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P60520 (GBRL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid receptor-associated protein-like 2
Alternative name(s):
GABA(A) receptor-associated protein-like 2
Ganglioside expression factor 2
Short name=GEF-2
General protein transport factor p16
Golgi-associated ATPase enhancer of 16 kDa
Short name=GATE-16
MAP1 light chain 3-related protein
Gene names
Name:GABARAPL2
Synonyms:FLC3A, GEF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 By similarity. Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Ref.17 Ref.26

Subunit structure

Monomer. Interacts with GABRG2, NSF, GOSR1 and beta-tubulin By similarity. Interacts with ATG3, ATG7, ATG13 and ULK1. Interacts with TP53INP1 and TP53INP2. Interacts with TBC1D25. Directly interacts with SQSTM1 and BNIP3. Interacts with TECPR2 and PCM1. Ref.1 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26

Subcellular location

Golgi apparatus By similarity. Cytoplasmic vesicleautophagosome Ref.11 Ref.12 Ref.13 Ref.15 Ref.24.

Tissue specificity

Ubiquitous. Expressed at high levels in the brain, heart, prostate, ovary, spleen and skeletal muscle. Expressed at very low levels in lung, thymus and small intestine. Ref.1 Ref.2

Post-translational modification

The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAPL2-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAPL2-II. ATG4B also mediates the delipidation required for GABARAPL1 recycling when autophagosomes fuse with lysosomes. Ref.12

The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine By similarity.

Sequence similarities

Belongs to the ATG8 family.

Ontologies

Keywords
   Biological processAutophagy
Protein transport
Transport
   Cellular componentCytoplasmic vesicle
Golgi apparatus
   Coding sequence diversityPolymorphism
   PTMAcetylation
Lipoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Non-traceable author statement Ref.11. Source: UniProtKB

intra-Golgi vesicle-mediated transport

Inferred from sequence or structural similarity PubMed 10747018. Source: UniProtKB

negative regulation of proteasomal protein catabolic process

Inferred from mutant phenotype PubMed 21669198. Source: BHF-UCL

positive regulation of ATPase activity

Inferred from sequence or structural similarity PubMed 10747018. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

Golgi membrane

Inferred from sequence or structural similarity PubMed 10747018Ref.2. Source: UniProtKB

autophagic vacuole

Inferred from direct assay Ref.15. Source: UniProtKB

autophagic vacuole membrane

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 21669198. Source: BHF-UCL

cytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

intracellular

Inferred from direct assay. Source: LIFEdb

   Molecular_functionATPase binding

Inferred from sequence or structural similarity PubMed 10747018. Source: UniProtKB

GABA receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

SNARE binding

Inferred from sequence or structural similarity PubMed 10747018. Source: UniProtKB

beta-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 116116Gamma-aminobutyric acid receptor-associated protein-like 2
PRO_0000212373
Propeptide1171Removed in mature form
PRO_0000423070

Regions

Region1 – 2222Interaction with beta-tubulin By similarity
Region36 – 6833Interaction with GABRG2 Potential

Sites

Site116 – 1172Cleavage; by ATG4

Amino acid modifications

Modified residue241N6-acetyllysine Ref.16
Modified residue391Phosphoserine Ref.14
Lipidation1161Phosphatidylethanolamine amidated glycine Ref.11

Natural variations

Natural variant511V → A.
Corresponds to variant rs11556291 [ dbSNP | Ensembl ].
VAR_049756

Experimental info

Mutagenesis1161G → A: Impairs localization at the autophagosomal membrane. Ref.12
Sequence conflict291V → F in AAD27779. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P60520 [UniParc].

Last modified March 1, 2004. Version 1.
Checksum: 17ACB540FD5B975B

FASTA11713,667
        10         20         30         40         50         60 
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF 

        70         80         90        100        110 
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF 

« Hide

References

« Hide 'large scale' references
[1]"Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation."
Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y., Koga H., Muramatsu M.-A.
Brain Res. Mol. Brain Res. 85:1-12(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH ULK1.
Tissue: Frontal cortex.
[2]"Cloning, expression patterns, and chromosome localization of three human and two mouse homologues of GABA(A) receptor-associated protein."
Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R., Zhao S.
Genomics 74:408-413(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]Storch S., Braulke T.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Human GEF2 homolog gene."
Song H., Peng Y., Yu Y., Fu G., Mao M., Zhang Q., Zhu H., Li G., Luo M., Chen J., Hu R.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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].
Tissue: Brain.
[7]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].
[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].
Tissue: Brain and Testis.
[9]"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
J. Biol. Chem. 276:1701-1706(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG7.
[10]"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p."
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
J. Biol. Chem. 277:13739-13744(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG3.
[11]"GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3."
Tanida I., Komatsu M., Ueno T., Kominami E.
Biochem. Biophys. Res. Commun. 300:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPIDATION AT GLY-116, INTERACTION WITH ATG3 AND ATG7, SUBCELLULAR LOCATION.
[12]"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation."
Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T.
J. Cell Sci. 117:2805-2812(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-116.
[13]"p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy."
Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H., Overvatn A., Bjorkoy G., Johansen T.
J. Biol. Chem. 282:24131-24145(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"The TP53INP2 protein is required for autophagy in mammalian cells."
Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.
Mol. Biol. Cell 20:870-881(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53INP2.
[16]"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-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis."
Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.
EMBO J. 29:1792-1802(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Network organization of the human autophagy system."
Behrends C., Sowa M.E., Gygi S.P., Harper J.W.
Nature 466:68-76(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TECPR2.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation."
Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.
J. Cell Biol. 192:839-853(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBC1D25.
[21]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION PCM1.
[22]"TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death."
Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M., Carrier A., Iovanna J.L., Dusetti N.J.
Cell Death Differ. 19:1525-1535(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53INP1.
[23]"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 ATG13 AND ULK1.
[24]"Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens."
Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M., Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S., Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V., Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.
Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[25]"DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcription."
Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M., Johansen T., Zorzano A.
PLoS ONE 7:E34034-E34034(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53INP1 AND TP53INP2.
[26]"Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3 determines pro-survival mitophagy versus apoptosis."
Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R., Novak I., Dikic I., Hamacher-Brady A., Brady N.R.
J. Biol. Chem. 288:1099-1113(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BNIP3, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB030710 mRNA. Translation: BAB21548.1.
AF087848 mRNA. Translation: AAK20400.1.
AJ010569 mRNA. Translation: CAA09249.1.
AF077046 mRNA. Translation: AAD27779.1.
CR542217 mRNA. Translation: CAG47013.1.
AK289788 mRNA. Translation: BAF82477.1.
CH471114 Genomic DNA. Translation: EAW95630.1.
BC005985 mRNA. Translation: AAH05985.1.
BC014594 mRNA. Translation: AAH14594.1.
BC029601 mRNA. Translation: AAH29601.1.
RefSeqNP_009216.1. NM_007285.6.
UniGeneHs.461379.

3D structure databases

ProteinModelPortalP60520.
SMRP60520. Positions 1-117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116473. 59 interactions.
DIPDIP-35051N.
IntActP60520. 494 interactions.
MINTMINT-1414121.
STRING9606.ENSP00000037243.

PTM databases

PhosphoSiteP60520.

Polymorphism databases

DMDM44888808.

2D gel databases

UCD-2DPAGEP60520.

Proteomic databases

PaxDbP60520.
PRIDEP60520.

Protocols and materials databases

DNASU11345.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000037243; ENSP00000037243; ENSG00000034713.
GeneID11345.
KEGGhsa:11345.
UCSCuc002fen.3. human.

Organism-specific databases

CTD11345.
GeneCardsGC16P075600.
HGNCHGNC:13291. GABARAPL2.
HPAHPA036726.
MIM607452. gene.
neXtProtNX_P60520.
PharmGKBPA28482.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249730.
HOGENOMHOG000232034.
HOVERGENHBG051706.
InParanoidP60520.
KOK08341.
OMAIRRRITM.
OrthoDBEOG70KGRK.
PhylomeDBP60520.
TreeFamTF312964.

Gene expression databases

ArrayExpressP60520.
BgeeP60520.
CleanExHS_GABARAPL2.
GenevestigatorP60520.

Family and domain databases

InterProIPR004241. Atg8_like.
[Graphical view]
PANTHERPTHR10969. PTHR10969. 1 hit.
PfamPF02991. Atg8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGABARAPL2. human.
GeneWikiGABARAPL2.
GenomeRNAi11345.
NextBio43116.
PMAP-CutDBP60520.
PROP60520.
SOURCESearch...

Entry information

Entry nameGBRL2_HUMAN
AccessionPrimary (citable) accession number: P60520
Secondary accession number(s): O08765 expand/collapse secondary AC list , Q6FG91, Q9DCP8, Q9UQF7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: April 16, 2014
This is version 100 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM