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Q9Z0M6

- CD97_MOUSE

UniProt

Q9Z0M6 - CD97_MOUSE

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Protein
CD97 antigen
Gene
Cd97
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei513 – 5142Cleavage By similarity

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. transmembrane signaling receptor activity Source: MGI

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. neuropeptide signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiS63.036.

Names & Taxonomyi

Protein namesi
Recommended name:
CD97 antigen
Alternative name(s):
CD_antigen: CD97
Gene namesi
Name:Cd97
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1347095. Cd97.

Subcellular locationi

Cell membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 533510Extracellular Reviewed prediction
Add
BLAST
Transmembranei534 – 55421Helical; Name=1; Reviewed prediction
Add
BLAST
Topological domaini555 – 5628Cytoplasmic Reviewed prediction
Transmembranei563 – 58321Helical; Name=2; Reviewed prediction
Add
BLAST
Topological domaini584 – 60219Extracellular Reviewed prediction
Add
BLAST
Transmembranei603 – 62321Helical; Name=3; Reviewed prediction
Add
BLAST
Topological domaini624 – 63714Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei638 – 65821Helical; Name=4; Reviewed prediction
Add
BLAST
Topological domaini659 – 67921Extracellular Reviewed prediction
Add
BLAST
Transmembranei680 – 70021Helical; Name=5; Reviewed prediction
Add
BLAST
Topological domaini701 – 72323Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei724 – 74421Helical; Name=6; Reviewed prediction
Add
BLAST
Topological domaini745 – 7528Extracellular Reviewed prediction
Transmembranei753 – 77321Helical; Name=7; Reviewed prediction
Add
BLAST
Topological domaini774 – 81845Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: MGI
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 818795CD97 antigen
PRO_0000012869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 41 By similarity
Disulfide bondi35 ↔ 47 By similarity
Glycosylationi44 – 441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi49 ↔ 67 By similarity
Disulfide bondi73 ↔ 86 By similarity
Disulfide bondi80 ↔ 95 By similarity
Disulfide bondi97 ↔ 118 By similarity
Glycosylationi112 – 1121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi169 ↔ 182 By similarity
Disulfide bondi176 ↔ 191 By similarity
Disulfide bondi193 ↔ 212 By similarity
Disulfide bondi218 ↔ 231 By similarity
Disulfide bondi225 ↔ 240 By similarity
Glycosylationi227 – 2271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi242 ↔ 260 By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...)2 Publications
Glycosylationi395 – 3951N-linked (GlcNAc...)2 Publications
Glycosylationi407 – 4071N-linked (GlcNAc...); atypical2 Publications
Glycosylationi461 – 4611N-linked (GlcNAc...)1 Publication
Glycosylationi502 – 5021N-linked (GlcNAc...) Reviewed prediction
Modified residuei814 – 8141Phosphoserine By similarity
Modified residuei816 – 8161Phosphoserine By similarity

Post-translational modificationi

Proteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane subunit By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Z0M6.
PaxDbiQ9Z0M6.
PRIDEiQ9Z0M6.

PTM databases

PhosphoSiteiQ9Z0M6.

Expressioni

Tissue specificityi

Although predominantly expressed by cells of the immune system is expressed ubiquitously, with particularly high levels of expression in the lung and the thymus gland. In the spleen, expression is detected on most myeloid cells and variable portions of T-cells, B-cells and NK cells. In the bone marrow, expressed in nearly all myeloid cells, whereas little if any expression is found on erythroid cells.

Inductioni

Up-regulated during lymphocyte activation.

Gene expression databases

ArrayExpressiQ9Z0M6.
BgeeiQ9Z0M6.
CleanExiMM_CD97.
GenevestigatoriQ9Z0M6.

Interactioni

Subunit structurei

Forms a heterodimer, consisting of a large extracellular region (alpha subunit) non-covalently linked to a seven-transmembrane moiety (beta subunit). Interacts with complement decay-accelerating factor (DAF). The largest isoform (isoform 1) do not interact with DAF. Interacts also with chondroitin sulfate By similarity.1 Publication

Protein-protein interaction databases

IntActiQ9Z0M6. 1 interaction.
MINTiMINT-4090290.
STRINGi10090.ENSMUSP00000075240.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0M6.
SMRiQ9Z0M6. Positions 31-261, 557-780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6842EGF-like 1
Add
BLAST
Domaini69 – 11951EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Domaini165 – 21349EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini214 – 26148EGF-like 4; calcium-binding Reviewed prediction
Add
BLAST
Domaini479 – 52446GPS
Add
BLAST

Domaini

The first two EGF domains mediate the interaction with DAF. A third tandemly arranged EGF domain is necessary for the structural integrity of the binding region By similarity.
Binding to chondroitin sulfate is mediated by the fourth EGF domain By similarity.

Sequence similaritiesi

Contains 4 EGF-like domains.
Contains 1 GPS domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG320737.
GeneTreeiENSGT00710000106562.
HOGENOMiHOG000294115.
HOVERGENiHBG048917.
InParanoidiQ9Z0M6.
KOiK08446.
OrthoDBiEOG75J0MK.
PhylomeDBiQ9Z0M6.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR017981. GPCR_2-like.
IPR003056. GPCR_2_CD97.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 3 hits.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSiPR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 3 hits.
SM00303. GPS. 1 hit.
[Graphical view]
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 3 hits.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Z0M6-1) [UniParc]FASTAAdd to Basket

Also known as: EGF(1,2,X,3,4)

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

MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK    50
PGFSSEKELI TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG 100
YKLLSGAESF VNESENTCQA SVNTGTTPVP SRIHTVTTAP GNLPEQTTTV 150
HQTQMGDSEE RTPKDVNECI SGQNHCHQST HCINKLGGYS CICRQGWKPV 200
PGSPNGPVST VCEDVDECSS GQHQCHNSTV CKNTVGSYKC HCRPGWKPTS 250
GSLRGPDTIC QEPPFPTWTL LPTAHSQTLL RFSVEVQNLL RDFNPATVNY 300
TIQKLIEAVD KLLEDPMETQ TQQVAAQLLS NLEQSLRTLA QFLPKGPFTY 350
TSPSNTELSL MVKEQDNKDV TTVHHGQTWM ELDWAVTAGA KISENGSSVA 400
GILSSPNMEK LLGNTPLNLE QRRASLEDFY GSPIPSVSLK LLSNINSVFL 450
TNTNTEKLAS NVTFKFDFTS VESIEPRHEL ICAFWKAHNG NGYWDTDGCS 500
MNGTGFCHCN HLTSFAILMA QYHVQDPRLE LITKVGLLLS LICLLLCILT 550
FLLVKPIQSS RTMVHLHLCI CLFLGSIIFL VGVENEGGEV GLRCRLVAMM 600
LHFCFLAAFC WMALEGVELY FLVVRVFQGQ GLSTWQRCLI GYGVPLLIVA 650
ISMAVVKMDG YGHATYCWLD FRKQGFLWSF SGPVAFIIFC NAAIFVITVW 700
KLTKKFSEIN PNMKKLRKAR VLTITAIAQL LVLGCTWGFG LFLFNPHSTW 750
LSYIFTLLNC LQGLFLYVML CLLNKKVREE YWKWACMVTG SKYTEFNSST 800
TGTGTSQTRA LRSSESGM 818
Length:818
Mass (Da):90,413
Last modified:February 16, 2004 - v2
Checksum:iE59A292F2CF626C2
GO
Isoform 2 (identifier: Q9Z0M6-2) [UniParc]FASTAAdd to Basket

Also known as: EGF(1,2,4)

The sequence of this isoform differs from the canonical sequence as follows:
     120-213: Missing.

Show »
Length:724
Mass (Da):80,433
Checksum:i7DA1962863ED5A5F
GO
Isoform 3 (identifier: Q9Z0M6-3) [UniParc]FASTAAdd to Basket

Also known as: EGF(1,2,3,4)

The sequence of this isoform differs from the canonical sequence as follows:
     120-164: Missing.

Show »
Length:773
Mass (Da):85,657
Checksum:iE18D892177ECC3F9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei120 – 21394Missing in isoform 2.
VSP_009413Add
BLAST
Alternative sequencei120 – 16445Missing in isoform 3.
VSP_009414Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31G → S in CAB38246. 1 Publication
Sequence conflicti28 – 281S → I in CAB38246. 1 Publication
Sequence conflicti320 – 3201Q → E in AAH06676. 1 Publication
Sequence conflicti506 – 5061F → S in AAF67800. 1 Publication
Sequence conflicti599 – 5991M → V in AAH06676. 1 Publication
Sequence conflicti726 – 7261A → S1 Publication
Sequence conflicti726 – 7261A → S1 Publication
Sequence conflicti796 – 7961F → I in BAB25461. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18365 mRNA. Translation: CAB38246.1.
AF146344 mRNA. Translation: AAF67800.1.
BC006676 mRNA. Translation: AAH06676.1.
AK008101 mRNA. Translation: BAB25461.1.
CCDSiCCDS22461.1. [Q9Z0M6-1]
CCDS52610.1. [Q9Z0M6-2]
CCDS52611.1. [Q9Z0M6-3]
RefSeqiNP_001156501.1. NM_001163029.1.
UniGeneiMm.334648.

Genome annotation databases

EnsembliENSMUST00000002964; ENSMUSP00000002964; ENSMUSG00000002885.
GeneIDi26364.
KEGGimmu:26364.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y18365 mRNA. Translation: CAB38246.1 .
AF146344 mRNA. Translation: AAF67800.1 .
BC006676 mRNA. Translation: AAH06676.1 .
AK008101 mRNA. Translation: BAB25461.1 .
CCDSi CCDS22461.1. [Q9Z0M6-1 ]
CCDS52610.1. [Q9Z0M6-2 ]
CCDS52611.1. [Q9Z0M6-3 ]
RefSeqi NP_001156501.1. NM_001163029.1.
UniGenei Mm.334648.

3D structure databases

ProteinModelPortali Q9Z0M6.
SMRi Q9Z0M6. Positions 31-261, 557-780.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Z0M6. 1 interaction.
MINTi MINT-4090290.
STRINGi 10090.ENSMUSP00000075240.

Protein family/group databases

MEROPSi S63.036.
GPCRDBi Search...

PTM databases

PhosphoSitei Q9Z0M6.

Proteomic databases

MaxQBi Q9Z0M6.
PaxDbi Q9Z0M6.
PRIDEi Q9Z0M6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002964 ; ENSMUSP00000002964 ; ENSMUSG00000002885 .
GeneIDi 26364.
KEGGi mmu:26364.

Organism-specific databases

CTDi 976.
MGIi MGI:1347095. Cd97.

Phylogenomic databases

eggNOGi NOG320737.
GeneTreei ENSGT00710000106562.
HOGENOMi HOG000294115.
HOVERGENi HBG048917.
InParanoidi Q9Z0M6.
KOi K08446.
OrthoDBi EOG75J0MK.
PhylomeDBi Q9Z0M6.

Miscellaneous databases

ChiTaRSi CD97. mouse.
NextBioi 304231.
PROi Q9Z0M6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z0M6.
Bgeei Q9Z0M6.
CleanExi MM_CD97.
Genevestigatori Q9Z0M6.

Family and domain databases

InterProi IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR017981. GPCR_2-like.
IPR003056. GPCR_2_CD97.
IPR000832. GPCR_2_secretin-like.
IPR000203. GPS.
[Graphical view ]
Pfami PF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 3 hits.
PF01825. GPS. 1 hit.
[Graphical view ]
PRINTSi PR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 3 hits.
SM00303. GPS. 1 hit.
[Graphical view ]
PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
PS50026. EGF_3. 3 hits.
PS01187. EGF_CA. 3 hits.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
  2. "Structural characterization of mouse CD97 and study of its specific interaction with the murine decay-accelerating factor (DAF, CD55)."
    Qian Y.-M., Haino M., Kelly K., Song W.-C.
    Immunology 98:303-311(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH DAF, SUBCELLULAR LOCATION.
    Tissue: Testis.
  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).
  4. "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 607-818.
    Strain: C57BL/6J.
    Tissue: Small intestine.
  5. "The epidermal growth factor-seven transmembrane (EGF-TM7) receptor CD97 is required for neutrophil migration and host defense."
    Leemans J.C., te Velde A.A., Florquin S., Bennink R.J., de Bruin K., van Lier R.A.W., van der Poll T., Hamann J.
    J. Immunol. 172:1125-1131(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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-299; ASN-395; ASN-407 AND ASN-461.
    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-299; ASN-395 AND ASN-407.

Entry informationi

Entry nameiCD97_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0M6
Secondary accession number(s): Q923A1, Q9CVI5, Q9JLQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: July 9, 2014
This is version 126 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, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi