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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 – 5142CleavageBy similarity

GO - Molecular functioni

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

Enzyme and pathway databases

ReactomeiREACT_250061. Class B/2 (Secretin family receptors).

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 1 Publication; Multi-pass membrane protein 1 Publication

Topology

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 818795CD97 antigenPRO_0000012869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 47PROSITE-ProRule annotation
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi49 ↔ 67PROSITE-ProRule annotation
Disulfide bondi73 ↔ 86PROSITE-ProRule annotation
Disulfide bondi80 ↔ 95PROSITE-ProRule annotation
Disulfide bondi97 ↔ 118PROSITE-ProRule annotation
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi169 ↔ 182PROSITE-ProRule annotation
Disulfide bondi176 ↔ 191PROSITE-ProRule annotation
Disulfide bondi193 ↔ 212PROSITE-ProRule annotation
Disulfide bondi218 ↔ 231PROSITE-ProRule annotation
Disulfide bondi225 ↔ 240PROSITE-ProRule annotation
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi242 ↔ 260PROSITE-ProRule annotation
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...)Sequence Analysis
Modified residuei814 – 8141PhosphoserineBy similarity
Modified residuei816 – 8161PhosphoserineBy 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

BgeeiQ9Z0M6.
CleanExiMM_CD97.
ExpressionAtlasiQ9Z0M6. baseline and differential.
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).By similarity

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9Z0M6.
SMRiQ9Z0M6. Positions 31-261, 531-780.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 6842EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini69 – 11951EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini165 – 21349EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini214 – 26148EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini479 – 52446GPSPROSITE-ProRule annotationAdd
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).By similarity
Binding to chondroitin sulfate is mediated by the fourth EGF domain.By similarity

Sequence similaritiesi

Contains 4 EGF-like domains.PROSITE-ProRule annotation
Contains 1 GPS domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG320737.
GeneTreeiENSGT00760000118787.
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

        10         20         30         40         50
MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK
60 70 80 90 100
PGFSSEKELI TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG
110 120 130 140 150
YKLLSGAESF VNESENTCQA SVNTGTTPVP SRIHTVTTAP GNLPEQTTTV
160 170 180 190 200
HQTQMGDSEE RTPKDVNECI SGQNHCHQST HCINKLGGYS CICRQGWKPV
210 220 230 240 250
PGSPNGPVST VCEDVDECSS GQHQCHNSTV CKNTVGSYKC HCRPGWKPTS
260 270 280 290 300
GSLRGPDTIC QEPPFPTWTL LPTAHSQTLL RFSVEVQNLL RDFNPATVNY
310 320 330 340 350
TIQKLIEAVD KLLEDPMETQ TQQVAAQLLS NLEQSLRTLA QFLPKGPFTY
360 370 380 390 400
TSPSNTELSL MVKEQDNKDV TTVHHGQTWM ELDWAVTAGA KISENGSSVA
410 420 430 440 450
GILSSPNMEK LLGNTPLNLE QRRASLEDFY GSPIPSVSLK LLSNINSVFL
460 470 480 490 500
TNTNTEKLAS NVTFKFDFTS VESIEPRHEL ICAFWKAHNG NGYWDTDGCS
510 520 530 540 550
MNGTGFCHCN HLTSFAILMA QYHVQDPRLE LITKVGLLLS LICLLLCILT
560 570 580 590 600
FLLVKPIQSS RTMVHLHLCI CLFLGSIIFL VGVENEGGEV GLRCRLVAMM
610 620 630 640 650
LHFCFLAAFC WMALEGVELY FLVVRVFQGQ GLSTWQRCLI GYGVPLLIVA
660 670 680 690 700
ISMAVVKMDG YGHATYCWLD FRKQGFLWSF SGPVAFIIFC NAAIFVITVW
710 720 730 740 750
KLTKKFSEIN PNMKKLRKAR VLTITAIAQL LVLGCTWGFG LFLFNPHSTW
760 770 780 790 800
LSYIFTLLNC LQGLFLYVML CLLNKKVREE YWKWACMVTG SKYTEFNSST
810
TGTGTSQTRA LRSSESGM
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31G → S in CAB38246. (PubMed:10744645)Curated
Sequence conflicti28 – 281S → I in CAB38246. (PubMed:10744645)Curated
Sequence conflicti320 – 3201Q → E in AAH06676. (PubMed:15489334)Curated
Sequence conflicti506 – 5061F → S in AAF67800. (PubMed:10540231)Curated
Sequence conflicti599 – 5991M → V in AAH06676. (PubMed:15489334)Curated
Sequence conflicti726 – 7261A → S(PubMed:15489334)Curated
Sequence conflicti726 – 7261A → S(PubMed:16141072)Curated
Sequence conflicti796 – 7961F → I in BAB25461. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei120 – 21394Missing in isoform 2. 3 PublicationsVSP_009413Add
BLAST
Alternative sequencei120 – 16445Missing in isoform 3. 2 PublicationsVSP_009414Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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, 531-780.
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 ENSGT00760000118787.
HOGENOMi HOG000294115.
HOVERGENi HBG048917.
InParanoidi Q9Z0M6.
KOi K08446.
OrthoDBi EOG75J0MK.
PhylomeDBi Q9Z0M6.

Enzyme and pathway databases

Reactomei REACT_250061. Class B/2 (Secretin family receptors).

Miscellaneous databases

ChiTaRSi Cd97. mouse.
NextBioi 304231.
PROi Q9Z0M6.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z0M6.
CleanExi MM_CD97.
ExpressionAtlasi Q9Z0M6. baseline and differential.
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: November 26, 2014
This is version 129 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