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Q9NSD9

- SYFB_HUMAN

UniProt

Q9NSD9 - SYFB_HUMAN

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Protein

Phenylalanine--tRNA ligase beta subunit

Gene

FARSB

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

Functioni

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. phenylalanine-tRNA ligase activity Source: ProtInc
  4. RNA binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. phenylalanyl-tRNA aminoacylation Source: InterPro
  3. translation Source: ProtInc
  4. tRNA aminoacylation for protein translation Source: Reactome
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

BRENDAi6.1.1.20. 2681.
ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase beta subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name:
PheRS
Gene namesi
Name:FARSB
Synonyms:FARSLB, FRSB
ORF Names:HSPC173
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:17800. FARSB.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162388068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Phenylalanine--tRNA ligase beta subunitPRO_0000127016Add
BLAST

Proteomic databases

MaxQBiQ9NSD9.
PaxDbiQ9NSD9.
PRIDEiQ9NSD9.

PTM databases

PhosphoSiteiQ9NSD9.

Expressioni

Gene expression databases

BgeeiQ9NSD9.
CleanExiHS_FARSB.
ExpressionAtlasiQ9NSD9. baseline and differential.
GenevestigatoriQ9NSD9.

Organism-specific databases

HPAiHPA036678.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Protein-protein interaction databases

BioGridi115367. 35 interactions.
DIPiDIP-32869N.
IntActiQ9NSD9. 7 interactions.
MINTiMINT-3073662.
STRINGi9606.ENSP00000281828.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi8 – 158Combined sources
Helixi23 – 308Combined sources
Beta strandi34 – 407Combined sources
Helixi41 – 455Combined sources
Beta strandi48 – 503Combined sources
Beta strandi56 – 6611Combined sources
Helixi77 – 8711Combined sources
Beta strandi97 – 993Combined sources
Beta strandi107 – 1104Combined sources
Turni112 – 1176Combined sources
Beta strandi120 – 1267Combined sources
Helixi133 – 14513Combined sources
Turni146 – 15510Combined sources
Beta strandi156 – 1638Combined sources
Helixi164 – 1663Combined sources
Beta strandi171 – 1766Combined sources
Beta strandi178 – 1803Combined sources
Helixi194 – 2007Combined sources
Turni205 – 21410Combined sources
Beta strandi220 – 2245Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 2404Combined sources
Beta strandi251 – 2588Combined sources
Helixi260 – 27415Combined sources
Helixi275 – 2773Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi305 – 3106Combined sources
Helixi311 – 3188Combined sources
Helixi324 – 33310Combined sources
Beta strandi337 – 3404Combined sources
Beta strandi342 – 35110Combined sources
Helixi361 – 37212Combined sources
Helixi374 – 3763Combined sources
Helixi392 – 40615Combined sources
Beta strandi416 – 4183Combined sources
Helixi420 – 4234Combined sources
Helixi425 – 4273Combined sources
Beta strandi438 – 4414Combined sources
Helixi445 – 4473Combined sources
Beta strandi448 – 4503Combined sources
Helixi455 – 46410Combined sources
Turni465 – 4673Combined sources
Beta strandi472 – 48312Combined sources
Beta strandi490 – 50516Combined sources
Helixi508 – 52114Combined sources
Turni528 – 5314Combined sources
Beta strandi532 – 5376Combined sources
Beta strandi543 – 55311Combined sources
Beta strandi556 – 5649Combined sources
Helixi566 – 5716Combined sources
Beta strandi578 – 5847Combined sources
Helixi586 – 5883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4GX-ray3.30B/D/F/H/J/L/N/P1-589[»]
ProteinModelPortaliQ9NSD9.
SMRiQ9NSD9. Positions 1-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini302 – 37978B5PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 B5 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0072.
GeneTreeiENSGT00530000063489.
HOGENOMiHOG000105095.
HOVERGENiHBG009523.
InParanoidiQ9NSD9.
KOiK01890.
OMAiEVMPLIL.
OrthoDBiEOG7R2BJ6.
PhylomeDBiQ9NSD9.
TreeFamiTF105681.

Family and domain databases

Gene3Di3.30.56.20. 1 hit.
InterProiIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 2 hits.
SSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR00471. pheT_arch. 1 hit.
PROSITEiPS51483. B5. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NSD9-1) [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
MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG
60 70 80 90 100
NVKAAGASDV VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM
110 120 130 140 150
PDGKIQKLII TEETAKIRPF AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI
160 170 180 190 200
CRKRALVAIG THDLDTLSGP FTYTAKRPSD IKFKPLNKTK EYTACELMNI
210 220 230 240 250
YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD HSRITVNTRN
260 270 280 290 300
IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP
310 320 330 340 350
ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE
360 370 380 390 400
IPPTRADIIH ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL
410 420 430 440 450
RHDMAAAGFT EALTFALCSQ EDIADKLGVD ISATKAVHIS NPKTAEFQVA
460 470 480 490 500
RTTLLPGLLK TIAANRKMPL PLKLFEISDI VIKDSNTDVG AKNYRHLCAV
510 520 530 540 550
YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG PAFFPGRCAE
560 570 580
IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL
Length:589
Mass (Da):66,116
Last modified:May 18, 2010 - v3
Checksum:i6425BA46D124BC08
GO
Isoform 2 (identifier: Q9NSD9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Note: No experimental confirmation available

Show »
Length:490
Mass (Da):54,861
Checksum:iEB9B48047A2AF094
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811Q → R in AAF29136. (PubMed:11042152)Curated
Sequence conflicti555 – 5551G → V in BAA95608. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti585 – 5851V → I.
Corresponds to variant rs7185 [ dbSNP | Ensembl ].
VAR_071245

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9999Missing in isoform 2. 1 PublicationVSP_056866Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84430 mRNA. Translation: BAA95608.1.
AF042346 mRNA. Translation: AAD02220.1.
AF161521 mRNA. Translation: AAF29136.1.
AK294158 mRNA. Translation: BAG57481.1.
AC097461 Genomic DNA. Translation: AAX88958.1.
AC104772 Genomic DNA. Translation: AAX81986.1.
CH471063 Genomic DNA. Translation: EAW70804.1.
BC017783 mRNA. Translation: AAH17783.1.
CCDSiCCDS2454.1.
RefSeqiNP_005678.3. NM_005687.3.
XP_006712231.1. XM_006712168.1.
XP_006712232.1. XM_006712169.1.
XP_006712233.1. XM_006712170.1.
UniGeneiHs.471452.

Genome annotation databases

EnsembliENST00000281828; ENSP00000281828; ENSG00000116120. [Q9NSD9-1]
GeneIDi10056.
KEGGihsa:10056.
UCSCiuc002vne.1. human. [Q9NSD9-1]

Polymorphism databases

DMDMi296452943.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84430 mRNA. Translation: BAA95608.1 .
AF042346 mRNA. Translation: AAD02220.1 .
AF161521 mRNA. Translation: AAF29136.1 .
AK294158 mRNA. Translation: BAG57481.1 .
AC097461 Genomic DNA. Translation: AAX88958.1 .
AC104772 Genomic DNA. Translation: AAX81986.1 .
CH471063 Genomic DNA. Translation: EAW70804.1 .
BC017783 mRNA. Translation: AAH17783.1 .
CCDSi CCDS2454.1.
RefSeqi NP_005678.3. NM_005687.3.
XP_006712231.1. XM_006712168.1.
XP_006712232.1. XM_006712169.1.
XP_006712233.1. XM_006712170.1.
UniGenei Hs.471452.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L4G X-ray 3.30 B/D/F/H/J/L/N/P 1-589 [» ]
ProteinModelPortali Q9NSD9.
SMRi Q9NSD9. Positions 1-589.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115367. 35 interactions.
DIPi DIP-32869N.
IntActi Q9NSD9. 7 interactions.
MINTi MINT-3073662.
STRINGi 9606.ENSP00000281828.

Chemistry

DrugBanki DB00120. L-Phenylalanine.

PTM databases

PhosphoSitei Q9NSD9.

Polymorphism databases

DMDMi 296452943.

Proteomic databases

MaxQBi Q9NSD9.
PaxDbi Q9NSD9.
PRIDEi Q9NSD9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281828 ; ENSP00000281828 ; ENSG00000116120 . [Q9NSD9-1 ]
GeneIDi 10056.
KEGGi hsa:10056.
UCSCi uc002vne.1. human. [Q9NSD9-1 ]

Organism-specific databases

CTDi 10056.
GeneCardsi GC02M223435.
H-InvDB HIX0002878.
HGNCi HGNC:17800. FARSB.
HPAi HPA036678.
MIMi 609690. gene.
neXtProti NX_Q9NSD9.
PharmGKBi PA162388068.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0072.
GeneTreei ENSGT00530000063489.
HOGENOMi HOG000105095.
HOVERGENi HBG009523.
InParanoidi Q9NSD9.
KOi K01890.
OMAi EVMPLIL.
OrthoDBi EOG7R2BJ6.
PhylomeDBi Q9NSD9.
TreeFami TF105681.

Enzyme and pathway databases

BRENDAi 6.1.1.20. 2681.
Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi FARSB. human.
GeneWikii FARSB.
GenomeRNAii 10056.
NextBioi 37993.
PROi Q9NSD9.
SOURCEi Search...

Gene expression databases

Bgeei Q9NSD9.
CleanExi HS_FARSB.
ExpressionAtlasi Q9NSD9. baseline and differential.
Genevestigatori Q9NSD9.

Family and domain databases

Gene3Di 3.30.56.20. 1 hit.
InterProi IPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view ]
Pfami PF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view ]
SMARTi SM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view ]
SUPFAMi SSF46955. SSF46955. 2 hits.
SSF56037. SSF56037. 1 hit.
TIGRFAMsi TIGR00471. pheT_arch. 1 hit.
PROSITEi PS51483. B5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Motegi H., Noda T., Shiba K.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-585.
  2. "Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells."
    Rodova M., Ankilova V., Safro M.G.
    Biochem. Biophys. Res. Commun. 255:765-773(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-585.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-585.
    Tissue: Umbilical cord blood.
  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] (ISOFORM 2), VARIANT ILE-585.
    Tissue: Brain cortex.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-585.
  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] (ISOFORM 1), VARIANT ILE-585.
    Tissue: Testis.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYFB_HUMAN
AccessioniPrimary (citable) accession number: Q9NSD9
Secondary accession number(s): B4DFM0
, O95708, Q4ZFX1, Q57ZJ5, Q9NZZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 137 of the entry and version 3 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