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P14222

- PERF_HUMAN

UniProt

P14222 - PERF_HUMAN

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Protein

Perforin-1

Gene

PRF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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 Source: UniProtKB-KW
  4. extracellular region Source: UniProtKB-KW
  5. integral component of membrane Source: UniProtKB
  6. membrane Source: UniProtKB
  7. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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.
ExpressionAtlasiP14222. baseline and differential.
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.
GeneTreeiENSGT00530000063725.
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

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

SGAVW
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00530000063725.
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.
ExpressionAtlasi P14222. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 158 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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