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Protein

Lymphocyte antigen 75

Gene

Ly75

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. Causes reduced proliferation of B lymphocytes (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphocyte antigen 75
Short name:
Ly-75
Alternative name(s):
DEC-205
CD_antigen: CD205
Gene namesi
Name:Ly75
Synonyms:Cd205
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:106662. Ly75.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 16671640ExtracellularSequence analysisAdd
BLAST
Transmembranei1668 – 169225HelicalSequence analysisAdd
BLAST
Topological domaini1693 – 172331CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27272 PublicationsAdd
BLAST
Chaini28 – 17231696Lymphocyte antigen 75PRO_0000017554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi169 ↔ 194By similarity
Disulfide bondi183 ↔ 209By similarity
Disulfide bondi247 ↔ 340By similarity
Disulfide bondi317 ↔ 332By similarity
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi389 ↔ 485By similarity
Disulfide bondi462 ↔ 477By similarity
Glycosylationi529 – 5291N-linked (GlcNAc...)1 Publication
Disulfide bondi597 ↔ 614By similarity
Disulfide bondi678 ↔ 790By similarity
Disulfide bondi752 ↔ 782By similarity
Glycosylationi843 – 8431N-linked (GlcNAc...)Sequence analysis
Glycosylationi865 – 8651N-linked (GlcNAc...)2 Publications
Modified residuei934 – 9341PhosphotyrosineBy similarity
Glycosylationi935 – 9351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1061 ↔ 1081By similarity
Glycosylationi1077 – 10771N-linked (GlcNAc...)1 Publication
Glycosylationi1104 – 11041N-linked (GlcNAc...)1 Publication
Disulfide bondi1198 ↔ 1212By similarity
Glycosylationi1226 – 12261N-linked (GlcNAc...)Sequence analysis
Glycosylationi1321 – 13211N-linked (GlcNAc...)Sequence analysis
Glycosylationi1393 – 13931N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1489 ↔ 1503By similarity
Glycosylationi1594 – 15941N-linked (GlcNAc...)Sequence analysis
Glycosylationi1627 – 16271N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1636 ↔ 1651By similarity
Modified residuei1704 – 17041PhosphoserineCombined sources
Modified residuei1720 – 17201PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ60767.
MaxQBiQ60767.
PaxDbiQ60767.
PRIDEiQ60767.

PTM databases

iPTMnetiQ60767.
PhosphoSiteiQ60767.

Expressioni

Tissue specificityi

Expressed in dendritic and thymic epithelial cells and lymph nodes.2 Publications

Gene expression databases

BgeeiQ60767.
CleanExiMM_LY75.
ExpressionAtlasiQ60767. baseline and differential.

Interactioni

Protein-protein interaction databases

IntActiQ60767. 1 interaction.
MINTiMINT-4100766.
STRINGi10090.ENSMUSP00000028362.

Structurei

3D structure databases

ProteinModelPortaliQ60767.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 182150Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini164 – 21148Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Domaini225 – 341117C-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 486119C-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Domaini493 – 625133C-type lectin 3PROSITE-ProRule annotationAdd
BLAST
Domaini652 – 791140C-type lectin 4PROSITE-ProRule annotationAdd
BLAST
Domaini959 – 1092134C-type lectin 5PROSITE-ProRule annotationAdd
BLAST
Domaini1111 – 1223113C-type lectin 6PROSITE-ProRule annotationAdd
BLAST
Domaini1252 – 1375124C-type lectin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1402 – 1514113C-type lectin 8PROSITE-ProRule annotationAdd
BLAST
Domaini1543 – 1662120C-type lectin 9PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 9 C-type lectin domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000232050.
HOVERGENiHBG045579.
InParanoidiQ60767.
KOiK06559.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 10 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 9 hits.
[Graphical view]
SMARTiSM00034. CLECT. 10 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 10 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 2 hits.
PS50041. C_TYPE_LECTIN_2. 9 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTGRVTPGL AAGLLLLLLR SFGLVEPSES SGNDPFTIVH ENTGKCIQPL
60 70 80 90 100
SDWVVAQDCS GTNNMLWKWV SQHRLFHLES QKCLGLDITK ATDNLRMFSC
110 120 130 140 150
DSTVMLWWKC EHHSLYTAAQ YRLALKDGYA VANTNTSDVW KKGGSEENLC
160 170 180 190 200
AQPYHEIYTR DGNSYGRPCE FPFLIGETWY HDCIHDEDHS GPWCATTLSY
210 220 230 240 250
EYDQKWGICL LPESGCEGNW EKNEQIGSCY QFNNQEILSW KEAYVSCQNQ
260 270 280 290 300
GADLLSIHSA AELAYITGKE DIARLVWLGL NQLYSARGWE WSDFRPLKFL
310 320 330 340 350
NWDPGTPVAP VIGGSSCARM DTESGLWQSV SCESQQPYVC KKPLNNTLEL
360 370 380 390 400
PDVWTYTDTH CHVGWLPNNG FCYLLANESS SWDAAHLKCK AFGADLISMH
410 420 430 440 450
SLADVEVVVT KLHNGDVKKE IWTGLKNTNS PALFQWSDGT EVTLTYWNEN
460 470 480 490 500
EPSVPFNKTP NCVSYLGKLG QWKVQSCEKK LRYVCKKKGE ITKDAESDKL
510 520 530 540 550
CPPDEGWKRH GETCYKIYEK EAPFGTNCNL TITSRFEQEF LNYMMKNYDK
560 570 580 590 600
SLRKYFWTGL RDPDSRGEYS WAVAQGVKQA VTFSNWNFLE PASPGGCVAM
610 620 630 640 650
STGKTLGKWE VKNCRSFRAL SICKKVSEPQ EPEEAAPKPD DPCPEGWHTF
660 670 680 690 700
PSSLSCYKVF HIERIVRKRN WEEAERFCQA LGAHLPSFSR REEIKDFVHL
710 720 730 740 750
LKDQFSGQRW LWIGLNKRSP DLQGSWQWSD RTPVSAVMME PEFQQDFDIR
760 770 780 790 800
DCAAIKVLDV PWRRVWHLYE DKDYAYWKPF ACDAKLEWVC QIPKGSTPQM
810 820 830 840 850
PDWYNPERTG IHGPPVIIEG SEYWFVADPH LNYEEAVLYC ASNHSFLATI
860 870 880 890 900
TSFTGLKAIK NKLANISGEE QKWWVKTSEN PIDRYFLGSR RRLWHHFPMT
910 920 930 940 950
FGDECLHMSA KTWLVDLSKR ADCNAKLPFI CERYNVSSLE KYSPDPAAKV
960 970 980 990 1000
QCTEKWIPFQ NKCFLKVNSG PVTFSQASGI CHSYGGTLPS VLSRGEQDFI
1010 1020 1030 1040 1050
ISLLPEMEAS LWIGLRWTAY ERINRWTDNR ELTYSNFHPL LVGRRLSIPT
1060 1070 1080 1090 1100
NFFDDESHFH CALILNLKKS PLTGTWNFTS CSERHSLSLC QKYSETEDGQ
1110 1120 1130 1140 1150
PWENTSKTVK YLNNLYKIIS KPLTWHGALK ECMKEKMRLV SITDPYQQAF
1160 1170 1180 1190 1200
LAVQATLRNS SFWIGLSSQD DELNFGWSDG KRLQFSNWAG SNEQLDDCVI
1210 1220 1230 1240 1250
LDTDGFWKTA DCDDNQPGAI CYYPGNETEE EVRALDTAKC PSPVQSTPWI
1260 1270 1280 1290 1300
PFQNSCYNFM ITNNRHKTVT PEEVQSTCEK LHSKAHSLSI RNEEENTFVV
1310 1320 1330 1340 1350
EQLLYFNYIA SWVMLGITYE NNSLMWFDKT ALSYTHWRTG RPTVKNGKFL
1360 1370 1380 1390 1400
AGLSTDGFWD IQSFNVIEET LHFYQHSISA CKIEMVDYED KHNGTLPQFI
1410 1420 1430 1440 1450
PYKDGVYSVI QKKVTWYEAL NACSQSGGEL ASVHNPNGKL FLEDIVNRDG
1460 1470 1480 1490 1500
FPLWVGLSSH DGSESSFEWS DGRAFDYVPW QSLQSPGDCV VLYPKGIWRR
1510 1520 1530 1540 1550
EKCLSVKDGA ICYKPTKDKK LIFHVKSSKC PVAKRDGPQW VQYGGHCYAS
1560 1570 1580 1590 1600
DQVLHSFSEA KQVCQELDHS ATVVTIADEN ENKFVSRLMR ENYNITMRVW
1610 1620 1630 1640 1650
LGLSQHSLDQ SWSWLDGLDV TFVKWENKTK DGDGKCSILI ASNETWRKVH
1660 1670 1680 1690 1700
CSRGYARAVC KIPLSPDYTG IAILFAVLCL LGLISLAIWF LLQRSHIRWT
1710 1720
GFSSVRYEHG TNEDEVMLPS FHD
Length:1,723
Mass (Da):197,352
Last modified:July 27, 2011 - v2
Checksum:i5FACCFE712C08B1C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511S → F AA sequence (PubMed:7553896).Curated
Sequence conflicti1283 – 12831S → P in AAA80215 (PubMed:7753172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19271 mRNA. Translation: AAA80215.1.
AF395445 mRNA. Translation: AAK81722.1.
AK049301 mRNA. Translation: BAC33668.1.
BC150734 mRNA. Translation: AAI50735.1.
CCDSiCCDS38126.1.
PIRiS58880.
RefSeqiNP_038853.2. NM_013825.3.
UniGeneiMm.2074.

Genome annotation databases

EnsembliENSMUST00000028362; ENSMUSP00000028362; ENSMUSG00000026980.
GeneIDi17076.
KEGGimmu:17076.
UCSCiuc008jud.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

DEC-205

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19271 mRNA. Translation: AAA80215.1.
AF395445 mRNA. Translation: AAK81722.1.
AK049301 mRNA. Translation: BAC33668.1.
BC150734 mRNA. Translation: AAI50735.1.
CCDSiCCDS38126.1.
PIRiS58880.
RefSeqiNP_038853.2. NM_013825.3.
UniGeneiMm.2074.

3D structure databases

ProteinModelPortaliQ60767.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60767. 1 interaction.
MINTiMINT-4100766.
STRINGi10090.ENSMUSP00000028362.

PTM databases

iPTMnetiQ60767.
PhosphoSiteiQ60767.

Proteomic databases

EPDiQ60767.
MaxQBiQ60767.
PaxDbiQ60767.
PRIDEiQ60767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028362; ENSMUSP00000028362; ENSMUSG00000026980.
GeneIDi17076.
KEGGimmu:17076.
UCSCiuc008jud.1. mouse.

Organism-specific databases

CTDi4065.
MGIiMGI:106662. Ly75.

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000232050.
HOVERGENiHBG045579.
InParanoidiQ60767.
KOiK06559.

Miscellaneous databases

NextBioi291198.
PROiQ60767.
SOURCEiSearch...

Gene expression databases

BgeeiQ60767.
CleanExiMM_LY75.
ExpressionAtlasiQ60767. baseline and differential.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 10 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 9 hits.
[Graphical view]
SMARTiSM00034. CLECT. 10 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 10 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 2 hits.
PS50041. C_TYPE_LECTIN_2. 9 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing."
    Jiang W., Swiggard W.J., Heufler C., Peng M., Mirza A., Steinman R.M., Nussenzweig M.C.
    Nature 375:151-155(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, GLYCOSYLATION.
    Strain: BALB/cJ.
    Tissue: Dendritic cell and Thymus.
  2. Park C.G., Steinman R.M.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Spleen.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-485.
    Strain: C57BL/6J.
  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].
    Tissue: Brain.
  5. "DEC-205, a 205-kDa protein abundant on mouse dendritic cells and thymic epithelium that is detected by the monoclonal antibody NLDC-145: purification, characterization, and N-terminal amino acid sequence."
    Swiggard W.J., Mirza A., Nussenzweig M.C., Steinman R.M.
    Cell. Immunol. 165:302-311(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-52, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    Strain: BALB/cJ.
    Tissue: Thymus.
  6. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-865.
    Tissue: Myoblast.
  7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-529; ASN-865; ASN-1077 AND ASN-1104.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1704 AND SER-1720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiLY75_MOUSE
AccessioniPrimary (citable) accession number: Q60767
Secondary accession number(s): B2RWW5
, Q8C7T3, Q91XL8, Q9QUZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.