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Protein

UBX domain-containing protein 7

Gene

UBXN7

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

Functioni

Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.1 Publication

GO - Molecular functioni

  • transcription factor binding Source: BHF-UCL
  • ubiquitin binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
UBX domain-containing protein 7
Gene namesi
Name:UBXN7
Synonyms:KIAA0794, UBXD7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:29119. UBXN7.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • VCP-NPL4-UFD1 AAA ATPase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi288 – 2881S → A or D: No effect on interactions with CUL2 and HIF1A. 1 Publication
Mutagenesisi297 – 2971S → A or H: Severely reduces interaction neddylated CUL2. 1 Publication
Mutagenesisi459 – 4591P → G: Abolishes interaction with VCP/p97. 1 Publication

Organism-specific databases

PharmGKBiPA162408447.

Polymorphism and mutation databases

BioMutaiUBXN7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 489488UBX domain-containing protein 7PRO_0000211035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki99 – 99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei278 – 2781Phosphoserine1 Publication
Modified residuei285 – 2851Phosphoserine1 Publication
Modified residuei288 – 2881Phosphoserine6 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO94888.
PaxDbiO94888.
PRIDEiO94888.

PTM databases

PhosphoSiteiO94888.

Miscellaneous databases

PMAP-CutDBO94888.

Expressioni

Gene expression databases

BgeeiO94888.
CleanExiHS_UBXN7.
ExpressionAtlasiO94888. baseline and differential.
GenevisibleiO94888. HS.

Organism-specific databases

HPAiHPA048441.
HPA049442.

Interactioni

Subunit structurei

Interacts with neddylated CUL2, ubiquitinated HIF1A, and VCP/p97.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HIF1AQ166653EBI-1993627,EBI-447269

Protein-protein interaction databases

BioGridi117507. 78 interactions.
DIPiDIP-47029N.
IntActiO94888. 38 interactions.
STRINGi9606.ENSP00000296328.

Structurei

Secondary structure

1
489
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2313Combined sources
Helixi28 – 369Combined sources
Turni37 – 393Combined sources
Helixi42 – 5110Combined sources
Turni146 – 1483Combined sources
Helixi154 – 16411Combined sources
Beta strandi167 – 1737Combined sources
Turni177 – 1793Combined sources
Helixi180 – 1867Combined sources
Turni187 – 1893Combined sources
Helixi191 – 1999Combined sources
Beta strandi201 – 21010Combined sources
Helixi211 – 22010Combined sources
Beta strandi224 – 2318Combined sources
Turni233 – 2353Combined sources
Beta strandi240 – 2445Combined sources
Helixi247 – 26014Combined sources
Beta strandi412 – 4187Combined sources
Beta strandi424 – 4307Combined sources
Helixi435 – 44612Combined sources
Turni449 – 4513Combined sources
Beta strandi452 – 4554Combined sources
Beta strandi457 – 4593Combined sources
Beta strandi468 – 4703Combined sources
Turni472 – 4765Combined sources
Beta strandi479 – 4813Combined sources
Beta strandi484 – 4874Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJ4NMR-A377-487[»]
2DALNMR-A6-54[»]
2DLXNMR-A131-270[»]
ProteinModelPortaliO94888.
SMRiO94888. Positions 13-51, 130-265, 376-487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 5453UBAAdd
BLAST
Domaini285 – 30420UIMAdd
BLAST
Domaini408 – 48578UBXPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi337 – 3426Poly-Glu

Domaini

The UIM (ubiquitin-interacting motif) is required to engage the NEDD8 modification on cullins.1 Publication
The UBX domain mediates interaction with VCP/p97.1 Publication
The UBA domain is required for binding ubiquitinated-protein substrates.1 Publication

Sequence similaritiesi

Contains 1 UBA domain.
Contains 1 UBX domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG322646.
GeneTreeiENSGT00390000018687.
HOGENOMiHOG000143398.
HOVERGENiHBG057394.
InParanoidiO94888.
OMAiPEKSDGI.
PhylomeDBiO94888.
TreeFamiTF323635.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR006577. UAS.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR017346. UBX_7/2.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF00789. UBX. 1 hit.
[Graphical view]
PIRSFiPIRSF037991. UCP037991_UBX7/2. 1 hit.
SMARTiSM00594. UAS. 1 hit.
SM00166. UBX. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50033. UBX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O94888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAHGGSAAS SALKGLIQQF TTITGASESV GKHMLEACNN NLEMAVTMFL
60 70 80 90 100
DGGGIAEEPS TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGAPKR
110 120 130 140 150
RRPARSIFDG FRDFQTETIR QEQELRNGGA IDKKLTTLAD LFRPPIDLMH
160 170 180 190 200
KGSFETAKEC GQMQNKWLMI NIQNVQDFAC QCLNRDVWSN EAVKNIIREH
210 220 230 240 250
FIFWQVYHDS EEGQRYIQFY KLGDFPYVSI LDPRTGQKLV EWHQLDVSSF
260 270 280 290 300
LDQVTGFLGE HGQLDGLSSS PPKKCARSES LIDASEDSQL EAAIRASLQE
310 320 330 340 350
THFDSTQTKQ DSRSDEESES ELFSGSEEFI SVCGSDEEEE VENLAKSRKS
360 370 380 390 400
PHKDLGHRKE ENRRPLTEPP VRTDPGTATN HQGLPAVDSE ILEMPPEKAD
410 420 430 440 450
GVVEGIDVNG PKAQLMLRYP DGKREQITLP EQAKLLALVK HVQSKGYPNE
460 470 480
RFELLTNFPR RKLSHLDYDI TLQEAGLCPQ ETVFVQERN
Length:489
Mass (Da):54,862
Last modified:August 16, 2005 - v2
Checksum:i3C894533B1A2C41A
GO

Sequence cautioni

The sequence BAA34514.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC85247.1 differs from that shown.Unlikely isoform. Aberrant splice sites.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018337 mRNA. Translation: BAA34514.1. Different initiation.
AK129880 mRNA. Translation: BAC85247.1. Sequence problems.
CH471191 Genomic DNA. Translation: EAW53652.1.
CH471191 Genomic DNA. Translation: EAW53654.1.
BC028986 mRNA. Translation: AAH28986.1.
CCDSiCCDS43191.1.
RefSeqiNP_056377.1. NM_015562.1.
UniGeneiHs.518524.

Genome annotation databases

EnsembliENST00000296328; ENSP00000296328; ENSG00000163960.
GeneIDi26043.
KEGGihsa:26043.
UCSCiuc003fwm.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018337 mRNA. Translation: BAA34514.1. Different initiation.
AK129880 mRNA. Translation: BAC85247.1. Sequence problems.
CH471191 Genomic DNA. Translation: EAW53652.1.
CH471191 Genomic DNA. Translation: EAW53654.1.
BC028986 mRNA. Translation: AAH28986.1.
CCDSiCCDS43191.1.
RefSeqiNP_056377.1. NM_015562.1.
UniGeneiHs.518524.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WJ4NMR-A377-487[»]
2DALNMR-A6-54[»]
2DLXNMR-A131-270[»]
ProteinModelPortaliO94888.
SMRiO94888. Positions 13-51, 130-265, 376-487.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117507. 78 interactions.
DIPiDIP-47029N.
IntActiO94888. 38 interactions.
STRINGi9606.ENSP00000296328.

PTM databases

PhosphoSiteiO94888.

Polymorphism and mutation databases

BioMutaiUBXN7.

Proteomic databases

MaxQBiO94888.
PaxDbiO94888.
PRIDEiO94888.

Protocols and materials databases

DNASUi26043.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296328; ENSP00000296328; ENSG00000163960.
GeneIDi26043.
KEGGihsa:26043.
UCSCiuc003fwm.4. human.

Organism-specific databases

CTDi26043.
GeneCardsiGC03M196074.
HGNCiHGNC:29119. UBXN7.
HPAiHPA048441.
HPA049442.
neXtProtiNX_O94888.
PharmGKBiPA162408447.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322646.
GeneTreeiENSGT00390000018687.
HOGENOMiHOG000143398.
HOVERGENiHBG057394.
InParanoidiO94888.
OMAiPEKSDGI.
PhylomeDBiO94888.
TreeFamiTF323635.

Miscellaneous databases

ChiTaRSiUBXN7. human.
EvolutionaryTraceiO94888.
GenomeRNAii26043.
NextBioi47875.
PMAP-CutDBO94888.
PROiO94888.

Gene expression databases

BgeeiO94888.
CleanExiHS_UBXN7.
ExpressionAtlasiO94888. baseline and differential.
GenevisibleiO94888. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR006577. UAS.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR017346. UBX_7/2.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF00789. UBX. 1 hit.
[Graphical view]
PIRSFiPIRSF037991. UCP037991_UBX7/2. 1 hit.
SMARTiSM00594. UAS. 1 hit.
SM00166. UBX. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50033. UBX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "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: Heart.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 32-489.
    Tissue: Testis.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, 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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation."
    Bandau S., Knebel A., Gage Z.O., Wood N.T., Alexandru G.
    BMC Biol. 10:36-36(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UIM MOTIF, UBA DOMAIN, MUTAGENESIS OF SER-288; SER-297 AND PRO-459, INTERACTION WITH CUL2; HIF1A AND VCP.
  16. "Solution structure of the UBX domain of KIAA0794 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 376-487.
  17. "Solution structure of the novel identified UBA-like domain in the N-terminal of human FAS associated factor 1 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 5-54.
  18. "Solution structure of the UAS domain of human UBX domain-containing protein 7."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 131-270.

Entry informationi

Entry nameiUBXN7_HUMAN
AccessioniPrimary (citable) accession number: O94888
Secondary accession number(s): D3DXB3
, Q6ZP77, Q86X20, Q8N327
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 22, 2015
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.