Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28799 (GRN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

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

Names and origin

Protein namesRecommended name:
Granulins
Alternative name(s):
Proepithelin
Short name=PEPI

Cleaved into the following 9 chains:

  1. Acrogranin
    Alternative name(s):
    Glycoprotein of 88 Kda
    Progranulin
  2. Paragranulin
  3. Granulin-1
    Alternative name(s):
    Granulin G
  4. Granulin-2
    Alternative name(s):
    Granulin F
  5. Granulin-3
    Alternative name(s):
    Granulin B
  6. Granulin-4
    Alternative name(s):
    Granulin A
  7. Granulin-5
    Alternative name(s):
    Granulin C
  8. Granulin-6
    Alternative name(s):
    Granulin D
  9. Granulin-7
    Alternative name(s):
    Granulin E
Gene names
Name:GRN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Acrogranin/Progranulin is secreted as a homodimer. Ref.17

Subcellular location

Secreted.

Tissue specificity

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.

Post-translational modification

Granulins are disulfide bridged.

Involvement in disease

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. Ref.13 Ref.20 Ref.21

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. Ref.16

Sequence similarities

Belongs to the granulin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28799-1)

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.
Isoform 2 (identifier: P28799-2)

The sequence of this isoform differs from the canonical sequence as follows:
     377-531: Missing.
Isoform 3 (identifier: P28799-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 593576Acrogranin
PRO_0000012693
Peptide18 – ?4730Paragranulin
PRO_0000012694
Peptide?58 – ?11356Granulin-1
PRO_0000012695
Peptide123 – 17957Granulin-2
PRO_0000012696
Peptide206 – 26156Granulin-3
PRO_0000012697
Peptide281 – 33656Granulin-4
PRO_0000012698
Peptide364 – 41754Granulin-5
PRO_0000012699
Peptide442 – ?49655Granulin-6
PRO_0000012700
Peptide?518 – ?57356Granulin-7
PRO_0000012701

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Ref.15
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Ref.14 Ref.15
Glycosylation3681N-linked (GlcNAc...) Ref.15
Glycosylation5301N-linked (GlcNAc...) Ref.15
Disulfide bond126 ↔ 139 Ref.19
Disulfide bond133 ↔ 149 Ref.19
Disulfide bond284 ↔ 296 Ref.19
Disulfide bond290 ↔ 306 Ref.19
Disulfide bond297 ↔ 314 Ref.19
Disulfide bond307 ↔ 321 Ref.19
Disulfide bond315 ↔ 328 Ref.19
Disulfide bond322 ↔ 335 Ref.19
Disulfide bond366 ↔ 378 Ref.19
Disulfide bond372 ↔ 388 Ref.19
Disulfide bond397 ↔ 410 Ref.19
Disulfide bond404 ↔ 416 Ref.19

Natural variations

Alternative sequence1 – 7171MWTLV…CSAGH → MAITAAHGASTAVQTGDPAS KDQVTTPWVPSSALIVSSNA RTSPRAVLWSMAPGGAAPCP RLPAVKTGCTA in isoform 3.
VSP_053472
Alternative sequence72 – 251180Missing in isoform 3.
VSP_053473
Alternative sequence377 – 531155Missing in isoform 2.
VSP_001837
Natural variant91A → 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. Ref.20 Ref.21
VAR_044451
Natural variant191R → W. Ref.22
Corresponds to variant rs63750723 [ dbSNP | Ensembl ].
VAR_064625
Natural variant551R → W. Ref.22
VAR_064626
Natural variant691A → T. Ref.22
Corresponds to variant rs199944486 [ dbSNP | Ensembl ].
VAR_064627
Natural variant1191Missing. Ref.22
VAR_064628
Natural variant1201S → Y. Ref.22
VAR_064629
Natural variant1821T → M. Ref.22
Corresponds to variant rs63750479 [ dbSNP | Ensembl ].
VAR_064630
Natural variant2211C → S. Ref.22
VAR_064631
Natural variant2751P → L. Ref.22
VAR_064632
Natural variant3761D → N. Ref.22
VAR_064633
Natural variant3981S → L. Ref.22
VAR_064634
Natural variant4331R → Q. Ref.22
Corresponds to variant rs114248177 [ dbSNP | Ensembl ].
VAR_064635
Natural variant5151G → A. Ref.22
Corresponds to variant rs25647 [ dbSNP | Ensembl ].
VAR_014830
Natural variant5641R → H. Ref.22
VAR_064636

Experimental info

Sequence conflict2191S → H AA sequence Ref.11
Sequence conflict2901C → S AA sequence Ref.12
Sequence conflict3861W → H AA sequence Ref.11
Sequence conflict4281K → E in BAD96242. Ref.8
Sequence conflict4541Q → G in AAA58617. Ref.3

Secondary structure

................................. 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 2.
Checksum: 4E5947F1B4EDE619

FASTA59363,544
        10         20         30         40         50         60 
MWTLVSWVAL TAGLVAGTRC PDGQFCPVAC CLDPGGASYS CCRPLLDKWP TTLSRHLGGP 

        70         80         90        100        110        120 
CQVDAHCSAG HSCIFTVSGT SSCCPFPEAV ACGDGHHCCP RGFHCSADGR SCFQRSGNNS 

       130        140        150        160        170        180 
VGAIQCPDSQ FECPDFSTCC VMVDGSWGCC PMPQASCCED RVHCCPHGAF CDLVHTRCIT 

       190        200        210        220        230        240 
PTGTHPLAKK LPAQRTNRAV ALSSSVMCPD ARSRCPDGST CCELPSGKYG CCPMPNATCC 

       250        260        270        280        290        300 
SDHLHCCPQD TVCDLIQSKC LSKENATTDL LTKLPAHTVG DVKCDMEVSC PDGYTCCRLQ 

       310        320        330        340        350        360 
SGAWGCCPFT QAVCCEDHIH CCPAGFTCDT QKGTCEQGPH QVPWMEKAPA HLSLPDPQAL 

       370        380        390        400        410        420 
KRDVPCDNVS SCPSSDTCCQ LTSGEWGCCP IPEAVCCSDH QHCCPQGYTC VAEGQCQRGS 

       430        440        450        460        470        480 
EIVAGLEKMP ARRASLSHPR DIGCDQHTSC PVGQTCCPSL GGSWACCQLP HAVCCEDRQH 

       490        500        510        520        530        540 
CCPAGYTCNV KARSCEKEVV SAQPATFLAR SPHVGVKDVE CGEGHFCHDN QTCCRDNRQG 

       550        560        570        580        590 
WACCPYRQGV CCADRRHCCP AGFRCAARGT KCLRREAPRW DAPLRDPALR QLL 

« Hide

Isoform 2 [UniParc].

Checksum: 558B72CBAF3B991F
Show »

FASTA43846,991
Isoform 3 [UniParc].

Checksum: 0E3767A44BE314EC
Show »

FASTA41344,132

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Granulins, a novel class of peptide from leukocytes."
Bateman A., Belcourt D.R., Bennett H.P., Lazure C., Solomon S.
Biochem. Biophys. Res. Commun. 173:1161-1168(1990) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17."
Baker M., Mackenzie I.R., Pickering-Brown S.M., Gass J., Rademakers R., Lindholm C., Snowden J., Adamson J., Sadovnick A.D., Rollinson S., Cannon A., Dwosh E., Neary D., Melquist S., Richardson A., Dickson D., Berger Z., Eriksen J. expand/collapse author list , Robinson T., Zehr C., Dickey C.A., Crook R., McGowan E., Mann D., Boeve B., Feldman H., Hutton M.
Nature 442:916-919(2006) [PubMed] [Europe PMC] [Abstract]
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]"Strikingly different clinicopathological phenotypes determined by progranulin-mutation dosage."
Smith K.R., Damiano J., Franceschetti S., Carpenter S., Canafoglia L., Morbin M., Rossi G., Pareyson D., Mole S.E., Staropoli J.F., Sims K.B., Lewis J., Lin W.L., Dickson D.W., Dahl H.H., Bahlo M., Berkovic S.F.
Am. J. Hum. Genet. 90:1102-1107(2012) [PubMed] [Europe PMC] [Abstract]
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]"Molecular characterization of novel progranulin (GRN) mutations in frontotemporal dementia."
Mukherjee O., Wang J., Gitcho M., Chakraverty S., Taylor-Reinwald L., Shears S., Kauwe J.S.K., Norton J., Levitch D., Bigio E.H., Hatanpaa K.J., White C.L., Morris J.C., Cairns N.J., Goate A.
Hum. Mutat. 29:512-521(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11483.1. [P28799-1]
PIRGYHU. JC1284.
RefSeqNP_002078.1. NM_002087.2. [P28799-1]
XP_005257310.1. XM_005257253.1. [P28799-1]
UniGeneHs.514220.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G26NMR-A281-311[»]
2JYENMR-A281-337[»]
2JYTNMR-A364-417[»]
2JYUNMR-A364-417[»]
2JYVNMR-A123-179[»]
ProteinModelPortalP28799.
SMRP28799. Positions 123-154, 210-263, 281-337, 364-418, 441-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109153. 36 interactions.
DIPDIP-41742N.
IntActP28799. 42 interactions.
MINTMINT-271687.
STRING9606.ENSP00000053867.

PTM databases

PhosphoSiteP28799.

Polymorphism databases

DMDM77416865.

Proteomic databases

MaxQBP28799.
PaxDbP28799.
PRIDEP28799.

Protocols and materials databases

DNASU2896.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000053867; ENSP00000053867; ENSG00000030582. [P28799-1]
GeneID2896.
KEGGhsa:2896.
UCSCuc002igp.1. human. [P28799-1]

Organism-specific databases

CTD2896.
GeneCardsGC17P042422.
GeneReviewsGRN.
HGNCHGNC:4601. GRN.
HPACAB019394.
HPA008763.
HPA028747.
MIM138945. gene.
607485. phenotype.
614706. phenotype.
neXtProtNX_P28799.
Orphanet275864. Behavioral variant of frontotemporal dementia.
314629. CLN11 disease.
100070. Progressive non-fluent aphasia.
100069. Semantic dementia.
PharmGKBPA28998.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270518.
HOVERGENHBG000845.
InParanoidP28799.
OMACCPYPNA.
OrthoDBEOG751NF3.
PhylomeDBP28799.
TreeFamTF319678.

Gene expression databases

ArrayExpressP28799.
BgeeP28799.
CleanExHS_GRN.
GenevestigatorP28799.

Family and domain databases

InterProIPR006150. Cys_repeat_1.
IPR000118. Granulin.
[Graphical view]
PfamPF00396. Granulin. 7 hits.
[Graphical view]
SMARTSM00277. GRAN. 7 hits.
SM00289. WR1. 5 hits.
[Graphical view]
PROSITEPS00799. GRANULINS. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGRN. human.
EvolutionaryTraceP28799.
GeneWikiGranulin.
GenomeRNAi2896.
NextBio11459.
PMAP-CutDBP28799.
PROP28799.
SOURCESearch...

Entry information

Entry nameGRN_HUMAN
AccessionPrimary (citable) accession number: P28799
Secondary accession number(s): D3DX55 expand/collapse secondary AC list , P23781, P23782, P23783, P23784, Q53HQ8, Q53Y88, Q540U8, Q9BWE7, Q9H8S1, Q9UCH0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM