Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Threonine aspartase 1

Gene

TASP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protease involved in KMT2A/MLL1 processing and, consequently, in the correct expression of the early HOXA gene cluster.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei234 – 2341Nucleophile1 Publication

GO - Molecular functioni

  • threonine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • proteolysis Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT02.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine aspartase 1 (EC:3.4.25.-)
Short name:
Taspase-1
Cleaved into the following 2 chains:
Gene namesi
Name:TASP1
Synonyms:C20orf13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15859. TASP1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi233 – 2331D → A: 0.1% enzymatic activity; no intramolecular processing. 2 Publications
Mutagenesisi234 – 2341T → A: Complete loss of enzymatic activity; no intramolecular processing. 1 Publication

Organism-specific databases

PharmGKBiPA25671.

Chemistry

ChEMBLiCHEMBL6153.
GuidetoPHARMACOLOGYi2419.

Polymorphism and mutation databases

BioMutaiTASP1.
DMDMi29839766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233Threonine aspartase subunit alphaPRO_0000002350Add
BLAST
Chaini234 – 420187Threonine aspartase subunit betaPRO_0000002351Add
BLAST

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

EPDiQ9H6P5.
MaxQBiQ9H6P5.
PaxDbiQ9H6P5.
PRIDEiQ9H6P5.

PTM databases

iPTMnetiQ9H6P5.
PhosphoSiteiQ9H6P5.

Expressioni

Gene expression databases

BgeeiQ9H6P5.
CleanExiHS_TASP1.
ExpressionAtlasiQ9H6P5. baseline and differential.
GenevisibleiQ9H6P5. HS.

Organism-specific databases

HPAiHPA030824.
HPA030825.

Interactioni

Subunit structurei

Intramolecular proteolysis generates 2 subunits, alpha and beta, which reassemble through a non-covalent association to form the fully active enzyme.1 Publication

Protein-protein interaction databases

BioGridi120757. 2 interactions.
DIPiDIP-48456N.
MINTiMINT-4539345.
STRINGi9606.ENSP00000338624.

Chemistry

BindingDBiQ9H6P5.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 5211Combined sources
Helixi57 – 7721Combined sources
Helixi82 – 9514Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi115 – 1217Combined sources
Turni122 – 1243Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi135 – 1373Combined sources
Helixi139 – 15113Combined sources
Turni152 – 1543Combined sources
Beta strandi163 – 1664Combined sources
Helixi167 – 17610Combined sources
Helixi184 – 1874Combined sources
Helixi190 – 20415Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi246 – 2527Combined sources
Helixi265 – 2673Combined sources
Turni269 – 2713Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi282 – 29211Combined sources
Helixi294 – 2996Combined sources
Helixi302 – 3098Combined sources
Helixi315 – 32511Combined sources
Turni326 – 3294Combined sources
Helixi331 – 3333Combined sources
Beta strandi341 – 3488Combined sources
Beta strandi365 – 38319Combined sources
Turni384 – 3863Combined sources
Beta strandi390 – 3956Combined sources
Turni402 – 4043Combined sources
Beta strandi407 – 4148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8IX-ray2.00A/B1-420[»]
2A8JX-ray1.90A/B1-420[»]
2A8LX-ray2.00A/B1-420[»]
2A8MX-ray2.60A/B1-420[»]
ProteinModelPortaliQ9H6P5.
SMRiQ9H6P5. Positions 41-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H6P5.

Family & Domainsi

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Phylogenomic databases

eggNOGiKOG1592. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000286029.
HOVERGENiHBG058647.
InParanoidiQ9H6P5.
KOiK08657.
OMAiCRLESPE.
OrthoDBiEOG78SQHV.
PhylomeDBiQ9H6P5.
TreeFamiTF106358.

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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H6P5-1) [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

        10         20         30         40         50
MTMEKGMSSG EGLPSRSSQV SAGKITAKEL ETKQSYKEKR GGFVLVHAGA
60 70 80 90 100
GYHSESKAKE YKHVCKRACQ KAIEKLQAGA LATDAVTAAL VELEDSPFTN
110 120 130 140 150
AGMGSNLNLL GEIECDASIM DGKSLNFGAV GALSGIKNPV SVANRLLCEG
160 170 180 190 200
QKGKLSAGRI PPCFLVGEGA YRWAVDHGIP SCPPNIMTTR FSLAAFKRNK
210 220 230 240 250
RKLELAERVD TDFMQLKKRR QSSEKENDSG TLDTVGAVVV DHEGNVAAAV
260 270 280 290 300
SSGGLALKHP GRVGQAALYG CGCWAENTGA HNPYSTAVST SGCGEHLVRT
310 320 330 340 350
ILARECSHAL QAEDAHQALL ETMQNKFISS PFLASEDGVL GGVIVLRSCR
360 370 380 390 400
CSAEPDSSQN KQTLLVEFLW SHTTESMCVG YMSAQDGKAK THISRLPPGA
410 420
VAGQSVAIEG GVCRLESPVN
Length:420
Mass (Da):44,455
Last modified:March 1, 2001 - v1
Checksum:iD0C1020E708B0FCF
GO
Isoform 2 (identifier: Q9H6P5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-129: DSPFTNAGMGSNLNLLGEIECDASIMDGKSLNFGA → VYTHSYTSWSCIQPSIHVLLVKRQRKSPLPRISTF
     130-420: Missing.

Note: No experimental confirmation available.
Show »
Length:129
Mass (Da):14,140
Checksum:i3C1C2FCB9C18572E
GO
Isoform 3 (identifier: Q9H6P5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-145: SPFTNAGMGS...IKNPVSVANR → VESILCAPYW...LPVKMACLAE
     146-420: Missing.

Note: No experimental confirmation available.
Show »
Length:145
Mass (Da):15,946
Checksum:iF9110EA1814DC0CC
GO

Sequence cautioni

The sequence CAC01509.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti357 – 3571S → F in BAA91018 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei95 – 12935DSPFT…LNFGA → VYTHSYTSWSCIQPSIHVLL VKRQRKSPLPRISTF in isoform 2. 1 PublicationVSP_056327Add
BLAST
Alternative sequencei96 – 14550SPFTN…SVANR → VESILCAPYWLENVHMLYKL RMLTKPCWRLCKTSLSVHLS LPVKMACLAE in isoform 3. 1 PublicationVSP_056533Add
BLAST
Alternative sequencei130 – 420291Missing in isoform 2. 1 PublicationVSP_056328Add
BLAST
Alternative sequencei146 – 420275Missing in isoform 3. 1 PublicationVSP_056534Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000219 mRNA. Translation: BAA91018.1.
AK025671 mRNA. Translation: BAB15209.1.
AK299940 mRNA. Translation: BAH13176.1.
AK304488 mRNA. Translation: BAH14199.1.
AK316311 mRNA. Translation: BAH14682.1.
AL050320 Genomic DNA. No translation available.
AL121754 Genomic DNA. Translation: CAC01509.1. Sequence problems.
AL121754, AL121782 Genomic DNA. Translation: CAI22071.1.
AL121782, AL121754 Genomic DNA. Translation: CAI21890.1.
AL133463 Genomic DNA. No translation available.
AL158089 Genomic DNA. No translation available.
BC025266 mRNA. Translation: AAH25266.1.
CCDSiCCDS13116.1. [Q9H6P5-1]
RefSeqiNP_060184.2. NM_017714.2. [Q9H6P5-1]
XP_011527591.1. XM_011529289.1. [Q9H6P5-1]
UniGeneiHs.348297.

Genome annotation databases

EnsembliENST00000337743; ENSP00000338624; ENSG00000089123. [Q9H6P5-1]
GeneIDi55617.
KEGGihsa:55617.
UCSCiuc002woi.4. human. [Q9H6P5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000219 mRNA. Translation: BAA91018.1.
AK025671 mRNA. Translation: BAB15209.1.
AK299940 mRNA. Translation: BAH13176.1.
AK304488 mRNA. Translation: BAH14199.1.
AK316311 mRNA. Translation: BAH14682.1.
AL050320 Genomic DNA. No translation available.
AL121754 Genomic DNA. Translation: CAC01509.1. Sequence problems.
AL121754, AL121782 Genomic DNA. Translation: CAI22071.1.
AL121782, AL121754 Genomic DNA. Translation: CAI21890.1.
AL133463 Genomic DNA. No translation available.
AL158089 Genomic DNA. No translation available.
BC025266 mRNA. Translation: AAH25266.1.
CCDSiCCDS13116.1. [Q9H6P5-1]
RefSeqiNP_060184.2. NM_017714.2. [Q9H6P5-1]
XP_011527591.1. XM_011529289.1. [Q9H6P5-1]
UniGeneiHs.348297.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8IX-ray2.00A/B1-420[»]
2A8JX-ray1.90A/B1-420[»]
2A8LX-ray2.00A/B1-420[»]
2A8MX-ray2.60A/B1-420[»]
ProteinModelPortaliQ9H6P5.
SMRiQ9H6P5. Positions 41-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120757. 2 interactions.
DIPiDIP-48456N.
MINTiMINT-4539345.
STRINGi9606.ENSP00000338624.

Chemistry

BindingDBiQ9H6P5.
ChEMBLiCHEMBL6153.
GuidetoPHARMACOLOGYi2419.

Protein family/group databases

MEROPSiT02.004.

PTM databases

iPTMnetiQ9H6P5.
PhosphoSiteiQ9H6P5.

Polymorphism and mutation databases

BioMutaiTASP1.
DMDMi29839766.

Proteomic databases

EPDiQ9H6P5.
MaxQBiQ9H6P5.
PaxDbiQ9H6P5.
PRIDEiQ9H6P5.

Protocols and materials databases

DNASUi55617.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337743; ENSP00000338624; ENSG00000089123. [Q9H6P5-1]
GeneIDi55617.
KEGGihsa:55617.
UCSCiuc002woi.4. human. [Q9H6P5-1]

Organism-specific databases

CTDi55617.
GeneCardsiTASP1.
HGNCiHGNC:15859. TASP1.
HPAiHPA030824.
HPA030825.
MIMi608270. gene.
neXtProtiNX_Q9H6P5.
PharmGKBiPA25671.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1592. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000286029.
HOVERGENiHBG058647.
InParanoidiQ9H6P5.
KOiK08657.
OMAiCRLESPE.
OrthoDBiEOG78SQHV.
PhylomeDBiQ9H6P5.
TreeFamiTF106358.

Miscellaneous databases

ChiTaRSiTASP1. human.
EvolutionaryTraceiQ9H6P5.
GeneWikiiTASP1.
GenomeRNAii55617.
PROiQ9H6P5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H6P5.
CleanExiHS_TASP1.
ExpressionAtlasiQ9H6P5. baseline and differential.
GenevisibleiQ9H6P5. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Brain, Colon mucosa, Hepatoma and Uterus.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
    Tissue: Ovary.
  4. "Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression."
    Hsieh J.J.-D., Cheng E.H.-Y., Korsmeyer S.J.
    Cell 115:293-303(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 124-145, FUNCTION, MUTAGENESIS OF ASP-233 AND THR-234.
  5. "Crystal structure of human Taspase1, a crucial protease regulating the function of MLL."
    Khan J.A., Dunn B.M., Tong L.
    Structure 13:1443-1452(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), ACTIVE SITE, SUBUNIT, MUTAGENESIS OF THR-234.

Entry informationi

Entry nameiTASP1_HUMAN
AccessioniPrimary (citable) accession number: Q9H6P5
Secondary accession number(s): B7Z690
, B7Z963, Q5TDU9, Q9BQN0, Q9NQ08, Q9NTS6, Q9NXJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 131 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 20
    Human chromosome 20: 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

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 one 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.