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P09341

- GROA_HUMAN

UniProt

P09341 - GROA_HUMAN

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Protein

Growth-regulated alpha protein

Gene
CXCL1, GRO, GRO1, GROA, MGSA, SCYB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity.2 Publications

GO - Molecular functioni

  1. chemokine activity Source: ProtInc
  2. enzyme activator activity Source: ProtInc
  3. receptor binding Source: ProtInc

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. cell chemotaxis Source: GOC
  3. cell proliferation Source: ProtInc
  4. chemotaxis Source: ProtInc
  5. G-protein coupled receptor signaling pathway Source: ProtInc
  6. immune response Source: InterPro
  7. inflammatory response Source: ProtInc
  8. intracellular signal transduction Source: ProtInc
  9. negative regulation of cell proliferation Source: ProtInc
  10. nervous system development Source: ProtInc
  11. positive regulation of catalytic activity Source: GOC
  12. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Keywords - Biological processi

Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_15344. Chemokine receptors bind chemokines.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Growth-regulated alpha protein
Alternative name(s):
C-X-C motif chemokine 1
GRO-alpha(1-73)
Melanoma growth stimulatory activity
Short name:
MGSA
Neutrophil-activating protein 3
Short name:
NAP-3
Cleaved into the following 3 chains:
Gene namesi
Name:CXCL1
Synonyms:GRO, GRO1, GROA, MGSA, SCYB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4602. CXCL1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35050.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34345 PublicationsAdd
BLAST
Chaini35 – 10773Growth-regulated alpha proteinPRO_0000005049Add
BLAST
Chaini38 – 10770GRO-alpha(4-73)PRO_0000005050Add
BLAST
Chaini39 – 10769GRO-alpha(5-73)PRO_0000005051Add
BLAST
Chaini40 – 10768GRO-alpha(6-73)PRO_0000005052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 69
Disulfide bondi45 ↔ 85

Post-translational modificationi

N-terminal processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) are produced by proteolytic cleavage after secretion from peripheral blood monocytes.

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP09341.
PaxDbiP09341.
PRIDEiP09341.

PTM databases

PhosphoSiteiP09341.

Miscellaneous databases

PMAP-CutDBP09341.

Expressioni

Gene expression databases

ArrayExpressiP09341.
BgeeiP09341.
CleanExiHS_CXCL1.
GenevestigatoriP09341.

Interactioni

Protein-protein interaction databases

BioGridi109176. 3 interactions.
DIPiDIP-5896N.
IntActiP09341. 1 interaction.
STRINGi9606.ENSP00000379110.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 433
Beta strandi49 – 513
Turni54 – 563
Beta strandi57 – 637
Beta strandi73 – 786
Beta strandi83 – 864
Helixi91 – 10313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MGSNMR-A/B35-107[»]
1MSGNMR-A/B35-106[»]
1MSHNMR-A/B35-106[»]
1RODNMR-A/B40-62[»]
A/B89-107[»]
ProteinModelPortaliP09341.
SMRiP09341. Positions 35-107.

Miscellaneous databases

EvolutionaryTraceiP09341.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG266004.
HOGENOMiHOG000220915.
HOVERGENiHBG107789.
InParanoidiP09341.
KOiK05505.
OrthoDBiEOG7NSB57.
PhylomeDBiP09341.
TreeFamiTF333433.

Family and domain databases

InterProiIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PANTHERiPTHR10179. PTHR10179. 1 hit.
PfamiPF00048. IL8. 1 hit.
[Graphical view]
PRINTSiPR00437. SMALLCYTKCXC.
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09341-1 [UniParc]FASTAAdd to Basket

« Hide

MARAALSAAP SNPRLLRVAL LLLLLVAAGR RAAGASVATE LRCQCLQTLQ    50
GIHPKNIQSV NVKSPGPHCA QTEVIATLKN GRKACLNPAS PIVKKIIEKM 100
LNSDKSN 107
Length:107
Mass (Da):11,301
Last modified:July 1, 1989 - v1
Checksum:i17048A6B4D765CA2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03561 mRNA. Translation: AAA35933.1.
X12510 mRNA. Translation: CAA31027.1.
X54489 Genomic DNA. Translation: CAA38361.1.
BT006880 mRNA. Translation: AAP35526.1.
BC011976 mRNA. Translation: AAH11976.1.
CCDSiCCDS47074.1.
PIRiS13669. A28414.
RefSeqiNP_001502.1. NM_001511.3.
UniGeneiHs.708652.
Hs.789.

Genome annotation databases

EnsembliENST00000395761; ENSP00000379110; ENSG00000163739.
GeneIDi2919.
KEGGihsa:2919.
UCSCiuc003hhh.3. human.

Polymorphism databases

DMDMi121622.

Cross-referencesi

Web resourcesi

Wikipedia

CXCL1 entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03561 mRNA. Translation: AAA35933.1 .
X12510 mRNA. Translation: CAA31027.1 .
X54489 Genomic DNA. Translation: CAA38361.1 .
BT006880 mRNA. Translation: AAP35526.1 .
BC011976 mRNA. Translation: AAH11976.1 .
CCDSi CCDS47074.1.
PIRi S13669. A28414.
RefSeqi NP_001502.1. NM_001511.3.
UniGenei Hs.708652.
Hs.789.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MGS NMR - A/B 35-107 [» ]
1MSG NMR - A/B 35-106 [» ]
1MSH NMR - A/B 35-106 [» ]
1ROD NMR - A/B 40-62 [» ]
A/B 89-107 [» ]
ProteinModelPortali P09341.
SMRi P09341. Positions 35-107.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109176. 3 interactions.
DIPi DIP-5896N.
IntActi P09341. 1 interaction.
STRINGi 9606.ENSP00000379110.

PTM databases

PhosphoSitei P09341.

Polymorphism databases

DMDMi 121622.

Proteomic databases

MaxQBi P09341.
PaxDbi P09341.
PRIDEi P09341.

Protocols and materials databases

DNASUi 2919.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000395761 ; ENSP00000379110 ; ENSG00000163739 .
GeneIDi 2919.
KEGGi hsa:2919.
UCSCi uc003hhh.3. human.

Organism-specific databases

CTDi 2919.
GeneCardsi GC04P074724.
H-InvDB HIX0120073.
HGNCi HGNC:4602. CXCL1.
MIMi 155730. gene.
neXtProti NX_P09341.
PharmGKBi PA35050.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266004.
HOGENOMi HOG000220915.
HOVERGENi HBG107789.
InParanoidi P09341.
KOi K05505.
OrthoDBi EOG7NSB57.
PhylomeDBi P09341.
TreeFami TF333433.

Enzyme and pathway databases

Reactomei REACT_15344. Chemokine receptors bind chemokines.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

ChiTaRSi CXCL1. human.
EvolutionaryTracei P09341.
GeneWikii CXCL1.
GenomeRNAii 2919.
NextBioi 11573.
PMAP-CutDB P09341.
PROi P09341.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09341.
Bgeei P09341.
CleanExi HS_CXCL1.
Genevestigatori P09341.

Family and domain databases

InterProi IPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view ]
PANTHERi PTHR10179. PTHR10179. 1 hit.
Pfami PF00048. IL8. 1 hit.
[Graphical view ]
PRINTSi PR00437. SMALLCYTKCXC.
SMARTi SM00199. SCY. 1 hit.
[Graphical view ]
SUPFAMi SSF54117. SSF54117. 1 hit.
PROSITEi PS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Constitutive overexpression of a growth-regulated gene in transformed Chinese hamster and human cells."
    Anisowicz A., Bardwell L., Sager R.
    Proc. Natl. Acad. Sci. U.S.A. 84:7188-7192(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular characterization and chromosomal mapping of melanoma growth stimulatory activity, a growth factor structurally related to beta-thromboglobulin."
    Richmond A., Balentien E., Thomas H.G., Flaggs G., Barton D.E., Spiess J., Bordoni R., Francke U., Derynck R.
    EMBO J. 7:2025-2033(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nucleotide sequence of the human melanoma growth stimulatory activity (MGSA) gene."
    Baker N.E., Kucera G., Richmond A.
    Nucleic Acids Res. 18:6453-6453(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  4. "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].
  5. "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].
    Tissue: Ovary.
  6. "Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from tumor cells and leukocytes reveals NH2-terminal heterogeneity. Functional comparison of different natural isoforms."
    Wuyts A., Govaerts C., Struyf S., Lenaerts J.-P., Put W., Conings R., Proost P., Van Damme J.
    Eur. J. Biochem. 260:421-429(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-107, IDENTIFICATION OF GRO-ALPHA(4-73); GRO-ALPHA(5-73) AND GRO-ALPHA(6-73), PROTEOLYTIC PROCESSING OF N-TERMINAL, FUNCTION.
    Tissue: Peripheral blood monocyte.
  7. "Lipopolysaccharide-stimulated human monocytes secrete, apart from neutrophil-activating peptide 1/interleukin 8, a second neutrophil-activating protein. NH2-terminal amino acid sequence identity with melanoma growth stimulatory activity."
    Schroeder J.-M., Persoon N.L.M., Christophers E.
    J. Exp. Med. 171:1091-1100(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-65.
  8. "Inflammatory cytokines induce synthesis and secretion of gro protein and a neutrophil chemotactic factor but not beta 2-microglobulin in human synovial cells and fibroblasts."
    Golds E.E., Mason P., Nyirkos P.
    Biochem. J. 259:585-588(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-57.
  9. "Biochemical and biological characterization of NAP-1/IL-8-related cytokines in lesional psoriatic scale."
    Schroeder J.-M.
    Adv. Exp. Med. Biol. 305:97-107(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-51.
    Tissue: Skin.
  10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-49.
  11. "Expression and secretion of gro/MGSA by stimulated human endothelial cells."
    Wen D., Rowland A., Derynck R.
    EMBO J. 8:1761-1766(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION.
  12. "1H assignment and secondary structure determination of human melanoma growth stimulating activity (MGSA) by NMR spectroscopy."
    Fairbrother W.J., Reilly D., Colby T., Horuk R.
    FEBS Lett. 330:302-306(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  13. "The solution structure of melanoma growth stimulating activity."
    Fairbrother W.J., Reilly D., Colby T., Hesselgesser J., Horuk R.
    J. Mol. Biol. 242:252-270(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  14. "Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy."
    Kim K.S., Clark-Lewis I., Sykes B.D.
    J. Biol. Chem. 269:32909-32915(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiGROA_HUMAN
AccessioniPrimary (citable) accession number: P09341
Secondary accession number(s): Q9UCR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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