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Q96P31 (FCRL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Fc receptor-like protein 3

Short name=FcR-like protein 3
Short name=FcRL3
Alternative name(s):
Fc receptor homolog 3
Short name=FcRH3
IFGP family protein 3
Short name=hIFGP3
Immune receptor translocation-associated protein 3
SH2 domain-containing phosphatase anchor protein 2
CD_antigen=CD307c
Gene names
Name:FCRL3
Synonyms:FCRH3, IFGP3, IRTA3, SPAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length734 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Interacts with PTPN6, PTPN11, SYK and ZAP70. Ref.2

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.14.

Tissue specificity

Primarily expressed in secondary lymphoid tissues by mature subsets of B-cells. Detected in spleen, lymph node, peripheral blood lymphocytes, thymus, bone marrow, kidney, salivary gland, adrenal gland and uterus. Expressed a low levels in naive, germinal center and memory B-cells but also expressed in NK cells (at protein level). Ref.1 Ref.2 Ref.8 Ref.9 Ref.14

Post-translational modification

Phosphorylated on cytoplasmic tyrosines; required for interaction with protein tyrosine phosphatases and protein tyrosine kinases. Ref.2

Involvement in disease

Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.9 Ref.15 Ref.18

Genetic variation in FCRL3 may influence susceptibility to autoimmune disorders, including Graves disease. Graves disease is an autoimmune disorder associated with overactivity of the thyroid gland and hyperthyroidism. Ref.9 Ref.15 Ref.18

Sequence similarities

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96P31-1)

Also known as: Spap2a;

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: Q96P31-2)

Also known as: Spap2b;

The sequence of this isoform differs from the canonical sequence as follows:
     187-282: ELFLHPVLRA...SLRSQIRVQR → G
Isoform 3 (identifier: Q96P31-3)

Also known as: Spap2c;

The sequence of this isoform differs from the canonical sequence as follows:
     378-378: I → TLLSPSV
Isoform 4 (identifier: Q96P31-4)

Also known as: Spap2d;

The sequence of this isoform differs from the canonical sequence as follows:
     187-189: ELF → GNG
     190-734: Missing.
Isoform 5 (identifier: Q96P31-5)

The sequence of this isoform differs from the canonical sequence as follows:
     188-199: LFLHPVLRASSS → ARCPAAILPLQR
     200-734: Missing.
Isoform 6 (identifier: Q96P31-6)

The sequence of this isoform differs from the canonical sequence as follows:
     725-734: VPRVLLASDH → ILNPRKNKVQDFPCLCNT
Note: No experimental confirmation available.
Isoform 7 (identifier: Q96P31-7)

The sequence of this isoform differs from the canonical sequence as follows:
     698-707: THPDDSAGEA → EQSSRFSMSL
     708-734: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 734717Fc receptor-like protein 3
PRO_0000331640

Regions

Topological domain18 – 573556Extracellular Potential
Transmembrane574 – 59421Helical; Potential
Topological domain595 – 734140Cytoplasmic Potential
Domain21 – 9878Ig-like C2-type 1
Domain99 – 18284Ig-like C2-type 2
Domain192 – 27079Ig-like C2-type 3
Domain284 – 36986Ig-like C2-type 4
Domain383 – 47088Ig-like C2-type 5
Domain476 – 56388Ig-like C2-type 6
Motif648 – 6536ITIM motif 1
Motif660 – 6656ITIM motif 2
Motif690 – 6956ITIM motif 3
Motif720 – 7256ITIM motif 4

Amino acid modifications

Glycosylation5611N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 82 By similarity
Disulfide bond120 ↔ 163 By similarity
Disulfide bond211 ↔ 260 By similarity
Disulfide bond309 ↔ 358 By similarity
Disulfide bond404 ↔ 451 By similarity
Disulfide bond497 ↔ 544 By similarity

