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P14222 (PERF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Perforin-1

Short name=P1
Alternative name(s):
Cytolysin
Lymphocyte pore-forming protein
Short name=PFP
Gene names
Name:PRF1
Synonyms:PFP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCytolysis
   Cellular componentCell membrane
Endosome
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Familial hemophagocytic lymphohistiocytosis
   DomainEGF-like domain
Signal
Transmembrane
Transmembrane beta strand
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic 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

transmembrane transport

Inferred from direct assay Ref.14. Source: GOC

   Cellular_componentcytolytic granule

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: Ensembl

endosome lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from direct assay Ref.14. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11911826. Source: IntAct

wide pore channel activity

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GZMBP101443EBI-724466,EBI-2505785

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 555534Perforin-1
PRO_0000023609

Regions

Domain27 – 375349MACPF
Domain376 – 40833EGF-like
Domain416 – 49883C2

Sites

Metal binding4361Calcium 1 By similarity
Metal binding4841Calcium 1 By similarity
Metal binding4861Calcium 2; via carbonyl oxygen By similarity
Metal binding4911Calcium 2 By similarity
Site2141Important for oligomerization By similarity
Site3441Important for oligomerization By similarity

Amino acid modifications

Glycosylation2051N-linked (GlcNAc...) Ref.12
Glycosylation5491N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 76 By similarity
Disulfide bond31 ↔ 73 By similarity
Disulfide bond102 ↔ 176 By similarity
Disulfide bond242 ↔ 408 By similarity
Disulfide bond377 ↔ 393 By similarity
Disulfide bond381 ↔ 395 By similarity
Disulfide bond397 ↔ 407 By similarity
Disulfide bond497 ↔ 510 By similarity
Disulfide bond525 ↔ 534 By similarity

Natural variations

Natural variant41R → H.
Corresponds to variant rs35418374 [ dbSNP | Ensembl ].
VAR_061504
Natural variant501V → M in FHL2. Ref.19
VAR_010772
Natural variant911A → V.
Corresponds to variant rs35947132 [ dbSNP | Ensembl ].
VAR_050482
Natural variant1231R → H. Ref.20
VAR_010773
Natural variant1351V → M.
Corresponds to variant rs12263572 [ dbSNP | Ensembl ].
VAR_029773
Natural variant1831V → G in FHL2. Ref.18
VAR_010744
Natural variant2241I → N in FHL2. Ref.19
VAR_010774
Natural variant2251R → W in FHL2. Ref.18
Corresponds to variant rs28933973 [ dbSNP | Ensembl ].
VAR_010745
Natural variant2521N → S in FHL2. Ref.18
Corresponds to variant rs28933375 [ dbSNP | Ensembl ].
VAR_010746
Natural variant2791C → Y in FHL2. Ref.18
VAR_010747
Natural variant2851Missing in FHL2. Ref.19
VAR_010775
Natural variant3451P → L in FHL2. Ref.18
Corresponds to variant rs28933374 [ dbSNP | Ensembl ].
VAR_010748
Natural variant4291G → E in FHL2. Ref.18
VAR_010749

Experimental info

Sequence conflict3321L → V in CAA31612. Ref.1
Sequence conflict4261G → S in CAA31612. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P14222 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: DDEDE0D1CAB7586E

FASTA55561,377
        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 

« Hide

References

« Hide '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. 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].
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. expand/collapse author list , 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. 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].
[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.
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. expand/collapse author list , 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

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.
CCDSCCDS7305.1.
PIRA37181. A45816.
RefSeqNP_001076585.1. NM_001083116.1.
NP_005032.2. NM_005041.4.
UniGeneHs.2200.

3D structure databases

ProteinModelPortalP14222.
SMRP14222. Positions 22-552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111542. 4 interactions.
DIPDIP-53288N.
IntActP14222. 4 interactions.
MINTMINT-1401322.
STRING9606.ENSP00000316746.

Chemistry

BindingDBP14222.
ChEMBLCHEMBL5480.

Polymorphism databases

DMDM129819.

Proteomic databases

PaxDbP14222.
PRIDEP14222.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373209; ENSP00000362305; ENSG00000180644.
ENST00000441259; ENSP00000398568; ENSG00000180644.
GeneID5551.
KEGGhsa:5551.
UCSCuc001jrf.4. human.

Organism-specific databases

CTD5551.
GeneCardsGC10M072357.
GeneReviewsPRF1.
HGNCHGNC:9360. PRF1.
HPACAB002436.
MIM170280. gene.
603553. phenotype.
neXtProtNX_P14222.
Orphanet540. Familial hemophagocytic lymphohistiocytosis.
391343. Fatal post-viral neurodegenerative disorder.
88. Idiopathic aplastic anemia.
PharmGKBPA33732.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39137.
HOGENOMHOG000236309.
HOVERGENHBG008168.
InParanoidP14222.
KOK07818.
OMANYGTHFI.
OrthoDBEOG7SJD49.
PhylomeDBP14222.
TreeFamTF330498.

Gene expression databases

BgeeP14222.
CleanExHS_PRF1.
GenevestigatorP14222.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR020864. MACPF.
IPR020863. MACPF_CS.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF01823. MACPF. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00457. MACPF. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPerforin.
GenomeRNAi5551.
NextBio21512.
PROP14222.
SOURCESearch...

Entry information

Entry namePERF_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 156 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM