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Protein

Zinc finger RNA-binding protein

Gene

ZFR

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

Functioni

Involved in postimplantation and gastrulation stages of development. Involved in the nucleocytoplasmic shuttling of STAU2. Binds to DNA and RNA (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger RNA-binding protein
Short name:
hZFR
Alternative name(s):
M-phase phosphoprotein homolog
Gene namesi
Name:ZFR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:17277. ZFR.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cytoplasmic granule By similarity
  • Chromosome By similarity

  • Note: Associated with chromosome foci in meiotic cells. Localizes in somatodendritic compartment of primary hippocampal neurons. Colocalizes with STAU2 in several cytosolic RNA granules (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti401840. Autosomal recessive spastic paraplegia type 71.
PharmGKBiPA38219.

Polymorphism and mutation databases

BioMutaiZFR.
DMDMi162416228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10741074Zinc finger RNA-binding proteinPRO_0000312719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei509 – 5091N6-acetyllysine1 Publication
Modified residuei516 – 5161N6-acetyllysineBy similarity
Modified residuei1054 – 10541Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96KR1.
PaxDbiQ96KR1.
PRIDEiQ96KR1.

PTM databases

PhosphoSiteiQ96KR1.

Expressioni

Tissue specificityi

Expressed in lung, liver, lymphocytes, heart, pancreas, placenta, brain and kidney.1 Publication

Gene expression databases

BgeeiQ96KR1.
CleanExiHS_ZFR.
ExpressionAtlasiQ96KR1. baseline and differential.
GenevestigatoriQ96KR1.

Organism-specific databases

HPAiHPA016666.

Interactioni

Subunit structurei

Found in a cytoplasmic RNP complex with STAU2. Interacts with STAU2. Does not interact with STAU1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SMAD2Q157962EBI-2513582,EBI-1040141

Protein-protein interaction databases

BioGridi119667. 52 interactions.
DIPiDIP-47293N.
IntActiQ96KR1. 15 interactions.
MINTiMINT-4655113.

Structurei

3D structure databases

ProteinModelPortaliQ96KR1.
SMRiQ96KR1. Positions 722-1039.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini703 – 1073371DZFPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 302267Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 DZF domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG292385.
GeneTreeiENSGT00550000074528.
HOVERGENiHBG108765.
InParanoidiQ96KR1.
KOiK13203.
OMAiNNCTVNT.
OrthoDBiEOG72ZCDC.
PhylomeDBiQ96KR1.
TreeFamiTF320194.

Family and domain databases

InterProiIPR006561. DZF_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF07528. DZF. 1 hit.
[Graphical view]
SMARTiSM00572. DZF. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
SM00451. ZnF_U1. 3 hits.
[Graphical view]
PROSITEiPS51703. DZF. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96KR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA
60 70 80 90 100
SGVAYSHPTT VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA
110 120 130 140 150
ATAAAYGGYP TAHTATDYGY TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA
160 170 180 190 200
PAVAYDSKQY YQQPTATAAA VAAAAQPQPS VAETYYQTAP KAGYSQGATQ
210 220 230 240 250
YTQAQQTRQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA ATVVPSYTQS
260 270 280 290 300
ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT
310 320 330 340 350
AAWTGTTFTK KAPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL
360 370 380 390 400
EGQKHKKKEA ALKASQNTSS SNSSTRGTQN QLRCELCDVS CTGADAYAAH
410 420 430 440 450
IRGAKHQKVV KLHTKLGKPI PSTEPNVVSQ ATSSTAVSAS KPTASPSSIA
460 470 480 490 500
ANNCTVNTSS VATSSMKGLT TTGNSSLNST SNTKVSAVPT NMAAKKTSTP
510 520 530 540 550
KINFVGGNKL QSTGNKAEDI KGTECVKSTP VTSAVQIPEV KQDTVSEPVT
560 570 580 590 600
PASLAALQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH
610 620 630 640 650
LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QKEEYWRRRE
660 670 680 690 700
EEERWRMEMR RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL
710 720 730 740 750
GVRPGMPPQP QGPAPLRRPD SSDDRYVMTK HATIYPTEEE LQAVQKIVSI
760 770 780 790 800
TERALKLVSD SLSEHEKNKN KEGDDKKEGG KDRALKGVLR VGVLAKGLLL
810 820 830 840 850
RGDRNVNLVL LCSEKPSKTL LSRIAENLPK QLAVISPEKY DIKCAVSEAA
860 870 880 890 900
IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL
910 920 930 940 950
DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL
960 970 980 990 1000
VEKAISSASS PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA
1010 1020 1030 1040 1050
TMTDQQREDI TSSAQFALRL LAFRQIHKVL GMDPLPQMSQ RFNIHNNRKR
1060 1070
RRDSDGVDGF EAEGKKDKKD YDNF
Length:1,074
Mass (Da):117,012
Last modified:December 4, 2007 - v2
Checksum:i3E43654E7134E9FC
GO

