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Protein

Threonine synthase-like 1

Gene

THNSL1

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

Functioni

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase-like 1
Short name:
TSH1
Gene namesi
Name:THNSL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:26160. THNSL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134906927.

Chemistry

DrugBankiDB00156. L-Threonine.

Polymorphism and mutation databases

BioMutaiTHNSL1.
DMDMi62511212.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 743743Threonine synthase-like 1PRO_0000185646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei281 – 2811N6-acetyllysine1 Publication
Modified residuei351 – 3511N6-(pyridoxal phosphate)lysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8IYQ7.
PaxDbiQ8IYQ7.
PeptideAtlasiQ8IYQ7.
PRIDEiQ8IYQ7.

PTM databases

PhosphoSiteiQ8IYQ7.

Expressioni

Gene expression databases

BgeeiQ8IYQ7.
CleanExiHS_THNSL1.
GenevisibleiQ8IYQ7. HS.

Organism-specific databases

HPAiHPA037585.
HPA044875.

Interactioni

Protein-protein interaction databases

BioGridi122980. 11 interactions.
IntActiQ8IYQ7. 1 interaction.
STRINGi9606.ENSP00000365534.

Structurei

3D structure databases

ProteinModelPortaliQ8IYQ7.
SMRiQ8IYQ7. Positions 42-226, 251-682.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Phylogenomic databases

eggNOGiCOG0703.
GeneTreeiENSGT00530000063879.
HOGENOMiHOG000065776.
HOVERGENiHBG055015.
InParanoidiQ8IYQ7.
OMAiCSKIAPV.
OrthoDBiEOG7QZG93.
PhylomeDBiQ8IYQ7.
TreeFamiTF329641.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.90.1380.10. 1 hit.
HAMAPiMF_00109. Shikimate_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR000623. Shikimate_kinase/TSH1.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF01202. SKI. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8IYQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHFNRCHHL KKITQKCFSS IHVKTDKHAQ RFLSRTFALA ELRKSWYSTH
60 70 80 90 100
SLVGDKNIIL MGPPGAGKTT VGRIIGQKLG CCVIDVDDDI LEKTWNMSVS
110 120 130 140 150
EKLQDVGNEQ FLEEEGKAVL NFSASGSVIS LTGSNPMHDA SMWHLKKNGI
160 170 180 190 200
IVYLDVPLLD LICRLKLMKT DRIVGQNSGT SMKDLLKFRR QYYKKWYDAR
210 220 230 240 250
VFCESGASPE EVADKVLNAI KRYQDVDSET FISTRHVWPE DCEQKVSAKF
260 270 280 290 300
FSEAVIEGLA SDGGLFVPAK EFPKLSCGEW KSLVGATYVE RAQILLERCI
310 320 330 340 350
HPADIPAARL GEMIETAYGE NFACSKIAPV RHLSGNQFIL ELFHGPTGSF
360 370 380 390 400
KDLSLQLMPH IFAHCIPPSC NYMILVATSG DTGSAVLNGF SRLNKNDKQR
410 420 430 440 450
IAVVAFFPEN GVSDFQKAQI IGSQRENGWA VGVESDFDFC QTAIKRIFND
460 470 480 490 500
SDFTGFLTVE YGTILSSANS INWGRLLPQV VYHASAYLDL VSQGFISFGS
510 520 530 540 550
PVDVCIPTGN FGNILAAVYA KMMGIPIRKF ICASNQNHVL TDFIKTGHYD
560 570 580 590 600
LRERKLAQTF SPSIDILKSS NLERHLHLMA NKDGQLMTEL FNRLESQHHF
610 620 630 640 650
QIEKALVEKL QQDFVADWCS EGECLAAINS TYNTSGYILD PHTAVAKVVA
660 670 680 690 700
DRVQDKTCPV IISSTAHYSK FAPAIMQALK IKEINETSSS QLYLLGSYNA
710 720 730 740
LPPLHEALLE RTKQQEKMEY QVCAADMNVL KSHVEQLVQN QFI
Length:743
Mass (Da):83,070
Last modified:April 12, 2005 - v2
Checksum:i0C166A57EF34A682
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941T → N in AAH35132 (PubMed:15489334).Curated
Sequence conflicti705 – 7051H → R in AAH35132 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541L → P.
Corresponds to variant rs35827877 [ dbSNP | Ensembl ].
VAR_052545
Natural varianti239 – 2391P → R.
Corresponds to variant rs41279890 [ dbSNP | Ensembl ].
VAR_061893
Natural varianti248 – 2481A → E.
Corresponds to variant rs34929144 [ dbSNP | Ensembl ].
VAR_052546
Natural varianti399 – 3991Q → R.
Corresponds to variant rs41279894 [ dbSNP | Ensembl ].
VAR_058869

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK125249 mRNA. Translation: BAG54173.1.
AL512598 Genomic DNA. Translation: CAH70791.1.
CH471072 Genomic DNA. Translation: EAW86113.1.
CH471072 Genomic DNA. Translation: EAW86114.1.
BC035132 mRNA. Translation: AAH35132.1.
CCDSiCCDS7147.1.
RefSeqiNP_079114.3. NM_024838.4.
XP_005252654.1. XM_005252597.1.
UniGeneiHs.645274.

Genome annotation databases

EnsembliENST00000376356; ENSP00000365534; ENSG00000185875.
ENST00000524413; ENSP00000434887; ENSG00000185875.
GeneIDi79896.
KEGGihsa:79896.
UCSCiuc001isi.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK125249 mRNA. Translation: BAG54173.1.
AL512598 Genomic DNA. Translation: CAH70791.1.
CH471072 Genomic DNA. Translation: EAW86113.1.
CH471072 Genomic DNA. Translation: EAW86114.1.
BC035132 mRNA. Translation: AAH35132.1.
CCDSiCCDS7147.1.
RefSeqiNP_079114.3. NM_024838.4.
XP_005252654.1. XM_005252597.1.
UniGeneiHs.645274.

3D structure databases

ProteinModelPortaliQ8IYQ7.
SMRiQ8IYQ7. Positions 42-226, 251-682.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122980. 11 interactions.
IntActiQ8IYQ7. 1 interaction.
STRINGi9606.ENSP00000365534.

Chemistry

DrugBankiDB00156. L-Threonine.

PTM databases

PhosphoSiteiQ8IYQ7.

Polymorphism and mutation databases

BioMutaiTHNSL1.
DMDMi62511212.

Proteomic databases

MaxQBiQ8IYQ7.
PaxDbiQ8IYQ7.
PeptideAtlasiQ8IYQ7.
PRIDEiQ8IYQ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376356; ENSP00000365534; ENSG00000185875.
ENST00000524413; ENSP00000434887; ENSG00000185875.
GeneIDi79896.
KEGGihsa:79896.
UCSCiuc001isi.4. human.

Organism-specific databases

CTDi79896.
GeneCardsiGC10P025345.
HGNCiHGNC:26160. THNSL1.
HPAiHPA037585.
HPA044875.
MIMi611260. gene.
neXtProtiNX_Q8IYQ7.
PharmGKBiPA134906927.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0703.
GeneTreeiENSGT00530000063879.
HOGENOMiHOG000065776.
HOVERGENiHBG055015.
InParanoidiQ8IYQ7.
OMAiCSKIAPV.
OrthoDBiEOG7QZG93.
PhylomeDBiQ8IYQ7.
TreeFamiTF329641.

Miscellaneous databases

GenomeRNAii79896.
NextBioi69730.
PROiQ8IYQ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IYQ7.
CleanExiHS_THNSL1.
GenevisibleiQ8IYQ7. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.90.1380.10. 1 hit.
HAMAPiMF_00109. Shikimate_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR000623. Shikimate_kinase/TSH1.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF01202. SKI. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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].
    Tissue: Brain.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTHNS1_HUMAN
AccessioniPrimary (citable) accession number: Q8IYQ7
Secondary accession number(s): B3KWL1, D3DRV3, Q5VV21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: June 24, 2015
This is version 104 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.