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Protein

Fermitin family homolog 3

Gene

FERMT3

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

Functioni

Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity).By similarity
Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.3 Publications

GO - Molecular functioni

  1. integrin binding Source: UniProtKB

GO - Biological processi

  1. integrin activation Source: UniProtKB
  2. integrin-mediated signaling pathway Source: UniProtKB
  3. leukocyte cell-cell adhesion Source: UniProtKB
  4. platelet aggregation Source: UniProtKB
  5. regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
  6. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Fermitin family homolog 3
Alternative name(s):
Kindlin-3
MIG2-like protein
Unc-112-related protein 2
Gene namesi
Name:FERMT3
Synonyms:KIND3, MIG2B, URP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:23151. FERMT3.

Subcellular locationi

Cell projectionpodosome By similarity
Note: Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection

Pathology & Biotechi

Involvement in diseasei

Leukocyte adhesion deficiency 35 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by recurrent bacterial infections without pus formation, leukocytosis and major bleeding disorders.

See also OMIM:612840

Organism-specific databases

MIMi612840. phenotype.
Orphaneti99844. Leukocyte adhesion deficiency type III.
PharmGKBiPA162388384.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667Fermitin family homolog 3PRO_0000219454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphotyrosine2 Publications
Modified residuei504 – 5041Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86UX7.
PaxDbiQ86UX7.
PRIDEiQ86UX7.

PTM databases

PhosphoSiteiQ86UX7.

Miscellaneous databases

PMAP-CutDBQ86UX7.

Expressioni

Tissue specificityi

Highly expressed in lymph node. Expressed in thymus, spleen and leukocytes. Weakly expressed in placenta, small intestine, stomach, testis and lung. Overexpressed in B-cell malignancies.2 Publications

Gene expression databases

BgeeiQ86UX7.
CleanExiHS_FERMT3.
ExpressionAtlasiQ86UX7. baseline and differential.
GenevestigatoriQ86UX7.

Interactioni

Subunit structurei

Interacts with ITGB1, ITGB2 and ITGB3 (via cytoplasmic tails).By similarity

Protein-protein interaction databases

BioGridi123735. 8 interactions.
IntActiQ86UX7. 6 interactions.
STRINGi9606.ENSP00000279227.

Structurei

Secondary structure

1
667
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi370 – 3734Combined sources
Beta strandi377 – 3804Combined sources
Beta strandi385 – 3906Combined sources
Turni391 – 3955Combined sources
Turni404 – 4063Combined sources
Beta strandi408 – 4114Combined sources
Helixi415 – 4173Combined sources
Beta strandi419 – 4279Combined sources
Beta strandi429 – 44113Combined sources
Helixi442 – 45615Combined sources
Helixi465 – 48016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YS3NMR-A349-482[»]
ProteinModelPortaliQ86UX7.
SMRiQ86UX7. Positions 7-98, 342-480, 488-639.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86UX7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini229 – 558330FERMAdd
BLAST
Domaini354 – 457104PHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 1559Poly-Lys

Domaini

The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain.

Sequence similaritiesi

Belongs to the kindlin family.Curated
Contains 1 FERM domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG277845.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiQ86UX7.
KOiK17084.
OMAiEMMLFGA.
OrthoDBiEOG7T7GSC.
PhylomeDBiQ86UX7.
TreeFamiTF314677.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
PROSITEiPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q86UX7-1) [UniParc]FASTAAdd to basket

Also known as: Long, URP2LF

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
MAGMKTASGD YIDSSWELRV FVGEEDPEAE SVTLRVTGES HIGGVLLKIV
60 70 80 90 100
EQINRKQDWS DHAIWWEQKR QWLLQTHWTL DKYGILADAR LFFGPQHRPV
110 120 130 140 150
ILRLPNRRAL RLRASFSQPL FQAVAAICRL LSIRHPEELS LLRAPEKKEK
160 170 180 190 200
KKKEKEPEEE LYDLSKVVLA GGVAPALFRG MPAHFSDSAQ TEACYHMLSR
210 220 230 240 250
PQPPPDPLLL QRLPRPSSLS DKTQLHSRWL DSSRCLMQQG IKAGDALWLR
260 270 280 290 300
FKYYSFFDLD PKTDPVRLTQ LYEQARWDLL LEEIDCTEEE MMVFAALQYH
310 320 330 340 350
INKLSQSGEV GEPAGTDPGL DDLDVALSNL EVKLEGSAPT DVLDSLTTIP
360 370 380 390 400
ELKDHLRIFR IPRRPRKLTL KGYRQHWVVF KETTLSYYKS QDEAPGDPIQ
410 420 430 440 450
QLNLKGCEVV PDVNVSGQKF CIKLLVPSPE GMSEIYLRCQ DEQQYARWMA
460 470 480 490 500
GCRLASKGRT MADSSYTSEV QAILAFLSLQ RTGSGGPGNH PHGPDASAEG
510 520 530 540 550
LNPYGLVAPR FQRKFKAKQL TPRILEAHQN VAQLSLAEAQ LRFIQAWQSL
560 570 580 590 600
PDFGISYVMV RFKGSRKDEI LGIANNRLIR IDLAVGDVVK TWRFSNMRQW
610 620 630 640 650
NVNWDIRQVA IEFDEHINVA FSCVSASCRI VHEYIGGYIF LSTRERARGE
660
ELDEDLFLQL TGGHEAF
Length:667
Mass (Da):75,953
Last modified:June 1, 2003 - v1
Checksum:i5ACE15EB689B91B5
GO
Isoform 2 (identifier: Q86UX7-2) [UniParc]FASTAAdd to basket

Also known as: Short, URP2SF

The sequence of this isoform differs from the canonical sequence as follows:
     360-363: Missing.

Show »
Length:663
Mass (Da):75,430
Checksum:i243CA27636C67079
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti472 – 4721A → P in BAC04220 (PubMed:14702039).Curated
Sequence conflicti480 – 4801Q → R in BAC04220 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei360 – 3634Missing in isoform 2. 3 PublicationsVSP_009226

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY093951 mRNA. Translation: AAM19736.1.
AY093952 mRNA. Translation: AAM19737.1.
AK093719 mRNA. Translation: BAC04220.1.
BC004347 mRNA. Translation: AAH04347.2.
BC013366 mRNA. Translation: AAH13366.1.
BC015584 mRNA. Translation: AAH15584.1.
CCDSiCCDS8059.1. [Q86UX7-2]
CCDS8060.1. [Q86UX7-1]
RefSeqiNP_113659.3. NM_031471.5. [Q86UX7-2]
NP_848537.1. NM_178443.2. [Q86UX7-1]
XP_006718766.1. XM_006718703.1. [Q86UX7-2]
UniGeneiHs.180535.

Genome annotation databases

EnsembliENST00000279227; ENSP00000279227; ENSG00000149781. [Q86UX7-1]
ENST00000345728; ENSP00000339950; ENSG00000149781. [Q86UX7-2]
GeneIDi83706.
KEGGihsa:83706.
UCSCiuc001nyl.2. human. [Q86UX7-1]
uc001nym.2. human. [Q86UX7-2]

Polymorphism databases

DMDMi41018464.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY093951 mRNA. Translation: AAM19736.1.
AY093952 mRNA. Translation: AAM19737.1.
AK093719 mRNA. Translation: BAC04220.1.
BC004347 mRNA. Translation: AAH04347.2.
BC013366 mRNA. Translation: AAH13366.1.
BC015584 mRNA. Translation: AAH15584.1.
CCDSiCCDS8059.1. [Q86UX7-2]
CCDS8060.1. [Q86UX7-1]
RefSeqiNP_113659.3. NM_031471.5. [Q86UX7-2]
NP_848537.1. NM_178443.2. [Q86UX7-1]
XP_006718766.1. XM_006718703.1. [Q86UX7-2]
UniGeneiHs.180535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YS3NMR-A349-482[»]
ProteinModelPortaliQ86UX7.
SMRiQ86UX7. Positions 7-98, 342-480, 488-639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123735. 8 interactions.
IntActiQ86UX7. 6 interactions.
STRINGi9606.ENSP00000279227.

PTM databases

PhosphoSiteiQ86UX7.

Polymorphism databases

DMDMi41018464.

Proteomic databases

MaxQBiQ86UX7.
PaxDbiQ86UX7.
PRIDEiQ86UX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279227; ENSP00000279227; ENSG00000149781. [Q86UX7-1]
ENST00000345728; ENSP00000339950; ENSG00000149781. [Q86UX7-2]
GeneIDi83706.
KEGGihsa:83706.
UCSCiuc001nyl.2. human. [Q86UX7-1]
uc001nym.2. human. [Q86UX7-2]

Organism-specific databases

CTDi83706.
GeneCardsiGC11P063975.
HGNCiHGNC:23151. FERMT3.
MIMi607901. gene.
612840. phenotype.
neXtProtiNX_Q86UX7.
Orphaneti99844. Leukocyte adhesion deficiency type III.
PharmGKBiPA162388384.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG277845.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiQ86UX7.
KOiK17084.
OMAiEMMLFGA.
OrthoDBiEOG7T7GSC.
PhylomeDBiQ86UX7.
TreeFamiTF314677.

Miscellaneous databases

EvolutionaryTraceiQ86UX7.
GeneWikiiFERMT3.
GenomeRNAii83706.
NextBioi72692.
PMAP-CutDBQ86UX7.
PROiQ86UX7.
SOURCEiSearch...

Gene expression databases

BgeeiQ86UX7.
CleanExiHS_FERMT3.
ExpressionAtlasiQ86UX7. baseline and differential.
GenevestigatoriQ86UX7.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
PROSITEiPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas."
    Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.
    Biochim. Biophys. Acta 1637:207-216(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
  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] (ISOFORM 2).
    Tissue: Thymus.
  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] (ISOFORM 2).
    Tissue: Lung and Lymph.
  4. "Proteomic analysis of the cell-surface membrane in chronic lymphocytic leukemia: identification of two novel proteins, BCNP1 and MIG2B."
    Boyd R.S., Adam P.J., Patel S., Loader J.A., Berry J., Redpath N.T., Poyser H.R., Fletcher G.C., Burgess N.A., Stamps A.C., Hudson L., Smith P., Griffiths M., Willis T.G., Karran E.L., Oscier D.G., Catovsky D., Terrett J.A., Dyer M.J.S.
    Leukemia 17:1605-1612(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-35; 424-438 AND 569-577, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and apoptosis."
    Wang L., Deng W., Shi T., Ma D.
    Biochem. Biophys. Res. Commun. 368:899-906(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION (ISOFORM 2).
  6. Cited for: INVOLVEMENT IN LAD3.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. "Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions."
    Manevich-Mendelson E., Feigelson S.W., Pasvolsky R., Aker M., Grabovsky V., Shulman Z., Kilic S.S., Rosenthal-Allieri M.A., Ben-Dor S., Mory A., Bernard A., Moser M., Etzioni A., Alon R.
    Blood 114:2344-2353(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LAD3.
  9. Cited for: INVOLVEMENT IN LAD3, FUNCTION.
  10. "Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation."
    Svensson L., Howarth K., McDowall A., Patzak I., Evans R., Ussar S., Moser M., Metin A., Fried M., Tomlinson I., Hogg N.
    Nat. Med. 15:306-312(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LAD3, FUNCTION.
  11. "A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans."
    Malinin N.L., Zhang L., Choi J., Ciocea A., Razorenova O., Ma Y.-Q., Podrez E.A., Tosi M., Lennon D.P., Caplan A.I., Shurin S.B., Plow E.F., Byzova T.V.
    Nat. Med. 15:313-318(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LAD3, FUNCTION.
  12. "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 TYR-11 AND TYR-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of the PH domain of kindlin-3 from human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 349-478.

Entry informationi

Entry nameiURP2_HUMAN
AccessioniPrimary (citable) accession number: Q86UX7
Secondary accession number(s): Q8IUA1, Q8N207, Q9BT48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2003
Last modified: March 4, 2015
This is version 117 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.