTD10.
ExpressionAtlasiQ9H3F6. baseline and differential.
GenevisibleiQ9H3F6. HS.

Family and domain databases

InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
[Graphical view]
PfamiPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a human uterine leiomyoma related gene through bioinformatics."
    Li B., Hu Z.-H., Yang J., Zhang Y.-L.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Uterine leiomyoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aorta.
  3. Li H., Zhong G., Ke R., Shen C., Zhou G., Lin L., Yang S.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "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 1).
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Coronary artery.
  7. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Eye.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "KCTD10 interacts with proliferating cell nuclear antigen and its down-regulation could inhibit cell proliferation."
    Wang Y., Zheng Y., Luo F., Fan X., Chen J., Zhang C., Hui R.
    J. Cell. Biochem. 106:409-413(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PCNA.
  11. "Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement."
    Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., Peng H.B., Shao F.
    Mol. Cell 35:841-855(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBACD3_HUMAN
AccessioniPrimary (citable) accession number: Q9H3F6
Secondary accession number(s): Q53HN2
, Q59FV1, Q6PL47, Q96SU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 111 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.