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Q9NQ94 (A1CF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
APOBEC1 complementation factor
Alternative name(s):
APOBEC1-stimulating protein
Gene names
Name:A1CF
Synonyms:ACF, ASP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also protects the edited APOB mRNA from nonsense-mediated decay. Ref.1 Ref.2 Ref.11

Subunit structure

Part of the apolipoprotein B mRNA editing complex with APOBEC1. Interacts with TNPO2; TNPO2 may be responsible for transport of A1CF into the nucleus. Interacts with SYNCRIP. Interacts with CELF2/CUGBP2 By similarity. Ref.1 Ref.2 Ref.8 Ref.12 UniProtKB Q923K9

Subcellular location

Nucleus. Endoplasmic reticulum By similarity. Cytoplasm. Note: Predominantly nuclear where it localizes to heterochromatin. Also cytoplasmic where it is found at the outer surface of the endoplasmic reticulum By similarity. Shuttles between the nucleus and cytoplasm. May be transported into the nucleus by the nuclear import protein TNPO2/TRN2 or by APOBEC1. Ref.11

Tissue specificity

Widely expressed with highest levels in brain, liver, pancreas, colon and spleen. Ref.2

Domain

The RRM domains are necessary but not sufficient for binding to APOB mRNA. Additional residues in the pre-RRM and C-terminal regions are required for RNA-binding and for complementing APOBEC1 activity. Ref.10

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Sequence caution

The sequence BAA91086.1 differs from that shown. Reason: Frameshift at position 148.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9NQ94-1)

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 Ref.1 Ref.2 Ref.3 (identifier: Q9NQ94-2)

The sequence of this isoform differs from the canonical sequence as follows:
     381-388: Missing.
Note: Major isoform found in 66-78% of cDNA clones.
Isoform 3 Ref.3 (identifier: Q9NQ94-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQ → MLCSPSFCKLCWKRKK
     381-388: Missing.
Isoform 4 (identifier: Q9NQ94-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MESNHKSGDGLSGTQKEAALRALVQRTGYSLVQ → MEAVCLGTCPEPEASMSTAIPGLKKGNNALQSIILQTLLEK
     381-388: Missing.
Note: Does not exhibit APOBEC1 complementation activity.
Isoform 5 Ref.9 (identifier: Q9NQ94-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.
Note: Does not exhibit APOBEC1 complementation activity.
Isoform 6 Ref.9 (identifier: Q9NQ94-6)

The sequence of this isoform differs from the canonical sequence as follows:
     202-256: Missing.
Note: Minor isoform found in 2-3% of cDNA clones.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594APOBEC1 complementation factor
PRO_0000081482

Regions

Domain56 – 13479RRM 1
Domain136 – 21883RRM 2
Domain231 – 30373RRM 3
Region360 – 40950Required for nuclear localization Ref.12

Natural variations

Alternative sequence1 – 8484Missing in isoform 5. Ref.9
VSP_051925
Alternative sequence1 – 3333MESNH…YSLVQ → MLCSPSFCKLCWKRKK in isoform 3. Ref.3
VSP_051926
Alternative sequence1 – 3333MESNH…YSLVQ → MEAVCLGTCPEPEASMSTAI PGLKKGNNALQSIILQTLLE K in isoform 4.
VSP_051927
Alternative sequence202 – 25655Missing in isoform 6. Ref.9
VSP_051928
Alternative sequence381 – 3888Missing in isoform 2, isoform 3 and isoform 4. Ref.1 Ref.2 Ref.3
VSP_051929
Natural variant5551V → M.
Corresponds to variant rs9073 [ dbSNP | Ensembl ].
VAR_052201
Natural variant5581A → S.
Corresponds to variant rs11817448 [ dbSNP | Ensembl ].
VAR_059821

Experimental info

Mutagenesis591F → A: Greatly reduced RNA binding. Ref.10
Mutagenesis1001F → A: Greatly reduced RNA binding. Ref.10
Mutagenesis1391F → A: Greatly reduced RNA binding. Ref.10
Mutagenesis1831F → A: Greatly reduced RNA binding. Ref.10
Mutagenesis2341Y → A: Slightly reduced RNA binding. Ref.10
Mutagenesis2701F → A: Slightly reduced RNA binding. Ref.10
Sequence conflict1911A → T in AAF34824. Ref.2
Sequence conflict2771E → K Ref.2
Sequence conflict2771E → K Ref.3

Secondary structure

............. 594
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: AA5EF76BD8815807

FASTA59465,202
        10         20         30         40         50         60 
MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDAA PPERGCEIFI 

        70         80         90        100        110        120 
GKLPRDLFED ELIPLCEKIG KIYEMRMMMD FNGNNRGYAF VTFSNKVEAK NAIKQLNNYE 

       130        140        150        160        170        180 
IRNGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG 

       190        200        210        220        230        240 
FAFVEYESHR AAAMARRKLL PGRIQLWGHG IAVDWAEPEV EVDEDTMSSV KILYVRNLML 

       250        260        270        280        290        300 
STSEEMIEKE FNNIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL 

       310        320        330        340        350        360 
AKPVDKDSYV RYTRGTGGRG TMLQGEYTYS LGQVYDPTTT YLGAPVFYAP QTYAAIPSLH 

       370        380        390        400        410        420 
FPATKGHLSN RAIIRAPSVR EIYMNVPVGA AGVRGLGGRG YLAYTGLGRG YQVKGDKRED 

       430        440        450        460        470        480 
KLYDILPGME LTPMNPVTLK PQGIKLAPQI LEEICQKNNW GQPVYQLHSA IGQDQRQLFL 

       490        500        510        520        530        540 
YKITIPALAS QNPAIHPFTP PKLSAFVDEA KTYAAEYTLQ TLGIPTDGGD GTMATAAAAA 

       550        560        570        580        590 
TAFPGYAVPN ATAPVSAAQL KQAVTLGQDL AAYTTYEVYP TFAVTARGDG YGTF 

« Hide

Isoform 2 [UniParc].

Checksum: A836BBA98FD1BD51
Show »

FASTA58664,256
Isoform 3 [UniParc].

Checksum: F185421309CBA29F
Show »

FASTA56962,682
Isoform 4 [UniParc].

Checksum: 2F2C8897629F9E3C
Show »

FASTA59465,024
Isoform 5 [UniParc].

Checksum: 70E050F5DB3F4DA2
Show »

FASTA51055,962
Isoform 6 [UniParc].

Checksum: 924E9C2A43A6788C
Show »

FASTA53958,871

References

« Hide 'large scale' references
[1]"Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex."
Lellek H., Kirsten R., Diehl I., Apostel F., Buck F., Greeve J.
J. Biol. Chem. 275:19848-19856(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH APOBEC1.
Tissue: Liver and Small intestine.
[2]"Molecular cloning of APOBEC-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA."
Mehta A., Kinter M.T., Sherman N.E., Driscoll D.M.
Mol. Cell. Biol. 20:1846-1854(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH APOBEC1, TISSUE SPECIFICITY.
[3]"Human APOBEC-1 complementation factor related protein."
Sowden M.P., Smith H.C.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Liver.
[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. 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: Small intestine.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 4).
[8]"Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing."
Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A., Scott J., Davidson N.O.
J. Biol. Chem. 276:10272-10283(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNCRIP.
[9]"Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene."
Henderson J.O., Blanc V., Davidson N.O.
Biochim. Biophys. Acta 1522:22-30(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE STRUCTURE, ALTERNATIVE SPLICING.
[10]"Identification of domains in apobec-1 complementation factor required for RNA binding and apolipoprotein-B mRNA editing."
Mehta A., Driscoll D.M.
RNA 8:69-82(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING DOMAIN, MUTAGENESIS OF PHE-59; PHE-100; PHE-139; PHE-183; TYR-234 AND PHE-270.
[11]"The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay."
Chester A., Somasekaram A., Tzimina M., Jarmuz A., Gisbourne J., O'Keefe R., Scott J., Navaratnam N.
EMBO J. 22:3971-3982(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"A novel nuclear localization signal in the auxiliary domain of apobec-1 complementation factor regulates nucleocytoplasmic import and shuttling."
Blanc V., Kennedy S., Davidson N.O.
J. Biol. Chem. 278:41198-41204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH TNPO2.
[13]"Solution structure of the RNA recognition motif of human APOBEC-1 complementation factor, ACF."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 223-308.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ272078 mRNA. Translation: CAB94754.1.
AJ272079 mRNA. Translation: CAB94755.1.
AF209192 mRNA. Translation: AAF34824.1.
AF271789 mRNA. Translation: AAF76221.1.
AF271790 mRNA. Translation: AAF76222.1.
AK000324 mRNA. Translation: BAA91086.1. Frameshift.
AK291982 mRNA. Translation: BAF84671.1.
AL512366, AL589794 Genomic DNA. Translation: CAI14233.1.
AL512366, AL589794 Genomic DNA. Translation: CAI14235.1.
AL512366, AL589794 Genomic DNA. Translation: CAI14236.1.
AL589794, AL512366 Genomic DNA. Translation: CAI15762.1.
AL589794, AL512366 Genomic DNA. Translation: CAI15763.1.
AL589794, AL512366 Genomic DNA. Translation: CAI15764.1.
CH471083 Genomic DNA. Translation: EAW54133.1.
CH471083 Genomic DNA. Translation: EAW54134.1.
CH471083 Genomic DNA. Translation: EAW54135.1.
BC130519 mRNA. Translation: AAI30520.1.
BC144196 mRNA. Translation: AAI44197.1.
RefSeqNP_001185747.1. NM_001198818.1.
NP_001185748.1. NM_001198819.1.
NP_001185749.1. NM_001198820.1.
NP_055391.2. NM_014576.3.
NP_620310.1. NM_138932.2.
NP_620311.1. NM_138933.2.
XP_005269775.1. XM_005269718.1.
XP_005269776.1. XM_005269719.1.
XP_005269777.1. XM_005269720.1.
UniGeneHs.282795.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPDNMR-A223-308[»]
ProteinModelPortalQ9NQ94.
SMRQ9NQ94. Positions 14-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119004. 6 interactions.
IntActQ9NQ94. 1 interaction.

PTM databases

PhosphoSiteQ9NQ94.

Polymorphism databases

DMDM74761651.

Proteomic databases

PaxDbQ9NQ94.
PRIDEQ9NQ94.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282641; ENSP00000282641; ENSG00000148584. [Q9NQ94-1]
ENST00000373993; ENSP00000363105; ENSG00000148584. [Q9NQ94-1]
ENST00000373995; ENSP00000363107; ENSG00000148584. [Q9NQ94-4]
ENST00000373997; ENSP00000363109; ENSG00000148584. [Q9NQ94-2]
ENST00000374001; ENSP00000363113; ENSG00000148584. [Q9NQ94-2]
ENST00000395495; ENSP00000378873; ENSG00000148584. [Q9NQ94-6]
GeneID29974.
KEGGhsa:29974.
UCSCuc001jjh.3. human. [Q9NQ94-4]
uc001jji.3. human. [Q9NQ94-2]
uc001jjj.3. human. [Q9NQ94-1]

Organism-specific databases

CTD29974.
GeneCardsGC10M052566.
HGNCHGNC:24086. A1CF.
HPAHPA037779.
HPA044079.
neXtProtNX_Q9NQ94.
PharmGKBPA162375098.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258596.
HOVERGENHBG051917.
InParanoidQ9NQ94.
OMALIQRTGY.
OrthoDBEOG73JKW2.
PhylomeDBQ9NQ94.
TreeFamTF314932.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NQ94.
BgeeQ9NQ94.
CleanExHS_A1CF.
GenevestigatorQ9NQ94.

Family and domain databases

Gene3D3.30.160.20. 1 hit.
3.30.70.330. 2 hits.
InterProIPR014720. dsRNA-bd_dom.
IPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01648. hnRNP-R-Q. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NQ94.
GeneWikiACF_(gene).
GenomeRNAi29974.
NextBio52719.
PROQ9NQ94.

Entry information

Entry nameA1CF_HUMAN
AccessionPrimary (citable) accession number: Q9NQ94
Secondary accession number(s): A1L4F2 expand/collapse secondary AC list , A8K7G7, B7ZM14, Q5SZQ0, Q9NQ93, Q9NQX8, Q9NQX9, Q9NXC9, Q9NZD3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 118 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM