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Q13596 (SNX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorting nexin-1
Gene names
Name:SNX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in several stages of intracellular trafficking. Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Ref.8 Ref.10 Ref.12

Subunit structure

Homodimer. Self-assembles into a complex of approximately 300 kDa By similarity. Interacts with HGS By similarity. Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with SNX6. Ref.2 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14

Subcellular location

Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatustrans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Potential. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Ref.8 Ref.9 Ref.10 Ref.12 Ref.19

Miscellaneous

Binds phosphatidylinositol 3-phosphate (PtdIns-3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2) in liposome-based assays. Can bind PtdIns(3,4,5)P3 in protein:lipid overlay assays, but not in liposome-based assays.

Sequence similarities

Belongs to the sorting nexin family.

Contains 1 BAR domain.

Contains 1 PX (phox homology) domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13596-1)

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 1A (identifier: Q13596-2)

The sequence of this isoform differs from the canonical sequence as follows:
     91-155: Missing.
Isoform 3 (identifier: Q13596-3)

The sequence of this isoform differs from the canonical sequence as follows:
     507-522: LAKYWEAFLPEAKAIS → AGEQLGIRSGILLTKKLPRYSKFFSTVHKFCAAASLWKWGFFLSAYLSYLF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Sorting nexin-1
PRO_0000213835

Regions

Domain143 – 272130PX
Domain302 – 522221BAR

Sites

Binding site1861Phosphatidylinositol 3-phosphate By similarity
Binding site1881Phosphatidylinositol 3-phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site2141Phosphatidylinositol 3-phosphate By similarity
Binding site2381Phosphatidylinositol 3-phosphate By similarity

Amino acid modifications

Modified residue321Phosphoserine Ref.13
Modified residue391Phosphoserine Ref.13
Modified residue1881Phosphoserine Ref.13 Ref.15 Ref.17
Modified residue2371N6-acetyllysine Ref.16

Natural variations

Alternative sequence91 – 15565Missing in isoform 1A.
VSP_006189
Alternative sequence507 – 52216LAKYW…AKAIS → AGEQLGIRSGILLTKKLPRY SKFFSTVHKFCAAASLWKWG FFLSAYLSYLF in isoform 3.
VSP_044823
Natural variant1151S → Y.
Corresponds to variant rs1049501 [ dbSNP | Ensembl ].
VAR_052477
Natural variant4661D → N.
Corresponds to variant rs1802376 [ dbSNP | Ensembl ].
VAR_034507

Experimental info

Mutagenesis2141K → A: Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location. Ref.8 Ref.10
Mutagenesis429 – 4313KKR → EEE: Loss of endosomal location. Ref.10
Sequence conflict1171P → S in AAC17182. Ref.2
Sequence conflict2111P → S in AAC17182. Ref.2
Sequence conflict2111P → S in AAC17183. Ref.2
Sequence conflict5021Y → C in BAC87312. Ref.4

Secondary structure

............................. 522
Helix Strand Turn

Details...

Sequences

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

Last modified November 16, 2001. Version 3.
Checksum: 6AC8AA0A589513E3

FASTA52259,070
        10         20         30         40         50         60 
MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK 

        70         80         90        100        110        120 
ITTSLLPINN GSKENGIHEE QDQEPQDLFA DATVELSLDS TQNNQKKVLA KTLISLPPQE 

       130        140        150        160        170        180 
ATNSSKPQPT YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPLFRSKQ 

       190        200        210        220        230        240 
FAVKRRFSDF LGLYEKLSEK HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA 

       250        260        270        280        290        300 
ALERYLQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQTLS GAGLLKMFNK ATDAVSKMTI 

       310        320        330        340        350        360 
KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTAQFAKS LAMLGSSEDN 

       370        380        390        400        410        420 
TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW 

       430        440        450        460        470        480 
QDAQATLQKK REAEARLLWA NKPDKLQQAK DEILEWESRV TQYERDFERI STVVRKEVIR 

       490        500        510        520 
FEKEKSKDFK NHVIKYLETL LYSQQQLAKY WEAFLPEAKA IS 

« Hide

Isoform 1A [UniParc].

Checksum: 3F844B9E84C258C2
Show »

FASTA45751,813
Isoform 3 [UniParc].

Checksum: A03926548995DDA2
Show »

FASTA55763,082

References

« Hide 'large scale' references
[1]"Enhanced degradation of EGF receptors by a sorting nexin, SNX1."
Kurten R.C., Cadena D.L., Gill G.N.
Science 272:1008-1010(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of a family of sorting nexin molecules and characterization of their association with receptors."
Haft C.R., de la Luz Sierra M., Barr V.A., Haft D.H., Taylor S.I.
Mol. Cell. Biol. 18:7278-7287(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, INTERACTION WITH VPS26A; VPS29; VPS35 AND SNX2.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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 1 AND 3).
Tissue: Placenta and Testis.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [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].
Tissue: Muscle.
[8]"The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation."
Cozier G.E., Carlton J., McGregor A.H., Gleeson P.A., Teasdale R.D., Mellor H., Cullen P.J.
J. Biol. Chem. 277:48730-48736(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214, INTERACTION WITH PHOSPHATIDYLINOSITIDES.
[9]"Endosomal localization and function of sorting nexin 1."
Zhong Q., Lazar C.S., Tronchere H., Sato T., Meerloo T., Yeo M., Songyang Z., Emr S.D., Gill G.N.
Proc. Natl. Acad. Sci. U.S.A. 99:6767-6772(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX2.
[10]"Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides."
Carlton J., Bujny M., Peter B.J., Oorschot V.M., Rutherford A., Mellor H., Klumperman J., McMahon H.T., Cullen P.J.
Curr. Biol. 14:1791-1800(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-214 AND 429-LYS--ARG-431.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors."
Rojas R., Kametaka S., Haft C.R., Bonifacino J.S.
Mol. Cell. Biol. 27:1112-1124(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-39 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport."
Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.
Cell Res. 19:1334-1349(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX6.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"Determinants of the endosomal localization of sorting nexin 1."
Zhong Q., Watson M.J., Lazar C.S., Hounslow A.M., Waltho J.P., Gill G.N.
Mol. Biol. Cell 16:2049-2057(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 142-269, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U53225 mRNA. Translation: AAA98672.1.
AF065483 mRNA. Translation: AAC17182.1.
AF065484 mRNA. Translation: AAC17183.1.
BT006983 mRNA. Translation: AAP35629.1.
AK128179 mRNA. Translation: BAC87312.1.
AK291752 mRNA. Translation: BAF84441.1.
AC021541 Genomic DNA. No translation available.
AC100840 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77663.1.
CH471082 Genomic DNA. Translation: EAW77665.1.
BC000357 mRNA. Translation: AAH00357.1.
PIRG02522.
RefSeqNP_001229862.1. NM_001242933.1.
NP_003090.2. NM_003099.4.
NP_683758.1. NM_148955.3.
UniGeneHs.188634.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I4KNMR-A142-269[»]
4FZSX-ray2.80A/B301-522[»]
ProteinModelPortalQ13596.
SMRQ13596. Positions 142-269, 305-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112525. 30 interactions.
DIPDIP-398N.
IntActQ13596. 10 interactions.
MINTMINT-4135098.
STRING9606.ENSP00000369638.

PTM databases

PhosphoSiteQ13596.

Polymorphism databases

DMDM17380569.

Proteomic databases

PaxDbQ13596.
PRIDEQ13596.

Protocols and materials databases

DNASU6642.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261889; ENSP00000261889; ENSG00000028528. [Q13596-3]
ENST00000559844; ENSP00000453785; ENSG00000028528. [Q13596-1]
ENST00000561026; ENSP00000453567; ENSG00000028528. [Q13596-2]
GeneID6642.
KEGGhsa:6642.
UCSCuc002amv.3. human. [Q13596-1]
uc002amx.3. human. [Q13596-2]

Organism-specific databases

CTD6642.
GeneCardsGC15P064875.
HGNCHGNC:11172. SNX1.
HPAHPA047373.
HPA052761.
MIM601272. gene.
neXtProtNX_Q13596.
PharmGKBPA36011.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5391.
HOVERGENHBG000618.
InParanoidQ13596.
KOK17917.
OMAPQPTYEE.
OrthoDBEOG7HHWSB.
PhylomeDBQ13596.
TreeFamTF313698.

Gene expression databases

ArrayExpressQ13596.
BgeeQ13596.
CleanExHS_SNX1.
GenevestigatorQ13596.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR001683. Phox.
IPR028660. SNX1.
IPR005329. Sorting_nexin_N.
IPR015404. Vps5_C.
[Graphical view]
PANTHERPTHR10555:SF30. PTHR10555:SF30. 1 hit.
PfamPF00787. PX. 1 hit.
PF03700. Sorting_nexin. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
SMARTSM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNX1. human.
EvolutionaryTraceQ13596.
GeneWikiSNX1.
GenomeRNAi6642.
NextBio25881.
PROQ13596.
SOURCESearch...

Entry information

Entry nameSNX1_HUMAN
AccessionPrimary (citable) accession number: Q13596
Secondary accession number(s): A6NM19 expand/collapse secondary AC list , A8K6T7, H0Y2M5, O60750, O60751, Q6ZRJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 16, 2001
Last modified: April 16, 2014
This is version 130 of the entry and version 3 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 15

Human chromosome 15: entries, gene names and cross-references to MIM