Skip Header

Contribute Send feedback
Read comments (?) or add your own

P48960 (CD97_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD97 antigen
Alternative name(s):
Leukocyte antigen CD97
CD_antigen=CD97

Cleaved into the following 2 chains:

  1. CD97 antigen subunit alpha
  2. CD97 antigen subunit beta
Gene names
Name:CD97
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length835 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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 1) interacts with chondroitin sulfate. Ref.10 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein.

CD97 antigen subunit alpha: Secretedextracellular space.

Tissue specificity

Broadly expressed, found on most hematopoietic cells, including activated lymphocytes, monocytes, macrophages, dendritic cells, and granulocytes. Expressed also abundantly by smooth muscle cells. Expressed in thyroid, colorectal, gastric, esophageal and pancreatic carcinomas too. Expression are increased under inflammatory conditions in the CNS of multiple sclerosis and in synovial tissue of patients with rheumatoid arthritis. Increased expression of CD97 in the synovium is accompanied by detectable levels of soluble CD97 in the synovial fluid.

Induction

Rapid up-regulation during lymphocyte activation.

Domain

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.

Binding to chondroitin sulfate is mediated by the fourth EGF domain.

Post-translational modification

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

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 5 EGF-like domains.

Contains 1 GPS domain.

Sequence caution

The sequence AAC27673.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAC06178.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48960-1)

Also known as: EGF(1,2,3,4,5);

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: P48960-2)

Also known as: EGF(1,2,5);

The sequence of this isoform differs from the canonical sequence as follows:
     116-208: Missing.
Isoform 3 (identifier: P48960-3)

Also known as: EGF(1,2,3,5);

The sequence of this isoform differs from the canonical sequence as follows:
     160-208: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 835815CD97 antigen
PRO_0000012868
Chain21 – 530510CD97 antigen subunit alpha By similarity
PRO_0000296235
Chain531 – 835305CD97 antigen subunit beta By similarity
PRO_0000296236

Regions

Topological domain21 – 552532Extracellular Potential
Transmembrane553 – 57220Helical; Name=1; Potential
Topological domain573 – 5819Cytoplasmic Potential
Transmembrane582 – 60120Helical; Name=2; Potential
Topological domain602 – 62019Extracellular Potential
Transmembrane621 – 64222Helical; Name=3; Potential
Topological domain643 – 65311Cytoplasmic Potential
Transmembrane654 – 67421Helical; Name=4; Potential
Topological domain675 – 69117Extracellular Potential
Transmembrane692 – 71221Helical; Name=5; Potential
Topological domain713 – 73927Cytoplasmic Potential
Transmembrane740 – 76021Helical; Name=6; Potential
Topological domain761 – 7666Extracellular Potential
Transmembrane767 – 78923Helical; Name=7; Potential
Topological domain790 – 83546Cytoplasmic Potential
Domain22 – 6342EGF-like 1
Domain64 – 11552EGF-like 2; calcium-binding Potential
Domain116 – 15944EGF-like 3; calcium-binding Potential
Domain160 – 20849EGF-like 4; calcium-binding Potential
Domain209 – 25749EGF-like 5; calcium-binding Potential
Domain492 – 54251GPS

Sites

Site530 – 5312Cleavage By similarity

Amino acid modifications

Modified residue8311Phosphoserine Ref.17
Modified residue8331Phosphoserine Ref.17
Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Ref.16
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Ref.15
Glycosylation5201N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 36 By similarity
Disulfide bond30 ↔ 42 By similarity
Disulfide bond44 ↔ 62 By similarity
Disulfide bond68 ↔ 82 By similarity
Disulfide bond76 ↔ 91 By similarity
Disulfide bond93 ↔ 114 By similarity
Disulfide bond120 ↔ 133 By similarity
Disulfide bond127 ↔ 142 By similarity
Disulfide bond144 ↔ 158 By similarity
Disulfide bond164 ↔ 177 By similarity
Disulfide bond171 ↔ 186 By similarity
Disulfide bond188 ↔ 207 By similarity
Disulfide bond213 ↔ 226 By similarity
Disulfide bond220 ↔ 235 By similarity
Disulfide bond237 ↔ 256 By similarity

Natural variations

Alternative sequence116 – 20893Missing in isoform 2.
VSP_009411
Alternative sequence160 – 20849Missing in isoform 3.
VSP_009412
Natural variant3671R → Q.
Corresponds to variant rs2230748 [ dbSNP | Ensembl ].
VAR_017760

Experimental info

Sequence conflict1031A → T in AAB36682. Ref.4
Sequence conflict5121G → V Ref.1
Sequence conflict5121G → V Ref.2
Sequence conflict5341A → T Ref.1
Sequence conflict5341A → T Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (EGF(1,2,3,4,5)) [UniParc].

Last modified March 21, 2006. Version 4.
Checksum: 06DDDE9178BC494B

FASTA83591,869
        10         20         30         40         50         60 
MGGRVFLAFC VWLTLPGAET QDSRGCARWC PQNSSCVNAT ACRCNPGFSS FSEIITTPTE 

        70         80         90        100        110        120 
TCDDINECAT PSKVSCGKFS DCWNTEGSYD CVCSPGYEPV SGAKTFKNES ENTCQDVDEC 

       130        140        150        160        170        180 
QQNPRLCKSY GTCVNTLGSY TCQCLPGFKF IPEDPKVCTD VNECTSGQNP CHSSTHCLNN 

       190        200        210        220        230        240 
VGSYQCRCRP GWQPIPGSPN GPNNTVCEDV DECSSGQHQC DSSTVCFNTV GSYSCRCRPG 

       250        260        270        280        290        300 
WKPRHGIPNN QKDTVCEDMT FSTWTPPPGV HSQTLSRFFD KVQDLGRDSK TSSAEVTIQN 

       310        320        330        340        350        360 
VIKLVDELME APGDVEALAP PVRHLIATQL LSNLEDIMRI LAKSLPKGPF TYISPSNTEL 

       370        380        390        400        410        420 
TLMIQERGDK NVTMGQSSAR MKLNWAVAAG AEDPGPAVAG ILSIQNMTTL LANASLNLHS 

       430        440        450        460        470        480 
KKQAELEEIY ESSIRGVQLR RLSAVNSIFL SHNNTKELNS PILFAFSHLE SSDGEAGRDP 

       490        500        510        520        530        540 
PAKDVMPGPR QELLCAFWKS DSDRGGHWAT EGCQVLGSKN GSTTCQCSHL SSFAILMAHY 

       550        560        570        580        590        600 
DVEDWKLTLI TRVGLALSLF CLLLCILTFL LVRPIQGSRT TIHLHLCICL FVGSTIFLAG 

       610        620        630        640        650        660 
IENEGGQVGL RCRLVAGLLH YCFLAAFCWM SLEGLELYFL VVRVFQGQGL STRWLCLIGY 

       670        680        690        700        710        720 
GVPLLIVGVS AAIYSKGYGR PRYCWLDFEQ GFLWSFLGPV TFIILCNAVI FVTTVWKLTQ 

       730        740        750        760        770        780 
KFSEINPDMK KLKKARALTI TAIAQLFLLG CTWVFGLFIF DDRSLVLTYV FTILNCLQGA 

       790        800        810        820        830 
FLYLLHCLLN KKVREEYRKW ACLVAGGSKY SEFTSTTSGT GHNQTRALRA SESGI 

« Hide

Isoform 2 (EGF(1,2,5)) [UniParc].

Checksum: C98F20493CA3E482
Show »

FASTA74281,743
Isoform 3 (EGF(1,2,3,5)) [UniParc].

Checksum: 03982263B73EFA2A
Show »

FASTA78686,628

References

« Hide 'large scale' references
[1]"Expression cloning and chromosomal mapping of the leukocyte activation antigen CD97, a new seven-span transmembrane molecule of the secretion receptor superfamily with an unusual extracellular domain."
Hamann J., Eichler W., Hamann D., Kerstens H.M.J., Poddighe P.J., Hoovers J.M.N., Hartmann J.M., Strauss M., van Lier R.A.W.
J. Immunol. 155:1942-1950(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Structure of the human CD97 gene: exon shuffling has generated a new type of seven-span transmembrane molecule related to the secretin receptor superfamily."
Hamann J., Hartmann E., van Lier R.A.W.
Genomics 32:144-147(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Foreskin.
[3]Hamann J.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"CD97 is a processed, seven-transmembrane, heterodimeric receptor associated with inflammation."
Gray J.X., Haino M., Roth M.J., Maguire J.E., Jensen P.N., Yarme A., Stetler-Stevenson M.-A., Siebenlist U., Kelly K.
J. Immunol. 157:5438-5447(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[5]"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Placenta and Synovium.
[7]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: Colon adenocarcinoma.
[10]"Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex."
Lin H.-H., Stacey M., Saxby C., Knott V., Chaudhry Y., Evans D., Gordon S., McKnight A.J., Handford P., Lea S.
J. Biol. Chem. 276:24160-24169(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAF.
[11]"The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans."
Stacey M., Chang G.-W., Davies J.Q., Kwakkenbos M.J., Sanderson R.D., Hamann J., Gordon S., Lin H.-H.
Blood 102:2916-2924(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHONDROITIN SULFATE.
[12]"The EGF-TM7 family: a postgenomic view."
Kwakkenbos M.J., Kop E.N., Stacey M., Matmati M., Gordon S., Lin H.H., Hamann J.
Immunogenetics 55:655-666(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-453, MASS SPECTROMETRY.
Tissue: Liver.
[16]"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-371, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831 AND SER-833, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84700 mRNA. Translation: CAA59173.1.
X94630 expand/collapse EMBL AC list , X94631, X94632, X94633, Z99830, Z99831, X94634, X94635, X94636, X94637, X94638, X94639, X94640, X94641, X94642, X94643, X94644, X94645, X94646, X94647 Genomic DNA. Translation: CAA64333.1.
U76764 mRNA. Translation: AAB36682.1.
AB065966 Genomic DNA. Translation: BAC06178.1. Sequence problems.
AC005327 Genomic DNA. Translation: AAC27673.1. Sequence problems.
AK292159 mRNA. Translation: BAF84848.1.
AK314697 mRNA. Translation: BAG37246.1.
CH471106 Genomic DNA. Translation: EAW84412.1.
CH471106 Genomic DNA. Translation: EAW84413.1.
BC026690 mRNA. Translation: AAH26690.1.
IPIIPI00299412.
IPI00397229.
IPI00397230.
PIRI37225.
RefSeqNP_001020331.1. NM_001025160.2.
NP_001775.2. NM_001784.4.
NP_510966.1. NM_078481.3.
UniGeneHs.466039.

3D structure databases

ProteinModelPortalP48960.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-52292N.
IntActP48960. 3 interactions.
MINTMINT-4531069.
STRING9606.ENSP00000242786.

Protein family/group databases

MEROPSS63.002.
GPCRDBSearch...

PTM databases

PhosphoSiteP48960.

Polymorphism databases

DMDM90110013.

Proteomic databases

PaxDbP48960.
PRIDEP48960.

Protocols and materials databases

DNASU976.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242786; ENSP00000242786; ENSG00000123146.
ENST00000357355; ENSP00000349918; ENSG00000123146.
ENST00000358600; ENSP00000351413; ENSG00000123146.
GeneID976.
KEGGhsa:976.
UCSCuc002myl.3. human.
uc002mym.3. human.
uc002myn.3. human.

Organism-specific databases

CTD976.
GeneCardsGC19P014492.
HGNCHGNC:1711. CD97.
HPAHPA013707.
MIM601211. gene.
neXtProtNX_P48960.
PharmGKBPA26248.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320737.
HOVERGENHBG048917.
InParanoidP48960.
KOK08446.
OMAREEYRKW.
OrthoDBEOG45X7WF.
PhylomeDBP48960.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP48960.
CleanExHS_CD97.
GenevestigatorP48960.
GermOnlineENSG00000123146. Homo sapiens.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
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.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS_dom.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 4 hits.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSPR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.
SMARTSM00179. EGF_CA. 4 hits.
SM00303. GPS. 1 hit.
[Graphical view]
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 4 hits.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD97. human.
GenomeRNAi976.
NextBio4094.
SOURCESearch...

Entry information

Entry nameCD97_HUMAN
AccessionPrimary (citable) accession number: P48960
Secondary accession number(s): A8K7Z4 expand/collapse secondary AC list , B2RBJ9, O00718, O76101, Q8NG72, Q8TBQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: March 21, 2006
Last modified: May 1, 2013
This is version 138 of the entry and version 4 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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

Human cell differentiation molecules

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

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families