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Q8IYQ7

- THNS1_HUMAN

UniProt

Q8IYQ7 - THNS1_HUMAN

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Protein

Threonine synthase-like 1

Gene

THNSL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Cofactori

Pyridoxal phosphate.By similarity

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: Chromosome 10

Organism-specific databases

HGNCiHGNC:26160. THNSL1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. mitochondrion Source: HPA
  3. nucleus Source: HPA
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134906927.

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.
ExpressionAtlasiQ8IYQ7. baseline and differential.
GenevestigatoriQ8IYQ7.

Organism-specific databases

HPAiHPA037585.
HPA044875.

Interactioni

Protein-protein interaction databases

BioGridi122980. 7 interactions.
IntActiQ8IYQ7. 1 interaction.
STRINGi9606.ENSP00000365534.

Structurei

3D structure databases

ProteinModelPortaliQ8IYQ7.
SMRiQ8IYQ7. Positions 42-223, 228-679.
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]
PRINTSiPR01100. SHIKIMTKNASE.
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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi62511212.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7147.1.
RefSeqi NP_079114.3. NM_024838.4.
XP_005252654.1. XM_005252597.1.
UniGenei Hs.645274.

3D structure databases

ProteinModelPortali Q8IYQ7.
SMRi Q8IYQ7. Positions 42-223, 228-679.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122980. 7 interactions.
IntActi Q8IYQ7. 1 interaction.
STRINGi 9606.ENSP00000365534.

Chemistry

DrugBanki DB00156. L-Threonine.

PTM databases

PhosphoSitei Q8IYQ7.

Polymorphism databases

DMDMi 62511212.

Proteomic databases

MaxQBi Q8IYQ7.
PaxDbi Q8IYQ7.
PeptideAtlasi Q8IYQ7.
PRIDEi Q8IYQ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376356 ; ENSP00000365534 ; ENSG00000185875 .
ENST00000524413 ; ENSP00000434887 ; ENSG00000185875 .
GeneIDi 79896.
KEGGi hsa:79896.
UCSCi uc001isi.4. human.

Organism-specific databases

CTDi 79896.
GeneCardsi GC10P025345.
HGNCi HGNC:26160. THNSL1.
HPAi HPA037585.
HPA044875.
MIMi 611260. gene.
neXtProti NX_Q8IYQ7.
PharmGKBi PA134906927.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0703.
GeneTreei ENSGT00530000063879.
HOGENOMi HOG000065776.
HOVERGENi HBG055015.
InParanoidi Q8IYQ7.
OMAi CSKIAPV.
OrthoDBi EOG7QZG93.
PhylomeDBi Q8IYQ7.
TreeFami TF329641.

Miscellaneous databases

GenomeRNAii 79896.
NextBioi 69730.
PROi Q8IYQ7.
SOURCEi Search...

Gene expression databases

Bgeei Q8IYQ7.
CleanExi HS_THNSL1.
ExpressionAtlasi Q8IYQ7. baseline and differential.
Genevestigatori Q8IYQ7.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
3.90.1380.10. 1 hit.
HAMAPi MF_00109. Shikimate_kinase.
InterProi IPR027417. P-loop_NTPase.
IPR000623. Shikimate_kinase/TSH1.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
PF01202. SKI. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view ]
PRINTSi PR01100. SHIKIMTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00260. thrC. 1 hit.
ProtoNeti Search...

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].

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: October 29, 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

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