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Q9H0A0

- NAT10_HUMAN

UniProt

Q9H0A0 - NAT10_HUMAN

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Protein

N-acetyltransferase 10

Gene

NAT10

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

Functioni

Has protein acetyltransferase activity in vitro. Can acetylate both histones and microtubules. Histone acetylation may regulate transcription and mitotic chromosome de-condensation. Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization. Acetylates alpha-tubulin, which may affect microtubule stability and cell division.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi284 – 2918ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. N-acetyltransferase activity Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyltransferase 10 (EC:2.3.1.-)
Gene namesi
Name:NAT10
Synonyms:ALP, KIAA1709
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:29830. NAT10.

Subcellular locationi

Nucleusnucleolus 3 Publications
Note: Nucleolar in interphase and redistributes to the perichromosomal layer and to the midbody during telophase.

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025N-acetyltransferase 10PRO_0000215883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei426 – 4261N6-acetyllysine1 Publication
Modified residuei934 – 9341Phosphoserine1 Publication
Modified residuei984 – 9841Phosphoserine1 Publication
Modified residuei987 – 9871Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0A0.
PaxDbiQ9H0A0.
PRIDEiQ9H0A0.

2D gel databases

SWISS-2DPAGEQ9H0A0.

PTM databases

PhosphoSiteiQ9H0A0.

Expressioni

Inductioni

Transcriptionally activated by genotoxic agents; possible role in DNA damage and induction of cellular resistance to genotoxic agents.1 Publication

Gene expression databases

BgeeiQ9H0A0.
CleanExiHS_NAT10.
ExpressionAtlasiQ9H0A0. baseline and differential.
GenevestigatoriQ9H0A0.

Organism-specific databases

HPAiCAB035546.

Interactioni

Subunit structurei

Interacts with SUN1 (via N-terminus). Also interacts with TERT.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LYARQ9NX581EBI-876527,EBI-713507

Protein-protein interaction databases

BioGridi120521. 29 interactions.
IntActiQ9H0A0. 18 interactions.
MINTiMINT-2817086.
STRINGi9606.ENSP00000257829.

Structurei

3D structure databases

ProteinModelPortaliQ9H0A0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini558 – 753196N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni702 – 1025324Required for localization to the nucleolus and midbodyAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi989 – 102537Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the UPF0202 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1444.
GeneTreeiENSGT00390000009140.
HOGENOMiHOG000210833.
HOVERGENiHBG052206.
InParanoidiQ9H0A0.
KOiK14521.
OMAiKFLQQMV.
OrthoDBiEOG7QK0B5.
PhylomeDBiQ9H0A0.
TreeFamiTF300601.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR013562. DUF1726.
IPR000182. GNAT_dom.
IPR007807. Helicase_dom.
IPR027992. tRNA_bind_dom.
[Graphical view]
PfamiPF08351. DUF1726. 1 hit.
PF13718. GNAT_acetyltr_2. 1 hit.
PF05127. Helicase_RecD. 1 hit.
PF13725. tRNA_bind_2. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0A0-1) [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
MHRKKVDNRI RILIENGVAE RQRSLFVVVG DRGKDQVVIL HHMLSKATVK
60 70 80 90 100
ARPSVLWCYK KELGFSSHRK KRMRQLQKKI KNGTLNIKQD DPFELFIAAT
110 120 130 140 150
NIRYCYYNET HKILGNTFGM CVLQDFEALT PNLLARTVET VEGGGLVVIL
160 170 180 190 200
LRTMNSLKQL YTVTMDVHSR YRTEAHQDVV GRFNERFILS LASCKKCLVI
210 220 230 240 250
DDQLNILPIS SHVATMEALP PQTPDESLGP SDLELRELKE SLQDTQPVGV
260 270 280 290 300
LVDCCKTLDQ AKAVLKFIEG ISEKTLRSTV ALTAARGRGK SAALGLAIAG
310 320 330 340 350
AVAFGYSNIF VTSPSPDNLH TLFEFVFKGF DALQYQEHLD YEIIQSLNPE
360 370 380 390 400
FNKAVIRVNV FREHRQTIQY IHPADAVKLG QAELVVIDEA AAIPLPLVKS
410 420 430 440 450
LLGPYLVFMA STINGYEGTG RSLSLKLIQQ LRQQSAQSQV STTAENKTTT
460 470 480 490 500
TARLASARTL YEVSLQESIR YAPGDAVEKW LNDLLCLDCL NITRIVSGCP
510 520 530 540 550
LPEACELYYV NRDTLFCYHK ASEVFLQRLM ALYVASHYKN SPNDLQMLSD
560 570 580 590 600
APAHHLFCLL PPVPPTQNAL PEVLAVIQVC LEGEISRQSI LNSLSRGKKA
610 620 630 640 650
SGDLIPWTVS EQFQDPDFGG LSGGRVVRIA VHPDYQGMGY GSRALQLLQM
660 670 680 690 700
YYEGRFPCLE EKVLETPQEI HTVSSEAVSL LEEVITPRKD LPPLLLKLNE
710 720 730 740 750
RPAERLDYLG VSYGLTPRLL KFWKRAGFVP VYLRQTPNDL TGEHSCIMLK
760 770 780 790 800
TLTDEDEADQ GGWLAAFWKD FRRRFLALLS YQFSTFSPSL ALNIIQNRNM
810 820 830 840 850
GKPAQPALSR EELEALFLPY DLKRLEMYSR NMVDYHLIMD MIPAISRIYF
860 870 880 890 900
LNQLGDLALS AAQSALLLGI GLQHKSVDQL EKEIELPSGQ LMGLFNRIIR
910 920 930 940 950
KVVKLFNEVQ EKAIEEQMVA AKDVVMEPTM KTLSDDLDEA AKEFQEKHKK
960 970 980 990 1000
EVGKLKSMDL SEYIIRGDDE EWNEVLNKAG PNASIISLKS DKKRKLEAKQ
1010 1020
EPKQSKKLKN RETKNKKDMK LKRKK
Length:1,025
Mass (Da):115,730
Last modified:November 30, 2010 - v2
Checksum:i88734933A46EB0EE
GO
Isoform 2 (identifier: Q9H0A0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:953
Mass (Da):107,297
Checksum:iFC718FD5410FEAAA
GO

Sequence cautioni

The sequence AAO49126.1 differs from that shown. Reason: Frameshift at position 981.
The sequence BAB21800.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261F → L in BAA91800. (PubMed:14702039)Curated
Sequence conflicti162 – 1621T → A in AAO49126. (PubMed:14592445)Curated
Sequence conflicti315 – 3151S → C in BAB13995. (PubMed:14702039)Curated
Sequence conflicti405 – 4051Y → C in BAG57396. (PubMed:14702039)Curated
Sequence conflicti879 – 8791Q → R in BAB13995. (PubMed:14702039)Curated
Sequence conflicti971 – 9711E → G in BAG57396. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611Y → H.6 Publications
Corresponds to variant rs2957516 [ dbSNP | Ensembl ].
VAR_059858
Natural varianti983 – 9831A → T.
Corresponds to variant rs36006049 [ dbSNP | Ensembl ].
VAR_061894

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_054018Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB051496 mRNA. Translation: BAB21800.1. Different initiation.
AL136882 mRNA. Translation: CAB66816.1.
AK001636 mRNA. Translation: BAA91800.1.
AK022241 mRNA. Translation: BAB13995.1.
AK294044 mRNA. Translation: BAG57396.1.
AC090469 Genomic DNA. No translation available.
BC035558 mRNA. Translation: AAH35558.1.
AF489535 mRNA. Translation: AAO49126.1. Frameshift.
CCDSiCCDS44568.1. [Q9H0A0-2]
CCDS7889.1. [Q9H0A0-1]
RefSeqiNP_001137502.1. NM_001144030.1.
NP_078938.2. NM_024662.2.
XP_005253056.1. XM_005252999.1. [Q9H0A0-1]
UniGeneiHs.577281.

Genome annotation databases

EnsembliENST00000257829; ENSP00000257829; ENSG00000135372. [Q9H0A0-1]
ENST00000531159; ENSP00000433011; ENSG00000135372. [Q9H0A0-2]
GeneIDi55226.
KEGGihsa:55226.
UCSCiuc001mvk.3. human. [Q9H0A0-1]

Polymorphism databases

DMDMi313104140.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB051496 mRNA. Translation: BAB21800.1 . Different initiation.
AL136882 mRNA. Translation: CAB66816.1 .
AK001636 mRNA. Translation: BAA91800.1 .
AK022241 mRNA. Translation: BAB13995.1 .
AK294044 mRNA. Translation: BAG57396.1 .
AC090469 Genomic DNA. No translation available.
BC035558 mRNA. Translation: AAH35558.1 .
AF489535 mRNA. Translation: AAO49126.1 . Frameshift.
CCDSi CCDS44568.1. [Q9H0A0-2 ]
CCDS7889.1. [Q9H0A0-1 ]
RefSeqi NP_001137502.1. NM_001144030.1.
NP_078938.2. NM_024662.2.
XP_005253056.1. XM_005252999.1. [Q9H0A0-1 ]
UniGenei Hs.577281.

3D structure databases

ProteinModelPortali Q9H0A0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120521. 29 interactions.
IntActi Q9H0A0. 18 interactions.
MINTi MINT-2817086.
STRINGi 9606.ENSP00000257829.

PTM databases

PhosphoSitei Q9H0A0.

Polymorphism databases

DMDMi 313104140.

2D gel databases

SWISS-2DPAGE Q9H0A0.

Proteomic databases

MaxQBi Q9H0A0.
PaxDbi Q9H0A0.
PRIDEi Q9H0A0.

Protocols and materials databases

DNASUi 55226.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257829 ; ENSP00000257829 ; ENSG00000135372 . [Q9H0A0-1 ]
ENST00000531159 ; ENSP00000433011 ; ENSG00000135372 . [Q9H0A0-2 ]
GeneIDi 55226.
KEGGi hsa:55226.
UCSCi uc001mvk.3. human. [Q9H0A0-1 ]

Organism-specific databases

CTDi 55226.
GeneCardsi GC11P034084.
HGNCi HGNC:29830. NAT10.
HPAi CAB035546.
MIMi 609221. gene.
neXtProti NX_Q9H0A0.
PharmGKBi PA143485555.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1444.
GeneTreei ENSGT00390000009140.
HOGENOMi HOG000210833.
HOVERGENi HBG052206.
InParanoidi Q9H0A0.
KOi K14521.
OMAi KFLQQMV.
OrthoDBi EOG7QK0B5.
PhylomeDBi Q9H0A0.
TreeFami TF300601.

Miscellaneous databases

ChiTaRSi NAT10. human.
GeneWikii NAT10.
GenomeRNAii 55226.
NextBioi 35500237.
PROi Q9H0A0.
SOURCEi Search...

Gene expression databases

Bgeei Q9H0A0.
CleanExi HS_NAT10.
ExpressionAtlasi Q9H0A0. baseline and differential.
Genevestigatori Q9H0A0.

Family and domain databases

Gene3Di 3.40.630.30. 2 hits.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR013562. DUF1726.
IPR000182. GNAT_dom.
IPR007807. Helicase_dom.
IPR027992. tRNA_bind_dom.
[Graphical view ]
Pfami PF08351. DUF1726. 1 hit.
PF13718. GNAT_acetyltr_2. 1 hit.
PF05127. Helicase_RecD. 1 hit.
PF13725. tRNA_bind_2. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-461.
    Tissue: Testis.
  3. "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] (ISOFORMS 1 AND 2), VARIANT HIS-461.
    Tissue: Cerebellum and Mammary gland.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 HIS-461.
    Tissue: Brain.
  6. "Molecular cloning of a novel human gene encoding histone acetyltransferase-like protein involved in transcriptional activation of hTERT."
    Lv J., Liu H., Wang Q., Tang Z., Hou L., Zhang B.
    Biochem. Biophys. Res. Commun. 311:506-513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-1025, FUNCTION, SUBCELLULAR LOCATION, VARIANT HIS-461.
    Tissue: Cervix carcinoma.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Histone acetyltransferase hALP and nuclear membrane protein hsSUN1 function in de-condensation of mitotic chromosomes."
    Chi Y.-H., Haller K., Peloponese J.-M. Jr., Jeang K.-T.
    J. Biol. Chem. 282:27447-27458(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUN1.
  9. "Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation."
    Fu D., Collins K.
    Mol. Cell 28:773-785(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TERT.
  10. "DNA damage induces N-acetyltransferase NAT10 gene expression through transcriptional activation."
    Liu H., Ling Y., Gong Y., Sun Y., Hou L., Zhang B.
    Mol. Cell. Biochem. 300:249-258(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY GENOTOXIC AGENTS.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-934; SER-984 AND SER-987, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "NAT10, a nucleolar protein, localizes to the midbody and regulates cytokinesis and acetylation of microtubules."
    Shen Q., Zheng X., McNutt M.A., Guang L., Sun Y., Wang J., Gong Y., Hou L., Zhang B.
    Exp. Cell Res. 315:1653-1667(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "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-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNAT10_HUMAN
AccessioniPrimary (citable) accession number: Q9H0A0
Secondary accession number(s): B4DFD5
, E7ESU4, E9PMN9, Q86WK5, Q9C0F4, Q9HA61, Q9NVF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 128 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 11
    Human chromosome 11: 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
  6. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

External Data

Dasty 3