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Protein

Syntaxin-16

Gene

STX16

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

Functioni

SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network.1 Publication

GO - Molecular functioni

  1. SNAP receptor activity Source: HGNC
  2. SNARE binding Source: GO_Central
  3. syntaxin binding Source: UniProtKB

GO - Biological processi

  1. Golgi ribbon formation Source: UniProtKB
  2. intracellular protein transport Source: GO_Central
  3. intra-Golgi vesicle-mediated transport Source: InterPro
  4. retrograde transport, endosome to Golgi Source: UniProtKB
  5. vesicle docking Source: GO_Central
  6. vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-16
Short name:
Syn16
Gene namesi
Name:STX16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11431. STX16.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 301301CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei302 – 32221Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini323 – 3253VesicularSequence Analysis

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endomembrane system Source: GO_Central
  4. focal adhesion Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB
  6. Golgi cisterna Source: UniProtKB
  7. Golgi membrane Source: UniProtKB-SubCell
  8. integral component of membrane Source: GO_Central
  9. intracellular membrane-bounded organelle Source: UniProtKB
  10. membrane Source: UniProtKB
  11. nucleolus Source: HPA
  12. perinuclear region of cytoplasm Source: UniProtKB
  13. SNARE complex Source: HGNC
  14. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Pseudohypoparathyroidism 1B2 Publications

The gene represented in this entry is involved in disease pathogenesis. Microdeletions involving STX16 can cause loss of methylation at exon A/B of GNAS, resulting in PHP1B.

Disease descriptionA disorder characterized by end-organ resistance to parathyroid hormone, hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH.

See also OMIM:603233

Organism-specific databases

MIMi603233. phenotype.
Orphaneti94089. Pseudohypoparathyroidism type 1B.
PharmGKBiPA36231.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Syntaxin-16PRO_0000210226Add
BLAST

Proteomic databases

MaxQBiO14662.
PaxDbiO14662.
PRIDEiO14662.

PTM databases

PhosphoSiteiO14662.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO14662.
ExpressionAtlasiO14662. baseline and differential.
GenevestigatoriO14662.

Organism-specific databases

HPAiHPA041019.
HPA042033.

Interactioni

Subunit structurei

Interacts with GCC2.1 Publication

Protein-protein interaction databases

BioGridi114223. 9 interactions.
IntActiO14662. 3 interactions.
MINTiMINT-1196639.

Structurei

3D structure databases

ProteinModelPortaliO14662.
SMRiO14662. Positions 77-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini230 – 29263t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5325.
GeneTreeiENSGT00550000075126.
HOVERGENiHBG057612.
InParanoidiO14662.
KOiK08489.
OMAiGFHDCHR.
PhylomeDBiO14662.
TreeFamiTF314090.

Family and domain databases

InterProiIPR028673. STX16.
IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR19957:SF79. PTHR19957:SF79. 1 hit.
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: O14662-1) [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
MATRRLTDAF LLLRNNSIQN RQLLAEQVSS HITSSPLHSR SIAAELDELA
60 70 80 90 100
DDRMALVSGI SLDPEAAIGV TKRPPPKWVD GVDEIQYDVG RIKQKMKELA
110 120 130 140 150
SLHDKHLNRP TLDDSSEEEH AIEITTQEIT QLFHRCQRAV QALPSRARAC
160 170 180 190 200
SEQEGRLLGN VVASLAQALQ ELSTSFRHAQ SGYLKRMKNR EERSQHFFDT
210 220 230 240 250
SVPLMDDGDD NTLYHRGFTE DQLVLVEQNT LMVEEREREI RQIVQSISDL
260 270 280 290 300
NEIFRDLGAM IVEQGTVLDR IDYNVEQSCI KTEDGLKQLH KAEQYQKKNR
310 320
KMLVILILFV IIIVLIVVLV GVKSR
Length:325
Mass (Da):37,031
Last modified:January 24, 2006 - v3
Checksum:i65F566541A042C3C
GO
Isoform A (identifier: O14662-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-48: Missing.

Show »
Length:304
Mass (Da):34,813
Checksum:i9EEF54F753B7AB83
GO
Isoform C (identifier: O14662-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-44: Missing.
     132-132: L → A
     133-325: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:115
Mass (Da):13,018
Checksum:i51BBBACE2158720E
GO
Isoform D (identifier: O14662-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-44: Missing.

Show »
Length:308
Mass (Da):35,299
Checksum:i1915107ACB686EAA
GO
Isoform E (identifier: O14662-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     45-48: Missing.

Show »
Length:321
Mass (Da):36,545
Checksum:i9F8316610F6C97C0
GO
Isoform 6 (identifier: O14662-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Note: No experimental confirmation available.

Show »
Length:272
Mass (Da):31,074
Checksum:i8EE1A85AE716237C
GO

Sequence cautioni

The sequence AAB69282.1 differs from that shown. Reason: Frameshift at positions 142, 163 and 165. Curated
The sequence AAB69283.1 differs from that shown. Reason: Frameshift at positions 142, 163 and 165. Curated
The sequence AAC05647.1 differs from that shown. Reason: Frameshift at positions 142, 163 and 165. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991L → S in AAB69282 (PubMed:9587053).Curated
Sequence conflicti99 – 991L → S in AAB69283 (PubMed:9587053).Curated
Sequence conflicti147 – 1471A → E in AAC05647 (PubMed:9587053).Curated
Sequence conflicti243 – 2431I → M in AAB69282 (PubMed:9587053).Curated
Sequence conflicti243 – 2431I → M in AAB69283 (PubMed:9587053).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5353Missing in isoform 6. 1 PublicationVSP_045073Add
BLAST
Alternative sequencei28 – 4821Missing in isoform A. 2 PublicationsVSP_006348Add
BLAST
Alternative sequencei28 – 4417Missing in isoform C and isoform D. 2 PublicationsVSP_006349Add
BLAST
Alternative sequencei45 – 484Missing in isoform E. 1 PublicationVSP_043849
Alternative sequencei132 – 1321L → A in isoform C. 1 PublicationVSP_006350
Alternative sequencei133 – 325193Missing in isoform C. 1 PublicationVSP_006351Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008936 mRNA. Translation: AAB69283.1. Frameshift.
AF008935 mRNA. Translation: AAB69282.1. Frameshift.
AF008937 mRNA. Translation: AAB69284.1.
AF038897 mRNA. Translation: AAC05647.1. Frameshift.
AL139349, AL050327 Genomic DNA. Translation: CAX14989.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14990.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14991.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23277.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23278.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23279.1.
AL050327, AL139349 Genomic DNA. Translation: CAM28341.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14992.1.
CH471077 Genomic DNA. Translation: EAW75481.1.
CH471077 Genomic DNA. Translation: EAW75482.1.
CH471077 Genomic DNA. Translation: EAW75484.1.
CH471077 Genomic DNA. Translation: EAW75485.1.
CH471077 Genomic DNA. Translation: EAW75486.1.
BC019042 mRNA. Translation: AAH19042.1.
BC073876 mRNA. Translation: AAH73876.1.
BX396221 mRNA. No translation available.
CCDSiCCDS13468.1. [O14662-1]
CCDS13469.1. [O14662-2]
CCDS46619.1. [O14662-5]
CCDS46620.1. [O14662-4]
CCDS56199.1. [O14662-6]
PIRiJC5927.
RefSeqiNP_001001433.1. NM_001001433.2. [O14662-1]
NP_001128244.1. NM_001134772.2. [O14662-5]
NP_001128245.1. NM_001134773.2. [O14662-4]
NP_001191797.1. NM_001204868.1. [O14662-6]
NP_003754.2. NM_003763.5. [O14662-2]
UniGeneiHs.307913.

Genome annotation databases

EnsembliENST00000355957; ENSP00000348229; ENSG00000124222. [O14662-4]
ENST00000358029; ENSP00000350723; ENSG00000124222. [O14662-5]
ENST00000359617; ENSP00000352634; ENSG00000124222. [O14662-6]
ENST00000361830; ENSP00000354445; ENSG00000124222. [O14662-6]
ENST00000371132; ENSP00000360173; ENSG00000124222. [O14662-2]
ENST00000371141; ENSP00000360183; ENSG00000124222. [O14662-1]
ENST00000467096; ENSP00000434369; ENSG00000124222. [O14662-3]
GeneIDi8675.
KEGGihsa:8675.
UCSCiuc002xzi.3. human. [O14662-1]
uc002xzj.3. human. [O14662-2]
uc002xzk.3. human. [O14662-4]
uc002xzm.3. human. [O14662-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008936 mRNA. Translation: AAB69283.1. Frameshift.
AF008935 mRNA. Translation: AAB69282.1. Frameshift.
AF008937 mRNA. Translation: AAB69284.1.
AF038897 mRNA. Translation: AAC05647.1. Frameshift.
AL139349, AL050327 Genomic DNA. Translation: CAX14989.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14990.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14991.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23277.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23278.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23279.1.
AL050327, AL139349 Genomic DNA. Translation: CAM28341.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14992.1.
CH471077 Genomic DNA. Translation: EAW75481.1.
CH471077 Genomic DNA. Translation: EAW75482.1.
CH471077 Genomic DNA. Translation: EAW75484.1.
CH471077 Genomic DNA. Translation: EAW75485.1.
CH471077 Genomic DNA. Translation: EAW75486.1.
BC019042 mRNA. Translation: AAH19042.1.
BC073876 mRNA. Translation: AAH73876.1.
BX396221 mRNA. No translation available.
CCDSiCCDS13468.1. [O14662-1]
CCDS13469.1. [O14662-2]
CCDS46619.1. [O14662-5]
CCDS46620.1. [O14662-4]
CCDS56199.1. [O14662-6]
PIRiJC5927.
RefSeqiNP_001001433.1. NM_001001433.2. [O14662-1]
NP_001128244.1. NM_001134772.2. [O14662-5]
NP_001128245.1. NM_001134773.2. [O14662-4]
NP_001191797.1. NM_001204868.1. [O14662-6]
NP_003754.2. NM_003763.5. [O14662-2]
UniGeneiHs.307913.

3D structure databases

ProteinModelPortaliO14662.
SMRiO14662. Positions 77-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114223. 9 interactions.
IntActiO14662. 3 interactions.
MINTiMINT-1196639.

PTM databases

PhosphoSiteiO14662.

Proteomic databases

MaxQBiO14662.
PaxDbiO14662.
PRIDEiO14662.

Protocols and materials databases

DNASUi8675.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355957; ENSP00000348229; ENSG00000124222. [O14662-4]
ENST00000358029; ENSP00000350723; ENSG00000124222. [O14662-5]
ENST00000359617; ENSP00000352634; ENSG00000124222. [O14662-6]
ENST00000361830; ENSP00000354445; ENSG00000124222. [O14662-6]
ENST00000371132; ENSP00000360173; ENSG00000124222. [O14662-2]
ENST00000371141; ENSP00000360183; ENSG00000124222. [O14662-1]
ENST00000467096; ENSP00000434369; ENSG00000124222. [O14662-3]
GeneIDi8675.
KEGGihsa:8675.
UCSCiuc002xzi.3. human. [O14662-1]
uc002xzj.3. human. [O14662-2]
uc002xzk.3. human. [O14662-4]
uc002xzm.3. human. [O14662-5]

Organism-specific databases

CTDi8675.
GeneCardsiGC20P057226.
HGNCiHGNC:11431. STX16.
HPAiHPA041019.
HPA042033.
MIMi603233. phenotype.
603666. gene.
neXtProtiNX_O14662.
Orphaneti94089. Pseudohypoparathyroidism type 1B.
PharmGKBiPA36231.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5325.
GeneTreeiENSGT00550000075126.
HOVERGENiHBG057612.
InParanoidiO14662.
KOiK08489.
OMAiGFHDCHR.
PhylomeDBiO14662.
TreeFamiTF314090.

Miscellaneous databases

ChiTaRSiSTX16. human.
GeneWikiiSTX16.
GenomeRNAii8675.
NextBioi32541.
PROiO14662.
SOURCEiSearch...

Gene expression databases

BgeeiO14662.
ExpressionAtlasiO14662. baseline and differential.
GenevestigatoriO14662.

Family and domain databases

InterProiIPR028673. STX16.
IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR19957:SF79. PTHR19957:SF79. 1 hit.
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Syntaxin-16, a putative Golgi t-SNARE."
    Simonsen A., Bremnes B., Ronning E., Aasland R., Stenmark H.
    Eur. J. Cell Biol. 75:223-231(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D).
    Tissue: Brain.
  2. "Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins."
    Tang B.L., Low D.Y.H., Lee S.S., Tan A.E.H., Ho W.
    Biochem. Biophys. Res. Commun. 242:673-679(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS A AND E).
    Tissue: Kidney.
  6. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-251 (ISOFORM 6).
    Tissue: Placenta.
  7. "Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS."
    Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G., Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L., Slyper A.H., Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.
    J. Clin. Invest. 112:1255-1263(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PHP1B.
  8. "A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS."
    Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.
    Am. J. Hum. Genet. 76:804-814(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PHP1B.
  9. "A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells."
    Ganley I.G., Espinosa E., Pfeffer S.R.
    J. Cell Biol. 180:159-172(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GCC2.

Entry informationi

Entry nameiSTX16_HUMAN
AccessioniPrimary (citable) accession number: O14662
Secondary accession number(s): A6NK32
, A6NN69, A8MPP0, B7ZBN1, B7ZBN2, B7ZBN3, E1P5M0, E1P607, O14661, O14663, O60517, Q5W084, Q5W086, Q5W087, Q5XKI6, Q6GMS8, Q9H0Z0, Q9H1T7, Q9H1T8, Q9UIX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 24, 2006
Last modified: March 4, 2015
This is version 144 of the entry and version 3 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.