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P28799

- GRN_HUMAN

UniProt

P28799 - GRN_HUMAN

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

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
Complete GO annotation...

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
Complete GO annotation...

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.3 Publications
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. 2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 593576Acrogranin
PRO_0000012693Add
BLAST
Peptidei18 – ?4730Paragranulin
PRO_0000012694Add
BLAST
Peptidei?58 – ?11356Granulin-1
PRO_0000012695Add
BLAST
Peptidei123 – 17957Granulin-2
PRO_0000012696Add
BLAST
Peptidei206 – 26156Granulin-3
PRO_0000012697Add
BLAST
Peptidei281 – 33656Granulin-4
PRO_0000012698Add
BLAST
Peptidei364 – 41754Granulin-5
PRO_0000012699Add
BLAST
Peptidei442 – ?49655Granulin-6
PRO_0000012700Add
BLAST
Peptidei?518 – ?57356Granulin-7
PRO_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...) Reviewed prediction
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

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.

Miscellaneous databases

EvolutionaryTraceiP28799.

Family & Domainsi

Sequence similaritiesi

Belongs to the granulin family.

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

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. 2 Publications
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.
VSP_053472Add
BLAST
Alternative sequencei72 – 251180Missing in isoform 3.
VSP_053473Add
BLAST
Alternative sequencei377 – 531155Missing in isoform 2.
VSP_001837Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 159 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

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