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Protein

Protein UXT

Gene

UXT

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

Functioni

Involved in gene transcription regulation. Acts in concert with the corepressor URI1 to regulate androgen receptor transcription (AR). AR N-terminus-associated coactivator which may play a role in facilitating receptor-induced transcriptional activation (PubMed:11854421). Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling (PubMed:11827465). Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC (PubMed:17554592). May be a nuclear chaperone that promotes formation of the NF-kappa-B enhanceosome and which is essential for its nuclear function (PubMed:17620405). Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM (PubMed:17635584). Together with URI1, associates with chromatin to the NKX3-1 promoter region.7 Publications

GO - Molecular functioni

  • beta-tubulin binding Source: HGNC
  • chromatin binding Source: UniProtKB
  • microtubule binding Source: HGNC
  • RNA polymerase II transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • centrosome organization Source: HGNC
  • microtubule cytoskeleton organization Source: HGNC
  • mitochondrion transport along microtubule Source: HGNC
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chaperone, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein UXT
Alternative name(s):
Androgen receptor trapped clone 27 protein
Short name:
ART-27
Ubiquitously expressed transcript protein
Gene namesi
Name:UXT
ORF Names:HSPC024
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12641. UXT.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: HGNC
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: HGNC
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501L → P: Causes dislocation from the centrosome; when associated with L-59. 1 Publication
Mutagenesisi59 – 591L → P: Causes dislocation from the centrosome; when associated with L-50. 1 Publication

Organism-specific databases

PharmGKBiPA37265.

Polymorphism and mutation databases

BioMutaiUXT.
DMDMi8928445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157Protein UXTPRO_0000065751Add
BLAST

Proteomic databases

MaxQBiQ9UBK9.
PaxDbiQ9UBK9.
PRIDEiQ9UBK9.

PTM databases

PhosphoSiteiQ9UBK9.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in prostate epithelial cells. Overexpressed in a number of tumor tissues (PubMed:16221885). Highest levels in the heart, skeletal muscle, pancreas, kidney, liver, adrenal gland, peripheral blood leukocytes, lymph node, prostate, and thyroid and the lowest levels in bladder and uterus.4 Publications

Gene expression databases

BgeeiQ9UBK9.
CleanExiHS_UXT.
ExpressionAtlasiQ9UBK9. baseline and differential.
GenevisibleiQ9UBK9. HS.

Organism-specific databases

HPAiHPA050499.
HPA058400.

Interactioni

Subunit structurei

Homohexamer. Interacts with LRPPRC. Interacts with AR N-terminus. In the nucleus interacts specifically with RELA and forms a dynamic complex with NF-kappa-B and is recruited to the NF-kappa-B enhanceosome upon stimulation. Interacts with MECOM and URI1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT31Q153233EBI-357355,EBI-948001
KRT40Q6A1623EBI-357355,EBI-10171697
KRTAP10-7P604093EBI-357355,EBI-10172290
KRTAP10-8P604103EBI-357355,EBI-10171774
MECOMQ031125EBI-357355,EBI-1384862
NOTCH2NLQ7Z3S93EBI-357355,EBI-945833
PAK7Q8TB933EBI-357355,EBI-741896
RELAQ042065EBI-357355,EBI-73886
RPAP3Q9H6T32EBI-357355,EBI-356928
SARM1Q0D2N82EBI-357355,EBI-8716526
SIAH1Q8IUQ43EBI-357355,EBI-747107

Protein-protein interaction databases

BioGridi113997. 29 interactions.
IntActiQ9UBK9. 35 interactions.
MINTiMINT-1143575.
STRINGi9606.ENSP00000337393.

Structurei

3D structure databases

ProteinModelPortaliQ9UBK9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UXT family.Curated

Phylogenomic databases

eggNOGiNOG263764.
GeneTreeiENSGT00390000018078.
HOGENOMiHOG000005748.
HOVERGENiHBG001087.
InParanoidiQ9UBK9.
OrthoDBiEOG7T7GW2.
PhylomeDBiQ9UBK9.
TreeFamiTF323827.

Family and domain databases

Gene3Di1.10.287.370. 1 hit.
InterProiIPR009053. Prefoldin.
IPR004127. Prefoldin_subunit_alpha.
IPR003994. UXT.
[Graphical view]
PfamiPF02996. Prefoldin. 1 hit.
[Graphical view]
PRINTSiPR01502. UXTPROTEIN.
SUPFAMiSSF46579. SSF46579. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9UBK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPPKRRAV EATGEKVLRY ETFISDVLQR DLRKVLDHRD KVYEQLAKYL
60 70 80 90 100
QLRNVIERLQ EAKHSELYMQ VDLGCNFFVD TVVPDTSRIY VALGYGFFLE
110 120 130 140 150
LTLAEALKFI DRKSSLLTEL SNSLTKDSMN IKAHIHMLLE GLRELQGLQN

FPEKPHH
Length:157
Mass (Da):18,246
Last modified:May 1, 2000 - v1
Checksum:i94CE14C462DEE308
GO

Sequence cautioni

The sequence AAD39840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI42447.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092737 mRNA. Translation: AAD28698.1.
AF083241 mRNA. Translation: AAD39839.1.
AF083242 mRNA. Translation: AAD39840.1. Different initiation.
AL009172 Genomic DNA. Translation: CAI42447.1. Different initiation.
AL009172 Genomic DNA. Translation: CAI42448.1.
AK312072 mRNA. Translation: BAG35008.1.
CH471164 Genomic DNA. Translation: EAW59326.1.
BC000720 mRNA. Translation: AAH00720.1.
BC008890 mRNA. Translation: AAH08890.1.
CCDSiCCDS14285.1.
RefSeqiNP_004173.1. NM_004182.3.
NP_705582.1. NM_153477.2.
UniGeneiHs.172791.
Hs.735566.

