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O75143 (ATG13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autophagy-related protein 13
Gene names
Name:ATG13
Synonyms:KIAA0652
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

Part of a complex consisting of ATG13, ULK1 and RB1CC1. Interacts with ATG101. Interacts with ULK1 (via C-terminus). Interacts with ULK2 (via C-terminus). Interacts (via the LIR motif) with GABARAP, GABARAPL, GABARAPL2, and LC3A. Interacts with TAB2 and TAB3. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17

Subcellular location

Cytoplasmcytosol By similarity. Preautophagosomal structure By similarity. Note: Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation By similarity.

Domain

The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and LC3A. Ref.17

Post-translational modification

Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-355 is required for efficient clearance of depolarized mitochondria. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Sequence similarities

Belongs to the ATG13 metazoan family.

Sequence caution

The sequence BAA31627.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAD97323.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: O75143-1)

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.
Isoform 2 (identifier: O75143-2)

The sequence of this isoform differs from the canonical sequence as follows:
     265-301: Missing.
Isoform 3 (identifier: O75143-3)

The sequence of this isoform differs from the canonical sequence as follows:
     265-301: Missing.
     428-442: HSDGSSGGSSGNTHD → PCSWPLPCLLSPSTV
     443-517: Missing.
Isoform 4 (identifier: O75143-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     263-299: Missing.
Isoform 5 (identifier: O75143-5)

The sequence of this isoform differs from the canonical sequence as follows:
     262-262: S → SQCVFTVTKAHFQTPTPVVTDTLRVPMAGLAFSH
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Autophagy-related protein 13
PRO_0000050767

Regions

Motif444 – 4474LIR
Compositional bias41 – 444Poly-Ser

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.18
Modified residue3551Phosphoserine; by ULK1
Modified residue3611Phosphoserine By similarity

Natural variations

Alternative sequence1 – 7979Missing in isoform 4.
VSP_044503
Alternative sequence2621S → SQCVFTVTKAHFQTPTPVVT DTLRVPMAGLAFSH in isoform 5.
VSP_044640
Alternative sequence263 – 29937Missing in isoform 4.
VSP_044504
Alternative sequence265 – 30137Missing in isoform 2 and isoform 3.
VSP_002431
Alternative sequence428 – 44215HSDGS…GNTHD → PCSWPLPCLLSPSTV in isoform 3.
VSP_002432
Alternative sequence443 – 51775Missing in isoform 3.
VSP_002433

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 4D6905985EAB78A7

FASTA51756,572
        10         20         30         40         50         60 
METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE 

        70         80         90        100        110        120 
VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYTVYNR 

       130        140        150        160        170        180 
LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV 

       190        200        210        220        230        240 
GTITLSCAYR INLAFMSTRQ FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV 

       250        260        270        280        290        300 
IYPSVEDSQE VCTTSFSTSP PSQLSSSRLS YQPAALGVGS ADLAYPVVFA AGLNATHPHQ 

       310        320        330        340        350        360 
LMVPGKEGGV PLAPNQPVHG TQADQERLAT CTPSDRTHCA ATPSSSEDTE TVSNSSEGRA 

       370        380        390        400        410        420 
SPHDVLETIF VRKVGAFVNK PINQVTLTSL DIPFAMFAPK NLELEDTDPM VNPPDSPETE 

       430        440        450        460        470        480 
SPLQGSLHSD GSSGGSSGNT HDDFVMIDFK PAFSKDDILP MDLGTFYREF QNPPQLSSLS 

       490        500        510 
IDIGAQSMAE DLDSLPEKLA VHEKNVREFD AFVETLQ 

« Hide

Isoform 2 [UniParc].

Checksum: 4EB66893A99956A1
Show »

FASTA48052,823
Isoform 3 [UniParc].

Checksum: F2CE69C9082ABFA5
Show »

FASTA40544,487
Isoform 4 [UniParc].

Checksum: 157846C39C54650F
Show »

FASTA40144,093
Isoform 5 [UniParc].

Checksum: 0965E80906316BD0
Show »

FASTA55060,155

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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. expand/collapse author list , 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 2 AND 4).
Tissue: Brain cortex and Thyroid.
[3]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] (ISOFORM 5).
Tissue: Brain.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 2 AND 3).
Tissue: Cervix, Lung and Muscle.
[7]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Atg101, a novel mammalian autophagy protein interacting with Atg13."
Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.
Autophagy 5:973-979(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG101; ULK1 AND RB1CC1.
[9]"A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy."
Mercer C.A., Kaliappan A., Dennis P.B.
Autophagy 5:649-662(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AUTOPHAGY FACTOR, PHOSPHORYLATION, INTERACTION WITH ULK1 AND ATG101.
[10]"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., Mizushima N.
Mol. Biol. Cell 20:1981-1991(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ULK1 AND RB1CC1, PHOSPHORYLATION.
[11]"ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery."
Jung C.H., Jun C.B., Ro S.H., Kim Y.M., Otto N.M., Cao J., Kundu M., Kim D.H.
Mol. Biol. Cell 20:1992-2003(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ULK1; ULK2 AND RB1CC1, PHOSPHORYLATION BY ULK1; ULK2 AND MTOR, FUNCTION.
[12]"Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated mitophagy."
Joo J.H., Dorsey F.C., Joshi A., Hennessy-Walters K.M., Rose K.L., McCastlain K., Zhang J., Iyengar R., Jung C.H., Suen D.F., Steeves M.A., Yang C.Y., Prater S.M., Kim D.H., Thompson C.B., Youle R.J., Ney P.A., Cleveland J.L., Kundu M.
Mol. Cell 43:572-585(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ULK1, PHOSPHORYLATION BY ULK1 AT SER-355.
[13]"Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism."
Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.
Mol. Cell. Biol. 29:157-171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AUTOPHAGY FACTOR, INTERACTION WITH ULK1 AND ULK2, PHOSPHORYLATION BY ULK1 AND ULK2.
[14]"ULK1 inhibits the kinase activity of mTORC1 and cell proliferation."
Jung C.H., Seo M., Otto N.M., Kim D.H.
Autophagy 7:1212-1221(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."
Kim J., Kundu M., Viollet B., Guan K.L.
Nat. Cell Biol. 13:132-141(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH ULK1 AND RB1CC1.
[16]"TGFbeta-activated kinase 1 (TAK1)-binding proteins (TAB) 2 and 3 negatively regulate autophagy."
Takaesu G., Kobayashi T., Yoshimura A.
J. Biochem. 151:157-166(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAB2 AND TAB3.
[17]"ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
J. Biol. Chem. 287:39275-39290(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABARAP; GABARAPL1; GABARAPL2 AND LC3A, DOMAIN, MUTAGENESIS.
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014552 mRNA. Translation: BAA31627.2. Different initiation.
AK023867 mRNA. Translation: BAB14707.1.
AK294110 mRNA. Translation: BAG57445.1.
AK223603 mRNA. Translation: BAD97323.1. Different initiation.
AC115088 Genomic DNA. No translation available.
AC127035 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW67985.1.
CH471064 Genomic DNA. Translation: EAW67986.1.
CH471064 Genomic DNA. Translation: EAW67987.1.
CH471064 Genomic DNA. Translation: EAW67988.1.
CH471064 Genomic DNA. Translation: EAW67989.1.
CH471064 Genomic DNA. Translation: EAW67990.1.
CH471064 Genomic DNA. Translation: EAW67991.1.
BC001331 mRNA. Translation: AAH01331.1.
BC002378 mRNA. Translation: AAH02378.1.
BC006191 mRNA. Translation: AAH06191.1.
CCDSCCDS44582.1. [O75143-1]
CCDS55760.1. [O75143-5]
CCDS55761.1. [O75143-4]
CCDS7921.1. [O75143-2]
RefSeqNP_001136145.1. NM_001142673.2. [O75143-1]
NP_001192048.1. NM_001205119.1. [O75143-5]
NP_001192049.1. NM_001205120.1. [O75143-1]
NP_001192050.1. NM_001205121.1. [O75143-2]
NP_001192051.1. NM_001205122.1. [O75143-4]
NP_055556.2. NM_014741.4. [O75143-2]
XP_005253319.1. XM_005253262.1. [O75143-5]
XP_005253320.1. XM_005253263.1. [O75143-5]
XP_005253322.1. XM_005253265.1. [O75143-5]
XP_005253323.1. XM_005253266.1. [O75143-5]
XP_005253325.1. XM_005253268.1. [O75143-5]
XP_006718457.1. XM_006718394.1. [O75143-5]
XP_006718458.1. XM_006718395.1. [O75143-5]
XP_006718459.1. XM_006718396.1. [O75143-5]
UniGeneHs.127403.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3WANX-ray1.77A/B436-447[»]
3WAOX-ray2.60A/B/C/D436-447[»]
3WAPX-ray3.10A436-447[»]
ProteinModelPortalO75143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115120. 14 interactions.
DIPDIP-60540N.
IntActO75143. 13 interactions.
MINTMINT-8247472.

PTM databases

PhosphoSiteO75143.

Proteomic databases

MaxQBO75143.
PaxDbO75143.
PRIDEO75143.

Protocols and materials databases

DNASU9776.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312040; ENSP00000310321; ENSG00000175224. [O75143-1]
ENST00000359513; ENSP00000352500; ENSG00000175224. [O75143-1]
ENST00000434074; ENSP00000400642; ENSG00000175224. [O75143-1]
ENST00000451945; ENSP00000404900; ENSG00000175224. [O75143-2]
ENST00000524625; ENSP00000433543; ENSG00000175224. [O75143-2]
ENST00000526508; ENSP00000431974; ENSG00000175224. [O75143-1]
ENST00000528494; ENSP00000432412; ENSG00000175224. [O75143-5]
ENST00000529655; ENSP00000433756; ENSG00000175224. [O75143-2]
ENST00000530500; ENSP00000434390; ENSG00000175224. [O75143-4]
GeneID9776.
KEGGhsa:9776.
UCSCuc001ncz.3. human. [O75143-2]
uc001ndb.3. human. [O75143-1]
uc010rgv.2. human. [O75143-4]

Organism-specific databases

CTD9776.
GeneCardsGC11P046638.
HGNCHGNC:29091. ATG13.
HPAHPA039350.
MIM615088. gene.
neXtProtNX_O75143.
PharmGKBPA165543187.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266388.
HOGENOMHOG000008446.
KOK08331.
OMAMCVEISL.
OrthoDBEOG744T8P.
PhylomeDBO75143.
TreeFamTF321599.

Gene expression databases

ArrayExpressO75143.
BgeeO75143.
CleanExHS_KIAA0652.
GenevestigatorO75143.

Family and domain databases

InterProIPR018731. Autophagy-rel_p13.
[Graphical view]
PfamPF10033. ATG13. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATG13. human.
GeneWikiAutophagy-related_protein_13.
GenomeRNAi9776.
NextBio36806.
PROO75143.
SOURCESearch...

Entry information

Entry nameATG13_HUMAN
AccessionPrimary (citable) accession number: O75143
Secondary accession number(s): B4DFI4 expand/collapse secondary AC list , D3DQQ1, D3DQQ2, E9PQZ8, Q53EN6, Q9BRL3, Q9H8B0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM