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Q8IUH5 (ZDH17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Palmitoyltransferase ZDHHC17

EC=2.3.1.225
Alternative name(s):
Huntingtin yeast partner H
Huntingtin-interacting protein 14
Short name=HIP-14
Huntingtin-interacting protein 3
Short name=HIP-3
Huntingtin-interacting protein H
Putative MAPK-activating protein PM11
Putative NF-kappa-B-activating protein 205
Zinc finger DHHC domain-containing protein 17
Short name=DHHC-17
Gene names
Name:ZDHHC17
Synonyms:HIP14, HIP3, HYPH, KIAA0946
ORF Names:HSPC294
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg2+ transport. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Catalytic activity

Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.

Subunit structure

Interacts (via ANK repeats) with HD. This interaction is inversely correlated to the length of the polyglutamine tract added to the huntingtin protein in Huntington disease. Ref.1 Ref.6

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Note: Low extracellular Mg2+ induces increase in Golgi and in post-Golgi membrane vesicles. Ref.8 Ref.10

Tissue specificity

Expressed in all brain regions. Expression is highest in the cortex, cerebellum, occipital lobe and caudate and lowest in the spinal cord. Expression is also seen in testis, pancreas, heart and kidney. ZDHHC17 is the only palmitoyltransferase in erythrocytes. Ref.1 Ref.12

Domain

The DHHC domain is required for palmitoyltransferase activity.

Post-translational modification

Autopalmitoylated. Autopalmitoylation has a regulatory role in ZDHHC17-mediated Mg2+ transport. Ref.8

Miscellaneous

The early and prominent pathology of HD is observed in the medium spiny neurons that project into the globus.

Sequence similarities

Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.

Contains 5 ANK repeats.

Contains 1 DHHC-type zinc finger.

Biophysicochemical properties

Kinetic parameters:

KM=0.87 mM for for magnesium ions

Sequence caution

The sequence AAF28972.1 differs from that shown. Reason: Frameshift at positions 183 and 191.

The sequence AAH30990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA76790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC77366.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC77388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCytoplasmic vesicle
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainANK repeat
Repeat
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionAcyltransferase
Transferase
   PTMLipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipoprotein transport

Inferred from direct assay Ref.8. Source: UniProtKB

magnesium ion transport

Inferred from direct assay Ref.10. Source: GOC

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.3. Source: UniProtKB

protein palmitoylation

Inferred from direct assay PubMed 23034182. Source: UniProt

signal transduction

Inferred from mutant phenotype Ref.3. Source: GOC

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 16647879. Source: UniProt

Golgi membrane

Inferred from direct assay Ref.10. Source: UniProtKB

Golgi-associated vesicle membrane

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 24705354. Source: IntAct

magnesium ion transmembrane transporter activity

Inferred from direct assay Ref.10. Source: UniProtKB

palmitoyltransferase activity

Inferred from direct assay PubMed 23034182. Source: UniProt

protein binding

Inferred from physical interaction Ref.8PubMed 23275563PubMed 24705354. Source: IntAct

protein-cysteine S-palmitoyltransferase activity

Inferred from direct assay Ref.8. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype Ref.3. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IUH5-1)

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: Q8IUH5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.
     51-66: THIDDYSTWDIVKATQ → MSTIPKRAVCPFSTQR
     258-266: GESALDLAK → AILRCHMAL
     267-632: Missing.
Isoform 3 (identifier: Q8IUH5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     204-632: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 632632Palmitoyltransferase ZDHHC17
PRO_0000212900

Regions

Topological domain1 – 304304Cytoplasmic Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane326 – 34621Helical; Potential
Topological domain347 – 35711Cytoplasmic Potential
Transmembrane358 – 37821Helical; Potential
Topological domain379 – 3813Lumenal Potential
Transmembrane382 – 40221Helical; Potential
Topological domain403 – 48078Cytoplasmic Potential
Transmembrane481 – 50121Helical; Potential
Topological domain502 – 52928Lumenal Potential
Transmembrane530 – 55021Helical; Potential
Topological domain551 – 63282Cytoplasmic Potential
Repeat89 – 11830ANK 1
Repeat123 – 15533ANK 2
Repeat156 – 18833ANK 3
Repeat189 – 21931ANK 4
Repeat224 – 25330ANK 5
Zinc finger437 – 48751DHHC-type

Sites

Active site4671S-palmitoyl cysteine intermediate Probable

Natural variations

Alternative sequence1 – 5050Missing in isoform 2.
VSP_010021
Alternative sequence51 – 6616THIDD…VKATQ → MSTIPKRAVCPFSTQR in isoform 2.
VSP_010022
Alternative sequence204 – 632429Missing in isoform 3.
VSP_010023
Alternative sequence258 – 2669GESALDLAK → AILRCHMAL in isoform 2.
VSP_010024
Alternative sequence267 – 632366Missing in isoform 2.
VSP_010025
Natural variant3831N → S.
Corresponds to variant rs33996476 [ dbSNP | Ensembl ].
VAR_052978

Experimental info

Mutagenesis4671C → S: Abolishes palmitoyltransferase activity. Ref.9
Sequence conflict31R → G in AAF28972. Ref.7
Sequence conflict391Y → F in BAC22089. Ref.1
Sequence conflict1731V → VV in BAC22089. Ref.1
Sequence conflict1821D → E in AAF28972. Ref.7

Secondary structure

................................... 632
Helix Strand Turn

Details...

Sequences

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

Last modified April 13, 2004. Version 2.
Checksum: 3FD5FD592F2C617F

FASTA63272,640
        10         20         30         40         50         60 
MQREEGFNTK MADGPDEYDT EAGCVPLLHP EEIKPQSHYN HGYGEPLGRK THIDDYSTWD 

        70         80         90        100        110        120 
IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI SKGAIVDQLG 

       130        140        150        160        170        180 
GDLNSTPLHW ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG 

       190        200        210        220        230        240 
QDVDMMDQNG MTPLMWAAYR THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV 

       250        260        270        280        290        300 
ISLLLEAGAN VDAQNIKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE 

       310        320        330        340        350        360 
FRQKVMLGTP FLVIWLVGFI ADLNIDSWLI KGLMYGGVWA TVQFLSKSFF DHSMHSALPL 

       370        380        390        400        410        420 
GIYLATKFWM YVTWFFWFWN DLNFLFIHLP FLANSVALFY NFGKSWKSDP GIIKATEEQK 

       430        440        450        460        470        480 
KKTIVELAET GSLDLSIFCS TCLIRKPVRS KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR 

       490        500        510        520        530        540 
YFMGYLFFLL FMICWMIYGC ISYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF 

       550        560        570        580        590        600 
HFMWVAVLLM CQMYQISCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF 

       610        620        630 
RCCGLFRPVI VDWTRQYTIE YDQISGSGYQ LV 

« Hide

Isoform 2 [UniParc].

Checksum: A07B4620B70A6593
Show »

FASTA21623,941
Isoform 3 [UniParc].

Checksum: F37602D7183923C5
Show »

FASTA20322,845

References

« Hide 'large scale' references
[1]"HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis."
Singaraja R.R., Hadano S., Metzler M., Givan S., Wellington C.L., Warby S., Yanai A., Gutekunst C.-A., Leavitt B.R., Yi H., Fichter K., Gan L., McGutcheon K., Chopra V., Michel J., Hersch S.M., Ikeda J.E., Hayden M.R.
Hum. Mol. Genet. 11:2815-2828(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HD, TISSUE SPECIFICITY, FUNCTION.
Tissue: Brain.
[2]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung fibroblast.
[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] (ISOFORM 2).
[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] (ISOFORMS 1 AND 2).
Tissue: Bone marrow and Testis.
[6]"Huntingtin interacts with a family of WW domain proteins."
Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., MacDonald M.E.
Hum. Mol. Genet. 7:1463-1474(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-182, INTERACTION WITH HD.
Tissue: Testis.
[7]"Human partial CDS from CD34+ stem cells."
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 3).
Tissue: Umbilical cord blood.
[8]"Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins."
Huang K., Yanai A., Kang R., Arstikaitis P., Singaraja R.R., Metzler M., Mullard A., Haigh B., Gauthier-Campbell C., Gutekunst C.-A., Hayden M.R., El-Husseini A.
Neuron 44:977-986(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPALMITOYLATION.
[9]"Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase."
Ducker C.E., Stettler E.M., French K.J., Upson J.J., Smith C.D.
Oncogene 23:9230-9237(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-467.
[10]"Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions, palmitoyl acyltransferase and Mg2+ transport."
Goytain A., Hines R.M., Quamme G.A.
J. Biol. Chem. 283:33365-33374(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"ClipR-59 interacts with Akt and regulates Akt cellular compartmentalization."
Ding J., Du K.
Mol. Cell. Biol. 29:1459-1471(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells."
Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J., Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J., Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F.
J. Biol. Chem. 287:18974-18984(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]"The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding."
Gao T., Collins R.E., Horton J.R., Zhang X., Zhang R., Dhayalan A., Tamas R., Jeltsch A., Cheng X.
Proteins 76:772-777(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 51-288.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB024494 mRNA. Translation: BAC22089.1.
AB023163 mRNA. Translation: BAA76790.1. Different initiation.
AB097013 mRNA. Translation: BAC77366.1. Different initiation.
AB097035 mRNA. Translation: BAC77388.1. Different initiation.
AK299089 mRNA. Translation: BAG61151.1.
BC030990 mRNA. Translation: AAH30990.1. Different initiation.
BC050324 mRNA. Translation: AAH50324.1.
AF049612 mRNA. Translation: AAC26848.1.
AF161412 mRNA. Translation: AAF28972.1. Frameshift.
CCDSCCDS44946.1. [Q8IUH5-1]
RefSeqNP_056151.2. NM_015336.2. [Q8IUH5-1]
UniGeneHs.4014.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EU9X-ray1.99A/B/C51-288[»]
ProteinModelPortalQ8IUH5.
SMRQ8IUH5. Positions 19-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116965. 5 interactions.
IntActQ8IUH5. 224 interactions.
MINTMINT-1537511.
STRING9606.ENSP00000403397.

Protein family/group databases

TCDB9.B.37.1.1. the huntington-interacting protein 14 (hip14) family.

PTM databases

PhosphoSiteQ8IUH5.

Polymorphism databases

DMDM46395885.

Proteomic databases

MaxQBQ8IUH5.
PaxDbQ8IUH5.
PRIDEQ8IUH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334822; ENSP00000334868; ENSG00000186908. [Q8IUH5-1]
ENST00000359019; ENSP00000351913; ENSG00000186908. [Q8IUH5-2]
ENST00000426126; ENSP00000403397; ENSG00000186908. [Q8IUH5-1]
GeneID23390.
KEGGhsa:23390.
UCSCuc001syk.1. human. [Q8IUH5-1]

Organism-specific databases

CTD23390.
GeneCardsGC12P077157.
HGNCHGNC:18412. ZDHHC17.
HPAHPA016807.
MIM607799. gene.
neXtProtNX_Q8IUH5.
PharmGKBPA134991292.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG051907.
InParanoidQ8IUH5.
OMAFWNDAHL.
OrthoDBEOG70S74V.
PhylomeDBQ8IUH5.
TreeFamTF317342.

Gene expression databases

ArrayExpressQ8IUH5.
BgeeQ8IUH5.
CleanExHS_ZDHHC17.
GenevestigatorQ8IUH5.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamPF00023. Ank. 3 hits.
PF12796. Ank_2. 1 hit.
PF01529. zf-DHHC. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50216. ZF_DHHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8IUH5.
GeneWikiZDHHC17.
GenomeRNAi23390.
NextBio45515.
PROQ8IUH5.
SOURCESearch...

Entry information

Entry nameZDH17_HUMAN
AccessionPrimary (citable) accession number: Q8IUH5
Secondary accession number(s): B4DR39 expand/collapse secondary AC list , O75407, Q7Z2I0, Q86W89, Q86YK0, Q9P088, Q9UPZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 115 of the entry and version 2 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 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 12

Human chromosome 12: entries, gene names and cross-references to MIM