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Q7L266

- ASGL1_HUMAN

UniProt

Q7L266 - ASGL1_HUMAN

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Protein

Isoaspartyl peptidase/L-asparaginase

Gene
ASRGL1, ALP, CRASH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.1 Publication

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.2 Publications
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.2 Publications

Enzyme regulationi

Glycine accelerates autocleavage into an alpha and beta chain.1 Publication

Kineticsi

  1. KM=3.4 mM for L-asparagine (L-Asn)1 Publication
  2. KM=0.4 mM for L-aspartic acid beta-methyl ester
  3. KM=0.4 mM for L-Asp-L-Phe
  4. KM=1.0 mM for L-Asp-L-Ala

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei168 – 1681Nucleophile2 Publications

GO - Molecular functioni

  1. asparaginase activity Source: UniProtKB
  2. beta-aspartyl-peptidase activity Source: UniProtKB

GO - Biological processi

  1. asparagine catabolic process via L-aspartate Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Protein family/group databases

MEROPSiT02.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5, EC:3.5.1.1)
Alternative name(s):
Asparaginase-like protein 1
Beta-aspartyl-peptidase
Isoaspartyl dipeptidase
L-asparagine amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:ASRGL1
Synonyms:ALP, CRASH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16448. ASRGL1.

Subcellular locationi

Cytoplasm
Note: Midpiece of sperm tail.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681T → A or C: Abolishes activation by autocleavage. Abolishes enzyme activity. 2 Publications
Mutagenesisi168 – 1681T → S: Strongly reduced enzyme activity. 2 Publications

Organism-specific databases

PharmGKBiPA25059.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Isoaspartyl peptidase/L-asparaginase alpha chainPRO_0000305204Add
BLAST
Chaini168 – 308141Isoaspartyl peptidase/L-asparaginase beta chainPRO_0000420556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.

Keywords - PTMi

Acetylation, Autocatalytic cleavage

Proteomic databases

MaxQBiQ7L266.
PaxDbiQ7L266.
PRIDEiQ7L266.

2D gel databases

UCD-2DPAGEQ7L266.

PTM databases

PhosphoSiteiQ7L266.

Expressioni

Tissue specificityi

Expressed in brain, kidney, testis and tissues of the gastrointestinal tract. Present in sperm (at protein level). Over-expressed in uterine, mammary, prostatic and ovarian carcinoma.2 Publications

Inductioni

By 5-alpha-di-hydrotestosterone and progesterone.2 Publications

Gene expression databases

ArrayExpressiQ7L266.
BgeeiQ7L266.
CleanExiHS_ASRGL1.
GenevestigatoriQ7L266.

Organism-specific databases

HPAiHPA029725.

Interactioni

Subunit structurei

Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer.2 Publications

Protein-protein interaction databases

BioGridi123142. 5 interactions.
IntActiQ7L266. 4 interactions.
STRINGi9606.ENSP00000301776.

Structurei

Secondary structure

1
308
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Helixi17 – 3822
Turni39 – 413
Helixi44 – 5714
Beta strandi61 – 644
Beta strandi71 – 733
Beta strandi77 – 837
Turni84 – 863
Beta strandi89 – 957
Helixi101 – 11111
Beta strandi115 – 1184
Helixi119 – 12810
Helixi136 – 1383
Helixi142 – 15211
Beta strandi169 – 1746
Beta strandi180 – 1867
Turni203 – 2053
Beta strandi206 – 2105
Turni211 – 2133
Beta strandi214 – 2207
Helixi222 – 2287
Helixi230 – 23910
Helixi244 – 25916
Beta strandi263 – 2697
Beta strandi274 – 2829
Beta strandi285 – 2895
Beta strandi292 – 2987
Beta strandi303 – 3064

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TKJX-ray2.30A/B2-308[»]
4ET0X-ray3.30A/B2-308[»]
4O0CX-ray1.50A/B1-308[»]
4O0DX-ray1.95A/B1-308[»]
4O0EX-ray1.71A/B1-308[»]
4O0FX-ray1.92A/B1-308[»]
4O0GX-ray2.10A/B1-308[»]
4O0HX-ray1.97A/B1-308[»]
4OSXX-ray1.95A/B1-308[»]
4OSYX-ray1.91A/B1-308[»]
4PVPX-ray1.85A/B1-308[»]
4PVQX-ray2.13A/B1-308[»]
4PVRX-ray1.75A/B1-308[»]
4PVSX-ray1.84A/B1-308[»]
ProteinModelPortaliQ7L266.
SMRiQ7L266. Positions 1-308.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni196 – 1994Substrate binding
Regioni219 – 2224Substrate binding

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.

Phylogenomic databases

eggNOGiCOG1446.
HOGENOMiHOG000174613.
HOVERGENiHBG101662.
InParanoidiQ7L266.
KOiK13051.
OMAiLITERSK.
OrthoDBiEOG7TBC2N.
PhylomeDBiQ7L266.
TreeFamiTF323960.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7L266-1) [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

MNPIVVVHGG GAGPISKDRK ERVHQGMVRA ATVGYGILRE GGSAVDAVEG    50
AVVALEDDPE FNAGCGSVLN TNGEVEMDAS IMDGKDLSAG AVSAVQCIAN 100
PIKLARLVME KTPHCFLTDQ GAAQFAAAMG VPEIPGEKLV TERNKKRLEK 150
EKHEKGAQKT DCQKNLGTVG AVALDCKGNV AYATSTGGIV NKMVGRVGDS 200
PCLGAGGYAD NDIGAVSTTG HGESILKVNL ARLTLFHIEQ GKTVEEAADL 250
SLGYMKSRVK GLGGLIVVSK TGDWVAKWTS TSMPWAAAKD GKLHFGIDPD 300
DTTITDLP 308
Length:308
Mass (Da):32,055
Last modified:April 3, 2007 - v2
Checksum:i84E3D6C2D1555B32
GO
Isoform 2 (identifier: Q7L266-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.

Note: No experimental confirmation available.

Show »
Length:180
Mass (Da):18,981
Checksum:iE21C4620A2261D0C
GO

Sequence cautioni

The sequence BAB15302.1 differs from that shown. Reason: Contaminating sequence.
The sequence BAB15302.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128Missing in isoform 2. VSP_028287Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811A → T in AAM28434. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF411076 mRNA. Translation: AAM28434.1.
AK025969 mRNA. Translation: BAB15302.1. Different initiation.
AK091894 mRNA. Translation: BAG52437.1.
AK313069 mRNA. Translation: BAG35897.1.
CH471076 Genomic DNA. Translation: EAW74012.1.
BC021295 mRNA. Translation: AAH21295.3.
BC064963 mRNA. Translation: AAH64963.1.
BC093070 mRNA. Translation: AAH93070.1.
CCDSiCCDS8019.1. [Q7L266-1]
RefSeqiNP_001077395.1. NM_001083926.1. [Q7L266-1]
NP_079356.3. NM_025080.3. [Q7L266-1]
XP_005274362.1. XM_005274305.1. [Q7L266-2]
XP_005274363.1. XM_005274306.1. [Q7L266-2]
UniGeneiHs.535326.

Genome annotation databases

EnsembliENST00000301776; ENSP00000301776; ENSG00000162174. [Q7L266-1]
ENST00000415229; ENSP00000400057; ENSG00000162174. [Q7L266-1]
GeneIDi80150.
KEGGihsa:80150.
UCSCiuc001nte.4. human. [Q7L266-1]

Polymorphism databases

DMDMi158706477.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF411076 mRNA. Translation: AAM28434.1 .
AK025969 mRNA. Translation: BAB15302.1 . Different initiation.
AK091894 mRNA. Translation: BAG52437.1 .
AK313069 mRNA. Translation: BAG35897.1 .
CH471076 Genomic DNA. Translation: EAW74012.1 .
BC021295 mRNA. Translation: AAH21295.3 .
BC064963 mRNA. Translation: AAH64963.1 .
BC093070 mRNA. Translation: AAH93070.1 .
CCDSi CCDS8019.1. [Q7L266-1 ]
RefSeqi NP_001077395.1. NM_001083926.1. [Q7L266-1 ]
NP_079356.3. NM_025080.3. [Q7L266-1 ]
XP_005274362.1. XM_005274305.1. [Q7L266-2 ]
XP_005274363.1. XM_005274306.1. [Q7L266-2 ]
UniGenei Hs.535326.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TKJ X-ray 2.30 A/B 2-308 [» ]
4ET0 X-ray 3.30 A/B 2-308 [» ]
4O0C X-ray 1.50 A/B 1-308 [» ]
4O0D X-ray 1.95 A/B 1-308 [» ]
4O0E X-ray 1.71 A/B 1-308 [» ]
4O0F X-ray 1.92 A/B 1-308 [» ]
4O0G X-ray 2.10 A/B 1-308 [» ]
4O0H X-ray 1.97 A/B 1-308 [» ]
4OSX X-ray 1.95 A/B 1-308 [» ]
4OSY X-ray 1.91 A/B 1-308 [» ]
4PVP X-ray 1.85 A/B 1-308 [» ]
4PVQ X-ray 2.13 A/B 1-308 [» ]
4PVR X-ray 1.75 A/B 1-308 [» ]
4PVS X-ray 1.84 A/B 1-308 [» ]
ProteinModelPortali Q7L266.
SMRi Q7L266. Positions 1-308.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123142. 5 interactions.
IntActi Q7L266. 4 interactions.
STRINGi 9606.ENSP00000301776.

Chemistry

DrugBanki DB00174. L-Asparagine.
DB00128. L-Aspartic Acid.

Protein family/group databases

MEROPSi T02.002.

PTM databases

PhosphoSitei Q7L266.

Polymorphism databases

DMDMi 158706477.

2D gel databases

UCD-2DPAGE Q7L266.

Proteomic databases

MaxQBi Q7L266.
PaxDbi Q7L266.
PRIDEi Q7L266.

Protocols and materials databases

DNASUi 80150.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301776 ; ENSP00000301776 ; ENSG00000162174 . [Q7L266-1 ]
ENST00000415229 ; ENSP00000400057 ; ENSG00000162174 . [Q7L266-1 ]
GeneIDi 80150.
KEGGi hsa:80150.
UCSCi uc001nte.4. human. [Q7L266-1 ]

Organism-specific databases

CTDi 80150.
GeneCardsi GC11P062104.
HGNCi HGNC:16448. ASRGL1.
HPAi HPA029725.
MIMi 609212. gene.
neXtProti NX_Q7L266.
PharmGKBi PA25059.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1446.
HOGENOMi HOG000174613.
HOVERGENi HBG101662.
InParanoidi Q7L266.
KOi K13051.
OMAi LITERSK.
OrthoDBi EOG7TBC2N.
PhylomeDBi Q7L266.
TreeFami TF323960.

Miscellaneous databases

ChiTaRSi ASRGL1. human.
GeneWikii ASRGL1.
GenomeRNAii 80150.
NextBioi 70434.
PROi Q7L266.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7L266.
Bgeei Q7L266.
CleanExi HS_ASRGL1.
Genevestigatori Q7L266.

Family and domain databases

InterProi IPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view ]
PANTHERi PTHR10188. PTHR10188. 1 hit.
Pfami PF01112. Asparaginase_2. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel asparaginase-like protein is a sperm autoantigen in rats."
    Bush L.A., Herr J.C., Wolkowicz M., Sherman N.E., Shore A., Flickinger C.J.
    Mol. Reprod. Dev. 62:233-247(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Testis.
  2. "Identification of CRASH, a gene deregulated in gynecological tumors."
    Evtimova V., Zeillinger R., Kaul S., Weidle U.H.
    Int. J. Oncol. 24:33-41(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
  3. "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 1).
    Tissue: Corpus callosum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2).
    Tissue: Eye, Lung and Skin.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity."
    Cantor J.R., Stone E.M., Chantranupong L., Georgiou G.
    Biochemistry 48:11026-11031(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF THR-168, IDENTIFICATION BY MASS SPECTROMETRY, AUTOCATALYTIC CLEAVAGE.
  8. "Structures of apo and product-bound human L-asparaginase: insights into the mechanism of autoproteolysis and substrate hydrolysis."
    Nomme J., Su Y., Konrad M., Lavie A.
    Biochemistry 51:6816-6826(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH ASPARTATE, ACTIVE SITE, SUBUNIT, ENZYME REGULATION, AUTOCATALYTIC CLEAVAGE.
  9. "Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation."
    Li W., Cantor J.R., Yogesha S.D., Yang S., Chantranupong L., Liu J.Q., Agnello G., Georgiou G., Stone E.M., Zhang Y.
    ACS Chem. Biol. 7:1840-1847(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF THR-168, SUBUNIT.

Entry informationi

Entry nameiASGL1_HUMAN
AccessioniPrimary (citable) accession number: Q7L266
Secondary accession number(s): B2R7Q0
, Q567Q4, Q6P1P0, Q8NI34, Q9H6F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: April 3, 2007
Last modified: September 3, 2014
This is version 97 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 11
    Human chromosome 11: 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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