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Protein

Secretory carrier-associated membrane protein 3

Gene

SCAMP3

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

Functioni

Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • post-Golgi vesicle-mediated transport Source: ProtInc
  • protein transport Source: UniProtKB-KW
  • response to retinoic acid Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Secretory carrier-associated membrane protein 3
Short name:
Secretory carrier membrane protein 3
Gene namesi
Name:SCAMP3
Synonyms:C1orf3, PROPIN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10565. SCAMP3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 170170CytoplasmicSequence analysisAdd
BLAST
Transmembranei171 – 19121HelicalSequence analysisAdd
BLAST
Transmembranei197 – 21721HelicalSequence analysisAdd
BLAST
Transmembranei247 – 26721HelicalSequence analysisAdd
BLAST
Transmembranei277 – 29721HelicalSequence analysisAdd
BLAST
Topological domaini298 – 34750CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671P → L: Abolishes interaction with TSG101. 1 Publication

Organism-specific databases

PharmGKBiPA34978.

Polymorphism and mutation databases

BioMutaiSCAMP3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Secretory carrier-associated membrane protein 3PRO_0000191257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphoserineCombined sources
Modified residuei37 – 371PhosphothreonineCombined sources
Modified residuei41 – 411PhosphotyrosineCombined sources
Modified residuei53 – 531PhosphotyrosineCombined sources
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei76 – 761PhosphoserineCombined sources
Modified residuei83 – 831PhosphotyrosineBy similarity
Modified residuei85 – 851PhosphoserineCombined sources
Cross-linki313 – 313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources

Post-translational modificationi

Monoubiquitinated.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO14828.
MaxQBiO14828.
PaxDbiO14828.
PeptideAtlasiO14828.
PRIDEiO14828.

PTM databases

iPTMnetiO14828.
PhosphoSiteiO14828.
SwissPalmiO14828.

Miscellaneous databases

PMAP-CutDBO14828.

Expressioni

Tissue specificityi

Widely expressed, with highest expression in heart and skeletal muscle.

Gene expression databases

BgeeiO14828.
CleanExiHS_SCAMP3.
GenevisibleiO14828. HS.

Organism-specific databases

HPAiHPA005896.

Interactioni

Subunit structurei

Interacts with NEDD4, NEDD4L and TSG101. Interacts with RNF126.2 Publications

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115378. 56 interactions.
IntActiO14828. 29 interactions.
MINTiMINT-5003764.
STRINGi9606.ENSP00000307275.

Structurei

3D structure databases

ProteinModelPortaliO14828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SCAMP family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3088. Eukaryota.
ENOG410XSJN. LUCA.
GeneTreeiENSGT00390000014393.
HOGENOMiHOG000294221.
HOVERGENiHBG071938.
InParanoidiO14828.
KOiK19995.
OMAiNPFAEPG.
OrthoDBiEOG7FZ009.
PhylomeDBiO14828.
TreeFamiTF313797.

Family and domain databases

InterProiIPR007273. SCAMP.
[Graphical view]
PANTHERiPTHR10687. PTHR10687. 1 hit.
PfamiPF04144. SCAMP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14828-1) [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
MAQSRDGGNP FAEPSELDNP FQDPAVIQHR PSRQYATLDV YNPFETREPP
60 70 80 90 100
PAYEPPAPAP LPPPSAPSLQ PSRKLSPTEP KNYGSYSTQA SAAAATAELL
110 120 130 140 150
KKQEELNRKA EELDRREREL QHAALGGTAT RQNNWPPLPS FCPVQPCFFQ
160 170 180 190 200
DISMEIPQEF QKTVSTMYYL WMCSTLALLL NFLACLASFC VETNNGAGFG
210 220 230 240 250
LSILWVLLFT PCSFVCWYRP MYKAFRSDSS FNFFVFFFIF FVQDVLFVLQ
260 270 280 290 300
AIGIPGWGFS GWISALVVPK GNTAVSVLML LVALLFTGIA VLGIVMLKRI
310 320 330 340
HSLYRRTGAS FQKAQQEFAA GVFSNPAVRT AAANAAAGAA ENAFRAP
Length:347
Mass (Da):38,287
Last modified:September 23, 2008 - v3
Checksum:iD5B0870C66B84F9F
GO
Isoform 2 (identifier: O14828-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     23-48: Missing.

Note: No experimental confirmation available.
Show »
Length:321
Mass (Da):35,202
Checksum:i4F1819F7430A70C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31Q → R in AAB62724 (PubMed:9378760).Curated
Sequence conflicti74 – 741K → M in AAB62724 (PubMed:9378760).Curated
Sequence conflicti331 – 3311A → R in AAC51821 (PubMed:9331372).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381L → R.1 Publication
Corresponds to variant rs760073 [ dbSNP | Ensembl ].
VAR_011885
Natural varianti235 – 2351V → A.1 Publication
Corresponds to variant rs1318328 [ dbSNP | Ensembl ].
VAR_011886
Natural varianti239 – 2391I → N.1 Publication
Corresponds to variant rs909106 [ dbSNP | Ensembl ].
VAR_011887
Natural varianti242 – 2421V → D.1 Publication
Corresponds to variant rs909107 [ dbSNP | Ensembl ].
VAR_011888

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei23 – 4826Missing in isoform 2. 1 PublicationVSP_004381Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023268 Genomic DNA. Translation: AAC51821.1.
AF005039 mRNA. Translation: AAB62724.1.
AL713999 Genomic DNA. Translation: CAI95095.1.
AL713999 Genomic DNA. Translation: CAI95096.1.
CH471121 Genomic DNA. Translation: EAW53090.1.
CH471121 Genomic DNA. Translation: EAW53092.1.
BC000161 mRNA. Translation: AAH00161.1.
BC005135 mRNA. Translation: AAH05135.1.
BC010505 mRNA. Translation: AAH10505.1.
CCDSiCCDS1105.1. [O14828-1]
CCDS1106.1. [O14828-2]
PIRiT08826.
RefSeqiNP_005689.2. NM_005698.3. [O14828-1]
NP_443069.1. NM_052837.2. [O14828-2]
UniGeneiHs.200600.

Genome annotation databases

EnsembliENST00000302631; ENSP00000307275; ENSG00000116521. [O14828-1]
ENST00000355379; ENSP00000347540; ENSG00000116521. [O14828-2]
ENST00000570831; ENSP00000461521; ENSG00000263290. [O14828-1]
ENST00000573013; ENSP00000458542; ENSG00000263290. [O14828-2]
GeneIDi10067.
KEGGihsa:10067.
UCSCiuc001fjs.4. human. [O14828-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023268 Genomic DNA. Translation: AAC51821.1.
AF005039 mRNA. Translation: AAB62724.1.
AL713999 Genomic DNA. Translation: CAI95095.1.
AL713999 Genomic DNA. Translation: CAI95096.1.
CH471121 Genomic DNA. Translation: EAW53090.1.
CH471121 Genomic DNA. Translation: EAW53092.1.
BC000161 mRNA. Translation: AAH00161.1.
BC005135 mRNA. Translation: AAH05135.1.
BC010505 mRNA. Translation: AAH10505.1.
CCDSiCCDS1105.1. [O14828-1]
CCDS1106.1. [O14828-2]
PIRiT08826.
RefSeqiNP_005689.2. NM_005698.3. [O14828-1]
NP_443069.1. NM_052837.2. [O14828-2]
UniGeneiHs.200600.

3D structure databases

ProteinModelPortaliO14828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115378. 56 interactions.
IntActiO14828. 29 interactions.
MINTiMINT-5003764.
STRINGi9606.ENSP00000307275.

PTM databases

iPTMnetiO14828.
PhosphoSiteiO14828.
SwissPalmiO14828.

Polymorphism and mutation databases

BioMutaiSCAMP3.

Proteomic databases

EPDiO14828.
MaxQBiO14828.
PaxDbiO14828.
PeptideAtlasiO14828.
PRIDEiO14828.

Protocols and materials databases

DNASUi10067.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302631; ENSP00000307275; ENSG00000116521. [O14828-1]
ENST00000355379; ENSP00000347540; ENSG00000116521. [O14828-2]
ENST00000570831; ENSP00000461521; ENSG00000263290. [O14828-1]
ENST00000573013; ENSP00000458542; ENSG00000263290. [O14828-2]
GeneIDi10067.
KEGGihsa:10067.
UCSCiuc001fjs.4. human. [O14828-1]

Organism-specific databases

CTDi10067.
GeneCardsiSCAMP3.
HGNCiHGNC:10565. SCAMP3.
HPAiHPA005896.
MIMi606913. gene.
neXtProtiNX_O14828.
PharmGKBiPA34978.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3088. Eukaryota.
ENOG410XSJN. LUCA.
GeneTreeiENSGT00390000014393.
HOGENOMiHOG000294221.
HOVERGENiHBG071938.
InParanoidiO14828.
KOiK19995.
OMAiNPFAEPG.
OrthoDBiEOG7FZ009.
PhylomeDBiO14828.
TreeFamiTF313797.

Miscellaneous databases

ChiTaRSiSCAMP3. human.
GeneWikiiSCAMP3.
GenomeRNAii10067.
PMAP-CutDBO14828.
PROiO14828.
SOURCEiSearch...

Gene expression databases

BgeeiO14828.
CleanExiHS_SCAMP3.
GenevisibleiO14828. HS.

Family and domain databases

InterProiIPR007273. SCAMP.
[Graphical view]
PANTHERiPTHR10687. PTHR10687. 1 hit.
PfamiPF04144. SCAMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease."
    Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.
    Genome Res. 7:1020-1026(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ARG-38; ALA-235; ASN-239 AND ASP-242.
    Tissue: Brain.
  2. "Three mammalian SCAMPs (secretory carrier membrane proteins) are highly related products of distinct genes having similar subcellular distributions."
    Singleton D.R., Wu T.T., Castle J.D.
    J. Cell Sci. 110:2099-2107(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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 1 AND 2).
    Tissue: Brain, Cervix and Placenta.
  6. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "SCAMP3 negatively regulates epidermal growth factor receptor degradation and promotes receptor recycling."
    Aoh Q.L., Castle A.M., Hubbard C.H., Katsumata O., Castle J.D.
    Mol. Biol. Cell 20:1816-1832(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH NEDD4; NEDD4L AND TSG101, MUTAGENESIS OF PRO-67.
  10. "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-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF126.
  15. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; THR-37; SER-72 AND SER-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSCAM3_HUMAN
AccessioniPrimary (citable) accession number: O14828
Secondary accession number(s): A9Z1W6
, B1AVS6, O15128, Q96FR8, Q9BPY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 23, 2008
Last modified: July 6, 2016
This is version 157 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.