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P28799

- GRN_HUMAN

UniProt

P28799 - GRN_HUMAN

Protein

Granulins

Gene

GRN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling.
    Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.

    GO - Molecular functioni

    1. growth factor activity Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. blastocyst hatching Source: Ensembl
    2. cell death Source: UniProtKB-KW
    3. embryo implantation Source: Ensembl
    4. positive regulation of epithelial cell proliferation Source: Ensembl
    5. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Cytokine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Granulins
    Alternative name(s):
    Proepithelin
    Short name:
    PEPI
    Cleaved into the following 9 chains:
    Alternative name(s):
    Glycoprotein of 88 Kda
    Progranulin
    Alternative name(s):
    Granulin G
    Alternative name(s):
    Granulin F
    Alternative name(s):
    Granulin B
    Alternative name(s):
    Granulin A
    Alternative name(s):
    Granulin C
    Alternative name(s):
    Granulin D
    Alternative name(s):
    Granulin E
    Gene namesi
    Name:GRN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4601. GRN.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular membrane-bounded organelle Source: HPA
    4. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:607485]: Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91A → D in UP-FTD; no significant difference in the total mRNA between cases and controls; although the mutant protein is expressed it is not secreted and appears to be trapped within an intracellular compartment. 1 Publication
    VAR_044451
    Ceroid lipofuscinosis, neuronal, 11 (CLN11) [MIM:614706]: A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Neurodegeneration, Neuronal ceroid lipofuscinosis

    Organism-specific databases

    MIMi607485. phenotype.
    614706. phenotype.
    Orphaneti275864. Behavioral variant of frontotemporal dementia.
    314629. CLN11 disease.
    100070. Progressive non-fluent aphasia.
    100069. Semantic dementia.
    PharmGKBiPA28998.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 593576AcrograninPRO_0000012693Add
    BLAST
    Peptidei18 – ?4730ParagranulinPRO_0000012694Add
    BLAST
    Peptidei?58 – ?11356Granulin-1PRO_0000012695Add
    BLAST
    Peptidei123 – 17957Granulin-2PRO_0000012696Add
    BLAST
    Peptidei206 – 26156Granulin-3PRO_0000012697Add
    BLAST
    Peptidei281 – 33656Granulin-4PRO_0000012698Add
    BLAST
    Peptidei364 – 41754Granulin-5PRO_0000012699Add
    BLAST
    Peptidei442 – ?49655Granulin-6PRO_0000012700Add
    BLAST
    Peptidei?518 – ?57356Granulin-7PRO_0000012701Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi118 – 1181N-linked (GlcNAc...)1 Publication
    Disulfide bondi126 ↔ 1391 Publication
    Disulfide bondi133 ↔ 1491 Publication
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi265 – 2651N-linked (GlcNAc...)2 Publications
    Disulfide bondi284 ↔ 2961 Publication
    Disulfide bondi290 ↔ 3061 Publication
    Disulfide bondi297 ↔ 3141 Publication
    Disulfide bondi307 ↔ 3211 Publication
    Disulfide bondi315 ↔ 3281 Publication
    Disulfide bondi322 ↔ 3351 Publication
    Disulfide bondi366 ↔ 3781 Publication
    Glycosylationi368 – 3681N-linked (GlcNAc...)1 Publication
    Disulfide bondi372 ↔ 3881 Publication
    Disulfide bondi397 ↔ 4101 Publication
    Disulfide bondi404 ↔ 4161 Publication
    Glycosylationi530 – 5301N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Granulins are disulfide bridged.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP28799.
    PaxDbiP28799.
    PRIDEiP28799.

    PTM databases

    PhosphoSiteiP28799.

    Miscellaneous databases

    PMAP-CutDBP28799.

    Expressioni

    Tissue specificityi

    In myelogenous leukemic cell lines of promonocytic, promyelocytic, and proerythroid lineage, in fibroblasts, and very strongly in epithelial cell lines. Present in inflammatory cells and bone marrow. Highest levels in kidney.

    Gene expression databases

    ArrayExpressiP28799.
    BgeeiP28799.
    CleanExiHS_GRN.
    GenevestigatoriP28799.

    Organism-specific databases

    HPAiCAB019394.
    HPA008763.
    HPA028747.

    Interactioni

    Subunit structurei

    Acrogranin/Progranulin is secreted as a homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CACNA1AO005552EBI-747754,EBI-766279
    Hoxa1P090222EBI-747754,EBI-3957603From a different organism.
    TNFRSF1AP194384EBI-747754,EBI-299451
    TNFRSF1BP203335EBI-747754,EBI-358983

    Protein-protein interaction databases

    BioGridi109153. 36 interactions.
    DIPiDIP-41742N.
    IntActiP28799. 42 interactions.
    MINTiMINT-271687.
    STRINGi9606.ENSP00000053867.

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi137 – 1415
    Beta strandi143 – 1453
    Beta strandi147 – 1515
    Beta strandi282 – 2854
    Beta strandi288 – 2903
    Beta strandi294 – 2985
    Beta strandi304 – 3085
    Beta strandi315 – 3195
    Turni330 – 3334
    Turni367 – 3693
    Beta strandi377 – 3804
    Beta strandi382 – 3843
    Beta strandi386 – 3894
    Turni399 – 4024
    Beta strandi409 – 4113
    Turni412 – 4143
    Beta strandi415 – 4173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G26NMR-A281-311[»]
    2JYENMR-A281-337[»]
    2JYTNMR-A364-417[»]
    2JYUNMR-A364-417[»]
    2JYVNMR-A123-179[»]
    ProteinModelPortaliP28799.
    SMRiP28799. Positions 123-154, 210-263, 281-337, 364-418, 441-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28799.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the granulin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG270518.
    HOVERGENiHBG000845.
    InParanoidiP28799.
    OMAiCCPYPNA.
    OrthoDBiEOG751NF3.
    PhylomeDBiP28799.
    TreeFamiTF319678.

    Family and domain databases

    InterProiIPR006150. Cys_repeat_1.
    IPR000118. Granulin.
    [Graphical view]
    PfamiPF00396. Granulin. 7 hits.
    [Graphical view]
    SMARTiSM00277. GRAN. 7 hits.
    SM00289. WR1. 5 hits.
    [Graphical view]
    PROSITEiPS00799. GRANULINS. 7 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28799-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MWTLVSWVAL TAGLVAGTRC PDGQFCPVAC CLDPGGASYS CCRPLLDKWP    50
    TTLSRHLGGP CQVDAHCSAG HSCIFTVSGT SSCCPFPEAV ACGDGHHCCP 100
    RGFHCSADGR SCFQRSGNNS VGAIQCPDSQ FECPDFSTCC VMVDGSWGCC 150
    PMPQASCCED RVHCCPHGAF CDLVHTRCIT PTGTHPLAKK LPAQRTNRAV 200
    ALSSSVMCPD ARSRCPDGST CCELPSGKYG CCPMPNATCC SDHLHCCPQD 250
    TVCDLIQSKC LSKENATTDL LTKLPAHTVG DVKCDMEVSC PDGYTCCRLQ 300
    SGAWGCCPFT QAVCCEDHIH CCPAGFTCDT QKGTCEQGPH QVPWMEKAPA 350
    HLSLPDPQAL KRDVPCDNVS SCPSSDTCCQ LTSGEWGCCP IPEAVCCSDH 400
    QHCCPQGYTC VAEGQCQRGS EIVAGLEKMP ARRASLSHPR DIGCDQHTSC 450
    PVGQTCCPSL GGSWACCQLP HAVCCEDRQH CCPAGYTCNV KARSCEKEVV 500
    SAQPATFLAR SPHVGVKDVE CGEGHFCHDN QTCCRDNRQG WACCPYRQGV 550
    CCADRRHCCP AGFRCAARGT KCLRREAPRW DAPLRDPALR QLL 593
    Length:593
    Mass (Da):63,544
    Last modified:October 11, 2005 - v2
    Checksum:i4E5947F1B4EDE619
    GO
    Isoform 2 (identifier: P28799-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         377-531: Missing.

    Show »
    Length:438
    Mass (Da):46,991
    Checksum:i558B72CBAF3B991F
    GO
    Isoform 3 (identifier: P28799-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-71: MWTLVSWVAL...QVDAHCSAGH → MAITAAHGAS...LPAVKTGCTA
         72-251: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:413
    Mass (Da):44,132
    Checksum:i0E3767A44BE314EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti219 – 2191S → H AA sequence (PubMed:2268320)Curated
    Sequence conflicti290 – 2901C → S AA sequence (PubMed:8471426)Curated
    Sequence conflicti386 – 3861W → H AA sequence (PubMed:2268320)Curated
    Sequence conflicti428 – 4281K → E in BAD96242. 1 PublicationCurated
    Sequence conflicti454 – 4541Q → G in AAA58617. (PubMed:1542665)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91A → D in UP-FTD; no significant difference in the total mRNA between cases and controls; although the mutant protein is expressed it is not secreted and appears to be trapped within an intracellular compartment. 1 Publication
    VAR_044451
    Natural varianti19 – 191R → W.1 Publication
    Corresponds to variant rs63750723 [ dbSNP | Ensembl ].
    VAR_064625
    Natural varianti55 – 551R → W.1 Publication
    VAR_064626
    Natural varianti69 – 691A → T.1 Publication
    Corresponds to variant rs199944486 [ dbSNP | Ensembl ].
    VAR_064627
    Natural varianti119 – 1191Missing.1 Publication
    VAR_064628
    Natural varianti120 – 1201S → Y.1 Publication
    VAR_064629
    Natural varianti182 – 1821T → M.1 Publication
    Corresponds to variant rs63750479 [ dbSNP | Ensembl ].
    VAR_064630
    Natural varianti221 – 2211C → S.1 Publication
    VAR_064631
    Natural varianti275 – 2751P → L.1 Publication
    VAR_064632
    Natural varianti376 – 3761D → N.1 Publication
    VAR_064633
    Natural varianti398 – 3981S → L.1 Publication
    VAR_064634
    Natural varianti433 – 4331R → Q.1 Publication
    Corresponds to variant rs114248177 [ dbSNP | Ensembl ].
    VAR_064635
    Natural varianti515 – 5151G → A.1 Publication
    Corresponds to variant rs25647 [ dbSNP | Ensembl ].
    VAR_014830
    Natural varianti564 – 5641R → H.1 Publication
    VAR_064636

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7171MWTLV…CSAGH → MAITAAHGASTAVQTGDPAS KDQVTTPWVPSSALIVSSNA RTSPRAVLWSMAPGGAAPCP RLPAVKTGCTA in isoform 3. 1 PublicationVSP_053472Add
    BLAST
    Alternative sequencei72 – 251180Missing in isoform 3. 1 PublicationVSP_053473Add
    BLAST
    Alternative sequencei377 – 531155Missing in isoform 2. 2 PublicationsVSP_001837Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62320 mRNA. Translation: CAA44196.1.
    AF055008 mRNA. Translation: AAC09359.1.
    M75161 mRNA. Translation: AAA58617.1. Sequence problems.
    AY124489 mRNA. Translation: AAM94026.1.
    BT006844 mRNA. Translation: AAP35490.1.
    AK023348 mRNA. Translation: BAB14535.1.
    AK222522 mRNA. Translation: BAD96242.1.
    CH471178 Genomic DNA. Translation: EAW51599.1.
    CH471178 Genomic DNA. Translation: EAW51600.1.
    BC000324 mRNA. Translation: AAH00324.1.
    BC010577 mRNA. Translation: AAH10577.1.
    CCDSiCCDS11483.1. [P28799-1]
    PIRiJC1284. GYHU.
    RefSeqiNP_002078.1. NM_002087.2. [P28799-1]
    XP_005257310.1. XM_005257253.1. [P28799-1]
    UniGeneiHs.514220.

    Genome annotation databases

    EnsembliENST00000053867; ENSP00000053867; ENSG00000030582. [P28799-1]
    GeneIDi2896.
    KEGGihsa:2896.
    UCSCiuc002igp.1. human. [P28799-1]

    Polymorphism databases

    DMDMi77416865.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62320 mRNA. Translation: CAA44196.1 .
    AF055008 mRNA. Translation: AAC09359.1 .
    M75161 mRNA. Translation: AAA58617.1 . Sequence problems.
    AY124489 mRNA. Translation: AAM94026.1 .
    BT006844 mRNA. Translation: AAP35490.1 .
    AK023348 mRNA. Translation: BAB14535.1 .
    AK222522 mRNA. Translation: BAD96242.1 .
    CH471178 Genomic DNA. Translation: EAW51599.1 .
    CH471178 Genomic DNA. Translation: EAW51600.1 .
    BC000324 mRNA. Translation: AAH00324.1 .
    BC010577 mRNA. Translation: AAH10577.1 .
    CCDSi CCDS11483.1. [P28799-1 ]
    PIRi JC1284. GYHU.
    RefSeqi NP_002078.1. NM_002087.2. [P28799-1 ]
    XP_005257310.1. XM_005257253.1. [P28799-1 ]
    UniGenei Hs.514220.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G26 NMR - A 281-311 [» ]
    2JYE NMR - A 281-337 [» ]
    2JYT NMR - A 364-417 [» ]
    2JYU NMR - A 364-417 [» ]
    2JYV NMR - A 123-179 [» ]
    ProteinModelPortali P28799.
    SMRi P28799. Positions 123-154, 210-263, 281-337, 364-418, 441-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109153. 36 interactions.
    DIPi DIP-41742N.
    IntActi P28799. 42 interactions.
    MINTi MINT-271687.
    STRINGi 9606.ENSP00000053867.

    PTM databases

    PhosphoSitei P28799.

    Polymorphism databases

    DMDMi 77416865.

    Proteomic databases

    MaxQBi P28799.
    PaxDbi P28799.
    PRIDEi P28799.

    Protocols and materials databases

    DNASUi 2896.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000053867 ; ENSP00000053867 ; ENSG00000030582 . [P28799-1 ]
    GeneIDi 2896.
    KEGGi hsa:2896.
    UCSCi uc002igp.1. human. [P28799-1 ]

    Organism-specific databases

    CTDi 2896.
    GeneCardsi GC17P042422.
    GeneReviewsi GRN.
    HGNCi HGNC:4601. GRN.
    HPAi CAB019394.
    HPA008763.
    HPA028747.
    MIMi 138945. gene.
    607485. phenotype.
    614706. phenotype.
    neXtProti NX_P28799.
    Orphaneti 275864. Behavioral variant of frontotemporal dementia.
    314629. CLN11 disease.
    100070. Progressive non-fluent aphasia.
    100069. Semantic dementia.
    PharmGKBi PA28998.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270518.
    HOVERGENi HBG000845.
    InParanoidi P28799.
    OMAi CCPYPNA.
    OrthoDBi EOG751NF3.
    PhylomeDBi P28799.
    TreeFami TF319678.

    Miscellaneous databases

    ChiTaRSi GRN. human.
    EvolutionaryTracei P28799.
    GeneWikii Granulin.
    GenomeRNAii 2896.
    NextBioi 11459.
    PMAP-CutDB P28799.
    PROi P28799.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28799.
    Bgeei P28799.
    CleanExi HS_GRN.
    Genevestigatori P28799.

    Family and domain databases

    InterProi IPR006150. Cys_repeat_1.
    IPR000118. Granulin.
    [Graphical view ]
    Pfami PF00396. Granulin. 7 hits.
    [Graphical view ]
    SMARTi SM00277. GRAN. 7 hits.
    SM00289. WR1. 5 hits.
    [Graphical view ]
    PROSITEi PS00799. GRANULINS. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and chromosomal location of the human granulin gene."
      Bhandari V., Bateman A.
      Biochem. Biophys. Res. Commun. 188:57-63(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
    2. "The epithelin precursor encodes two proteins with opposing activities on epithelial cell growth."
      Plowman G.D., Green J.M., Neubauer M.G., Buckley S.D., McDonald V.L., Todaro G.J., Shoyab M.
      J. Biol. Chem. 267:13073-13078(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    3. "Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains."
      Bhandari V., Palfree R.G.E., Bateman A.
      Proc. Natl. Acad. Sci. U.S.A. 89:1715-1719(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Bone marrow.
    4. "PCDGF sequence from lambda phage human Jurkat T cell cDNA library (Clontech)."
      Lu R., Tian C., Serrero G.
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. Yu W., Gibbs R.A.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    7. "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] (ISOFORM 3).
      Tissue: Ovary.
    8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adipose tissue.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORMS 1 AND 2).
      Tissue: Cervix and Lung.
    11. Cited for: PROTEIN SEQUENCE OF 206-233; 281-336; 364-396 AND 442-447.
      Tissue: Leukocyte.
    12. "Characterisation of UGP and its relationship with beta-core fragment."
      Kardana A., Bagshawe K.D., Coles B., Read D., Taylor M.
      Br. J. Cancer 67:686-692(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 281-295.
    13. Cited for: INVOLVEMENT IN UP-FTD.
    14. "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-265.
      Tissue: Liver.
    15. "Development and application of mass spectrometric methods for the analysis of progranulin N-glycosylation."
      Songsrirote K., Li Z., Ashford D., Bateman A., Thomas-Oates J.
      J. Proteomics 73:1479-1490(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-118; ASN-265; ASN-368 AND ASN-530.
    16. Cited for: INVOLVEMENT IN CLN11.
    17. "Secreted progranulin is a homodimer and is not a component of high density lipoproteins (HDL)."
      Nguyen A.D., Nguyen T.A., Cenik B., Yu G., Herz J., Walther T.C., Davidson W.S., Farese R.V. Jr.
      J. Biol. Chem. 288:8627-8635(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    18. "Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A."
      Tolkatchev D., Ng A., Vranken W., Ni F.
      Biochemistry 39:2878-2886(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 284-311.
    19. "Structure dissection of human progranulin identifies well-folded granulin/epithelin modules with unique functional activities."
      Tolkatchev D., Malik S., Vinogradova A., Wang P., Chen Z., Xu P., Bennett H.P., Bateman A., Ni F.
      Protein Sci. 17:711-724(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 123-179; 281-337 AND 364-417, DISULFIDE BONDS.
    20. "HDDD2 is a familial frontotemporal lobar degeneration with ubiquitin-positive, tau-negative inclusions caused by a missense mutation in the signal peptide of progranulin."
      Mukherjee O., Pastor P., Cairns N.J., Chakraverty S., Kauwe J.S.K., Shears S., Behrens M.I., Budde J., Hinrichs A.L., Norton J., Levitch D., Taylor-Reinwald L., Gitcho M., Tu P.-H., Tenenholz Grinberg L., Liscic R.M., Armendariz J., Morris J.C., Goate A.M.
      Ann. Neurol. 60:314-322(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT UP-FTD ASP-9.
    21. Cited for: CHARACTERIZATION OF VARIANT UP-FTD ASP-9.
    22. "A thorough assessment of benign genetic variability in GRN and MAPT."
      Guerreiro R.J., Washecka N., Hardy J., Singleton A.
      Hum. Mutat. 31:E1126-E1140(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TRP-19; TRP-55; THR-69; ASN-119 DEL; TYR-120; MET-182; SER-221; LEU-275; ASN-376; LEU-398; GLN-433; ALA-515 AND HIS-564.

    Entry informationi

    Entry nameiGRN_HUMAN
    AccessioniPrimary (citable) accession number: P28799
    Secondary accession number(s): D3DX55
    , P23781, P23782, P23783, P23784, Q53HQ8, Q53Y88, Q540U8, Q9BWE7, Q9H8S1, Q9UCH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3