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P14868

- SYDC_HUMAN

UniProt

P14868 - SYDC_HUMAN

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Protein
Aspartate--tRNA ligase, cytoplasmic
Gene
DARS, PIG40
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

Catalytic activityi

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei229 – 2291Aspartate By similarity
Binding sitei273 – 2731Aspartate By similarity
Binding sitei424 – 4241ATP By similarity
Binding sitei427 – 4271Aspartate By similarity
Binding sitei431 – 4311Aspartate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi273 – 2753ATP By similarity
Nucleotide bindingi281 – 2833ATP By similarity
Nucleotide bindingi472 – 4754ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. aminoacylase activity Source: ProtInc
  3. aspartate-tRNA ligase activity Source: ProtInc
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: IntAct

GO - Biological processi

  1. aspartyl-tRNA aminoacylation Source: ProtInc
  2. gene expression Source: Reactome
  3. protein complex assembly Source: ProtInc
  4. tRNA aminoacylation for protein translation Source: Reactome
  5. translation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA ligase, cytoplasmic (EC:6.1.1.12)
Alternative name(s):
Aspartyl-tRNA synthetase
Short name:
AspRS
Cell proliferation-inducing gene 40 protein
Gene namesi
Name:DARS
ORF Names:PIG40
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2678. DARS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Hypomyelination with brainstem and spinal cord involvement and leg spasticity (HBSL) [MIM:615281]: An autosomal recessive leukoencephalopathy characterized by onset in the first year of life of severe spasticity, mainly affecting the lower limbs and resulting in an inability to achieve independent ambulation. Affected individuals show delayed motor development and nystagmus; some may have mild mental retardation. Brain MRI shows hypomyelination and white matter lesions in the cerebrum, brainstem, cerebellum, and spinal cord.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561M → L in HBSL. 1 Publication
VAR_070038
Natural varianti274 – 2741A → V in HBSL. 1 Publication
VAR_070039
Natural varianti367 – 3671D → Y in HBSL. 1 Publication
VAR_070040
Natural varianti460 – 4601R → H in HBSL. 1 Publication
VAR_070041
Natural varianti464 – 4641P → L in HBSL. 1 Publication
VAR_070042
Natural varianti487 – 4871R → C in HBSL. 1 Publication
VAR_070043
Natural varianti494 – 4941R → C in HBSL. 1 Publication
VAR_070044
Natural varianti494 – 4941R → G in HBSL. 1 Publication
VAR_070045

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615281. phenotype.
Orphaneti363412. Hypomyelination with brain stem and spinal cord involvement and leg spasticity.
PharmGKBiPA27146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Aspartate--tRNA ligase, cytoplasmic
PRO_0000111010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysine1 Publication
Modified residuei249 – 2491Phosphoserine1 Publication
Modified residuei374 – 3741N6-acetyllysine1 Publication
Modified residuei500 – 5001Phosphothreonine; by PKA Reviewed prediction

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14868.
PaxDbiP14868.
PeptideAtlasiP14868.
PRIDEiP14868.

2D gel databases

OGPiP14868.
REPRODUCTION-2DPAGEIPI00216951.

PTM databases

PhosphoSiteiP14868.

Expressioni

Tissue specificityi

Expression in the developing and adult brain shows similar patterns. Highly expressed in the ventricular and subventricular zones, including hippocampal subfields, the midlateral temporaal cortex and the frontal polar cortex. The cerebellum, cereral cortex, hippocampus, and lateral ventricle show preferential neuronal expression. Expression in the peripheral neurons is evident in the colon.1 Publication

Gene expression databases

ArrayExpressiP14868.
BgeeiP14868.
CleanExiHS_DARS.
GenevestigatoriP14868.

Organism-specific databases

HPAiHPA020451.
HPA029804.
HPA029805.

Interactioni

Subunit structurei

Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro.

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629932EBI-358730,EBI-401755

Protein-protein interaction databases

BioGridi107984. 52 interactions.
IntActiP14868. 12 interactions.
MINTiMINT-141082.
STRINGi9606.ENSP00000264161.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 283
Beta strandi29 – 313
Helixi48 – 503
Helixi53 – 553
Beta strandi59 – 7214
Beta strandi75 – 828
Beta strandi85 – 939
Turni94 – 963
Helixi99 – 1079
Beta strandi113 – 12210
Beta strandi134 – 14613
Helixi156 – 1605
Helixi176 – 1816
Helixi183 – 1864
Helixi190 – 21223
Helixi250 – 25910
Beta strandi264 – 2718
Beta strandi286 – 2949
Helixi300 – 32021
Helixi322 – 33110
Beta strandi344 – 3474
Helixi348 – 35710
Helixi370 – 38415
Beta strandi387 – 3926
Helixi396 – 3983
Beta strandi407 – 4093
Beta strandi412 – 4209
Beta strandi423 – 4319
Helixi435 – 44410
Helixi450 – 4523
Helixi453 – 4575
Turni458 – 4614
Beta strandi466 – 4727
Helixi473 – 4819
Helixi486 – 4894

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J15X-ray2.24A/B1-501[»]
ProteinModelPortaliP14868.
SMRiP14868. Positions 21-495.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2544Aspartate By similarity
Regioni411 – 4155Binding site for the 3'-end of tRNA Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0017.
HOVERGENiHBG001028.
InParanoidiP14868.
KOiK01876.
OMAiFCVGPVF.
OrthoDBiEOG7P5T0X.
PhylomeDBiP14868.
TreeFamiTF105676.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14868-1 [UniParc]FASTAAdd to Basket

« Hide

MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD    50
LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ 100
MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP 150
RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS 200
GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP 250
QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 300
EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE 350
ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP 400
FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE 450
KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT 500
P 501
Length:501
Mass (Da):57,136
Last modified:April 16, 2002 - v2
Checksum:iB181572DF0AF5F94
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti256 – 2561M → L in HBSL. 1 Publication
VAR_070038
Natural varianti274 – 2741A → V in HBSL. 1 Publication
VAR_070039
Natural varianti367 – 3671D → Y in HBSL. 1 Publication
VAR_070040
Natural varianti426 – 4261L → F.
Corresponds to variant rs1803165 [ dbSNP | Ensembl ].
VAR_027611
Natural varianti460 – 4601R → H in HBSL. 1 Publication
VAR_070041
Natural varianti464 – 4641P → L in HBSL. 1 Publication
VAR_070042
Natural varianti487 – 4871R → C in HBSL. 1 Publication
VAR_070043
Natural varianti494 – 4941R → C in HBSL. 1 Publication
VAR_070044
Natural varianti494 – 4941R → G in HBSL. 1 Publication
VAR_070045

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 73SAS → TQ in AAA35567. 1 Publication
Sequence conflicti31 – 311I → T in AAI07750. 1 Publication
Sequence conflicti38 – 381Q → H in BAD96196. 1 Publication
Sequence conflicti164 – 1641A → Q in AAA35567. 1 Publication
Sequence conflicti312 – 3121Q → H in AAX07827. 1 Publication
Sequence conflicti414 – 4141N → K in AAA35567. 1 Publication
Sequence conflicti447 – 4471I → N in AAA35567. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05032 mRNA. Translation: AAA35567.1.
AY762100 mRNA. Translation: AAX07827.1.
BT006710 mRNA. Translation: AAP35356.1.
AK222476 mRNA. Translation: BAD96196.1.
AK290607 mRNA. Translation: BAF83296.1.
CH471058 Genomic DNA. Translation: EAX11617.1.
CH471058 Genomic DNA. Translation: EAX11620.1.
BC000629 mRNA. Translation: AAH00629.1.
BC107749 mRNA. Translation: AAI07750.1.
CCDSiCCDS2180.1.
PIRiA34393. SYHUDT.
RefSeqiNP_001340.2. NM_001349.3.
UniGeneiHs.503787.

Genome annotation databases

EnsembliENST00000264161; ENSP00000264161; ENSG00000115866.
GeneIDi1615.
KEGGihsa:1615.
UCSCiuc002tux.1. human.

Polymorphism databases

DMDMi20178330.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05032 mRNA. Translation: AAA35567.1 .
AY762100 mRNA. Translation: AAX07827.1 .
BT006710 mRNA. Translation: AAP35356.1 .
AK222476 mRNA. Translation: BAD96196.1 .
AK290607 mRNA. Translation: BAF83296.1 .
CH471058 Genomic DNA. Translation: EAX11617.1 .
CH471058 Genomic DNA. Translation: EAX11620.1 .
BC000629 mRNA. Translation: AAH00629.1 .
BC107749 mRNA. Translation: AAI07750.1 .
CCDSi CCDS2180.1.
PIRi A34393. SYHUDT.
RefSeqi NP_001340.2. NM_001349.3.
UniGenei Hs.503787.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4J15 X-ray 2.24 A/B 1-501 [» ]
ProteinModelPortali P14868.
SMRi P14868. Positions 21-495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107984. 52 interactions.
IntActi P14868. 12 interactions.
MINTi MINT-141082.
STRINGi 9606.ENSP00000264161.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.

PTM databases

PhosphoSitei P14868.

Polymorphism databases

DMDMi 20178330.

2D gel databases

OGPi P14868.
REPRODUCTION-2DPAGE IPI00216951.

Proteomic databases

MaxQBi P14868.
PaxDbi P14868.
PeptideAtlasi P14868.
PRIDEi P14868.

Protocols and materials databases

DNASUi 1615.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264161 ; ENSP00000264161 ; ENSG00000115866 .
GeneIDi 1615.
KEGGi hsa:1615.
UCSCi uc002tux.1. human.

Organism-specific databases

CTDi 1615.
GeneCardsi GC02M136686.
HGNCi HGNC:2678. DARS.
HPAi HPA020451.
HPA029804.
HPA029805.
MIMi 603084. gene.
615281. phenotype.
neXtProti NX_P14868.
Orphaneti 363412. Hypomyelination with brain stem and spinal cord involvement and leg spasticity.
PharmGKBi PA27146.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0017.
HOVERGENi HBG001028.
InParanoidi P14868.
KOi K01876.
OMAi FCVGPVF.
OrthoDBi EOG7P5T0X.
PhylomeDBi P14868.
TreeFami TF105676.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi DARS. human.
GeneWikii DARS_(gene).
GenomeRNAii 1615.
NextBioi 6634.
PROi P14868.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14868.
Bgeei P14868.
CleanExi HS_DARS.
Genevestigatori P14868.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
InterProi IPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view ]
PANTHERi PTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
Pfami PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view ]
PRINTSi PR01042. TRNASYNTHASP.
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00458. aspS_nondisc. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase."
    Jacobo-Molina A., Peterson R., Yang D.C.H.
    J. Biol. Chem. 264:16608-16612(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of a cell proliferation-inducing gene."
    Kim J.W.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Heart.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Eye.
  8. "Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro."
    Guzzo C.M., Yang D.C.H.
    Biochem. Biophys. Res. Commun. 365:718-723(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KARS.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-74 AND LYS-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: TISSUE SPECIFICITY, VARIANTS HBSL LEU-256; VAL-274; TYR-367; HIS-460; LEU-464; CYS-487; CYS-494 AND GLY-494.

Entry informationi

Entry nameiSYDC_HUMAN
AccessioniPrimary (citable) accession number: P14868
Secondary accession number(s): A8K3J2
, D3DP77, Q2TNI3, Q32Q69, Q53HV4, Q53YC5, Q9BW52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 16, 2002
Last modified: September 3, 2014
This is version 151 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. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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