Q5I7T1 (AG10B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
EC=2.4.1.256

Alternative name(s):
Alpha-1,2-glucosyltransferase ALG10-A
Alpha-2-glucosyltransferase ALG10-B
Asparagine-linked glycosylation protein 10 homolog B
Potassium channel regulator 1

Gene names

Name:	ALG10B
Synonyms:	KCR1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Putative alpha-1,2-glucosyltransferase, which adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc2Man9GlcNAc(2)-PP-Dol. When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2. Ref.1 Ref.6
Catalytic activity	Dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Glc-alpha-(1->2)-D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with KCNH1 and KCNH2 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Highly expressed in heart, placenta, liver, kidney and pancreas. Weakly expressed in lung, skeletal muscle and brain. Ref.1
Polymorphism	Genetic variations in ALG10B may reduce susceptibility to acquired long QT syndrome.
Sequence similarities	Belongs to the ALG10 glucosyltransferase family.
Caution	Ref.6 reports a Val-447 variant, however there is evidence that the right variant is Val-446.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transferase activity, transferring hexosyl groups 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 – 473	473	Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase		PRO_0000215448
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Helical; Potential
	Topological domain	28 – 64	37	Extracellular Potential
	Transmembrane	65 – 85	21	Helical; Potential
	Topological domain	86 – 97	12	Cytoplasmic Potential
	Transmembrane	98 – 118	21	Helical; Potential
	Topological domain	119 – 126	8	Extracellular Potential
	Transmembrane	127 – 147	21	Helical; Potential
	Topological domain	148 – 150	3	Cytoplasmic Potential
	Transmembrane	151 – 171	21	Helical; Potential
	Topological domain	172 – 175	4	Extracellular Potential
	Transmembrane	176 – 196	21	Helical; Potential
	Topological domain	197 – 256	60	Cytoplasmic Potential
	Transmembrane	257 – 277	21	Helical; Potential
	Topological domain	278 – 283	6	Extracellular Potential
	Transmembrane	284 – 304	21	Helical; Potential
	Topological domain	305 – 317	13	Cytoplasmic Potential
	Transmembrane	318 – 338	21	Helical; Potential
	Topological domain	339 – 365	27	Extracellular Potential
	Transmembrane	366 – 386	21	Helical; Potential
	Topological domain	387 – 392	6	Cytoplasmic Potential
	Transmembrane	393 – 413	21	Helical; Potential
	Topological domain	414 – 436	23	Extracellular Potential
	Transmembrane	437 – 457	21	Helical; Potential
	Topological domain	458 – 473	16	Cytoplasmic Potential
Natural variations
	Natural variant	84	1	A → G. Ref.1 Ref.4 Ref.5 Corresponds to variant rs6582584 [ dbSNP | Ensembl ].		VAR_048217
	Natural variant	383	1	S → N. Corresponds to variant rs57963306 [ dbSNP | Ensembl ].		VAR_061002
	Natural variant	446	1	I → V in some patients with drug-induced cardiac repolarization defects; exerts a greater protective effect, relative to wild-type, against drug blockage of KCNH2 potassium channel. Ref.6		VAR_023753

Sequences

	Sequence		Length	Mass (Da)
	Q5I7T1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 47D0CF7B6C84B8EC	FASTA	473	55,448
	10 20 30 40 50 60 MAQLEGYCFS AALSCTFLVS CLLFSAFSRA LREPYMDEIF HLPQAQRYCE GHFSLSQWDP 70 80 90 100 110 120 MITTLPGLYL VSVGVVKPAI WIFAWSEHVV CSIGMLRFVN LLFSVGNFYL LYLLFHKVQP 130 140 150 160 170 180 RNKAASSIQR VLSTLTLAVF PTLYFFNFLY YTEAGSMFFT LFAYLMCLYG NHKTSAFLGF 190 200 210 220 230 240 CGFMFRQTNI IWAVFCAGNV IAQKLTEAWK TELQKKEDRL PPIKGPFAEF RKILQFLLAY 250 260 270 280 290 300 SMSFKNLSML FCLTWPYILL GFLFCAFVVV NGGIVIGDRS SHEACLHFPQ LFYFFSFTLF 310 320 330 340 350 360 FSFPHLLSPS KIKTFLSLVW KHGILFLVVT LVSVFLVWKF TYAHKYLLAD NRHYTFYVWK 370 380 390 400 410 420 RVFQRYAILK YLLVPAYIFA GWSIADSLKS KPIFWNLMFF ICLFIVIVPQ KLLEFRYFIL 430 440 450 460 470 PYVIYRLNIT LPPTSRLVCE LSCYAIVNFI TFYIFLNKTF QWPNSQDIQR FMW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The IKr drug response is modulated by KCR1 in transfected cardiac and noncardiac cell lines." Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S., Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R. FASEB J. 17:2263-2265(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT GLY-84.
[2]	George A.L. Jr. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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], VARIANT GLY-84.
[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], VARIANT GLY-84.
[6]	"In vivo identification of genes that modify ether-a-go-go-related gene activity in Caenorhabditis elegans may also affect human cardiac arrhythmia." Petersen C.I., McFarland T.R., Stepanovic S.Z., Yang P., Reiner D.J., Hayashi K., George A.L. Jr., Roden D.M., Thomas J.H., Balser J.R. Proc. Natl. Acad. Sci. U.S.A. 101:11773-11778(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VAL-446, CHARACTERIZATION OF VARIANT VAL-446, POSSIBLE PROTECTIVE ROLE IN SUSCEPTIBILITY TO ACQUIRED LONG QT SYNDROME.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY845858 mRNA. Translation: AAW31756.1. AC117372 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW57795.1. BC137413 mRNA. Translation: AAI37414.1. BC137414 mRNA. Translation: AAI37415.1.
IPI	IPI00105827.
RefSeq	NP_001013642.1. NM_001013620.3.
UniGene	Hs.259305.
3D structure databases
ProteinModelPortal	Q5I7T1.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000310120.
PTM databases
PhosphoSite	Q5I7T1.
Polymorphism databases
DMDM	296434391.
Proteomic databases
PaxDb	Q5I7T1.
PRIDE	Q5I7T1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308742; ENSP00000310120; ENSG00000175548.
GeneID	144245.
KEGG	hsa:144245.
UCSC	uc001rln.4. human.
Organism-specific databases
CTD	144245.
GeneCards	GC12P038710.
HGNC	HGNC:31088. ALG10B.
HPA	HPA043329.
MIM	603313. gene.
neXtProt	NX_Q5I7T1.
PharmGKB	PA134936082.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236252.
HOGENOM	HOG000240902.
HOVERGEN	HBG053222.
InParanoid	Q5I7T1.
KO	K03850.
OMA	PFYLWRK.
OrthoDB	EOG4THVSZ.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q5I7T1.
Bgee	Q5I7T1.
CleanEx	HS_ALG10B.
Genevestigator	Q5I7T1.
GermOnline	ENSG00000175548. Homo sapiens.
Family and domain databases
InterPro	IPR016900. Alpha1_2_glucosyltferase_Alg10. IPR007006. Glycosyltransferase_ALG10. [Graphical view]
PANTHER	PTHR12989. PTHR12989. 1 hit.
Pfam	PF04922. DIE2_ALG10. 1 hit. [Graphical view]
PIRSF	PIRSF028810. Alpha1_2_glucosyltferase_Alg10. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	144245.
NextBio	84873.
SOURCE	Search...

Entry information

Entry name

AG10B_HUMAN

Accession

Primary (citable) accession number: Q5I7T1
Secondary accession number(s): B2RPF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	May 18, 2010
Last modified:	April 3, 2013
This is version 74 of the entry and version 2 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.