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Protein

Cysteine and histidine-rich domain-containing protein 1

Gene

CHORDC1

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

Functioni

Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Zinc 1
Metal bindingi10 – 101Zinc 1
Metal bindingi24 – 241Zinc 1
Metal bindingi27 – 271Zinc 2
Metal bindingi42 – 421Zinc 2
Metal bindingi43 – 431Zinc 2
Metal bindingi59 – 591Zinc 2
Metal bindingi64 – 641Zinc 1
Metal bindingi157 – 1571Zinc 3PROSITE-ProRule annotation
Metal bindingi162 – 1621Zinc 3PROSITE-ProRule annotation
Metal bindingi176 – 1761Zinc 3PROSITE-ProRule annotation
Metal bindingi179 – 1791Zinc 4PROSITE-ProRule annotation
Metal bindingi194 – 1941Zinc 4PROSITE-ProRule annotation
Metal bindingi195 – 1951Zinc 4PROSITE-ProRule annotation
Metal bindingi211 – 2111Zinc 4PROSITE-ProRule annotation
Metal bindingi216 – 2161Zinc 3PROSITE-ProRule annotation

GO - Molecular functioni

  1. Hsp90 protein binding Source: UniProtKB
  2. zinc ion binding Source: Ensembl

GO - Biological processi

  1. chaperone-mediated protein folding Source: UniProtKB
  2. negative regulation of Rho-dependent protein serine/threonine kinase activity Source: Ensembl
  3. regulation of cellular response to heat Source: UniProtKB
  4. regulation of centrosome duplication Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine and histidine-rich domain-containing protein 1
Alternative name(s):
CHORD domain-containing protein 1
Short name:
CHORD-containing protein 1
Short name:
CHP-1
Protein morgana
Gene namesi
Name:CHORDC1
Synonyms:CHP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14525. CHORDC1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 332331Cysteine and histidine-rich domain-containing protein 1PRO_0000317770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei47 – 471Phosphothreonine1 Publication
Modified residuei51 – 511Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UHD1.
PaxDbiQ9UHD1.
PeptideAtlasiQ6IN49.
PRIDEiQ9UHD1.

Expressioni

Tissue specificityi

Underexpressed in many breast and lung cancers.1 Publication

Gene expression databases

BgeeiQ9UHD1.
CleanExiHS_CHORDC1.
ExpressionAtlasiQ9UHD1. baseline and differential.
GenevestigatoriQ9UHD1.

Organism-specific databases

HPAiHPA041040.

Interactioni

Subunit structurei

Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with HSP90AB1 and PPP5C (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AA1P079008EBI-2550959,EBI-296047

Protein-protein interaction databases

BioGridi117929. 29 interactions.
IntActiQ9UHD1. 17 interactions.
STRINGi9606.ENSP00000319255.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Turni16 – 183Combined sources
Turni21 – 233Combined sources
Beta strandi31 – 344Combined sources
Beta strandi37 – 448Combined sources
Beta strandi46 – 494Combined sources
Helixi50 – 534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRTNMR-A1-68[»]
ProteinModelPortaliQ9UHD1.
SMRiQ9UHD1. Positions 1-68, 157-216, 231-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHD1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6460CHORD 1PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 21660CHORD 2PROSITE-ProRule annotationAdd
BLAST
Domaini227 – 31690CSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7776Interaction with PPP5CBy similarityAdd
BLAST
Regioni65 – 316252Interaction with HSP90AA1 and HSP90AB1By similarityAdd
BLAST

Sequence similaritiesi

Contains 2 CHORD domains.PROSITE-ProRule annotation
Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG282821.
GeneTreeiENSGT00390000005180.
HOGENOMiHOG000207093.
HOVERGENiHBG052156.
InParanoidiQ9UHD1.
KOiK16729.
OMAiQRIGCNA.
OrthoDBiEOG7X6M0X.
PhylomeDBiQ9UHD1.
TreeFamiTF105394.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007051. CHORD.
IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04968. CHORD. 2 hits.
PF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51401. CHORD. 2 hits.
PS51203. CS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UHD1-1) [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
MALLCYNRGC GQRFDPETNS DDACTYHPGV PVFHDALKGW SCCKRRTTDF
60 70 80 90 100
SDFLSIVGCT KGRHNSEKPP EPVKPEVKTT EKKELCELKP KFQEHIIQAP
110 120 130 140 150
KPVEAIKRPS PDEPMTNLEL KISASLKQAL DKLKLSSGNE ENKKEEDNDE
160 170 180 190 200
IKIGTSCKNG GCSKTYQGLE SLEEVCVYHS GVPIFHEGMK YWSCCRRKTS
210 220 230 240 250
DFNTFLAQEG CTKGKHMWTK KDAGKKVVPC RHDWHQTGGE VTISVYAKNS
260 270 280 290 300
LPELSRVEAN STLLNVHIVF EGEKEFDQNV KLWGVIDVKR SYVTMTATKI
310 320 330
EITMRKAEPM QWASLELPAA KKQEKQKDAT TD
Length:332
Mass (Da):37,490
Last modified:February 4, 2008 - v2
Checksum:i3142D8EC8A879155
GO
Isoform 2 (identifier: Q9UHD1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-57: Missing.

Note: No experimental confirmation available.

Show »
Length:313
Mass (Da):35,286
Checksum:i3347F35622425A90
GO

Sequence cautioni

The sequence AAH17789.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341W → L in AAF18437 (PubMed:10571178).Curated
Sequence conflicti267 – 2671H → I in AAF18437 (PubMed:10571178).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti329 – 3291A → D.4 Publications
Corresponds to variant rs1045861 [ dbSNP | Ensembl ].
VAR_038676

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 5719Missing in isoform 2. 1 PublicationVSP_031150Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192466 mRNA. Translation: AAF18437.1.
AF123249 mRNA. Translation: AAG43237.1.
AK290231 mRNA. Translation: BAF82920.1.
AK312663 mRNA. Translation: BAG35545.1.
AP002364 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66868.1.
CH471065 Genomic DNA. Translation: EAW66870.1.
BC017789 mRNA. Translation: AAH17789.1. Different initiation.
BC072461 mRNA. Translation: AAH72461.1.
CCDSiCCDS44705.1. [Q9UHD1-2]
CCDS8289.1. [Q9UHD1-1]
RefSeqiNP_001137545.1. NM_001144073.1. [Q9UHD1-2]
NP_036256.2. NM_012124.2. [Q9UHD1-1]
UniGeneiHs.22857.

Genome annotation databases

EnsembliENST00000320585; ENSP00000319255; ENSG00000110172. [Q9UHD1-1]
ENST00000457199; ENSP00000401080; ENSG00000110172. [Q9UHD1-2]
GeneIDi26973.
KEGGihsa:26973.
UCSCiuc001pdg.2. human. [Q9UHD1-1]
uc009yvz.2. human. [Q9UHD1-2]

Polymorphism databases

DMDMi167008724.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192466 mRNA. Translation: AAF18437.1.
AF123249 mRNA. Translation: AAG43237.1.
AK290231 mRNA. Translation: BAF82920.1.
AK312663 mRNA. Translation: BAG35545.1.
AP002364 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66868.1.
CH471065 Genomic DNA. Translation: EAW66870.1.
BC017789 mRNA. Translation: AAH17789.1. Different initiation.
BC072461 mRNA. Translation: AAH72461.1.
CCDSiCCDS44705.1. [Q9UHD1-2]
CCDS8289.1. [Q9UHD1-1]
RefSeqiNP_001137545.1. NM_001144073.1. [Q9UHD1-2]
NP_036256.2. NM_012124.2. [Q9UHD1-1]
UniGeneiHs.22857.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YRTNMR-A1-68[»]
ProteinModelPortaliQ9UHD1.
SMRiQ9UHD1. Positions 1-68, 157-216, 231-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117929. 29 interactions.
IntActiQ9UHD1. 17 interactions.
STRINGi9606.ENSP00000319255.

Polymorphism databases

DMDMi167008724.

Proteomic databases

MaxQBiQ9UHD1.
PaxDbiQ9UHD1.
PeptideAtlasiQ6IN49.
PRIDEiQ9UHD1.

Protocols and materials databases

DNASUi26973.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320585; ENSP00000319255; ENSG00000110172. [Q9UHD1-1]
ENST00000457199; ENSP00000401080; ENSG00000110172. [Q9UHD1-2]
GeneIDi26973.
KEGGihsa:26973.
UCSCiuc001pdg.2. human. [Q9UHD1-1]
uc009yvz.2. human. [Q9UHD1-2]

Organism-specific databases

CTDi26973.
GeneCardsiGC11M089933.
H-InvDBHIX0010016.
HGNCiHGNC:14525. CHORDC1.
HPAiHPA041040.
MIMi604353. gene.
neXtProtiNX_Q9UHD1.
PharmGKBiPA26476.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282821.
GeneTreeiENSGT00390000005180.
HOGENOMiHOG000207093.
HOVERGENiHBG052156.
InParanoidiQ9UHD1.
KOiK16729.
OMAiQRIGCNA.
OrthoDBiEOG7X6M0X.
PhylomeDBiQ9UHD1.
TreeFamiTF105394.

Miscellaneous databases

ChiTaRSiCHORDC1. human.
EvolutionaryTraceiQ9UHD1.
GenomeRNAii26973.
NextBioi49424.
PROiQ9UHD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHD1.
CleanExiHS_CHORDC1.
ExpressionAtlasiQ9UHD1. baseline and differential.
GenevestigatoriQ9UHD1.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007051. CHORD.
IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04968. CHORD. 2 hits.
PF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51401. CHORD. 2 hits.
PS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans."
    Shirasu K., Lahaye T., Tan M.-W., Zhou F., Azevedo C., Schulze-Lefert P.
    Cell 99:355-366(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-329.
  2. "Isolation and characterization the chymotrypsin-like protein gene from human heart cDNA library."
    Zhao Y., Cao H., Jiang Y., Meng X., Zhao X., Liu D., Ding J.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-329.
    Tissue: Heart.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-329.
    Tissue: Thalamus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-329.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Uterus.
  7. Bienvenut W.V., Bilsland A.E., Keith W.N.
    Submitted (DEC-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-8; 47-61; 108-121; 249-256; 282-289; 291-299 AND 306-321, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: FUNCTION, INTERACTION WITH ROCK1 AND ROCK2, TISSUE SPECIFICITY.
  11. "A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein."
    Gano J.J., Simon J.A.
    Mol. Cell. Proteomics 9:255-270(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AA1.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Solution structure of the CHORD domain of human CHORD-containing protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-68.

Entry informationi

Entry nameiCHRD1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHD1
Secondary accession number(s): B2R6P8
, Q6IN49, Q8WVL9, Q9H3D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 4, 2008
Last sequence update: February 4, 2008
Last modified: March 3, 2015
This is version 98 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.