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P51124

- GRAM_HUMAN

UniProt

P51124 - GRAM_HUMAN

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Protein

Granzyme M

Gene

GZMM

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

Functioni

Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661Charge relay system1 Publication
Active sitei111 – 1111Charge relay system1 Publication
Active sitei207 – 2071Charge relay system1 Publication

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cytolysis Source: UniProtKB-KW
  3. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Apoptosis, Cytolysis, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_8001. Alternative complement activation.

Protein family/group databases

MEROPSiS01.139.

Names & Taxonomyi

Protein namesi
Recommended name:
Granzyme M (EC:3.4.21.-)
Alternative name(s):
Met-1 serine protease
Short name:
Hu-Met-1
Met-ase
Natural killer cell granular protease
Gene namesi
Name:GZMM
Synonyms:MET1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:4712. GZMM.

Subcellular locationi

Secreted. Cytoplasmic granule
Note: Granules of large granular lymphocytes.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29090.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 252Activation peptideSequence AnalysisPRO_0000027421
Chaini26 – 257232Granzyme MPRO_0000027422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 671 PublicationPROSITE-ProRule annotation
Disulfide bondi145 ↔ 2131 PublicationPROSITE-ProRule annotation
Disulfide bondi176 ↔ 1921 PublicationPROSITE-ProRule annotation
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi203 ↔ 2301 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP51124.
PRIDEiP51124.

PTM databases

PhosphoSiteiP51124.

Expressioni

Tissue specificityi

Highly and constitutively expressed in activated natural killer (NK) cells.1 Publication

Gene expression databases

BgeeiP51124.
CleanExiHS_GZMM.
GenevestigatoriP51124.

Organism-specific databases

HPAiHPA015624.

Interactioni

Protein-protein interaction databases

BioGridi109259. 5 interactions.
STRINGi9606.ENSP00000264553.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 456Combined sources
Beta strandi48 – 5710Combined sources
Beta strandi60 – 634Combined sources
Helixi65 – 684Combined sources
Helixi72 – 743Combined sources
Beta strandi75 – 806Combined sources
Beta strandi82 – 865Combined sources
Beta strandi89 – 9810Combined sources
Turni105 – 1073Combined sources
Beta strandi113 – 1197Combined sources
Beta strandi144 – 1496Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi164 – 1707Combined sources
Helixi173 – 1764Combined sources
Turni179 – 1846Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi210 – 2134Combined sources
Turni214 – 2174Combined sources
Beta strandi218 – 2236Combined sources
Beta strandi238 – 2425Combined sources
Helixi243 – 2453Combined sources
Helixi246 – 2538Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LZPmodel-A26-257[»]
2ZGCX-ray1.96A26-257[»]
2ZGHX-ray2.17A26-257[»]
2ZGJX-ray2.30A26-257[»]
2ZKSX-ray2.70A26-257[»]
ProteinModelPortaliP51124.
SMRiP51124. Positions 26-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51124.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 254229Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Granzyme subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP51124.
KOiK08649.
OMAiKDQAPCK.
OrthoDBiEOG7HQN8W.
PhylomeDBiP51124.
TreeFamiTF335738.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51124-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEACVSSLLV LALGALSVGS SFGTQIIGGR EVIPHSRPYM ASLQRNGSHL
60 70 80 90 100
CGGVLVHPKW VLTAAHCLAQ RMAQLRLVLG LHTLDSPGLT FHIKAAIQHP
110 120 130 140 150
RYKPVPALEN DLALLQLDGK VKPSRTIRPL ALPSKRQVVA AGTRCSMAGW
160 170 180 190 200
GLTHQGGRLS RVLRELDLQV LDTRMCNNSR FWNGSLSPSM VCLAADSKDQ
210 220 230 240 250
APCKGDSGGP LVCGKGRVLA RVLSFSSRVC TDIFKPPVAT AVAPYVSWIR

KVTGRSA
Length:257
Mass (Da):27,545
Last modified:May 18, 2010 - v2
Checksum:iB4E815CE455F7371
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211R → G.3 Publications
Corresponds to variant rs1599882 [ dbSNP | Ensembl ].
VAR_051829

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23134 mRNA. Translation: AAA59582.1.
L36922 Genomic DNA. Translation: AAA57262.1.
L36936 Genomic DNA. Translation: AAA57257.1.
AC011556 Genomic DNA. No translation available.
BC025701 mRNA. Translation: AAH25701.1.
CCDSiCCDS12031.1.
PIRiA55634.
RefSeqiNP_001245280.1. NM_001258351.1.
NP_005308.1. NM_005317.3.
UniGeneiHs.465511.

Genome annotation databases

EnsembliENST00000264553; ENSP00000264553; ENSG00000197540.
GeneIDi3004.
KEGGihsa:3004.
UCSCiuc002low.2. human.

Polymorphism databases

DMDMi296434527.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23134 mRNA. Translation: AAA59582.1 .
L36922 Genomic DNA. Translation: AAA57262.1 .
L36936 Genomic DNA. Translation: AAA57257.1 .
AC011556 Genomic DNA. No translation available.
BC025701 mRNA. Translation: AAH25701.1 .
CCDSi CCDS12031.1.
PIRi A55634.
RefSeqi NP_001245280.1. NM_001258351.1.
NP_005308.1. NM_005317.3.
UniGenei Hs.465511.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LZP model - A 26-257 [» ]
2ZGC X-ray 1.96 A 26-257 [» ]
2ZGH X-ray 2.17 A 26-257 [» ]
2ZGJ X-ray 2.30 A 26-257 [» ]
2ZKS X-ray 2.70 A 26-257 [» ]
ProteinModelPortali P51124.
SMRi P51124. Positions 26-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109259. 5 interactions.
STRINGi 9606.ENSP00000264553.

Protein family/group databases

MEROPSi S01.139.

PTM databases

PhosphoSitei P51124.

Polymorphism databases

DMDMi 296434527.

Proteomic databases

PaxDbi P51124.
PRIDEi P51124.

Protocols and materials databases

DNASUi 3004.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264553 ; ENSP00000264553 ; ENSG00000197540 .
GeneIDi 3004.
KEGGi hsa:3004.
UCSCi uc002low.2. human.

Organism-specific databases

CTDi 3004.
GeneCardsi GC19P000544.
HGNCi HGNC:4712. GZMM.
HPAi HPA015624.
MIMi 600311. gene.
neXtProti NX_P51124.
PharmGKBi PA29090.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118895.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P51124.
KOi K08649.
OMAi KDQAPCK.
OrthoDBi EOG7HQN8W.
PhylomeDBi P51124.
TreeFami TF335738.

Enzyme and pathway databases

Reactomei REACT_8001. Alternative complement activation.

Miscellaneous databases

EvolutionaryTracei P51124.
GeneWikii GZMM.
GenomeRNAii 3004.
NextBioi 11912.
PROi P51124.
SOURCEi Search...

Gene expression databases

Bgeei P51124.
CleanExi HS_GZMM.
Genevestigatori P51124.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Met-ase: cloning and distinct chromosomal location of a serine protease preferentially expressed in human natural killer cells."
    Smyth M.J., Sayers T.J., Wiltrout T., Powers J.C., Trapani J.A.
    J. Immunol. 151:6195-6205(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-221.
  2. "The human Met-ase gene (GZMM): structure, sequence, and close physical linkage to the serine protease gene cluster on 19p13.3."
    Pilat D., Fink T.M., Obermaier-Skrobanek B., Zimmer M., Wekerle H., Lichter P., Jenne D.E.
    Genomics 24:445-450(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-221.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 GLY-221.
    Tissue: Pancreas and Spleen.
  5. "NK cell protease granzyme M targets alpha-tubulin and disorganizes the microtubule network."
    Bovenschen N., de Koning P.J., Quadir R., Broekhuizen R., Damen J.M., Froelich C.J., Slijper M., Kummer J.A.
    J. Immunol. 180:8184-8191(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATES.
  6. "Cleavage of survivin by Granzyme M triggers degradation of the survivin-X-linked inhibitor of apoptosis protein (XIAP) complex to free caspase activity leading to cytolysis of target tumor cells."
    Hu D., Liu S., Shi L., Li C., Wu L., Fan Z.
    J. Biol. Chem. 285:18326-18335(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Structural basis for proteolytic specificity of the human apoptosis-inducing granzyme M."
    Wu L., Wang L., Hua G., Liu K., Yang X., Zhai Y., Bartlam M., Sun F., Fan Z.
    J. Immunol. 183:421-429(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 26-257, ACTIVE SITE, DISULFIDE BONDS.

Entry informationi

Entry nameiGRAM_HUMAN
AccessioniPrimary (citable) accession number: P51124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 123 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3