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Q9Y6H5 (SNCAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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:
Synphilin-1

Short name=Sph1
Alternative name(s):
Alpha-synuclein-interacting protein
Gene names
Name:SNCAIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 2 inhibits the ubiquitin ligase activity of SIAH1 and inhibits proteasomal degradation of target proteins. Isoform 2 inhibits autoubiquitination and proteasomal degradation of SIAH1, and thereby increases cellular levels of SIAH. Isoform 2 modulates SNCA monoubiquitination by SIAH1. Ref.3 Ref.11

Subunit structure

Homodimer Probable. Heterodimer of isoform 1 and isoform 2 Probable. Interacts with SIAH1, SIAH2, SNCA, RNF19A AND PARK2. Isoform 2 has a strong tendency to form aggregates and can sequester isoform 1. Ref.1 Ref.3 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Note: Detected in cytoplasmic inclusion bodies, together with SNCA. Ref.1 Ref.3 Ref.10 Ref.12

Tissue specificity

Detected in brain (at protein level). Widely expressed, with highest levels in brain, heart and placenta. Ref.1 Ref.3

Post-translational modification

Ubiquitinated; mediated by SIAH1, SIAH2 or RNF19A and leading to its subsequent proteasomal degradation. In the absence of proteasomal degradation, ubiquitinated SNCAIP accumulates in cytoplasmic inclusion bodies. Isoform 2 is subject to limited ubiquitination that does not lead to proteasomal degradation. Ref.7 Ref.8 Ref.9 Ref.10

Involvement in disease

Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.7 Ref.13 Ref.14

Miscellaneous

Constructs encoding portions of SNCA and SNCAIP co-transfected in mammalian cells promote cytosolic inclusions resembling the Lewy bodies of Parkinson disease. Coexpression of SNCA, SNCAIP, and PARK2 result in the formation of Lewy body-like. ubiquitin-positive cytosolic inclusions. SNCAIP isoform 2 is particularly aggregation-prone. Familial mutations in PARK2 disrupt the ubiquitination of SNCAIP and the formation of the ubiquitin-positive inclusions. These results provide a molecular basis for the ubiquitination of Lewy body-associated proteins and link PARK2 and SNCA in a common pathogenic mechanism through their interaction with SNCAIP.

Sequence similarities

Contains 6 ANK repeats.

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6H5-1)

Also known as: 1a;

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: Q9Y6H5-2)

Also known as: Synphilin-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-366: Missing.
     367-394: QHLTSLMGEDCLNERNTEKLTPAGLAIK → MTYLIQSHHSRRSQNCAEDVIRKTKTDQ
     919-919: A → EMYSSCINLSSNMLIEEHLCNDTRHNDINRKMKKSYSIKHIAEPESKELFL
Isoform 3 (identifier: Q9Y6H5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: S → SDNRSQGNRLQKLGLEDTDREDAMGFGSHRAKLTVVAALGACHCPENE
     919-919: A → EMYSSCINLSSNMLIEEHLCNDTRHNDINRKMKKSYSIKHIAEPESKELFL
Isoform 4 (identifier: Q9Y6H5-4)

Also known as: 1b;

The sequence of this isoform differs from the canonical sequence as follows:
     335-394: Missing.
Isoform 5 (identifier: Q9Y6H5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-366: Missing.
     367-394: QHLTSLMGEDCLNERNTEKLTPAGLAIK → MTYLIQSHHSRRSQNCAEDVIRKTKTDQ
Isoform 6 (identifier: Q9Y6H5-6)

Also known as: 1c;

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: S → SDNRSQGNRLQKLGLEDTDREDAMGFGSHRAKLTVVAALGACHCPENE
     476-541: LVEYGANVTM...QTVERVTLQN → RLKIQGTWNG...NQLPETKSSY
     542-919: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 919919Synphilin-1
PRO_0000067068

Regions

Repeat349 – 38032ANK 1
Repeat384 – 41330ANK 2
Repeat419 – 44830ANK 3
Repeat456 – 48530ANK 4
Repeat603 – 63230ANK 5
Repeat699 – 72931ANK 6
Coiled coil515 – 55238 Potential

Natural variations

Alternative sequence1 – 366366Missing in isoform 2 and isoform 5.
VSP_038839
Alternative sequence191S → SDNRSQGNRLQKLGLEDTDR EDAMGFGSHRAKLTVVAALG ACHCPENE in isoform 3 and isoform 6.
VSP_038840
Alternative sequence335 – 39460Missing in isoform 4.
VSP_038841
Alternative sequence367 – 39428QHLTS…GLAIK → MTYLIQSHHSRRSQNCAEDV IRKTKTDQ in isoform 2 and isoform 5.
VSP_038842
Alternative sequence476 – 54166LVEYG…VTLQN → RLKIQGTWNGSETCLFTHHF SSYPPISSGLQCQGQEGVLF IPDQVGAATNKQVLFQNQLP ETKSSY in isoform 6.
VSP_038843
Alternative sequence542 – 919378Missing in isoform 6.
VSP_038844
Alternative sequence9191A → EMYSSCINLSSNMLIEEHLC NDTRHNDINRKMKKSYSIKH IAEPESKELFL in isoform 2 and isoform 3.
VSP_038845
Natural variant441V → A. Ref.1 Ref.4 Ref.14
Corresponds to variant rs56285021 [ dbSNP | Ensembl ].
VAR_065358
Natural variant2351E → G.
Corresponds to variant rs6867105 [ dbSNP | Ensembl ].
VAR_048312
Natural variant6211R → C Found in patients with symptoms of Parkinson disease; unknown pathological significance; reduced number of cytoplasmic inclusions in cells expressing C-621 compared with cells expressing wild-type (wt) protein when subjected to proteasomal inhibition; C-621 transfected cells are more susceptible to staurosporine-induced cell death than cells expressin wt protein. Ref.13 Ref.14
Corresponds to variant rs28937592 [ dbSNP | Ensembl ].
VAR_025667
Natural variant7061E → Q. Ref.14
VAR_065359

Experimental info

Mutagenesis791V → N: Decreases interaction with SIAH1 and formation of cytoplasmic inclusion bodies; when associated with N-81. Ref.10
Mutagenesis811P → N: Decreases interaction with SIAH1 and formation of cytoplasmic inclusion bodies; when associated with N-79. Ref.10
Sequence conflict1881S → F in AAH40552. Ref.6
Sequence conflict6141E → G in AAH40552. Ref.6
Sequence conflict6961A → G in AAH40552. Ref.6
Sequence conflict7121D → G in AAH94759. Ref.6
Sequence conflict8011S → P in AAH33743. Ref.6
Sequence conflict9191A → E in AAH94759. Ref.6

Secondary structure

... 919
Helix Strand Turn

Details...

Sequences

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

Last modified July 22, 2008. Version 2.
Checksum: 55C5316F250D0480

FASTA919100,409
        10         20         30         40         50         60 
MEAPEYLDLD EIDFSDDISY SVTSLKTIPE LCRRCDTQNE DRSVSSSSWN CGISTLITNT 

        70         80         90        100        110        120 
QKPTGIADVY SKFRPVKRVS PLKHQPETLE NNESDDQKNQ KVVEYQKGGE SDLGPQPQEL 

       130        140        150        160        170        180 
GPGDGVGGPP GKSSEPSTSL GELEHYDLDM DEILDVPYIK SSQQLASFTK VTSEKRILGL 

       190        200        210        220        230        240 
CTTINGLSGK ACSTGSSESS SSNMAPFCVL SPVKSPHLRK ASAVIHDQHK LSTEETEISP 

       250        260        270        280        290        300 
PLVKCGSAYE PENQSKDFLN KTFSDPHGRK VEKTTPDCQL RAFHLQSSAA ESKPEEQVSG 

       310        320        330        340        350        360 
LNRTSSQGPE ERSEYLKKVK SILNIVKEGQ ISLLPHLAAD NLDKIHDENG NNLLHIAASQ 

       370        380        390        400        410        420 
GHAECLQHLT SLMGEDCLNE RNTEKLTPAG LAIKNGQLEC VRWMVSETEA IAELSCSKDF 

       430        440        450        460        470        480 
PSLIHYAGCY GQEKILLWLL QFMQEQGISL DEVDQDGNSA VHVASQHGYL GCIQTLVEYG 

       490        500        510        520        530        540 
ANVTMQNHAG EKPSQSAERQ GHTLCSRYLV VVETCMSLAS QVVKLTKQLK EQTVERVTLQ 

       550        560        570        580        590        600 
NQLQQFLEAQ KSEGKSLPSS PSSPSSPASR KSQWKSPDAD DDSVAKSKPG VQEGIQVLGS 

       610        620        630        640        650        660 
LSASSRARPK AKDEDSDKIL RQLLGKEISE NVCTQEKLSL EFQDAQASSR NSKKIPLEKR 

       670        680        690        700        710        720 
ELKLARLRQL MQRSLSESDT DSNNSEDPKT TPVRKADRPR PQPIVESVES MDSAESLHLM 

       730        740        750        760        770        780 
IKKHTLASGG RRFPFSIKAS KSLDGHSPSP TSESSEPDLE SQYPGSGSIP PNQPSGDPQQ 

       790        800        810        820        830        840 
PSPDSTAAQK VATSPKSALK SPSSKRRTSQ NLKLRVTFEE PVVQMEQPSL ELNGEKDKDK 

       850        860        870        880        890        900 
GRTLQRTSTS NESGDQLKRP FGAFRSIMET LSGNQNNNNN YQAANQLKTS TLPLTSLGRK 

       910 
TDAKGNPASS ASKGKNKAA 

« Hide

Isoform 2 (Synphilin-1A) [UniParc].

Checksum: 3C41F69D861CE493
Show »

FASTA60366,646
Isoform 3 [UniParc].

Checksum: 6EC840B66BA8217D
Show »

FASTA1,016111,455
Isoform 4 (1b) [UniParc].

Checksum: 949D53FF98FCE6E6
Show »

FASTA85993,930
Isoform 5 [UniParc].

Checksum: EAEBC23FCD35545A
Show »

FASTA55360,693
Isoform 6 (1c) [UniParc].

Checksum: EBF343E479576255
Show »

FASTA58864,469

References

« Hide 'large scale' references
[1]"Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions."
Engelender S., Kaminsky Z., Guo X., Sharp A.H., Amaravi R.K., Kleiderlein J.J., Margolis R.L., Troncoso J.C., Lanahan A., Worley P.F., Dawson V.L., Dawson T.M., Ross C.A.
Nat. Genet. 22:110-114(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SNCA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ALA-44.
Tissue: Brain.
[2]"Organization of the human synphilin-1 gene, a candidate for Parkinson's disease."
Engelender S., Wanner T., Kleiderlein J.J., Wakabayashi K., Tsuji S., Takahashi H., Ashworth R., Margolis R.L., Ross C.A.
Mamm. Genome 11:763-766(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]"Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients."
Eyal A., Szargel R., Avraham E., Liani E., Haskin J., Rott R., Engelender S.
Proc. Natl. Acad. Sci. U.S.A. 103:5917-5922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH SNCA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Identification and characterization of alternatively spliced form of human synphilin-1."
Lim M.K., Ohsawa Y., Kawamura T., Asakawa S., Takayanagi A., Minoshima S., Shimizu N.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 6), VARIANT ALA-44.
Tissue: Cerebellum and Testis.
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 2; 3 AND 5).
Tissue: Brain and Testis.
[7]"Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease."
Chung K.K.K., Zhang Y., Lim K.L., Tanaka Y., Huang H., Gao J., Ross C.A., Dawson V.L., Dawson T.M.
Nat. Med. 7:1144-1150(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARK2, UBIQUITINATION.
[8]"Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1."
Ito T., Niwa J., Hishikawa N., Ishigaki S., Doyu M., Sobue G.
J. Biol. Chem. 278:29106-29114(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF19A, UBIQUITINATION.
[9]"Siah-1 facilitates ubiquitination and degradation of synphilin-1."
Nagano Y., Yamashita H., Takahashi T., Kishida S., Nakamura T., Iseki E., Hattori N., Mizuno Y., Kikuchi A., Matsumoto M.
J. Biol. Chem. 278:51504-51514(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[10]"Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease."
Liani E., Eyal A., Avraham E., Shemer R., Szargel R., Berg D., Bornemann A., Riess O., Ross C.A., Rott R., Engelender S.
Proc. Natl. Acad. Sci. U.S.A. 101:5500-5505(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, INTERACTION WITH SIAH1 AND SIAH2, MUTAGENESIS OF VAL-79 AND PRO-81.
[11]"Synphilin-1A inhibits seven in absentia homolog (SIAH) and modulates alpha-synuclein monoubiquitylation and inclusion formation."
Szargel R., Rott R., Eyal A., Haskin J., Shani V., Balan L., Wolosker H., Engelender S.
J. Biol. Chem. 284:11706-11716(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIAH1.
[12]"Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication."
Xie Y.Y., Zhou C.J., Zhou Z.R., Hong J., Che M.X., Fu Q.S., Song A.X., Lin D.H., Hu H.Y.
FASEB J. 24:196-205(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 512-557, INTERACTION WITH SNCA, PROMOTION OF INCLUSION BODY FORMATION, SUBCELLULAR LOCATION.
[13]"Identification and functional characterization of a novel R621C mutation in the synphilin-1 gene in Parkinson's disease."
Marx F.P., Holzmann C., Strauss K.M., Li L., Eberhardt O., Gerhardt E., Cookson M.R., Hernandez D., Farrer M.J., Kachergus J., Engelender S., Ross C.A., Berger K., Schols L., Schulz J.B., Riess O., Kruger R.
Hum. Mol. Genet. 12:1223-1231(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-621, CHARACTERIZATION OF VARIANT CYS-621, POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO PARKINSON DISEASE.
[14]"Genetic association study of synphilin-1 in idiopathic Parkinson's disease."
Myhre R., Klungland H., Farrer M.J., Aasly J.O.
BMC Med. Genet. 9:19-19(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-44; CYS-621 AND GLN-706, LACK OF ASSOCIATION WITH PARKINSON DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF076929 mRNA. Translation: AAD30362.1.
AF167306 expand/collapse EMBL AC list , AF167301, AF167302, AF167303, AF167304, AF167305 Genomic DNA. Translation: AAG17478.1.
DQ227317 mRNA. Translation: ABB51162.1.
CH471086 Genomic DNA. Translation: EAW48889.1.
AB110788 mRNA. Translation: BAD19017.1.
AB110789 mRNA. Translation: BAD19018.1.
AB110790 mRNA. Translation: BAD19019.1.
CH471086 Genomic DNA. Translation: EAW48890.1.
BC033743 mRNA. Translation: AAH33743.1.
BC040552 mRNA. Translation: AAH40552.1.
BC094759 mRNA. Translation: AAH94759.1.
CCDSCCDS4131.1. [Q9Y6H5-1]
CCDS58964.1. [Q9Y6H5-2]
RefSeqNP_001229864.1. NM_001242935.1. [Q9Y6H5-2]
NP_005451.2. NM_005460.2. [Q9Y6H5-1]
XP_006714798.1. XM_006714735.1. [Q9Y6H5-1]
UniGeneHs.426463.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KESNMR-A512-557[»]
ProteinModelPortalQ9Y6H5.
SMRQ9Y6H5. Positions 320-510, 512-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114986. 28 interactions.
IntActQ9Y6H5. 14 interactions.
MINTMINT-1380209.
STRING9606.ENSP00000261368.

Chemistry

ChEMBLCHEMBL1926494.

PTM databases

PhosphoSiteQ9Y6H5.

Polymorphism databases

DMDM205831000.

Proteomic databases

PaxDbQ9Y6H5.
PRIDEQ9Y6H5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261367; ENSP00000261367; ENSG00000064692. [Q9Y6H5-3]
ENST00000261368; ENSP00000261368; ENSG00000064692. [Q9Y6H5-1]
ENST00000379533; ENSP00000368848; ENSG00000064692. [Q9Y6H5-3]
ENST00000379536; ENSP00000368851; ENSG00000064692. [Q9Y6H5-4]
ENST00000379538; ENSP00000368854; ENSG00000064692. [Q9Y6H5-2]
ENST00000395469; ENSP00000378852; ENSG00000064692. [Q9Y6H5-6]
ENST00000503116; ENSP00000423199; ENSG00000064692. [Q9Y6H5-6]
GeneID9627.
KEGGhsa:9627.
UCSCuc003ksw.1. human. [Q9Y6H5-1]
uc003ksx.1. human. [Q9Y6H5-3]
uc003ksy.1. human. [Q9Y6H5-2]
uc003ksz.1. human. [Q9Y6H5-5]

Organism-specific databases

CTD9627.
GeneCardsGC05P121675.
GeneReviewsSNCAIP.
H-InvDBHIX0005121.
HIX0018508.
HGNCHGNC:11139. SNCAIP.
HPACAB022597.
HPA003266.
MIM168600. phenotype.
603779. gene.
neXtProtNX_Q9Y6H5.
PharmGKBPA35987.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG061375.
KOK04558.
OMAQWKSPDA.
PhylomeDBQ9Y6H5.
TreeFamTF329095.

Gene expression databases

ArrayExpressQ9Y6H5.
BgeeQ9Y6H5.
CleanExHS_SNCAIP.
GenevestigatorQ9Y6H5.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF12796. Ank_2. 2 hits.
[Graphical view]
SMARTSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNCAIP. human.
EvolutionaryTraceQ9Y6H5.
GeneWikiSNCAIP.
GenomeRNAi9627.
NextBio36127.
PMAP-CutDBQ9Y6H5.
PROQ9Y6H5.
SOURCESearch...

Entry information

Entry nameSNCAP_HUMAN
AccessionPrimary (citable) accession number: Q9Y6H5
Secondary accession number(s): D3DSZ1 expand/collapse secondary AC list , Q05BS1, Q1PSC2, Q49AC6, Q504U9, Q6L984, Q6L985, Q6L986, Q9HC59
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 128 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 5

Human chromosome 5: entries, gene names and cross-references to MIM