Natural variations

Alternative sequence187 – 28296ELFLH…IRVQR → G in isoform 2.
VSP_033300
Alternative sequence187 – 1893ELF → GNG in isoform 4.
VSP_033301
Alternative sequence188 – 19912LFLHP…RASSS → ARCPAAILPLQR in isoform 5.
VSP_033302
Alternative sequence190 – 734545Missing in isoform 4.
VSP_033303
Alternative sequence200 – 734535Missing in isoform 5.
VSP_033304
Alternative sequence3781I → TLLSPSV in isoform 3.
VSP_033305
Alternative sequence698 – 70710THPDDSAGEA → EQSSRFSMSL in isoform 7.
VSP_033306
Alternative sequence708 – 73427Missing in isoform 7.
VSP_033307
Alternative sequence725 – 73410VPRVLLASDH → ILNPRKNKVQDFPCLCNT in isoform 6.
VSP_033308
Natural variant281N → D. Ref.3 Ref.6
Corresponds to variant rs7522061 [ dbSNP | Ensembl ].
VAR_042924
Natural variant3071L → F.
Corresponds to variant rs12041673 [ dbSNP | Ensembl ].
VAR_042925
Natural variant4451H → N in a breast cancer sample; somatic mutation. Ref.19
VAR_042926
Natural variant6601P → L.
Corresponds to variant rs944627 [ dbSNP | Ensembl ].
VAR_042927
Natural variant7211N → S.
Corresponds to variant rs2282284 [ dbSNP | Ensembl ].
VAR_042928

Experimental info

Mutagenesis6501Y → F: Loss of phosphorylation; when associated with F-662; F-692 and F-722. Alters binding with SYK and ZAP70; when associated with F-662. Ref.2
Mutagenesis6621Y → F: Loss of phosphorylation; when associated with F-650; F-692 and F-722. Alters binding with SYK and ZAP70; when associated with F-650. Ref.2
Mutagenesis6921Y → F: Loss of phosphorylation; when associated with F-650; F-662 and F-722. Alters binding with PTPN6 and PTPN11; when associated with F-772. Ref.2
Mutagenesis7221Y → F: Loss of phosphorylation; when associated with F-650; F-662 and F-692. Alters binding with PTPN6 and PTPN11; when associated with F-692. Ref.2
Sequence conflict2441R → K in AK098122. Ref.4
Sequence conflict6531V → A in AAK91779. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Spap2a) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: B3411B73A35EC668

FASTA73480,856
        10         20         30         40         50         60 
MLLWLLLLIL TPGREQSGVA PKAVLLLNPP WSTAFKGEKV ALICSSISHS LAQGDTYWYH 

        70         80         90        100        110        120 
DEKLLKIKHD KIQITEPGNY QCKTRGSSLS DAVHVEFSPD WLILQALHPV FEGDNVILRC 

       130        140        150        160        170        180 
QGKDNKNTHQ KVYYKDGKQL PNSYNLEKIT VNSVSRDNSK YHCTAYRKFY ILDIEVTSKP 

       190        200        210        220        230        240 
LNIQVQELFL HPVLRASSST PIEGSPMTLT CETQLSPQRP DVQLQFSLFR DSQTLGLGWS 

       250        260        270        280        290        300 
RSPRLQIPAM WTEDSGSYWC EVETVTHSIK KRSLRSQIRV QRVPVSNVNL EIRPTGGQLI 

       310        320        330        340        350        360 
EGENMVLICS VAQGSGTVTF SWHKEGRVRS LGRKTQRSLL AELHVLTVKE SDAGRYYCAA 

       370        380        390        400        410        420 
DNVHSPILST WIRVTVRIPV SHPVLTFRAP RAHTVVGDLL ELHCESLRGS PPILYRFYHE 

       430        440        450        460        470        480 
DVTLGNSSAP SGGGASFNLS LTAEHSGNYS CDADNGLGAQ HSHGVSLRVT VPVSRPVLTL 

       490        500        510        520        530        540 
RAPGAQAVVG DLLELHCESL RGSFPILYWF YHEDDTLGNI SAHSGGGASF NLSLTTEHSG 

       550        560        570        580        590        600 
NYSCEADNGL GAQHSKVVTL NVTGTSRNRT GLTAAGITGL VLSILVLAAA AALLHYARAR 

       610        620        630        640        650        660 
RKPGGLSATG TSSHSPSECQ EPSSSRPSRI DPQEPTHSKP LAPMELEPMY SNVNPGDSNP 

       670        680        690        700        710        720 
IYSQIWSIQH TKENSANCPM MHQEHEELTV LYSELKKTHP DDSAGEASSR GRAHEEDDEE 

       730 
NYENVPRVLL ASDH 

« Hide

Isoform 2 (Spap2b) [UniParc].

Checksum: DEAD7AD4E64CA984
Show »

FASTA63969,929
Isoform 3 (Spap2c) [UniParc].

Checksum: 038AFA83A2909E46
Show »

FASTA74081,441
Isoform 4 (Spap2d) [UniParc].

Checksum: E4A4CC249EBC65C9
Show »

FASTA18921,441
Isoform 5 [UniParc].

Checksum: D51D6112E9DA5603
Show »

FASTA19922,632
Isoform 6 [UniParc].

Checksum: B0650200E7CA19B8
Show »

FASTA74281,853
Isoform 7 [UniParc].

Checksum: AC6D131F97359E8E
Show »

FASTA70777,921

References

« Hide 'large scale' references
[1]"Identification of a family of Fc receptor homologs with preferential B cell expression."
Davis R.S., Wang Y.-H., Kubagawa H., Cooper M.D.
Proc. Natl. Acad. Sci. U.S.A. 98:9772-9777(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Lymph node.
[2]"SPAP2, an Ig family receptor containing both ITIMs and ITAMs."
Xu M.-J., Zhao R., Cao H., Zhao Z.J.
Biochem. Biophys. Res. Commun. 293:1037-1046(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), PHOSPHORYLATION, INTERACTION WITH PTPN6; PTPN11; SYK AND ZAP70, MUTAGENESIS OF TYR-650; TYR-662; TYR-692 AND TYR-722, TISSUE SPECIFICITY.
Tissue: Bone marrow.
[3]Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ASP-28.
[4]"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 7).
Tissue: Trachea.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-28.
[7]"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 6).
Tissue: Lymph.
[8]"IRTAs: a new family of immunoglobulin-like receptors differentially expressed in B cells."
Miller I., Hatzivassiliou G., Cattoretti G., Mendelsohn C., Dalla-Favera R.
Blood 99:2662-2669(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[9]"A functional variant in FCRL3, encoding Fc receptor-like 3, is associated with rheumatoid arthritis and several autoimmunities."
Kochi Y., Yamada R., Suzuki A., Harley J.B., Shirasawa S., Sawada T., Bae S.-C., Tokuhiro S., Chang X., Sekine A., Takahashi A., Tsunoda T., Ohnishi Y., Kaufman K.M., Kang C.P., Kang C., Otsubo S., Yumura W. expand/collapse author list , Mimori A., Koike T., Nakamura Y., Sasazuki T., Yamamoto K.
Nat. Genet. 37:478-485(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS AND GRAVES DISEASE, TISSUE SPECIFICITY.
[10]"Supportive evidence for a genetic association of the FCRL3 promoter polymorphism with rheumatoid arthritis."
Ikari K., Momohara S., Nakamura T., Hara M., Yamanaka H., Tomatsu T., Kamatani N.
Ann. Rheum. Dis. 65:671-673(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS.
[11]"Epistatic interaction between FCRL3 and NFkappaB1 genes in Spanish patients with rheumatoid arthritis."
Martinez A., Sanchez E., Valdivia A., Orozco G., Lopez-Nevot M.A., Pascual-Salcedo D., Balsa A., Fernandez-Gutierrez B., de la Concha E.G., Garcia-Sanchez A., Koeleman B.P.C., Urcelay E., Martin J.
Ann. Rheum. Dis. 65:1188-1191(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS.
[12]"Association of the FCRL3 gene with rheumatoid arthritis: a further example of population specificity?"
Eyre S., Bowes J., Potter C., Worthington J., Barton A.
Arthritis Res. Ther. 8:R117-R117(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS.
[13]"Rheumatoid arthritis association with the FCRL3 -169C polymorphism is restricted to PTPN22 1858T-homozygous individuals in a Canadian population."
Newman W.G., Zhang Q., Liu X., Walker E., Ternan H., Owen J., Johnson B., Greer W., Mosher D.P., Maksymowych W.P., Bykerk V.P., Keystone E.C., Amos C.I., Siminovitch K.A.
Arthritis Rheum. 54:3820-3827(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS.
[14]"Expression pattern of the human FcRH/IRTA receptors in normal tissue and in B-chronic lymphocytic leukemia."
Polson A.G., Zheng B., Elkins K., Chang W., Du C., Dowd P., Yen L., Tan C., Hongo J.-A., Koeppen H., Ebens A.
Int. Immunol. 18:1363-1373(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]"Contribution of single nucleotide polymorphisms within FCRL3 and MAP3K7IP2 to the pathogenesis of Graves' disease."
Simmonds M.J., Heward J.M., Carr-Smith J., Foxall H., Franklyn J.A., Gough S.C.L.
J. Clin. Endocrinol. Metab. 91:1056-1061(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GRAVES DISEASE.
[16]"FCRL3 promoter 169 CC homozygosity is associated with susceptibility to rheumatoid arthritis in Dutch Caucasians."
Thabet M.M., Wesoly J., Slagboom P.E., Toes R.E.M., Huizinga T.W.J.
Ann. Rheum. Dis. 66:803-806(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS.
[17]"Meta-analysis evidence of a differential risk of the FCRL3 -169T-->C polymorphism in white and East Asian rheumatoid arthritis patients."
Begovich A.B., Chang M., Schrodi S.J.
Arthritis Rheum. 56:3168-3171(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RHEUMATOID ARTHRITIS.
[18]"Association scan of 14,500 nonsynonymous SNPs in four diseases identifies autoimmunity variants."
The Wellcome Trust case control consortium, The Australo-Anglo-American spondylitis consortium
Nat. Genet. 39:1329-1337(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GRAVES DISEASE.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-445.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY043466 mRNA. Translation: AAK91779.1.
AF416901 mRNA. Translation: AAL13290.1.
AF416902 mRNA. Translation: AAL13291.1.
AF416903 mRNA. Translation: AAL13292.1.
AF416904 mRNA. Translation: AAL13293.1.
AF416905 mRNA. Translation: AAL13294.1.
EF064732 Genomic DNA. Translation: ABK41915.1.
AK098122 mRNA. No translation available.
AL356276 Genomic DNA. Translation: CAH73055.1.
AL356276 Genomic DNA. Translation: CAH73056.1.
AL356276 Genomic DNA. Translation: CAH73058.1.
CH471121 Genomic DNA. Translation: EAW52872.1.
CH471121 Genomic DNA. Translation: EAW52876.1.
CH471121 Genomic DNA. Translation: EAW52877.1.
BC028933 mRNA. Translation: AAH28933.1.
CCDSCCDS1167.1. [Q96P31-1]
RefSeqNP_443171.2. NM_052939.3. [Q96P31-1]
XP_006711208.1. XM_006711145.1. [Q96P31-1]
UniGeneHs.292449.

3D structure databases

ProteinModelPortalQ96P31.
SMRQ96P31. Positions 22-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125428. 4 interactions.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ96P31.

Polymorphism databases

DMDM74761021.

Proteomic databases

PaxDbQ96P31.
PRIDEQ96P31.

Protocols and materials databases

DNASU115352.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368184; ENSP00000357167; ENSG00000160856. [Q96P31-1]
ENST00000368186; ENSP00000357169; ENSG00000160856. [Q96P31-6]
ENST00000477837; ENSP00000433430; ENSG00000160856. [Q96P31-2]
ENST00000485028; ENSP00000434331; ENSG00000160856. [Q96P31-1]
ENST00000492769; ENSP00000435487; ENSG00000160856. [Q96P31-3]
GeneID115352.
KEGGhsa:115352.
UCSCuc001fqz.4. human. [Q96P31-6]
uc001frb.3. human. [Q96P31-1]

Organism-specific databases

CTD115352.
GeneCardsGC01M157646.
HGNCHGNC:18506. FCRL3.
HPAHPA015508.
MIM180300. phenotype.
606510. gene.
neXtProtNX_Q96P31.
PharmGKBPA142671767.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG151212.
HOVERGENHBG074073.
OMAENSANCP.
OrthoDBEOG7BP81V.
PhylomeDBQ96P31.
TreeFamTF351107.

Gene expression databases

BgeeQ96P31.
GenevestigatorQ96P31.

Family and domain databases

Gene3D2.60.40.10. 6 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
SMARTSM00409. IG. 4 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFCRL3.
GenomeRNAi115352.
NextBio79574.
PROQ96P31.
SOURCESearch...

Entry information

Entry nameFCRL3_HUMAN
AccessionPrimary (citable) accession number: Q96P31
Secondary accession number(s): A0N0M4 expand/collapse secondary AC list , A8MTH7, D3DVD2, Q5VXZ8, Q8N6S2, Q96LA4, Q96P27, Q96P28, Q96P29, Q96P30
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 109 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries