P14222 (PERF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Perforin-1
Short name=P1

Alternative name(s):
Cytolysin
Lymphocyte pore-forming protein
Short name=PFP

Gene names

Name:	PRF1
Synonyms:	PFP

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	555 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	Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17
Subunit structure	Monomer, as sobluble protein. Homooligomer. Oligomerization is required for pore formation. Ref.14 Ref.17
Subcellular location	Cytoplasmic granule lumen. Secreted. Cell membrane; Multi-pass membrane protein. Endosome lumen. Note: Stored in cytoplasmic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell. Inserts into the cell membrane of target cells and forms pores. Membrane insertion and pore formation requires a major conformation change. May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes. Ref.13 Ref.14 Ref.17
Induction	Repressed by contact with target cells. Ref.9
Domain	The C2 domain mediates calcium-dependent binding to lipid membranes. A subsequent conformation change leads to membrane insertion of beta-hairpin structures and pore formation. The pore is formed by transmembrane beta-strands. Ref.16
Post-translational modification	N-glycosylated By similarity.
Involvement in disease	Familial hemophagocytic lymphohistiocytosis 2 (FHL2) [MIM:603553]: A rare disorder characterized by immune dysregulation with hypercytokinemia, defective function of natural killer cell, and massive infiltration of several organs by activated lymphocytes and macrophages. The clinical features of the disease include fever, hepatosplenomegaly, cytopenia, and less frequently neurological abnormalities ranging from irritability and hypotonia to seizures, cranial nerve deficits and ataxia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19
Sequence similarities	Belongs to the complement C6/C7/C8/C9 family. Contains 1 C2 domain. Contains 1 EGF-like domain. Contains 1 MACPF domain.

Ontologies

Keywords
Biological process	Cytolysis
Cellular component	Cell membrane Endosome Membrane Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Familial hemophagocytic lymphohistiocytosis
Domain	EGF-like domain Signal Transmembrane Transmembrane beta strand
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement PubMed 10779745. Source: ProtInc cellular defense response Traceable author statement PubMed 10779745. Source: ProtInc cytolysis Inferred from sequence or structural similarity. Source: UniProtKB defense response to tumor cell Inferred from sequence or structural similarity. Source: UniProtKB defense response to virus Inferred from sequence or structural similarity. Source: UniProtKB immune response to tumor cell Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from direct assay Ref.14. Source: UniProtKB
Cellular_component	cytolytic granule Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: Compara endosome lumen Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from direct assay Ref.14. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB wide pore channel activity Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GZMB	P10144	3	EBI-724466,EBI-2505785

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21
	Chain	22 – 555	534	Perforin-1		PRO_0000023609
Regions
	Domain	27 – 375	349	MACPF
	Domain	376 – 408	33	EGF-like
	Domain	416 – 498	83	C2
Sites
	Metal binding	436	1	Calcium 1 By similarity
	Metal binding	484	1	Calcium 1 By similarity
	Metal binding	486	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	491	1	Calcium 2 By similarity
	Site	214	1	Important for oligomerization By similarity
	Site	344	1	Important for oligomerization By similarity
Amino acid modifications
	Glycosylation	205	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	549	1	N-linked (GlcNAc...) Potential
	Disulfide bond	23 ↔ 76		By similarity
	Disulfide bond	31 ↔ 73		By similarity
	Disulfide bond	102 ↔ 176		By similarity
	Disulfide bond	242 ↔ 408		By similarity
	Disulfide bond	377 ↔ 393		By similarity
	Disulfide bond	381 ↔ 395		By similarity
	Disulfide bond	397 ↔ 407		By similarity
	Disulfide bond	497 ↔ 510		By similarity
	Disulfide bond	525 ↔ 534		By similarity
Natural variations
	Natural variant	4	1	R → H. Corresponds to variant rs35418374 [ dbSNP | Ensembl ].		VAR_061504
	Natural variant	50	1	V → M in FHL2. Ref.19		VAR_010772
	Natural variant	91	1	A → V. Corresponds to variant rs35947132 [ dbSNP | Ensembl ].		VAR_050482
	Natural variant	123	1	R → H. Ref.20		VAR_010773
	Natural variant	135	1	V → M. Corresponds to variant rs12263572 [ dbSNP | Ensembl ].		VAR_029773
	Natural variant	183	1	V → G in FHL2. Ref.18		VAR_010744
	Natural variant	224	1	I → N in FHL2. Ref.19		VAR_010774
	Natural variant	225	1	R → W in FHL2. Ref.18 Corresponds to variant rs28933973 [ dbSNP | Ensembl ].		VAR_010745
	Natural variant	252	1	N → S in FHL2. Ref.18 Corresponds to variant rs28933375 [ dbSNP | Ensembl ].		VAR_010746
	Natural variant	279	1	C → Y in FHL2. Ref.18		VAR_010747
	Natural variant	285	1	Missing in FHL2. Ref.19		VAR_010775
	Natural variant	345	1	P → L in FHL2. Ref.18 Corresponds to variant rs28933374 [ dbSNP | Ensembl ].		VAR_010748
	Natural variant	429	1	G → E in FHL2. Ref.18		VAR_010749
Experimental info
	Sequence conflict	332	1	L → V in CAA31612. Ref.1
	Sequence conflict	426	1	G → S in CAA31612. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14222 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: DDEDE0D1CAB7586E	FASTA	555	61,377
	10 20 30 40 50 60 MAARLLLLGI LLLLLPLPVP APCHTAARSE CKRSHKFVPG AWLAGEGVDV TSLRRSGSFP 70 80 90 100 110 120 VDTQRFLRPD GTCTLCENAL QEGTLQRLPL ALTNWRAQGS GCQRHVTRAK VSSTEAVARD 130 140 150 160 170 180 AARSIRNDWK VGLDVTPKPT SNVHVSVAGS HSQAANFAAQ KTHQDQYSFS TDTVECRFYS 190 200 210 220 230 240 FHVVHTPPLH PDFKRALGDL PHHFNASTQP AYLRLISNYG THFIRAVELG GRISALTALR 250 260 270 280 290 300 TCELALEGLT DNEVEDCLTV EAQVNIGIHG SISAEAKACE EKKKKHKMTA SFHQTYRERH 310 320 330 340 350 360 SEVVGGHHTS INDLLFGIQA GPEQYSAWVN SLPGSPGLVD YTLEPLHVLL DSQDPRREAL 370 380 390 400 410 420 RRALSQYLTD RARWRDCSRP CPPGRQKSPR DPCQCVCHGS AVTTQDCCPR QRGLAQLEVT 430 440 450 460 470 480 FIQAWGLWGD WFTATDAYVK LFFGGQELRT STVWDNNNPI WSVRLDFGDV LLATGGPLRL 490 500 510 520 530 540 QVWDQDSGRD DDLLGTCDQA PKSGSHEVRC NLNHGHLKFR YHARCLPHLG GGTCLDYVPQ 550 MLLGEPPGNR SGAVW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of human perforin." Lichtenheld M.G., Olsen K.J., Lu P., Lowrey D.M., Hameed A., Hengartner H., Podack E.R. Nature 335:448-451(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Natural killer cell.
[2]	"Molecular cloning and chromosomal assignment of a human perforin (PFP) gene." Shinkai Y., Yoshida C.M., Maeda K., Kobata T., Maruyama K., Yodoi J., Yagita H., Okumura K. Immunogenetics 30:452-457(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure of the human perforin gene. A simple gene organization with interesting potential regulatory sequences." Lichtenheld M.G., Podack E.R. J. Immunol. 143:4267-4274(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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]. Tissue: Spleen.
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , 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].
[7]	"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].
[8]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-555. Tissue: Spleen.
[9]	"Target cell-induced perforin mRNA turnover in NK3.3 cells is mediated by multiple elements within the mRNA coding region." Goebel W.S., Schloemer R.H., Brahmi Z. Mol. Immunol. 33:341-349(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 520-555, INDUCTION. Tissue: Natural killer cell.
[10]	"Human autoreactive CD4+ T cell clones use perforin- or Fas/Fas ligand-mediated pathways for target cell lysis." Vergelli M., Hemmer B., Muraro P.A., Tranquill L., Biddison W.E., Sarin A., McFarland H.F., Martin R. J. Immunol. 158:2756-2761(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Perforin, Fas/Fas ligand, and TNF-alpha pathways as specific and bystander killing mechanisms of hepatitis C virus-specific human CTL." Ando K., Hiroishi K., Kaneko T., Moriyama T., Muto Y., Kayagaki N., Yagita H., Okumura K., Imawari M. J. Immunol. 158:5283-5291(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"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-205, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Perforin activates clathrin- and dynamin-dependent endocytosis, which is required for plasma membrane repair and delivery of granzyme B for granzyme-mediated apoptosis." Thiery J., Keefe D., Saffarian S., Martinvalet D., Walch M., Boucrot E., Kirchhausen T., Lieberman J. Blood 115:1582-1593(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Human perforin employs different avenues to damage membranes." Praper T., Sonnen A., Viero G., Kladnik A., Froelich C.J., Anderluh G., Dalla Serra M., Gilbert R.J. J. Biol. Chem. 286:2946-2955(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CALCIUM-DEPENDENT PORE FORMING ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, ELECTRON MICROSCOPY.
[15]	"Reciprocal granzyme/perforin-mediated death of human regulatory and responder T cells is regulated by interleukin-2 (IL-2)." Czystowska M., Strauss L., Bergmann C., Szajnik M., Rabinowich H., Whiteside T.L. J. Mol. Med. 88:577-588(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin." Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V. Jr., Tschopp J. Mol. Immunol. 27:589-602(1990) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF MEMBRANE-SPANNING DOMAIN (MSD).
[17]	"The structural basis for membrane binding and pore formation by lymphocyte perforin." Law R.H., Lukoyanova N., Voskoboinik I., Caradoc-Davies T.T., Baran K., Dunstone M.A., D'Angelo M.E., Orlova E.V., Coulibaly F., Verschoor S., Browne K.A., Ciccone A., Kuiper M.J., Bird P.I., Trapani J.A., Saibil H.R., Whisstock J.C. Nature 468:447-451(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF PORE COMPLEX, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[18]	"Perforin gene defects in familial hemophagocytic lymphohistiocytosis." Stepp S.E., Dufourcq-Lagelouse R., Le Deist F., Bhawan S., Certain S., Mathew P.A., Henter J.-I., Bennett M., Fischer A., de Saint Basile G., Kumar V. Science 286:1957-1959(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FHL2 GLY-183; TRP-225; SER-252; TYR-279; LEU-345 AND GLU-429.
[19]	"Spectrum of perforin gene mutations in familial hemophagocytic lymphohistiocytosis." Goeransdotter Ericson K., Fadeel B., Nilsson-Ardnor S., Soederhaell C., Samuelsson A., Janka G., Schneider M., Guergey A., Yalman N., Revesz T., Egeler R., Jahnukainen K., Storm-Mathiesen I., Haraldsson A., Poole J., de Saint Basile G., Nordenskjoeld M., Henter J.-I. Am. J. Hum. Genet. 68:590-597(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FHL2 MET-50; ASN-224 AND LYS-285 DEL.
[20]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-123.
+	Additional computationally mapped references.

Web resources

PRF1base

PRF1 mutation db

GeneReviews

Wikipedia

Perforin entry

Protein Spotlight

Our hollow architecture - Issue 126 of February 2011

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13224 mRNA. Translation: CAA31612.1. M28393 mRNA. Translation: AAA60065.1. M31951 Genomic DNA. Translation: AAA60167.1. AK312754 mRNA. Translation: BAG35621.1. AL355344 Genomic DNA. Translation: CAI41276.1. CH471083 Genomic DNA. Translation: EAW54407.1. BC047695 mRNA. Translation: AAH47695.2. BC063043 mRNA. Translation: AAH63043.1. AB209604 mRNA. Translation: BAD92841.1. L40557 mRNA. Translation: AAA63618.1.
IPI	IPI00293423.
PIR	A37181. A45816.
RefSeq	NP_001076585.1. NM_001083116.1. NP_005032.2. NM_005041.4.
UniGene	Hs.2200.
3D structure databases
ProteinModelPortal	P14222.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-53288N.
IntAct	P14222. 4 interactions.
MINT	MINT-1401322.
STRING	9606.ENSP00000316746.
Polymorphism databases
DMDM	129819.
Proteomic databases
PaxDb	P14222.
PRIDE	P14222.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000318971; ENSP00000316746; ENSG00000180644. ENST00000373209; ENSP00000362305; ENSG00000180644. ENST00000441259; ENSP00000398568; ENSG00000180644.
GeneID	5551.
KEGG	hsa:5551.
UCSC	uc001jrf.4. human.
Organism-specific databases
CTD	5551.
GeneCards	GC10M072357.
HGNC	HGNC:9360. PRF1.
HPA	CAB002436.
MIM	170280. gene. 603553. phenotype.
neXtProt	NX_P14222.
Orphanet	540. Familial hemophagocytic lymphohistiocytosis. 88. Idiopathic aplastic anemia.
PharmGKB	PA33732.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG39137.
HOGENOM	HOG000236309.
HOVERGEN	HBG008168.
InParanoid	P14222.
KO	K07818.
OMA	SNYGTHF.
OrthoDB	EOG42NJ0B.
PhylomeDB	P14222.
Enzyme and pathway databases
Pathway_Interaction_DB	caspase_pathway. Caspase cascade in apoptosis. cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells. il12_stat4pathway. IL12 signaling mediated by STAT4. il2_stat5pathway. IL2 signaling events mediated by STAT5. cd8tcrpathway. TCR signaling in naive CD8+ T cells.
Gene expression databases
Bgee	P14222.
CleanEx	HS_PRF1.
Genevestigator	P14222.
GermOnline	ENSG00000180644. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR020864. MACPF. IPR020863. MACPF_CS. [Graphical view]
Pfam	PF00168. C2. 1 hit. PF01823. MACPF. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. SM00457. MACPF. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. False negative. PS00279. MACPF_1. 1 hit. PS51412. MACPF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P14222.
ChEMBL	CHEMBL5480.
GenomeRNAi	5551.
NextBio	21512.
SOURCE	Search...

Entry information

Entry name

PERF_HUMAN

Accession

Primary (citable) accession number: P14222
Secondary accession number(s): B2R6X4, Q59F57, Q86WX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 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.