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Protein

Calcium homeostasis endoplasmic reticulum protein

Gene

CHERP

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

Functioni

Involved in calcium homeostasis, growth and proliferation.2 Publications

GO - Molecular functioni

  • ion channel binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cellular calcium ion homeostasis Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • nervous system development Source: ProtInc
  • positive regulation of NFAT protein import into nucleus Source: UniProtKB
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • RNA processing Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium homeostasis endoplasmic reticulum protein
Alternative name(s):
ERPROT 213-21
SR-related CTD-associated factor 6
Gene namesi
Name:CHERPImported
Synonyms:DAN26Imported, SCAF6Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:16930. CHERP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • sarcoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26459.

Polymorphism and mutation databases

BioMutaiCHERP.
DMDMi296439404.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916Calcium homeostasis endoplasmic reticulum proteinPRO_0000299492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei18 – 181N6-acetyllysineCombined sources
Modified residuei714 – 7141PhosphotyrosineBy similarity
Modified residuei813 – 8131PhosphoserineCombined sources
Modified residuei815 – 8151PhosphoserineCombined sources
Modified residuei817 – 8171PhosphoserineCombined sources
Modified residuei819 – 8191PhosphothreonineCombined sources
Modified residuei828 – 8281PhosphoserineCombined sources
Modified residuei855 – 8551PhosphoserineCombined sources
Modified residuei857 – 8571PhosphoserineCombined sources
Modified residuei879 – 8791N6-acetyllysineCombined sources
Modified residuei904 – 9041PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8IWX8.
MaxQBiQ8IWX8.
PaxDbiQ8IWX8.
PeptideAtlasiQ8IWX8.
PRIDEiQ8IWX8.

PTM databases

iPTMnetiQ8IWX8.
PhosphoSiteiQ8IWX8.

Expressioni

Tissue specificityi

Expressed in brain, placenta, lung, liver, kidney, pancreas, cardiac and skeletal muscle, and in cultured HEL and Dami cells.1 Publication

Gene expression databases

BgeeiQ8IWX8.
CleanExiHS_CHERP.
ExpressionAtlasiQ8IWX8. baseline and differential.
GenevisibleiQ8IWX8. HS.

Organism-specific databases

HPAiHPA050647.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX8Q145622EBI-2555370,EBI-2511477
FRA10AC1Q70Z532EBI-2555370,EBI-710176
LUC7LQ9NQ292EBI-2555370,EBI-473747
SF1Q156376EBI-2555370,EBI-744603
SNRNP27Q8WVK22EBI-2555370,EBI-2512550
U2AF2P263682EBI-2555370,EBI-742339

GO - Molecular functioni

  • ion channel binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115778. 67 interactions.
IntActiQ8IWX8. 42 interactions.
MINTiMINT-4654608.
STRINGi9606.ENSP00000439856.

Structurei

3D structure databases

ProteinModelPortaliQ8IWX8.
SMRiQ8IWX8. Positions 6-61.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati15 – 5743SURP motifSequence analysisAdd
BLAST
Domaini149 – 289141CIDPROSITE-ProRule annotationAdd
BLAST
Domaini841 – 89151G-patchPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi279 – 34668Gln-richSequence analysisAdd
BLAST
Compositional biasi355 – 682328Pro-richSequence analysisAdd
BLAST
Compositional biasi718 – 81699Arg-richSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 CID domain.PROSITE-ProRule annotation
Contains 1 G-patch domain.PROSITE-ProRule annotation
Contains 1 SURP motif repeat.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4368. Eukaryota.
ENOG410YVN1. LUCA.
GeneTreeiENSGT00730000111147.
HOGENOMiHOG000010294.
HOVERGENiHBG052716.
InParanoidiQ8IWX8.
KOiK12841.
OrthoDBiEOG7H1JK4.
PhylomeDBiQ8IWX8.
TreeFamiTF318512.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR000467. G_patch_dom.
IPR006903. RNA_pol_II-bd.
IPR000061. Surp.
[Graphical view]
PfamiPF04818. CTD_bind. 1 hit.
PF01585. G-patch. 1 hit.
PF01805. Surp. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
SM00648. SWAP. 1 hit.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
PS50174. G_PATCH. 1 hit.
PS50128. SURP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IWX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMPLPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG
60 70 80 90 100
EFYSYYKCKL ALEQQQLICK QQTPELEPAA TMPPLPQPPL APAAPIPPAQ
110 120 130 140 150
GAPSMDELIQ QSQWNLQQQE QHLLALRQEQ VTAAVAHAVE QQMQKLLEET
160 170 180 190 200
QLDMNEFDNL LQPIIDTCTK DAISAGKNWM FSNAKSPPHC ELMAGHLRNR
210 220 230 240 250
ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV VVPIYCTSFL
260 270 280 290 300
AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS
310 320 330 340 350
SVVQPVQLAF QQQIQTLKTQ HEEFVTSLAQ QQQQQQQQQQ QLQMPQMEAE
360 370 380 390 400
VKATPPPPAP PPAPAPAPAI PPTTQPDDSK PPIQMPGSSE YEAPGGVQDP
410 420 430 440 450
AAAGPRGPGP HDQIPPNKPP WFDQPHPVAP WGQQQPPEQP PYPHHQGGPP
460 470 480 490 500
HCPPWNNSHE GMWGEQRGDP GWNGQRDAPW NNQPDAAWNS QFEGPWNSQH
510 520 530 540 550
EQPPWGGGQR EPPFRMQRPP HFRGPFPPHQ QHPQFNQPPH PHNFNRFPPR
560 570 580 590 600
FMQDDFPPRH PFERPPYPHR FDYPQGDFPA EMGPPHHHPG HRMPHPGINE
610 620 630 640 650
HPPWAGPQHP DFGPPPHGFN GQPPHMRRQG PPHINHDDPS LVPNVPYFDL
660 670 680 690 700
PAGLMAPLVK LEDHEYKPLD PKDIRLPPPM PPSERLLAAV EAFYSPPSHD
710 720 730 740 750
RPRNSEGWEQ NGLYEFFRAK MRARRRKGQE KRNSGPSRSR SRSKSRGRSS
760 770 780 790 800
SRSNSRSSKS SGSYSRSRSR SCSRSYSRSR SRSRSRSRSS RSRSRSQSRS
810 820 830 840 850
RSKSYSPGRR RRSRSRSPTP PSSAGLGSNS APPIPDSRLG EENKGHQMLV
860 870 880 890 900
KMGWSGSGGL GAKEQGIQDP IKGGDVRDKW DQYKGVGVAL DDPYENYRRN
910
KSYSFIARMK ARDECK
Length:916
Mass (Da):103,702
Last modified:May 18, 2010 - v3
Checksum:i0C5D56F4DE4C5B9B
GO

Sequence cautioni

The sequence AAB53327.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH21294.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA69591.1 differs from that shown. Reason: Frameshift at position 450. Curated
The sequence CAA69591.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991A → D in CAA69591 (PubMed:8896557).Curated
Sequence conflicti175 – 1751A → G in CAA69591 (PubMed:8896557).Curated
Sequence conflicti185 – 1851K → T in CAA69591 (PubMed:8896557).Curated
Sequence conflicti189 – 1891H → Y in CAA69591 (PubMed:8896557).Curated
Sequence conflicti203 – 2031A → V in CAA69591 (PubMed:8896557).Curated
Sequence conflicti418 – 4181K → N in CAA69591 (PubMed:8896557).Curated
Sequence conflicti490 – 4901S → N in CAA69591 (PubMed:8896557).Curated
Sequence conflicti776 – 7761Y → S in AAN77183 (Ref. 1) Curated
Sequence conflicti778 – 7781R → C in AAN77183 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991N → H.2 Publications
Corresponds to variant rs1043448 [ dbSNP | Ensembl ].
VAR_034833

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF536542 mRNA. Translation: AAN77183.1.
AC008764 Genomic DNA. No translation available.
BC021294 mRNA. Translation: AAH21294.1. Different initiation.
Y08265 mRNA. Translation: CAA69591.1. Sequence problems.
U94836 mRNA. Translation: AAB53327.1. Different initiation.
CCDSiCCDS42518.1.
RefSeqiNP_006378.3. NM_006387.5.
UniGeneiHs.740364.

Genome annotation databases

EnsembliENST00000546361; ENSP00000439856; ENSG00000085872.
GeneIDi10523.
KEGGihsa:10523.
UCSCiuc002nei.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF536542 mRNA. Translation: AAN77183.1.
AC008764 Genomic DNA. No translation available.
BC021294 mRNA. Translation: AAH21294.1. Different initiation.
Y08265 mRNA. Translation: CAA69591.1. Sequence problems.
U94836 mRNA. Translation: AAB53327.1. Different initiation.
CCDSiCCDS42518.1.
RefSeqiNP_006378.3. NM_006387.5.
UniGeneiHs.740364.

3D structure databases

ProteinModelPortaliQ8IWX8.
SMRiQ8IWX8. Positions 6-61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115778. 67 interactions.
IntActiQ8IWX8. 42 interactions.
MINTiMINT-4654608.
STRINGi9606.ENSP00000439856.

PTM databases

iPTMnetiQ8IWX8.
PhosphoSiteiQ8IWX8.

Polymorphism and mutation databases

BioMutaiCHERP.
DMDMi296439404.

Proteomic databases

EPDiQ8IWX8.
MaxQBiQ8IWX8.
PaxDbiQ8IWX8.
PeptideAtlasiQ8IWX8.
PRIDEiQ8IWX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000546361; ENSP00000439856; ENSG00000085872.
GeneIDi10523.
KEGGihsa:10523.
UCSCiuc002nei.2. human.

Organism-specific databases

CTDi10523.
GeneCardsiCHERP.
HGNCiHGNC:16930. CHERP.
HPAiHPA050647.
neXtProtiNX_Q8IWX8.
PharmGKBiPA26459.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4368. Eukaryota.
ENOG410YVN1. LUCA.
GeneTreeiENSGT00730000111147.
HOGENOMiHOG000010294.
HOVERGENiHBG052716.
InParanoidiQ8IWX8.
KOiK12841.
OrthoDBiEOG7H1JK4.
PhylomeDBiQ8IWX8.
TreeFamiTF318512.

Miscellaneous databases

GenomeRNAii10523.
PROiQ8IWX8.

Gene expression databases

BgeeiQ8IWX8.
CleanExiHS_CHERP.
ExpressionAtlasiQ8IWX8. baseline and differential.
GenevisibleiQ8IWX8. HS.

Family and domain databases

Gene3Di1.25.40.90. 1 hit.
InterProiIPR006569. CID_dom.
IPR008942. ENTH_VHS.
IPR000467. G_patch_dom.
IPR006903. RNA_pol_II-bd.
IPR000061. Surp.
[Graphical view]
PfamiPF04818. CTD_bind. 1 hit.
PF01585. G-patch. 1 hit.
PF01805. Surp. 1 hit.
[Graphical view]
SMARTiSM00443. G_patch. 1 hit.
SM00648. SWAP. 1 hit.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 1 hit.
SSF48464. SSF48464. 1 hit.
PROSITEiPS51391. CID. 1 hit.
PS50174. G_PATCH. 1 hit.
PS50128. SURP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional characterization of the novel SR-related CTD associated factor, SCAF6."
    Sampson N.D., Hewitt J.E.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-199.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: UterusImported.
  4. "Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high sensitivity to expanded CAG/glutamine repeats."
    Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M., Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O., Stevanin G., Agid Y., Brice A.
    Nat. Genet. 14:285-291(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-607.
    Tissue: LymphoblastImported.
  5. "Cloning of human Ca2+ homoeostasis endoplasmic reticulum protein (CHERP): regulated expression of antisense cDNA depletes CHERP, inhibits intracellular Ca2+ mobilization and decreases cell proliferation."
    LaPlante J.M., O'Rourke F., Lu X., Fein A., Olsen A., Feinstein M.B.
    Biochem. J. 348:189-199(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-916, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT HIS-199.
  6. "Ca2+ release by inositol 1,4,5-trisphosphate is blocked by the K(+)-channel blockers apamin and tetrapentylammonium ion, and a monoclonal antibody to a 63 kDa membrane protein: reversal of blockade by K+ ionophores nigericin and valinomycin and purification of the 63 kDa antibody-binding protein."
    O'Rourke F., Soons K., Flaumenhauft R., Watras J., Baio-Larue C., Matthews E., Feinstein M.B.
    Biochem. J. 300:673-683(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Antisense-mediated loss of calcium homoeostasis endoplasmic reticulum protein (CHERP; ERPROT213-21) impairs Ca2+ mobilization, nuclear factor of activated T-cells (NFAT) activation and cell proliferation in Jurkat T-lymphocytes."
    O'Rourke F.A., LaPlante J.M., Feinstein M.B.
    Biochem. J. 373:133-143(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817; THR-819; SER-828 AND SER-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-815 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-18 AND LYS-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-813; SER-815; SER-817 AND THR-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-813; SER-815; SER-817; THR-819; SER-855 AND SER-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiCHERP_HUMAN
AccessioniPrimary (citable) accession number: Q8IWX8
Secondary accession number(s): O00302
, Q4G0Y5, Q8WU30, Q99492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 114 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 19
    Human chromosome 19: 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. 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.