P26842 (CD27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CD27 antigen

Alternative name(s):
CD27L receptor
T-cell activation antigen CD27
T14
Tumor necrosis factor receptor superfamily member 7
CD_antigen=CD27

Gene names

Name:	CD27
Synonyms:	TNFRSF7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for CD70/CD27L. May play a role in survival of activated T-cells. May play a role in apoptosis through association with SIVA1.
Subunit structure	Homodimer. Interacts with SIVA1 and TRAF2. Ref.8 Ref.9
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Found in most T-lymphocytes.
Post-translational modification	Phosphorylated. O-glycosylated with core 1 or possibly core 8 glycans. Ref.10
Sequence similarities	Contains 3 TNFR-Cys repeats.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Non-traceable author statement PubMed 14556986. Source: UniProtKB immunoglobulin mediated immune response Non-traceable author statement PubMed 14556986. Source: UniProtKB induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptotic process Inferred from direct assay PubMed 12324477. Source: UniProtKB positive regulation of B cell differentiation Non-traceable author statement PubMed 10809378. Source: UniProtKB positive regulation of JNK cascade Inferred from sequence or structural similarity. Source: UniProtKB release of cytoplasmic sequestered NF-kappaB Non-traceable author statement PubMed 12324477. Source: UniProtKB response to ethanol Inferred from electronic annotation. Source: Compara
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular region Non-traceable author statement PubMed 12624711. Source: UniProtKB integral to plasma membrane Non-traceable author statement PubMed 12324477. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from direct assay PubMed 12324477. Source: UniProtKB transmembrane signaling receptor activity Non-traceable author statement PubMed 14556986. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIVA1	O15304	3	EBI-520729,EBI-520756

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.7
	Chain	20 – 260	241	CD27 antigen		PRO_0000034571
Regions
	Topological domain	20 – 191	172	Extracellular Potential
	Transmembrane	192 – 212	21	Helical; Potential
	Topological domain	213 – 260	48	Cytoplasmic Potential
	Repeat	26 – 63	38	TNFR-Cys 1
	Repeat	64 – 104	41	TNFR-Cys 2
	Repeat	105 – 141	37	TNFR-Cys 3
Amino acid modifications
	Modified residue	219	1	Phosphoserine Potential
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	127	1	O-linked (GalNAc...) Ref.10
	Disulfide bond	27 ↔ 39		By similarity
	Disulfide bond	40 ↔ 53		By similarity
	Disulfide bond	43 ↔ 62		By similarity
	Disulfide bond	65 ↔ 81		By similarity
	Disulfide bond	84 ↔ 96		By similarity
	Disulfide bond	87 ↔ 104		By similarity
	Disulfide bond	106 ↔ 117		By similarity
	Disulfide bond	112 ↔ 120		By similarity
Natural variations
	Natural variant	59	1	A → T. Ref.2 Ref.3 Ref.4 Corresponds to variant rs25680 [ dbSNP | Ensembl ].		VAR_016148
	Natural variant	233	1	H → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Corresponds to variant rs2532502 [ dbSNP | Ensembl ].		VAR_052348

Sequences

	Sequence		Length	Mass (Da)
	P26842 [UniParc]. Last modified November 24, 2009. Version 2. Checksum: 43C38B895B2AD4E2	FASTA	260	29,137
	10 20 30 40 50 60 MARPHPWWLC VLGTLVGLSA TPAPKSCPER HYWAQGKLCC QMCEPGTFLV KDCDQHRKAA 70 80 90 100 110 120 QCDPCIPGVS FSPDHHTRPH CESCRHCNSG LLVRNCTITA NAECACRNGW QCRDKECTEC 130 140 150 160 170 180 DPLPNPSLTA RSSQALSPHP QPTHLPYVSE MLEARTAGHM QTLADFRQLP ARTLSTHWPP 190 200 210 220 230 240 QRSLCSSDFI RILVIFSGMF LVFTLAGALF LHQRRKYRSN KGESPVEPAE PCHYSCPREE 250 260 EGSTIPIQED YRKPEPACSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The T cell activation antigen CD27 is a member of the nerve growth factor/tumor necrosis factor receptor gene family." Camerini D., Walz G., Loenen W.A.M., Borst J., Seed B. J. Immunol. 147:3165-3169(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-233. Tissue: Monocyte.
[2]	"Genomic organization and chromosomal localization of the human CD27 gene." Loenen W.A., Gravestein L.A., Beumer S., Melief C.J., Hagemeijer A., Borst J. J. Immunol. 149:3937-3943(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-59 AND ARG-233.
[3]	"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. , 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], VARIANTS THR-59 AND ARG-233. Tissue: Thymus.
[4]	NIEHS SNPs program Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-59 AND ARG-233.
[5]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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], VARIANT ARG-233. Tissue: B-cell.
[7]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-34.
[8]	"The TNF receptor family member CD27 signals to Jun N-terminal kinase via Traf-2." Gravestein L.A., Amsen D., Boes M., Calvo C.R., Kruisbeek A.M., Borst J. Eur. J. Immunol. 28:2208-2216(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF2.
[9]	"CD27, a member of the tumor necrosis factor receptor family, induces apoptosis and binds to Siva, a proapoptotic protein." Prasad K.V.S., Ao Z., Yoon Y., Wu M.X., Rizk M., Jacquot S., Schlossman S.F. Proc. Natl. Acad. Sci. U.S.A. 94:6346-6351(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIVA1. Tissue: Cervix carcinoma and Thymus.
[10]	"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD." Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-127, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63928 mRNA. Translation: AAA58411.1. AK315732 mRNA. Translation: BAG38087.1. AY504961 Genomic DNA. Translation: AAR84239.1. AC005840 Genomic DNA. No translation available. BC012160 mRNA. Translation: AAH12160.1.
IPI	IPI00002435.
PIR	A46517.
RefSeq	NP_001233.1. NM_001242.4.
UniGene	Hs.355307.
3D structure databases
ProteinModelPortal	P26842.
SMR	P26842. Positions 36-122.
ModBase	Search...
Protein-protein interaction databases
IntAct	P26842. 3 interactions.
STRING	9606.ENSP00000266557.
PTM databases
PhosphoSite	P26842.
Proteomic databases
PaxDb	P26842.
PRIDE	P26842.
Protocols and materials databases
DNASU	939.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266557; ENSP00000266557; ENSG00000139193.
GeneID	939.
KEGG	hsa:939.
UCSC	uc001qod.3. human.
Organism-specific databases
CTD	939.
GeneCards	GC12P006554.
HGNC	HGNC:11922. CD27.
HPA	CAB002420.
MIM	186711. gene.
neXtProt	NX_P26842.
PharmGKB	PA162382107.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG39674.
HOGENOM	HOG000082545.
HOVERGEN	HBG018200.
InParanoid	P26842.
KO	K05144.
OMA	PGTFLVK.
OrthoDB	EOG4CG096.
PhylomeDB	P26842.
Gene expression databases
Bgee	P26842.
CleanEx	HS_CD27.
Genevestigator	P26842.
GermOnline	ENSG00000139193. Homo sapiens.
Family and domain databases
InterPro	IPR001368. TNFR/NGFR_Cys_rich_reg. IPR022328. TNFR_7. [Graphical view]
Pfam	PF00020. TNFR_c6. 2 hits. [Graphical view]
PRINTS	PR01960. TNFACTORR7.
SMART	SM00208. TNFR. 2 hits. [Graphical view]
PROSITE	PS00652. TNFR_NGFR_1. 1 hit. PS50050. TNFR_NGFR_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CD27. human.
GenomeRNAi	939.
NextBio	3890.
PMAP-CutDB	P26842.
SOURCE	Search...

Entry information

Entry name

CD27_HUMAN

Accession

Primary (citable) accession number: P26842
Secondary accession number(s): B2RDZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.