Sequence cautioni

The sequence AAD40385.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH30540.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI07418.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB15147.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC40818.1 differs from that shown. Reason: Frameshift at position 1057. Curated
The sequence CAC40818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71V → I in AAI07418 (PubMed:15489334).Curated
Sequence conflicti643 – 6431E → L in AAD40385 (PubMed:10931946).Curated
Sequence conflicti659 – 6591M → I in CAC40818 (PubMed:11574164).Curated
Sequence conflicti794 – 7941L → F in AAD40385 (PubMed:10931946).Curated
Sequence conflicti834 – 8341V → F in AAD40385 (PubMed:10931946).Curated
Sequence conflicti913 – 9131Q → QE in CAC40818 (PubMed:11574164).Curated
Sequence conflicti1016 – 10161F → K in CAC40818 (PubMed:11574164).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611V → I.1 Publication
Corresponds to variant rs4867440 [ dbSNP | Ensembl ].
VAR_037554
Natural varianti520 – 5201I → T.1 Publication
Corresponds to variant rs1051489 [ dbSNP | Ensembl ].
VAR_037555

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ314790 mRNA. Translation: CAC40818.1. Sequence problems.
AC008949 Genomic DNA. No translation available.
BC030540 mRNA. Translation: AAH30540.1. Sequence problems.
BC051893 mRNA. Translation: AAH51893.1.
BC062986 mRNA. Translation: AAH62986.1.
BC107417 mRNA. Translation: AAI07418.1. Sequence problems.
BC137084 mRNA. Translation: AAI37085.1.
AF100742 mRNA. Translation: AAD40385.1. Different initiation.
AK025481 mRNA. Translation: BAB15147.1. Different initiation.
AL137258 mRNA. Translation: CAB70659.1.
CCDSiCCDS34139.1.
PIRiT46329.
RefSeqiNP_057191.2. NM_016107.3.
UniGeneiHs.435231.

Genome annotation databases

EnsembliENST00000265069; ENSP00000265069; ENSG00000056097.
GeneIDi51663.
KEGGihsa:51663.
UCSCiuc003jhr.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ314790 mRNA. Translation: CAC40818.1. Sequence problems.
AC008949 Genomic DNA. No translation available.
BC030540 mRNA. Translation: AAH30540.1. Sequence problems.
BC051893 mRNA. Translation: AAH51893.1.
BC062986 mRNA. Translation: AAH62986.1.
BC107417 mRNA. Translation: AAI07418.1. Sequence problems.
BC137084 mRNA. Translation: AAI37085.1.
AF100742 mRNA. Translation: AAD40385.1. Different initiation.
AK025481 mRNA. Translation: BAB15147.1. Different initiation.
AL137258 mRNA. Translation: CAB70659.1.
CCDSiCCDS34139.1.
PIRiT46329.
RefSeqiNP_057191.2. NM_016107.3.
UniGeneiHs.435231.

3D structure databases

ProteinModelPortaliQ96KR1.
SMRiQ96KR1. Positions 722-1039.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119667. 52 interactions.
DIPiDIP-47293N.
IntActiQ96KR1. 15 interactions.
MINTiMINT-4655113.

PTM databases

PhosphoSiteiQ96KR1.

Polymorphism and mutation databases

BioMutaiZFR.
DMDMi162416228.

Proteomic databases

MaxQBiQ96KR1.
PaxDbiQ96KR1.
PRIDEiQ96KR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265069; ENSP00000265069; ENSG00000056097.
GeneIDi51663.
KEGGihsa:51663.
UCSCiuc003jhr.1. human.

Organism-specific databases

CTDi51663.
GeneCardsiGC05M032354.
H-InvDBHIX0004787.
HGNCiHGNC:17277. ZFR.
HPAiHPA016666.
MIMi615635. gene.
neXtProtiNX_Q96KR1.
Orphaneti401840. Autosomal recessive spastic paraplegia type 71.
PharmGKBiPA38219.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292385.
GeneTreeiENSGT00550000074528.
HOVERGENiHBG108765.
InParanoidiQ96KR1.
KOiK13203.
OMAiNNCTVNT.
OrthoDBiEOG72ZCDC.
PhylomeDBiQ96KR1.
TreeFamiTF320194.

Miscellaneous databases

ChiTaRSiZFR. human.
GenomeRNAii51663.
NextBioi55646.
PROiQ96KR1.
SOURCEiSearch...

Gene expression databases

BgeeiQ96KR1.
CleanExiHS_ZFR.
ExpressionAtlasiQ96KR1. baseline and differential.
GenevestigatoriQ96KR1.

Family and domain databases

InterProiIPR006561. DZF_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF07528. DZF. 1 hit.
[Graphical view]
SMARTiSM00572. DZF. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
SM00451. ZnF_U1. 3 hits.
[Graphical view]
PROSITEiPS51703. DZF. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the human single copy homologue of the mouse zinc finger protein zfr."
    Kleines M., Gaertner A., Ritter K., Schaade L.
    Gene 275:157-162(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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], VARIANTS ILE-461 AND THR-520.
    Tissue: Bone marrow, Duodenum, Eye, Lung and Uterus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 643-1074.
    Tissue: Pituitary.
  5. "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] OF 744-1074.
    Tissue: Hepatoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 970-1074.
    Tissue: Testis.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: 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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZFR_HUMAN
AccessioniPrimary (citable) accession number: Q96KR1
Secondary accession number(s): B2RNR5
, Q05C08, Q3B7X5, Q6P5A3, Q86UA0, Q9H6V4, Q9NTI1, Q9Y687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: April 29, 2015
This is version 107 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. 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.