Genome annotation databases

EnsembliENST00000333119; ENSP00000327797; ENSG00000126756.
GeneIDi8409.
KEGGihsa:8409.
UCSCiuc004dim.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092737 mRNA. Translation: AAD28698.1.
AF083241 mRNA. Translation: AAD39839.1.
AF083242 mRNA. Translation: AAD39840.1. Different initiation.
AL009172 Genomic DNA. Translation: CAI42447.1. Different initiation.
AL009172 Genomic DNA. Translation: CAI42448.1.
AK312072 mRNA. Translation: BAG35008.1.
CH471164 Genomic DNA. Translation: EAW59326.1.
BC000720 mRNA. Translation: AAH00720.1.
BC008890 mRNA. Translation: AAH08890.1.
CCDSiCCDS14285.1.
RefSeqiNP_004173.1. NM_004182.3.
NP_705582.1. NM_153477.2.
UniGeneiHs.172791.
Hs.735566.

3D structure databases

ProteinModelPortaliQ9UBK9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113997. 29 interactions.
IntActiQ9UBK9. 35 interactions.
MINTiMINT-1143575.
STRINGi9606.ENSP00000337393.

PTM databases

PhosphoSiteiQ9UBK9.

Polymorphism and mutation databases

BioMutaiUXT.
DMDMi8928445.

Proteomic databases

MaxQBiQ9UBK9.
PaxDbiQ9UBK9.
PRIDEiQ9UBK9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333119; ENSP00000327797; ENSG00000126756.
GeneIDi8409.
KEGGihsa:8409.
UCSCiuc004dim.3. human.

Organism-specific databases

CTDi8409.
GeneCardsiGC0XM047511.
HGNCiHGNC:12641. UXT.
HPAiHPA050499.
HPA058400.
MIMi300234. gene.
neXtProtiNX_Q9UBK9.
PharmGKBiPA37265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG263764.
GeneTreeiENSGT00390000018078.
HOGENOMiHOG000005748.
HOVERGENiHBG001087.
InParanoidiQ9UBK9.
OrthoDBiEOG7T7GW2.
PhylomeDBiQ9UBK9.
TreeFamiTF323827.

Miscellaneous databases

ChiTaRSiUXT. human.
GeneWikiiUXT.
GenomeRNAii8409.
NextBioi31482.
PROiQ9UBK9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBK9.
CleanExiHS_UXT.
ExpressionAtlasiQ9UBK9. baseline and differential.
GenevisibleiQ9UBK9. HS.

Family and domain databases

Gene3Di1.10.287.370. 1 hit.
InterProiIPR009053. Prefoldin.
IPR004127. Prefoldin_subunit_alpha.
IPR003994. UXT.
[Graphical view]
PfamiPF02996. Prefoldin. 1 hit.
[Graphical view]
PRINTSiPR01502. UXTPROTEIN.
SUPFAMiSSF46579. SSF46579. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of UXT, a novel gene in human Xp11, which is widely and abundantly expressed in tumor tissue."
    Schroer A., Schneider S., Ropers H.-H., Nothwang H.G.
    Genomics 56:340-343(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification and characterization of ART-27, a novel coactivator for the androgen receptor N terminus."
    Markus S.M., Taneja S.S., Logan S.K., Li W., Ha S., Hittelman A.B., Rogatsky I., Garabedian M.J.
    Mol. Biol. Cell 13:670-682(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
  3. "UXT interacts with the transcriptional repressor protein EVI1 and suppresses cell transformation."
    McGilvray R., Walker M., Bartholomew C.
    FEBS J. 274:3960-3971(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH MECOM.
  4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  5. Zhou J., Ye M., Fu G., Zhang Q., Shen Y., Huang Q., Xu S., He K., Chen S., Mao M., Chen Z.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  6. "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].
    Tissue: Mammary gland.
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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].
    Tissue: Placenta.
  10. "Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
    Liu L., McKeehan W.L.
    Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LRPPRC.
  11. "UXT is a novel centrosomal protein essential for cell viability."
    Zhao H., Wang Q., Zhang H., Liu Q., Du X., Richter M., Greene M.I.
    Mol. Biol. Cell 16:5857-5865(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-50 AND LEU-59.
  12. "UXT (Ubiquitously Expressed Transcript) causes mitochondrial aggregation."
    Moss T.N., Vo A., McKeehan W.L., Liu L.
    In Vitro Cell. Dev. Biol. Anim. 43:139-146(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "UXT is a novel and essential cofactor in the NF-kappaB transcriptional enhanceosome."
    Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.
    J. Cell Biol. 178:231-244(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RELA.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: FUNCTION, INTERACTION WITH URI1, TISSUE SPECIFICITY.

Entry informationi

Entry nameiUXT_HUMAN
AccessioniPrimary (citable) accession number: Q9UBK9
Secondary accession number(s): B2R561, Q5JZG3, Q9Y6E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 121 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 X
    Human chromosome X: 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. 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.