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P49589

- SYCC_HUMAN

UniProt

P49589 - SYCC_HUMAN

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Protein

Cysteine--tRNA ligase, cytoplasmic

Gene

CARS

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

Functioni

Catalytic activityi

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551ZincBy similarity
Metal bindingi348 – 3481ZincBy similarity
Metal bindingi373 – 3731ZincBy similarity
Metal bindingi377 – 3771ZincBy similarity
Binding sitei409 – 4091ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. cysteine-tRNA ligase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. protein homodimerization activity Source: UniProtKB
  5. tRNA binding Source: UniProtKB

GO - Biological processi

  1. cysteinyl-tRNA aminoacylation Source: UniProtKB
  2. gene expression Source: Reactome
  3. 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, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine--tRNA ligase, cytoplasmic (EC:6.1.1.16)
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name:
CysRS
Gene namesi
Name:CARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1493. CARS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving CARS is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;11)(p23;p15) with ALK.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA26079.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 748747Cysteine--tRNA ligase, cytoplasmicPRO_0000159550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei503 – 5031N6-acetyllysine1 Publication
Modified residuei746 – 7461Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49589.
PaxDbiP49589.
PRIDEiP49589.

PTM databases

PhosphoSiteiP49589.

Expressioni

Gene expression databases

BgeeiP49589.
CleanExiHS_CARS.
ExpressionAtlasiP49589. baseline and differential.
GenevestigatoriP49589.

Organism-specific databases

HPAiHPA002383.
HPA002384.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi107283. 32 interactions.
IntActiP49589. 4 interactions.
STRINGi9606.ENSP00000369897.

Structurei

3D structure databases

ProteinModelPortaliP49589.
SMRiP49589. Positions 18-134, 214-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 6711"HIGH" regionAdd
BLAST
Motifi406 – 4105"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0215.
GeneTreeiENSGT00390000006347.
HOGENOMiHOG000245252.
HOVERGENiHBG002089.
InParanoidiP49589.
KOiK01883.
OMAiEMFLSES.
PhylomeDBiP49589.
TreeFamiTF300384.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR00435. cysS. 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. Align

Isoform 1 (identifier: P49589-1) [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
MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV
60 70 80 90 100
TWYCCGPTVY DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD
110 120 130 140 150
KIIKRARQNH LFEQYREKRP EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ
160 170 180 190 200
MLERIQHAVQ LATEPLEKAV QSRLTGEEVN SCVEVLLEEA KDLLSDWLDS
210 220 230 240 250
TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR VSEYVPEIVN
260 270 280 290 300
FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG
310 320 330 340 350
EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA
360 370 380 390 400
MAGTLLGASM DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL
410 420 430 440 450
TIAGCKMSKS LKNFITIKDA LKKHSARQLR LAFLMHSWKD TLDYSSNTME
460 470 480 490 500
SALQYEKFLN EFFLNVKDIL RAPVDITGQF EKWGEEEAEL NKNFYDKKTA
510 520 530 540 550
IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN QALLENIALY
560 570 580 590 600
LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK
610 620 630 640 650
IAREQKVPEI LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE
660 670 680 690 700
REEKRRVEEE KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK
710 720 730 740
FDENGLPTHD MEGKELSKGQ AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ
Length:748
Mass (Da):85,473
Last modified:January 31, 2002 - v3
Checksum:iD0B7A29EC03AA87F
GO
Isoform 2 (identifier: P49589-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     705-748: GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ → VSMVCPHMTWRAKSSAKGKPRS

Note: Found in 20% of the mRNAs.

Show »
Length:726
Mass (Da):82,846
Checksum:i92C51DF9289FE47D
GO
Isoform 3 (identifier: P49589-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-9: G → APDYRSILSI...KGQPCRLQAS

Note: Contains a phosphoserine at position 79.

Show »
Length:831
Mass (Da):94,638
Checksum:iC0080CD332F79B8F
GO

Sequence cautioni

The sequence AAA73901.1 differs from that shown. Reason: Frameshift at position 619. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 91G → APDYRSILSISDEAARAQAL NEHLSTRSYVQGYSLSQADV DAFRQLSAPPADPQLFHVAR WFRHIEALLGSPCGKGQPCR LQAS in isoform 3. 2 PublicationsVSP_043571
Alternative sequencei705 – 74844GLPTH…NGSFQ → VSMVCPHMTWRAKSSAKGKP RS in isoform 2. 2 PublicationsVSP_006312Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06845 mRNA. Translation: AAA73901.1. Frameshift.
AF288206 mRNA. Translation: AAG00578.1.
AF288207 mRNA. Translation: AAG00579.1.
BT009913 mRNA. Translation: AAP88915.1.
AK302644 mRNA. Translation: BAG63885.1.
BX647906 mRNA. Translation: CAI46108.1.
AC108448 Genomic DNA. No translation available.
AC131971 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02541.1.
BC002880 mRNA. Translation: AAH02880.1.
CCDSiCCDS41600.1. [P49589-3]
CCDS41602.1. [P49589-2]
CCDS7742.1. [P49589-1]
RefSeqiNP_001014437.1. NM_001014437.2. [P49589-3]
NP_001742.1. NM_001751.5. [P49589-1]
NP_644802.1. NM_139273.3. [P49589-2]
UniGeneiHs.274873.

Genome annotation databases

EnsembliENST00000278224; ENSP00000278224; ENSG00000110619. [P49589-2]
ENST00000380525; ENSP00000369897; ENSG00000110619. [P49589-3]
ENST00000397111; ENSP00000380300; ENSG00000110619. [P49589-1]
GeneIDi833.
KEGGihsa:833.
UCSCiuc001lxf.3. human. [P49589-3]
uc001lxg.3. human. [P49589-2]
uc001lxh.3. human. [P49589-1]

Polymorphism databases

DMDMi20141641.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06845 mRNA. Translation: AAA73901.1 . Frameshift.
AF288206 mRNA. Translation: AAG00578.1 .
AF288207 mRNA. Translation: AAG00579.1 .
BT009913 mRNA. Translation: AAP88915.1 .
AK302644 mRNA. Translation: BAG63885.1 .
BX647906 mRNA. Translation: CAI46108.1 .
AC108448 Genomic DNA. No translation available.
AC131971 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02541.1 .
BC002880 mRNA. Translation: AAH02880.1 .
CCDSi CCDS41600.1. [P49589-3 ]
CCDS41602.1. [P49589-2 ]
CCDS7742.1. [P49589-1 ]
RefSeqi NP_001014437.1. NM_001014437.2. [P49589-3 ]
NP_001742.1. NM_001751.5. [P49589-1 ]
NP_644802.1. NM_139273.3. [P49589-2 ]
UniGenei Hs.274873.

3D structure databases

ProteinModelPortali P49589.
SMRi P49589. Positions 18-134, 214-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107283. 32 interactions.
IntActi P49589. 4 interactions.
STRINGi 9606.ENSP00000369897.

Chemistry

DrugBanki DB00151. L-Cysteine.

PTM databases

PhosphoSitei P49589.

Polymorphism databases

DMDMi 20141641.

Proteomic databases

MaxQBi P49589.
PaxDbi P49589.
PRIDEi P49589.

Protocols and materials databases

DNASUi 833.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000278224 ; ENSP00000278224 ; ENSG00000110619 . [P49589-2 ]
ENST00000380525 ; ENSP00000369897 ; ENSG00000110619 . [P49589-3 ]
ENST00000397111 ; ENSP00000380300 ; ENSG00000110619 . [P49589-1 ]
GeneIDi 833.
KEGGi hsa:833.
UCSCi uc001lxf.3. human. [P49589-3 ]
uc001lxg.3. human. [P49589-2 ]
uc001lxh.3. human. [P49589-1 ]

Organism-specific databases

CTDi 833.
GeneCardsi GC11M003022.
H-InvDB HIX0128660.
HGNCi HGNC:1493. CARS.
HPAi HPA002383.
HPA002384.
MIMi 123859. gene.
neXtProti NX_P49589.
Orphaneti 178342. Inflammatory myofibroblastic tumor.
PharmGKBi PA26079.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0215.
GeneTreei ENSGT00390000006347.
HOGENOMi HOG000245252.
HOVERGENi HBG002089.
InParanoidi P49589.
KOi K01883.
OMAi EMFLSES.
PhylomeDBi P49589.
TreeFami TF300384.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi CARS. human.
GenomeRNAii 833.
NextBioi 3450.
PROi P49589.
SOURCEi Search...

Gene expression databases

Bgeei P49589.
CleanExi HS_CARS.
ExpressionAtlasi P49589. baseline and differential.
Genevestigatori P49589.

Family and domain databases

Gene3Di 3.40.50.620. 2 hits.
HAMAPi MF_00041. Cys_tRNA_synth.
InterProi IPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view ]
PANTHERi PTHR10890. PTHR10890. 1 hit.
Pfami PF01406. tRNA-synt_1e. 1 hit.
[Graphical view ]
PRINTSi PR00983. TRNASYNTHCYS.
SUPFAMi SSF47323. SSF47323. 1 hit.
TIGRFAMsi TIGR00435. cysS. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase."
    Cruzen M.E., Arfin S.M.
    DNA Seq. 4:243-248(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase."
    Davidson E., Caffarella J., Vitseva O., Hou Y.M., King M.P.
    Biol. Chem. 382:399-406(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 3).
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Cervix.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Lung.
  9. "Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor."
    Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B., De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.
    Genes Chromosomes Cancer 34:354-362(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH ALK.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYCC_HUMAN
AccessioniPrimary (citable) accession number: P49589
Secondary accession number(s): Q53XI8
, Q5HYE4, Q9HD24, Q9HD25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 31, 2002
Last modified: November 26, 2014
This is version 140 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

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3