Q7L266 (ASGL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-asparaginase
EC=3.5.1.1

Alternative name(s):
Asparaginase-like protein 1
L-asparagine amidohydrolase

Gene names

Name:	ASRGL1
Synonyms:	ALP, CRASH

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	308 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in asparagine catabolism. May be involved in astroglial production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions By similarity.
Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subcellular location	Cytoplasm. Note: Midpiece of sperm tail. Ref.1
Tissue specificity	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. Ref.1 Ref.2
Induction	By 5-alpha-di-hydrotestosterone and progesterone. Ref.2
Sequence similarities	Belongs to the Ntn-hydrolase family.
Sequence caution	The sequence BAB15302.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	asparagine catabolic process via L-aspartate Inferred from sequence or structural similarity. Source: UniProtKB protein maturation Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7L266-1)

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: Q7L266-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 308	308	L-asparaginase		PRO_0000305204
Sites
	Active site	168	1	Nucleophile By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.6
Natural variations
	Alternative sequence	1 – 128	128	Missing in isoform 2.		VSP_028287
Experimental info
	Sequence conflict	181	1	A → T in AAM28434. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 84E3D6C2D1555B32	FASTA	308	32,055
	10 20 30 40 50 60 MNPIVVVHGG GAGPISKDRK ERVHQGMVRA ATVGYGILRE GGSAVDAVEG AVVALEDDPE 70 80 90 100 110 120 FNAGCGSVLN TNGEVEMDAS IMDGKDLSAG AVSAVQCIAN PIKLARLVME KTPHCFLTDQ 130 140 150 160 170 180 GAAQFAAAMG VPEIPGEKLV TERNKKRLEK EKHEKGAQKT DCQKNLGTVG AVALDCKGNV 190 200 210 220 230 240 AYATSTGGIV NKMVGRVGDS PCLGAGGYAD NDIGAVSTTG HGESILKVNL ARLTLFHIEQ 250 260 270 280 290 300 GKTVEEAADL SLGYMKSRVK GLGGLIVVSK TGDWVAKWTS TSMPWAAAKD GKLHFGIDPD DTTITDLP
	Isoform 2 [UniParc]. Checksum: E21C4620A2261D0C	FASTA	180	18,981
	10 20 30 40 50 60 MGVPEIPGEK LVTERNKKRL EKEKHEKGAQ KTDCQKNLGT VGAVALDCKG NVAYATSTGG 70 80 90 100 110 120 IVNKMVGRVG DSPCLGAGGY ADNDIGAVST TGHGESILKV NLARLTLFHI EQGKTVEEAA 130 140 150 160 170 180 DLSLGYMKSR VKGLGGLIVV SKTGDWVAKW TSTSMPWAAA KDGKLHFGID PDDTTITDLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11984834] [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: 14654938] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Corpus callosum.
[4]	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. , 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].
[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: 15489334] [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00555734. IPI00867663.
RefSeq	NP_001077395.1. NM_001083926.1. NP_079356.3. NM_025080.3.
UniGene	Hs.535326.
3D structure databases
HSSP	HSSP built from PDB template 2A8L based on UniProtKB Q9H6P5.
ProteinModelPortal	Q7L266.
SMR	Q7L266. Positions 2-300.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7L266.
Protein family/group databases
MEROPS	T02.002.
Polymorphism databases
DMDM	158706477.
2D gel databases
UCD-2DPAGE	Q7L266.
Proteomic databases
PRIDE	Q7L266.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301776; ENSP00000301776; ENSG00000162174. ENST00000415229; ENSP00000400057; ENSG00000162174.
GeneID	80150.
KEGG	hsa:80150.
UCSC	uc001nte.2. human. uc001ntg.2. human.
Organism-specific databases
CTD	80150.
GeneCards	GC11P062104.
H-InvDB	HIX0009707.
HGNC	HGNC:16448. ASRGL1.
HPA	HPA029725.
MIM	609212. gene.
neXtProt	NX_Q7L266.
PharmGKB	PA25059.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17315.
HOGENOM	HBG735787.
HOVERGEN	HBG101662.
InParanoid	Q7L266.
OMA	WAVKWTS.
OrthoDB	EOG4ZS93Q.
PhylomeDB	Q7L266.
Gene expression databases
ArrayExpress	Q7L266.
Bgee	Q7L266.
CleanEx	HS_ASRGL1.
Genevestigator	Q7L266.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
KO	K13051.
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00174. L-Asparagine. DB00128. L-Aspartic Acid.
NextBio	70434.
SOURCE	Search...

Entry information

Entry name

ASGL1_HUMAN

Accession

Primary (citable) accession number: Q7L266
Secondary accession number(s): B2R7Q0 , Q567Q4, Q6P1P0, Q8NI34, Q9H6F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	April 3, 2007
Last modified:	January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.