Q8IWX8 (CHERP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium homeostasis endoplasmic reticulum protein

Alternative name(s):
ERPROT 213-21
SR-related CTD-associated factor 6

Gene names

Name:	CHERP
Synonyms:	DAN26, SCAF6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	916 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in calcium homeostasis, growth and proliferation. Ref.5 Ref.7
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region. Endoplasmic reticulum. Note: Distributed throughout the cytoplasm and also localizes to the perinuclear region of both human erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with ITPR1. Ref.5 Ref.6 Ref.7
Tissue specificity	Expressed in brain, placenta, lung, liver, kidney, pancreas, cardiac and skeletal muscle, and in cultured HEL and Dami cells. Ref.5
Sequence similarities	Contains 1 CID domain. Contains 1 G-patch domain. Contains 1 SURP motif repeat.
Sequence caution	The sequence AAB53327.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH21294.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA69591.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA69591.1 differs from that shown. Reason: Frameshift at position 450.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro cellular calcium ion homeostasis Inferred from direct assay Ref.5. Source: MGI negative regulation of cell proliferation Inferred from direct assay Ref.5. Source: MGI nervous system development Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 916	916	Calcium homeostasis endoplasmic reticulum protein		PRO_0000299492
Regions
	Repeat	15 – 57	43	SURP motif
	Domain	149 – 289	141	CID
	Domain	841 – 891	51	G-patch
	Compositional bias	279 – 346	68	Gln-rich
	Compositional bias	355 – 682	328	Pro-rich
	Compositional bias	718 – 816	99	Arg-rich
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.9
	Modified residue	18	1	N6-acetyllysine Ref.11
	Modified residue	714	1	Phosphotyrosine By similarity
	Modified residue	813	1	Phosphoserine Ref.8 UniProtKB Q8CGZ0
	Modified residue	815	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	817	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	819	1	Phosphothreonine Ref.8 Ref.9
	Modified residue	822	1	Phosphoserine Ref.8 Ref.9
	Modified residue	823	1	Phosphoserine Ref.8
	Modified residue	828	1	Phosphoserine Ref.8
	Modified residue	830	1	Phosphoserine Ref.8
	Modified residue	879	1	N6-acetyllysine Ref.11
	Modified residue	901	1	N6-acetyllysine Ref.11
	Modified residue	904	1	Phosphoserine Ref.8
Natural variations
	Natural variant	199	1	N → H. Ref.1 Ref.5 Corresponds to variant rs1043448 [ dbSNP | Ensembl ].		VAR_034833
Experimental info
	Sequence conflict	99	1	A → D in CAA69591. Ref.4
	Sequence conflict	175	1	A → G in CAA69591. Ref.4
	Sequence conflict	185	1	K → T in CAA69591. Ref.4
	Sequence conflict	189	1	H → Y in CAA69591. Ref.4
	Sequence conflict	203	1	A → V in CAA69591. Ref.4
	Sequence conflict	418	1	K → N in CAA69591. Ref.4
	Sequence conflict	490	1	S → N in CAA69591. Ref.4
	Sequence conflict	776	1	Y → S in AAN77183. Ref.1
	Sequence conflict	778	1	R → C in AAN77183. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8IWX8 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 0C5D56F4DE4C5B9B	FASTA	916	103,702
	10 20 30 40 50 60 MEMPLPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL 70 80 90 100 110 120 ALEQQQLICK QQTPELEPAA TMPPLPQPPL APAAPIPPAQ GAPSMDELIQ QSQWNLQQQE 130 140 150 160 170 180 QHLLALRQEQ VTAAVAHAVE QQMQKLLEET QLDMNEFDNL LQPIIDTCTK DAISAGKNWM 190 200 210 220 230 240 FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV 250 260 270 280 290 300 VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS 310 320 330 340 350 360 SVVQPVQLAF QQQIQTLKTQ HEEFVTSLAQ QQQQQQQQQQ QLQMPQMEAE VKATPPPPAP 370 380 390 400 410 420 PPAPAPAPAI PPTTQPDDSK PPIQMPGSSE YEAPGGVQDP AAAGPRGPGP HDQIPPNKPP 430 440 450 460 470 480 WFDQPHPVAP WGQQQPPEQP PYPHHQGGPP HCPPWNNSHE GMWGEQRGDP GWNGQRDAPW 490 500 510 520 530 540 NNQPDAAWNS QFEGPWNSQH EQPPWGGGQR EPPFRMQRPP HFRGPFPPHQ QHPQFNQPPH 550 560 570 580 590 600 PHNFNRFPPR FMQDDFPPRH PFERPPYPHR FDYPQGDFPA EMGPPHHHPG HRMPHPGINE 610 620 630 640 650 660 HPPWAGPQHP DFGPPPHGFN GQPPHMRRQG PPHINHDDPS LVPNVPYFDL PAGLMAPLVK 670 680 690 700 710 720 LEDHEYKPLD PKDIRLPPPM PPSERLLAAV EAFYSPPSHD RPRNSEGWEQ NGLYEFFRAK 730 740 750 760 770 780 MRARRRKGQE KRNSGPSRSR SRSKSRGRSS SRSNSRSSKS SGSYSRSRSR SCSRSYSRSR 790 800 810 820 830 840 SRSRSRSRSS RSRSRSQSRS RSKSYSPGRR RRSRSRSPTP PSSAGLGSNS APPIPDSRLG 850 860 870 880 890 900 EENKGHQMLV KMGWSGSGGL GAKEQGIQDP IKGGDVRDKW DQYKGVGVAL DDPYENYRRN 910 KSYSFIARMK ARDECK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 15057824] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[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: 8896557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-607. Tissue: Lymphoblast.
[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: 10794731] [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: 8010949] [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: 12656674] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817; THR-819; SER-822; SER-823; SER-828; SER-830 AND SER-904, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815; SER-817; THR-819 AND SER-822, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815 AND SER-817, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-879 AND LYS-901, MASS SPECTROMETRY.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00333010.
RefSeq	NP_006378.3. NM_006387.5.
UniGene	Hs.728764.
3D structure databases
HSSP	HSSP built from PDB template 1UG0 based on UniProtKB Q8CH02.
ProteinModelPortal	Q8IWX8.
SMR	Q8IWX8. Positions 5-67.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IWX8. 2 interactions.
MINT	MINT-1637299.
STRING	Q8IWX8.
PTM databases
PhosphoSite	Q8IWX8.
Polymorphism databases
DMDM	296439404.
Proteomic databases
PRIDE	Q8IWX8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000198939; ENSP00000198939; ENSG00000085872.
GeneID	10523.
KEGG	hsa:10523.
UCSC	uc002nei.1. human. uc002nej.2. human.
Organism-specific databases
CTD	10523.
GeneCards	GC19M016629.
HGNC	HGNC:16930. CHERP.
neXtProt	NX_Q8IWX8.
PharmGKB	PA26459.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00600000084415.
HOGENOM	HBG445457.
HOVERGEN	HBG052716.
InParanoid	Q8IWX8.
OMA	HRFDYPQ.
OrthoDB	EOG4BCDMG.
PhylomeDB	Q8IWX8.
Gene expression databases
ArrayExpress	Q8IWX8.
Bgee	Q8IWX8.
CleanEx	HS_CHERP.
Genevestigator	Q8IWX8.
Family and domain databases
InterPro	IPR006903. DUF618. IPR008942. ENTH_VHS. IPR000467. G_patch. IPR006569. RNA_polymerase_II_lsu_CTD. IPR000061. Surp. [Graphical view]
Gene3D	G3DSA:1.25.40.90. ENTH_VHS. 1 hit.
KO	K12841.
Pfam	PF04818. DUF618. 1 hit. PF01585. G-patch. 1 hit. PF01805. Surp. 1 hit. [Graphical view]
SMART	SM00443. G_patch. 1 hit. SM00582. RPR. 1 hit. SM00648. SWAP. 1 hit. [Graphical view]
SUPFAM	SSF48464. ENTH_VHS. 1 hit.
PROSITE	PS51391. CID. 1 hit. PS50174. G_PATCH. 1 hit. PS50128. SURP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	39918.

Entry information

Entry name

CHERP_HUMAN

Accession

Primary (citable) accession number: Q8IWX8
Secondary accession number(s): O00302 , Q4G0Y5, Q8WU30, Q99492

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.