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P14222

- PERF_HUMAN

UniProt

P14222 - PERF_HUMAN

Protein

Perforin-1

Gene

PRF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei214 – 2141Important for oligomerizationBy similarity
    Sitei344 – 3441Important for oligomerizationBy similarity
    Metal bindingi436 – 4361Calcium 1By similarity
    Metal bindingi484 – 4841Calcium 1By similarity
    Metal bindingi486 – 4861Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi491 – 4911Calcium 2By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. wide pore channel activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cellular defense response Source: ProtInc
    3. cytolysis Source: UniProtKB
    4. defense response to tumor cell Source: UniProtKB
    5. defense response to virus Source: UniProtKB
    6. immune response to tumor cell Source: UniProtKB
    7. protein homooligomerization Source: UniProtKB
    8. transmembrane transport Source: GOC

    Keywords - Biological processi

    Cytolysis

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Perforin-1
    Short name:
    P1
    Alternative name(s):
    Cytolysin
    Lymphocyte pore-forming protein
    Short name:
    PFP
    Gene namesi
    Name:PRF1
    Synonyms:PFP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9360. PRF1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytolytic granule Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: Ensembl
    3. endosome lumen Source: UniProtKB-SubCell
    4. extracellular region Source: UniProtKB-SubCell
    5. integral component of membrane Source: UniProtKB
    6. membrane Source: UniProtKB
    7. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501V → M in FHL2. 1 Publication
    VAR_010772
    Natural varianti183 – 1831V → G in FHL2. 1 Publication
    VAR_010744
    Natural varianti224 – 2241I → N in FHL2. 1 Publication
    VAR_010774
    Natural varianti225 – 2251R → W in FHL2. 1 Publication
    Corresponds to variant rs28933973 [ dbSNP | Ensembl ].
    VAR_010745
    Natural varianti252 – 2521N → S in FHL2. 1 Publication
    Corresponds to variant rs28933375 [ dbSNP | Ensembl ].
    VAR_010746
    Natural varianti279 – 2791C → Y in FHL2. 1 Publication
    VAR_010747
    Natural varianti285 – 2851Missing in FHL2. 1 Publication
    VAR_010775
    Natural varianti345 – 3451P → L in FHL2. 1 Publication
    Corresponds to variant rs28933374 [ dbSNP | Ensembl ].
    VAR_010748
    Natural varianti429 – 4291G → E in FHL2. 1 Publication
    VAR_010749

    Keywords - Diseasei

    Disease mutation, Familial hemophagocytic lymphohistiocytosis

    Organism-specific databases

    MIMi603553. phenotype.
    Orphaneti540. Familial hemophagocytic lymphohistiocytosis.
    391343. Fatal post-viral neurodegenerative disorder.
    88. Idiopathic aplastic anemia.
    PharmGKBiPA33732.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 555534Perforin-1PRO_0000023609Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 76By similarity
    Disulfide bondi31 ↔ 73By similarity
    Disulfide bondi102 ↔ 176By similarity
    Glycosylationi205 – 2051N-linked (GlcNAc...)1 Publication
    Disulfide bondi242 ↔ 408By similarity
    Disulfide bondi377 ↔ 393By similarity
    Disulfide bondi381 ↔ 395By similarity
    Disulfide bondi397 ↔ 407By similarity
    Disulfide bondi497 ↔ 510By similarity
    Disulfide bondi525 ↔ 534By similarity
    Glycosylationi549 – 5491N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP14222.
    PRIDEiP14222.

    Expressioni

    Inductioni

    Repressed by contact with target cells.1 Publication

    Gene expression databases

    BgeeiP14222.
    CleanExiHS_PRF1.
    GenevestigatoriP14222.

    Organism-specific databases

    HPAiCAB002436.

    Interactioni

    Subunit structurei

    Monomer, as sobluble protein. Homooligomer. Oligomerization is required for pore formation.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GZMBP101443EBI-724466,EBI-2505785

    Protein-protein interaction databases

    BioGridi111542. 4 interactions.
    DIPiDIP-53288N.
    IntActiP14222. 4 interactions.
    MINTiMINT-1401322.
    STRINGi9606.ENSP00000316746.

    Structurei

    3D structure databases

    ProteinModelPortaliP14222.
    SMRiP14222. Positions 22-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 375349MACPFPROSITE-ProRule annotationAdd
    BLAST
    Domaini376 – 40833EGF-likeAdd
    BLAST
    Domaini416 – 49883C2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Belongs to the complement C6/C7/C8/C9 family.Curated
    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.Curated
    Contains 1 MACPF domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane beta strand

    Phylogenomic databases

    eggNOGiNOG39137.
    HOGENOMiHOG000236309.
    HOVERGENiHBG008168.
    InParanoidiP14222.
    KOiK07818.
    OMAiNYGTHFI.
    OrthoDBiEOG7SJD49.
    PhylomeDBiP14222.
    TreeFamiTF330498.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR020864. MACPF.
    IPR020863. MACPF_CS.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF01823. MACPF. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00457. MACPF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS00279. MACPF_1. 1 hit.
    PS51412. MACPF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14222-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAARLLLLGI LLLLLPLPVP APCHTAARSE CKRSHKFVPG AWLAGEGVDV    50
    TSLRRSGSFP VDTQRFLRPD GTCTLCENAL QEGTLQRLPL ALTNWRAQGS 100
    GCQRHVTRAK VSSTEAVARD AARSIRNDWK VGLDVTPKPT SNVHVSVAGS 150
    HSQAANFAAQ KTHQDQYSFS TDTVECRFYS FHVVHTPPLH PDFKRALGDL 200
    PHHFNASTQP AYLRLISNYG THFIRAVELG GRISALTALR TCELALEGLT 250
    DNEVEDCLTV EAQVNIGIHG SISAEAKACE EKKKKHKMTA SFHQTYRERH 300
    SEVVGGHHTS INDLLFGIQA GPEQYSAWVN SLPGSPGLVD YTLEPLHVLL 350
    DSQDPRREAL RRALSQYLTD RARWRDCSRP CPPGRQKSPR DPCQCVCHGS 400
    AVTTQDCCPR QRGLAQLEVT FIQAWGLWGD WFTATDAYVK LFFGGQELRT 450
    STVWDNNNPI WSVRLDFGDV LLATGGPLRL QVWDQDSGRD DDLLGTCDQA 500
    PKSGSHEVRC NLNHGHLKFR YHARCLPHLG GGTCLDYVPQ MLLGEPPGNR 550
    SGAVW 555
    Length:555
    Mass (Da):61,377
    Last modified:January 1, 1990 - v1
    Checksum:iDDEDE0D1CAB7586E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti332 – 3321L → V in CAA31612. (PubMed:3419519)Curated
    Sequence conflicti426 – 4261G → S in CAA31612. (PubMed:3419519)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41R → H.
    Corresponds to variant rs35418374 [ dbSNP | Ensembl ].
    VAR_061504
    Natural varianti50 – 501V → M in FHL2. 1 Publication
    VAR_010772
    Natural varianti91 – 911A → V.
    Corresponds to variant rs35947132 [ dbSNP | Ensembl ].
    VAR_050482
    Natural varianti123 – 1231R → H.1 Publication
    VAR_010773
    Natural varianti135 – 1351V → M.
    Corresponds to variant rs12263572 [ dbSNP | Ensembl ].
    VAR_029773
    Natural varianti183 – 1831V → G in FHL2. 1 Publication
    VAR_010744
    Natural varianti224 – 2241I → N in FHL2. 1 Publication
    VAR_010774
    Natural varianti225 – 2251R → W in FHL2. 1 Publication
    Corresponds to variant rs28933973 [ dbSNP | Ensembl ].
    VAR_010745
    Natural varianti252 – 2521N → S in FHL2. 1 Publication
    Corresponds to variant rs28933375 [ dbSNP | Ensembl ].
    VAR_010746
    Natural varianti279 – 2791C → Y in FHL2. 1 Publication
    VAR_010747
    Natural varianti285 – 2851Missing in FHL2. 1 Publication
    VAR_010775
    Natural varianti345 – 3451P → L in FHL2. 1 Publication
    Corresponds to variant rs28933374 [ dbSNP | Ensembl ].
    VAR_010748
    Natural varianti429 – 4291G → E in FHL2. 1 Publication
    VAR_010749

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS7305.1.
    PIRiA45816. A37181.
    RefSeqiNP_001076585.1. NM_001083116.1.
    NP_005032.2. NM_005041.4.
    UniGeneiHs.2200.

    Genome annotation databases

    EnsembliENST00000373209; ENSP00000362305; ENSG00000180644.
    ENST00000441259; ENSP00000398568; ENSG00000180644.
    GeneIDi5551.
    KEGGihsa:5551.
    UCSCiuc001jrf.4. human.

    Polymorphism databases

    DMDMi129819.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    PRF1base

    PRF1 mutation db

    Wikipedia

    Perforin entry

    Protein Spotlight

    Our hollow architecture - Issue 126 of February 2011

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS7305.1.
    PIRi A45816. A37181.
    RefSeqi NP_001076585.1. NM_001083116.1.
    NP_005032.2. NM_005041.4.
    UniGenei Hs.2200.

    3D structure databases

    ProteinModelPortali P14222.
    SMRi P14222. Positions 22-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111542. 4 interactions.
    DIPi DIP-53288N.
    IntActi P14222. 4 interactions.
    MINTi MINT-1401322.
    STRINGi 9606.ENSP00000316746.

    Chemistry

    BindingDBi P14222.
    ChEMBLi CHEMBL5480.

    Polymorphism databases

    DMDMi 129819.

    Proteomic databases

    PaxDbi P14222.
    PRIDEi P14222.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373209 ; ENSP00000362305 ; ENSG00000180644 .
    ENST00000441259 ; ENSP00000398568 ; ENSG00000180644 .
    GeneIDi 5551.
    KEGGi hsa:5551.
    UCSCi uc001jrf.4. human.

    Organism-specific databases

    CTDi 5551.
    GeneCardsi GC10M072357.
    GeneReviewsi PRF1.
    HGNCi HGNC:9360. PRF1.
    HPAi CAB002436.
    MIMi 170280. gene.
    603553. phenotype.
    neXtProti NX_P14222.
    Orphaneti 540. Familial hemophagocytic lymphohistiocytosis.
    391343. Fatal post-viral neurodegenerative disorder.
    88. Idiopathic aplastic anemia.
    PharmGKBi PA33732.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39137.
    HOGENOMi HOG000236309.
    HOVERGENi HBG008168.
    InParanoidi P14222.
    KOi K07818.
    OMAi NYGTHFI.
    OrthoDBi EOG7SJD49.
    PhylomeDBi P14222.
    TreeFami TF330498.

    Miscellaneous databases

    GeneWikii Perforin.
    GenomeRNAii 5551.
    NextBioi 21512.
    PROi P14222.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14222.
    CleanExi HS_PRF1.
    Genevestigatori P14222.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR020864. MACPF.
    IPR020863. MACPF_CS.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF01823. MACPF. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00457. MACPF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS00279. MACPF_1. 1 hit.
    PS51412. MACPF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. 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. 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. Cited for: ELECTRON MICROSCOPY OF PORE COMPLEX, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    18. Cited for: VARIANTS FHL2 GLY-183; TRP-225; SER-252; TYR-279; LEU-345 AND GLU-429.
    19. Cited for: VARIANTS FHL2 MET-50; ASN-224 AND LYS-285 DEL.
    20. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-123.

    Entry informationi

    Entry nameiPERF_HUMAN
    AccessioniPrimary (citable) accession number: P14222
    Secondary accession number(s): B2R6X4, Q59F57, Q86WX7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 157 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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