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Q86UX7 (URP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fermitin family homolog 3
Alternative name(s):
Kindlin-3
MIG2-like protein
Unc-112-related protein 2
Gene names
Name:FERMT3
Synonyms:KIND3, MIG2B, URP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.9 Ref.10 Ref.11

Isoform 2 may act as a repressor of NF-kappa-B and apoptosis. Ref.5 Ref.9 Ref.10 Ref.11

Subunit structure

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

Subcellular location

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. Ref.4

Tissue specificity

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. Ref.1 Ref.4

Domain

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

Involvement in disease

Leukocyte adhesion deficiency 3 (LAD3) [MIM:612840]: A disorder characterized by recurrent bacterial infections without pus formation, leukocytosis and major bleeding disorders.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the kindlin family.

Contains 1 FERM domain.

Contains 1 PH domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86UX7-1)

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.
Isoform 2 (identifier: Q86UX7-2)

Also known as: Short; URP2SF;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 667667Fermitin family homolog 3
PRO_0000219454

Regions

Domain229 – 558330FERM
Domain354 – 457104PH
Compositional bias147 – 1559Poly-Lys

Amino acid modifications

Modified residue111Phosphotyrosine Ref.7 Ref.12
Modified residue5041Phosphotyrosine Ref.12

Natural variations

Alternative sequence360 – 3634Missing in isoform 2.
VSP_009226

Experimental info

Sequence conflict4721A → P in BAC04220. Ref.2
Sequence conflict4801Q → R in BAC04220. Ref.2

Secondary structure

..................... 667
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (URP2LF) [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5ACE15EB689B91B5

FASTA66775,953
        10         20         30         40         50         60 
MAGMKTASGD YIDSSWELRV FVGEEDPEAE SVTLRVTGES HIGGVLLKIV EQINRKQDWS 

        70         80         90        100        110        120 
DHAIWWEQKR QWLLQTHWTL DKYGILADAR LFFGPQHRPV ILRLPNRRAL RLRASFSQPL 

       130        140        150        160        170        180 
FQAVAAICRL LSIRHPEELS LLRAPEKKEK KKKEKEPEEE LYDLSKVVLA GGVAPALFRG 

       190        200        210        220        230        240 
MPAHFSDSAQ TEACYHMLSR PQPPPDPLLL QRLPRPSSLS DKTQLHSRWL DSSRCLMQQG 

       250        260        270        280        290        300 
IKAGDALWLR FKYYSFFDLD PKTDPVRLTQ LYEQARWDLL LEEIDCTEEE MMVFAALQYH 

       310        320        330        340        350        360 
INKLSQSGEV GEPAGTDPGL DDLDVALSNL EVKLEGSAPT DVLDSLTTIP ELKDHLRIFR 

       370        380        390        400        410        420 
IPRRPRKLTL KGYRQHWVVF KETTLSYYKS QDEAPGDPIQ QLNLKGCEVV PDVNVSGQKF 

       430        440        450        460        470        480 
CIKLLVPSPE GMSEIYLRCQ DEQQYARWMA GCRLASKGRT MADSSYTSEV QAILAFLSLQ 

       490        500        510        520        530        540 
RTGSGGPGNH PHGPDASAEG LNPYGLVAPR FQRKFKAKQL TPRILEAHQN VAQLSLAEAQ 

       550        560        570        580        590        600 
LRFIQAWQSL PDFGISYVMV RFKGSRKDEI LGIANNRLIR IDLAVGDVVK TWRFSNMRQW 

       610        620        630        640        650        660 
NVNWDIRQVA IEFDEHINVA FSCVSASCRI VHEYIGGYIF LSTRERARGE ELDEDLFLQL 


TGGHEAF 

« Hide

Isoform 2 (Short) (URP2SF) [UniParc].

Checksum: 243CA27636C67079
Show »

FASTA66375,430

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Kindlin-3: a new gene involved in the pathogenesis of LAD-III."
Mory A., Feigelson S.W., Yarali N., Kilic S.S., Bayhan G.I., Gershoni-Baruch R., Etzioni A., Alon R.
Blood 112:2591-2591(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LAD3.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"LAD-1/variant syndrome is caused by mutations in FERMT3."
Kuijpers T.W., van de Vijver E., Weterman M.A.J., de Boer M., Tool A.T.J., van den Berg T.K., Moser M., Jakobs M.E., Seeger K., Sanal O., Uenal S., Cetin M., Roos D., Verhoeven A.J., Baas F.
Blood 113:4740-4746(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8059.1. [Q86UX7-2]
CCDS8060.1. [Q86UX7-1]
RefSeqNP_113659.3. NM_031471.5. [Q86UX7-2]
NP_848537.1. NM_178443.2. [Q86UX7-1]
XP_006718766.1. XM_006718703.1. [Q86UX7-2]
UniGeneHs.180535.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YS3NMR-A349-482[»]
ProteinModelPortalQ86UX7.
SMRQ86UX7. Positions 7-98, 342-480, 488-639.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123735. 8 interactions.
IntActQ86UX7. 6 interactions.
STRING9606.ENSP00000279227.

PTM databases

PhosphoSiteQ86UX7.

Polymorphism databases

DMDM41018464.

Proteomic databases

MaxQBQ86UX7.
PaxDbQ86UX7.
PRIDEQ86UX7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279227; ENSP00000279227; ENSG00000149781. [Q86UX7-1]
ENST00000345728; ENSP00000339950; ENSG00000149781. [Q86UX7-2]
GeneID83706.
KEGGhsa:83706.
UCSCuc001nyl.2. human. [Q86UX7-1]
uc001nym.2. human. [Q86UX7-2]

Organism-specific databases

CTD83706.
GeneCardsGC11P063975.
HGNCHGNC:23151. FERMT3.
HPAHPA053416.
MIM607901. gene.
612840. phenotype.
neXtProtNX_Q86UX7.
Orphanet99844. Leukocyte adhesion deficiency type III.
PharmGKBPA162388384.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277845.
HOGENOMHOG000231715.
HOVERGENHBG020688.
InParanoidQ86UX7.
KOK17084.
OMAEMMLFGA.
OrthoDBEOG7T7GSC.
PhylomeDBQ86UX7.
TreeFamTF314677.

Gene expression databases

ArrayExpressQ86UX7.
BgeeQ86UX7.
CleanExHS_FERMT3.
GenevestigatorQ86UX7.

Family and domain databases

Gene3D1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 2 hits.
PROSITEPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ86UX7.
GeneWikiFERMT3.
GenomeRNAi83706.
NextBio72692.
PMAP-CutDBQ86UX7.
PROQ86UX7.
SOURCESearch...

Entry information

Entry nameURP2_HUMAN
AccessionPrimary (citable) accession number: Q86UX7
Secondary accession number(s): Q8IUA1, Q8N207, Q9BT48
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM