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Protein

Serglycin

Gene

SRGN

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

Functioni

Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization.3 Publications

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. blood coagulation Source: Reactome
  3. granzyme-mediated apoptotic signaling pathway Source: UniProtKB
  4. maintenance of granzyme B location in T cell secretory granule Source: UniProtKB
  5. maintenance of protease location in mast cell secretory granule Source: UniProtKB
  6. mast cell secretory granule organization Source: UniProtKB
  7. negative regulation of bone mineralization Source: UniProtKB
  8. negative regulation of cytokine secretion Source: UniProtKB
  9. platelet activation Source: Reactome
  10. platelet degranulation Source: Reactome
  11. protein processing Source: UniProtKB
  12. T cell secretory granule organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Biomineralization

Enzyme and pathway databases

ReactomeiREACT_318. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serglycin
Alternative name(s):
Hematopoietic proteoglycan core protein
Platelet proteoglycan core protein
Short name:
P.PG
Secretory granule proteoglycan core protein
Gene namesi
Name:SRGN
Synonyms:PRG, PRG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:9361. SRGN.

Subcellular locationi

  1. Cytoplasmic granule By similarity
  2. Secretedextracellular space
  3. Golgi apparatus

  4. Note: Found in mast cell granules and in cytoplasmic granules of cytolytic T lymphocytes from where it is secreted upon cell activation. Secreted constitutively by endothelial cells and macrophages. Located to Golgi apparatus during neutrophil differentiation.

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. Golgi apparatus Source: UniProtKB
  4. Golgi membrane Source: Ensembl
  5. mast cell granule Source: UniProtKB
  6. platelet alpha granule lumen Source: Reactome
  7. zymogen granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33733.

Polymorphism and mutation databases

BioMutaiSRGN.
DMDMi269849659.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27272 PublicationsAdd
BLAST
Chaini28 – 158131SerglycinPRO_0000026679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 49Sequence Analysis
Glycosylationi94 – 941O-linked (Xyl...) (glycosaminoglycan)1 Publication
Glycosylationi96 – 961O-linked (Xyl...) (glycosaminoglycan)1 Publication
Glycosylationi100 – 1001O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi102 – 1021O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi104 – 1041O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi106 – 1061O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi108 – 1081O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis
Glycosylationi110 – 1101O-linked (Xyl...) (glycosaminoglycan)Sequence Analysis

Post-translational modificationi

O-glycosylated; contains chondroitin sulfate and heparan sulfate.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

MaxQBiP10124.
PaxDbiP10124.
PRIDEiP10124.

Expressioni

Inductioni

By Epstein-Barr virus (EBV).

Gene expression databases

BgeeiP10124.
CleanExiHS_SRGN.
GenevestigatoriP10124.

Organism-specific databases

HPAiHPA000759.

Interactioni

Subunit structurei

Binds to activated CD44 and to GZMB.

Binary interactionsi

WithEntry#Exp.IntActNotes
GZMBP101442EBI-744915,EBI-2505785
SGTAO437654EBI-744915,EBI-347996
UBQLN1Q9UMX03EBI-744915,EBI-741480
UBQLN1Q9UMX0-23EBI-744915,EBI-10173939

Protein-protein interaction databases

BioGridi111543. 8 interactions.
IntActiP10124. 17 interactions.
MINTiMINT-1466608.
STRINGi9606.ENSP00000242465.

Structurei

3D structure databases

ProteinModelPortaliP10124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati94 – 9521
Repeati96 – 9722
Repeati98 – 9923
Repeati100 – 10124
Repeati102 – 10325
Repeati104 – 10526
Repeati106 – 10727
Repeati108 – 10928
Repeati110 – 11129

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 111189 X 2 AA tandem repeats of [SF]-GAdd
BLAST

Sequence similaritiesi

Belongs to the serglycin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG44969.
GeneTreeiENSGT00390000000885.
HOGENOMiHOG000154415.
HOVERGENiHBG008180.
InParanoidiP10124.
KOiK06849.
OMAiSNSANCI.
OrthoDBiEOG7J9VS0.
PhylomeDBiP10124.
TreeFamiTF336310.

Family and domain databases

InterProiIPR007455. Serglycin.
[Graphical view]
PfamiPF04360. Serglycin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10124-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQKLLKCSR LVLALALILV LESSVQGYPT RRARYQWVRC NPDSNSANCL
60 70 80 90 100
EEKGPMFELL PGESNKIPRL RTDLFPKTRI QDLNRIFPLS EDYSGSGFGS
110 120 130 140 150
GSGSGSGSGS GFLTEMEQDY QLVDESDAFH DNLRSLDRNL PSDSQDLGQH

GLEEDFML
Length:158
Mass (Da):17,652
Last modified:November 24, 2009 - v3
Checksum:iBD7767F39FFBC477
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391N → S in CAA31255 (PubMed:3402609).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311R → Q.6 Publications
Corresponds to variant rs2805910 [ dbSNP | Ensembl ].
VAR_032761

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03223 mRNA. Translation: AAA60179.1.
X17042 mRNA. Translation: CAA34900.1.
M33651, M33649, M33650 Genomic DNA. Translation: AAA60322.1.
M90058 Genomic DNA. No translation available.
AK311873 mRNA. Translation: BAG34814.1.
AL442635 Genomic DNA. Translation: CAH71778.1.
CH471083 Genomic DNA. Translation: EAW54309.1.
BC015516 mRNA. Translation: AAH15516.1.
X12765 mRNA. Translation: CAA31255.1.
CCDSiCCDS7285.1.
PIRiA35183. A28058.
RefSeqiNP_002718.2. NM_002727.2.
UniGeneiHs.1908.

Genome annotation databases

EnsembliENST00000242465; ENSP00000242465; ENSG00000122862.
GeneIDi5552.
KEGGihsa:5552.
UCSCiuc001joz.3. human.

Polymorphism and mutation databases

BioMutaiSRGN.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03223 mRNA. Translation: AAA60179.1.
X17042 mRNA. Translation: CAA34900.1.
M33651, M33649, M33650 Genomic DNA. Translation: AAA60322.1.
M90058 Genomic DNA. No translation available.
AK311873 mRNA. Translation: BAG34814.1.
AL442635 Genomic DNA. Translation: CAH71778.1.
CH471083 Genomic DNA. Translation: EAW54309.1.
BC015516 mRNA. Translation: AAH15516.1.
X12765 mRNA. Translation: CAA31255.1.
CCDSiCCDS7285.1.
PIRiA35183. A28058.
RefSeqiNP_002718.2. NM_002727.2.
UniGeneiHs.1908.

3D structure databases

ProteinModelPortaliP10124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111543. 8 interactions.
IntActiP10124. 17 interactions.
MINTiMINT-1466608.
STRINGi9606.ENSP00000242465.

Polymorphism and mutation databases

BioMutaiSRGN.
DMDMi269849659.

Proteomic databases

MaxQBiP10124.
PaxDbiP10124.
PRIDEiP10124.

Protocols and materials databases

DNASUi5552.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242465; ENSP00000242465; ENSG00000122862.
GeneIDi5552.
KEGGihsa:5552.
UCSCiuc001joz.3. human.

Organism-specific databases

CTDi5552.
GeneCardsiGC10P070847.
HGNCiHGNC:9361. SRGN.
HPAiHPA000759.
MIMi177040. gene.
neXtProtiNX_P10124.
PharmGKBiPA33733.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44969.
GeneTreeiENSGT00390000000885.
HOGENOMiHOG000154415.
HOVERGENiHBG008180.
InParanoidiP10124.
KOiK06849.
OMAiSNSANCI.
OrthoDBiEOG7J9VS0.
PhylomeDBiP10124.
TreeFamiTF336310.

Enzyme and pathway databases

ReactomeiREACT_318. Platelet degranulation.

Miscellaneous databases

ChiTaRSiSRGN. human.
GeneWikiiSRGN.
GenomeRNAii5552.
NextBioi21518.
PROiP10124.
SOURCEiSearch...

Gene expression databases

BgeeiP10124.
CleanExiHS_SRGN.
GenevestigatoriP10124.

Family and domain databases

InterProiIPR007455. Serglycin.
[Graphical view]
PfamiPF04360. Serglycin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a cDNA that encodes the peptide core of the secretory granule proteoglycan of human promyelocytic leukemia HL-60 cells."
    Stevens R.L., Avraham S., Gartner M.C., Bruns G.A.P., Austen K.F., Weis J.H.
    J. Biol. Chem. 263:7287-7291(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-31.
  2. "Nucleotide sequence of a cDNA encoding a hemopoietic proteoglycan core protein."
    Stellrecht C.M., Saunders G.F.
    Nucleic Acids Res. 17:7523-7523(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-31.
  3. "Characterization of the human gene that encodes the peptide core of secretory granule proteoglycans in promyelocytic leukemia HL-60 cells and analysis of the translated product."
    Nicodemus C.F., Avraham S., Austen K.F., Purdy S., Jablonski J., Stevens R.L.
    J. Biol. Chem. 265:5889-5896(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-31.
  4. "The human serglycin gene. Nucleotide sequence and methylation pattern in human promyelocytic leukemia HL-60 cells and T-lymphoblast Molt-4 cells."
    Humphries D.E., Nicodemus C.F., Schiller V., Stevens R.L.
    J. Biol. Chem. 267:13558-13563(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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], VARIANT GLN-31.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-31.
  8. "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], VARIANT GLN-31.
    Tissue: Lung.
  9. "Complete amino acid sequence of a human platelet proteoglycan."
    Alliel P.M., Perin J.-P., Maillet P., Bonnet F., Rosa J.-P., Jolles P.
    FEBS Lett. 236:123-126(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-158, NUCLEOTIDE SEQUENCE [MRNA] OF 34-158, GLYCOSYLATION AT SER-94 AND SER-96.
  10. "Characterization and N-terminal sequence of human platelet proteoglycan."
    Perin J.-P., Bonnet F., Maillet P., Jolles P.
    Biochem. J. 255:1007-1013(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-93.
  11. "Synthesis, secretion, and subcellular localization of serglycin proteoglycan in human endothelial cells."
    Schick B.P., Gradowski J.F., San Antonio J.D.
    Blood 97:449-458(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Cytotoxic cell granule-mediated apoptosis: perforin delivers granzyme B-serglycin complexes into target cells without plasma membrane pore formation."
    Metkar S.S., Wang B., Aguilar-Santelises M., Raja S.M., Uhlin-Hansen L., Podack E., Trapani J.A., Froelich C.J.
    Immunity 16:417-428(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GZMB.
  13. "Cytotoxic cell granule-mediated apoptosis. Characterization of the macromolecular complex of granzyme B with serglycin."
    Raja S.M., Wang B., Dantuluri M., Desai U.R., Demeler B., Spiegel K., Metkar S.S., Froelich C.J.
    J. Biol. Chem. 277:49523-49530(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GZMB.
  14. "Localization of serglycin in human neutrophil granulocytes and their precursors."
    Niemann C.U., Cowland J.B., Klausen P., Askaa J., Calafat J., Borregaard N.
    J. Leukoc. Biol. 76:406-415(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Secretion of proteases in serglycin transfected Madin-Darby canine kidney cells."
    Zernichow L., Dalen K.T., Prydz K., Winberg J.-O., Kolset S.O.
    FEBS J. 273:536-547(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Serglycin constitutively secreted by myeloma plasma cells is a potent inhibitor of bone mineralization in vitro."
    Theocharis A.D., Seidel C., Borset M., Dobra K., Baykov V., Labropoulou V., Kanakis I., Dalas E., Karamanos N.K., Sundan A., Hjerpe A.
    J. Biol. Chem. 281:35116-35128(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSRGN_HUMAN
AccessioniPrimary (citable) accession number: P10124
Secondary accession number(s): B2R4L7, Q5VW06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 24, 2009
Last modified: April 29, 2015
This is version 141 of the entry and version 3 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, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.