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Protein

Sucrase-isomaltase, intestinal

Gene

SI

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

Functioni

Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.1 Publication

Catalytic activityi

Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei264Substrate1
Binding sitei388Substrate1
Active sitei505Nucleophile; for isomaltase activityPROSITE-ProRule annotation1 Publication1
Binding sitei588Substrate1
Active sitei604For isomaltase activity1 Publication1
Binding sitei662Substrate1
Active sitei1394Nucleophile; for sucrase activityPROSITE-ProRule annotation1 Publication1
Active sitei1397For sucrase activityBy similarity1
Active sitei1500Proton donor; for isomaltase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS01688-MONOMER.
ZFISH:HS01688-MONOMER.
BRENDAi3.2.1.10. 2681.
3.2.1.48. 2681.
ReactomeiR-HSA-189085. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrase-isomaltase, intestinal
Cleaved into the following 2 chains:
Gene namesi
Name:SI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10856. SI.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 12CytoplasmicAdd BLAST11
Transmembranei13 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini33 – 1827LumenalAdd BLAST1795

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • brush border Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: ProtInc
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital sucrase-isomaltase deficiency (CSID)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive intestinal disorder that is clinically characterized by fermentative diarrhea, abdominal pain, and cramps upon ingestion of sugar. The symptoms are the consequence of absent or drastically reduced enzymatic activities of sucrase and isomaltase. The prevalence of CSID is 0.02 % in individuals of European descent and appears to be much higher in Greenland, Alaskan, and Canadian native people. CSID arises due to post-translational perturbations in the intracellular transport, polarized sorting, aberrant processing, and defective function of SI.
See also OMIM:222900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025368117Q → R in CSID; missorting of the enzyme to the basolateral membrane. 1 PublicationCorresponds to variant rs121912612dbSNPEnsembl.1
Natural variantiVAR_025370341L → P in CSID; causes loss of anchored SI from the membrane. 1 PublicationCorresponds to variant rs267607049dbSNPEnsembl.1
Natural variantiVAR_025371577V → G in CSID. 1 PublicationCorresponds to variant rs121912615dbSNPEnsembl.1
Natural variantiVAR_025372594S → P in CSID. 1 PublicationCorresponds to variant rs765433197dbSNPEnsembl.1
Natural variantiVAR_025373620L → P in CSID; SI accumulates predominantly in the ER. 1 PublicationCorresponds to variant rs121912613dbSNPEnsembl.1
Natural variantiVAR_025374694T → P in CSID. 1 Publication1
Natural variantiVAR_0253751073G → D in CSID. 1 PublicationCorresponds to variant rs121912616dbSNPEnsembl.1
Natural variantiVAR_0078541098Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. 1 PublicationCorresponds to variant rs121912611dbSNPEnsembl.1
Natural variantiVAR_0253761229C → Y in CSID. 1 PublicationCorresponds to variant rs121912614dbSNPEnsembl.1
Natural variantiVAR_0253771367R → G in CSID. 1 PublicationCorresponds to variant rs143388292dbSNPEnsembl.1
Natural variantiVAR_0253791745F → C in CSID. 1 PublicationCorresponds to variant rs79717168dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi6476.
MalaCardsiSI.
MIMi222900. phenotype.
OpenTargetsiENSG00000090402.
Orphaneti306446. Congenital sucrase-isomaltase deficiency with minimal starch tolerance.
306474. Congenital sucrase-isomaltase deficiency with starch and lactose intolerance.
306436. Congenital sucrase-isomaltase deficiency with starch intolerance.
306462. Congenital sucrase-isomaltase deficiency without starch intolerance.
306486. Congenital sucrase-isomaltase deficiency without sucrose intolerance.
PharmGKBiPA35758.

Chemistry databases

ChEMBLiCHEMBL2748.
DrugBankiDB00284. Acarbose.
DB00747. Scopolamine.

Polymorphism and mutation databases

BioMutaiSI.
DMDMi317373594.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000185512 – 1827Sucrase-isomaltase, intestinalAdd BLAST1826
ChainiPRO_00000185522 – 1007IsomaltaseAdd BLAST1006
ChainiPRO_00000185531008 – 1827SucraseAdd BLAST820

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Phosphoserine; by PKA1 Publication1
Disulfide bondi63 ↔ 94PROSITE-ProRule annotation1 Publication
Disulfide bondi77 ↔ 93PROSITE-ProRule annotation1 Publication
Disulfide bondi88 ↔ 106PROSITE-ProRule annotation1 Publication
Glycosylationi99N-linked (GlcNAc...)1 Publication1
Modified residuei237SulfotyrosineSequence analysis1
Modified residuei239SulfotyrosineSequence analysis1
Modified residuei391SulfotyrosineSequence analysis1
Modified residuei400SulfotyrosineSequence analysis1
Glycosylationi437N-linked (GlcNAc...)Sequence analysis1
Glycosylationi455N-linked (GlcNAc...)1 Publication1
Disulfide bondi520 ↔ 545PROSITE-ProRule annotation1 Publication
Disulfide bondi635 ↔ 646PROSITE-ProRule annotation1 Publication
Modified residuei667SulfotyrosineSequence analysis1
Modified residuei763SulfotyrosineSequence analysis1
Modified residuei765SulfotyrosineSequence analysis1
Glycosylationi823N-linked (GlcNAc...)Sequence analysis1
Glycosylationi855N-linked (GlcNAc...)1 Publication1
Glycosylationi904N-linked (GlcNAc...)1 Publication1
Glycosylationi926N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1235N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1303N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1403N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1535N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1572N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1675N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1748N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1763N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1815N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.
Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP14410.
PaxDbiP14410.
PeptideAtlasiP14410.
PRIDEiP14410.

PTM databases

iPTMnetiP14410.
PhosphoSitePlusiP14410.

Expressioni

Tissue specificityi

Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon.1 Publication

Gene expression databases

BgeeiENSG00000090402.
CleanExiHS_SI.
ExpressionAtlasiP14410. baseline and differential.
GenevisibleiP14410. HS.

Organism-specific databases

HPAiHPA011897.

Interactioni

Subunit structurei

The resulting sucrase and isomaltase subunits stay associated with one another in a complex by non-covalent linkages.1 Publication

Protein-protein interaction databases

MINTiMINT-4998644.
STRINGi9606.ENSP00000264382.

Chemistry databases

BindingDBiP14410.

Structurei

Secondary structure

11827
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi65 – 68Combined sources4
Helixi71 – 73Combined sources3
Beta strandi75 – 77Combined sources3
Helixi85 – 91Combined sources7
Beta strandi99 – 103Combined sources5
Beta strandi105 – 107Combined sources3
Beta strandi114 – 121Combined sources8
Beta strandi123 – 132Combined sources10
Beta strandi138 – 140Combined sources3
Beta strandi144 – 154Combined sources11
Beta strandi157 – 163Combined sources7
Beta strandi175 – 177Combined sources3
Beta strandi189 – 195Combined sources7
Turni196 – 199Combined sources4
Beta strandi200 – 205Combined sources6
Turni206 – 209Combined sources4
Beta strandi210 – 214Combined sources5
Helixi215 – 217Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi226 – 232Combined sources7
Beta strandi234 – 236Combined sources3
Beta strandi238 – 244Combined sources7
Beta strandi247 – 250Combined sources4
Beta strandi254 – 261Combined sources8
Beta strandi278 – 284Combined sources7
Beta strandi291 – 296Combined sources6
Beta strandi302 – 307Combined sources6
Turni308 – 310Combined sources3
Beta strandi311 – 319Combined sources9
Beta strandi321 – 330Combined sources10
Helixi331 – 342Combined sources12
Helixi350 – 353Combined sources4
Helixi365 – 377Combined sources13
Beta strandi384 – 387Combined sources4
Helixi389 – 391Combined sources3
Helixi393 – 395Combined sources3
Turni402 – 407Combined sources6
Helixi408 – 417Combined sources10
Beta strandi421 – 426Combined sources6
Helixi442 – 450Combined sources9
Beta strandi459 – 462Combined sources4
Beta strandi465 – 467Combined sources3
Beta strandi470 – 473Combined sources4
Helixi480 – 496Combined sources17
Beta strandi500 – 504Combined sources5
Turni507 – 509Combined sources3
Beta strandi512 – 515Combined sources4
Turni524 – 526Combined sources3
Helixi535 – 537Combined sources3
Turni539 – 542Combined sources4
Helixi555 – 558Combined sources4
Helixi559 – 561Combined sources3
Helixi562 – 577Combined sources16
Beta strandi585 – 588Combined sources4
Helixi594 – 596Combined sources3
Beta strandi599 – 601Combined sources3
Beta strandi606 – 608Combined sources3
Helixi609 – 624Combined sources16
Beta strandi629 – 631Combined sources3
Beta strandi637 – 639Combined sources3
Helixi643 – 653Combined sources11
Beta strandi656 – 658Combined sources3
Helixi672 – 675Combined sources4
Helixi680 – 694Combined sources15
Helixi696 – 709Combined sources14
Beta strandi713 – 715Combined sources3
Helixi718 – 721Combined sources4
Helixi725 – 729Combined sources5
Beta strandi732 – 736Combined sources5
Turni737 – 739Combined sources3
Beta strandi740 – 743Combined sources4
Beta strandi751 – 757Combined sources7
Beta strandi762 – 764Combined sources3
Turni765 – 767Combined sources3
Beta strandi775 – 781Combined sources7
Beta strandi788 – 792Combined sources5
Beta strandi795 – 800Combined sources6
Helixi806 – 809Combined sources4
Beta strandi814 – 819Combined sources6
Beta strandi824 – 832Combined sources9
Beta strandi835 – 837Combined sources3
Helixi840 – 843Combined sources4
Beta strandi846 – 854Combined sources9
Beta strandi857 – 865Combined sources9
Helixi868 – 872Combined sources5
Beta strandi874 – 882Combined sources9
Beta strandi890 – 894Combined sources5
Beta strandi900 – 902Combined sources3
Beta strandi905 – 908Combined sources4
Turni909 – 912Combined sources4
Beta strandi913 – 916Combined sources4
Beta strandi927 – 930Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LPOX-ray3.20A/B/C/D62-931[»]
3LPPX-ray2.15A/B/C/D62-931[»]
ProteinModelPortaliP14410.
SMRiP14410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 110P-type 1PROSITE-ProRule annotationAdd BLAST50
Domaini932 – 978P-type 2PROSITE-ProRule annotationAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 1007IsomaltaseAdd BLAST898
Regioni1008 – 1827SucraseAdd BLAST820

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi43 – 60Ser/Thr-richAdd BLAST18

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated
Contains 2 P-type (trefoil) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1065. Eukaryota.
COG1501. LUCA.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiP14410.
KOiK01203.
OMAiDQLPGDN.
OrthoDBiEOG091G01E3.
PhylomeDBiP14410.
TreeFamiTF314577.

Family and domain databases

CDDicd00111. Trefoil. 2 hits.
Gene3Di4.10.110.10. 2 hits.
InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
IPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF16863. NtCtMGAM_N. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 4 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14410-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKKFSGLE ISLIVLFVIV TIIAIALIVV LATKTPAVDE ISDSTSTPAT
60 70 80 90 100
TRVTTNPSDS GKCPNVLNDP VNVRINCIPE QFPTEGICAQ RGCCWRPWND
110 120 130 140 150
SLIPWCFFVD NHGYNVQDMT TTSIGVEAKL NRIPSPTLFG NDINSVLFTT
160 170 180 190 200
QNQTPNRFRF KITDPNNRRY EVPHQYVKEF TGPTVSDTLY DVKVAQNPFS
210 220 230 240 250
IQVIRKSNGK TLFDTSIGPL VYSDQYLQIS TRLPSDYIYG IGEQVHKRFR
260 270 280 290 300
HDLSWKTWPI FTRDQLPGDN NNNLYGHQTF FMCIEDTSGK SFGVFLMNSN
310 320 330 340 350
AMEIFIQPTP IVTYRVTGGI LDFYILLGDT PEQVVQQYQQ LVGLPAMPAY
360 370 380 390 400
WNLGFQLSRW NYKSLDVVKE VVRRNREAGI PFDTQVTDID YMEDKKDFTY
410 420 430 440 450
DQVAFNGLPQ FVQDLHDHGQ KYVIILDPAI SIGRRANGTT YATYERGNTQ
460 470 480 490 500
HVWINESDGS TPIIGEVWPG LTVYPDFTNP NCIDWWANEC SIFHQEVQYD
510 520 530 540 550
GLWIDMNEVS SFIQGSTKGC NVNKLNYPPF TPDILDKLMY SKTICMDAVQ
560 570 580 590 600
NWGKQYDVHS LYGYSMAIAT EQAVQKVFPN KRSFILTRST FAGSGRHAAH
610 620 630 640 650
WLGDNTASWE QMEWSITGML EFSLFGIPLV GADICGFVAE TTEELCRRWM
660 670 680 690 700
QLGAFYPFSR NHNSDGYEHQ DPAFFGQNSL LVKSSRQYLT IRYTLLPFLY
710 720 730 740 750
TLFYKAHVFG ETVARPVLHE FYEDTNSWIE DTEFLWGPAL LITPVLKQGA
760 770 780 790 800
DTVSAYIPDA IWYDYESGAK RPWRKQRVDM YLPADKIGLH LRGGYIIPIQ
810 820 830 840 850
EPDVTTTASR KNPLGLIVAL GENNTAKGDF FWDDGETKDT IQNGNYILYT
860 870 880 890 900
FSVSNNTLDI VCTHSSYQEG TTLAFQTVKI LGLTDSVTEV RVAENNQPMN
910 920 930 940 950
AHSNFTYDAS NQVLLIADLK LNLGRNFSVQ WNQIFSENER FNCYPDADLA
960 970 980 990 1000
TEQKCTQRGC VWRTGSSLSK APECYFPRQD NSYSVNSARY SSMGITADLQ
1010 1020 1030 1040 1050
LNTANARIKL PSDPISTLRV EVKYHKNDML QFKIYDPQKK RYEVPVPLNI
1060 1070 1080 1090 1100
PTTPISTYED RLYDVEIKEN PFGIQIRRRS SGRVIWDSWL PGFAFNDQFI
1110 1120 1130 1140 1150
QISTRLPSEY IYGFGEVEHT AFKRDLNWNT WGMFTRDQPP GYKLNSYGFH
1160 1170 1180 1190 1200
PYYMALEEEG NAHGVFLLNS NAMDVTFQPT PALTYRTVGG ILDFYMFLGP
1210 1220 1230 1240 1250
TPEVATKQYH EVIGHPVMPA YWALGFQLCR YGYANTSEVR ELYDAMVAAN
1260 1270 1280 1290 1300
IPYDVQYTDI DYMERQLDFT IGEAFQDLPQ FVDKIRGEGM RYIIILDPAI
1310 1320 1330 1340 1350
SGNETKTYPA FERGQQNDVF VKWPNTNDIC WAKVWPDLPN ITIDKTLTED
1360 1370 1380 1390 1400
EAVNASRAHV AFPDFFRTST AEWWAREIVD FYNEKMKFDG LWIDMNEPSS
1410 1420 1430 1440 1450
FVNGTTTNQC RNDELNYPPY FPELTKRTDG LHFRTICMEA EQILSDGTSV
1460 1470 1480 1490 1500
LHYDVHNLYG WSQMKPTHDA LQKTTGKRGI VISRSTYPTS GRWGGHWLGD
1510 1520 1530 1540 1550
NYARWDNMDK SIIGMMEFSL FGMSYTGADI CGFFNNSEYH LCTRWMQLGA
1560 1570 1580 1590 1600
FYPYSRNHNI ANTRRQDPAS WNETFAEMSR NILNIRYTLL PYFYTQMHEI
1610 1620 1630 1640 1650
HANGGTVIRP LLHEFFDEKP TWDIFKQFLW GPAFMVTPVL EPYVQTVNAY
1660 1670 1680 1690 1700
VPNARWFDYH TGKDIGVRGQ FQTFNASYDT INLHVRGGHI LPCQEPAQNT
1710 1720 1730 1740 1750
FYSRQKHMKL IVAADDNQMA QGSLFWDDGE SIDTYERDLY LSVQFNLNQT
1760 1770 1780 1790 1800
TLTSTILKRG YINKSETRLG SLHVWGKGTT PVNAVTLTYN GNKNSLPFNE
1810 1820
DTTNMILRID LTTHNVTLEE PIEINWS
Length:1,827
Mass (Da):209,453
Last modified:January 11, 2011 - v6
Checksum:iDCB93F068AEEF83E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti300N → D in AAI16453 (PubMed:15489334).Curated1
Sequence conflicti460S → I in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti475P → S in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti548A → V in AAI16453 (PubMed:15489334).Curated1
Sequence conflicti584F → L in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti588R → C in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti633D → A in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti687Q → R in AAI16453 (PubMed:15489334).Curated1
Sequence conflicti884T → A in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti1016S → E AA sequence (PubMed:1677636).Curated1
Sequence conflicti1022V → T AA sequence (PubMed:1677636).Curated1
Sequence conflicti1155A → V in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti1203E → Q in CAA45140 (PubMed:1353958).Curated1
Sequence conflicti1782V → I in AAI15035 (PubMed:15489334).Curated1
Sequence conflicti1825N → S in AAI16453 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02536715V → F.4 PublicationsCorresponds to variant rs9290264dbSNPEnsembl.1
Natural variantiVAR_025368117Q → R in CSID; missorting of the enzyme to the basolateral membrane. 1 PublicationCorresponds to variant rs121912612dbSNPEnsembl.1
Natural variantiVAR_025369231T → A.5 PublicationsCorresponds to variant rs9283633dbSNPEnsembl.1
Natural variantiVAR_025370341L → P in CSID; causes loss of anchored SI from the membrane. 1 PublicationCorresponds to variant rs267607049dbSNPEnsembl.1
Natural variantiVAR_025371577V → G in CSID. 1 PublicationCorresponds to variant rs121912615dbSNPEnsembl.1
Natural variantiVAR_025372594S → P in CSID. 1 PublicationCorresponds to variant rs765433197dbSNPEnsembl.1
Natural variantiVAR_025373620L → P in CSID; SI accumulates predominantly in the ER. 1 PublicationCorresponds to variant rs121912613dbSNPEnsembl.1
Natural variantiVAR_025374694T → P in CSID. 1 Publication1
Natural variantiVAR_0253751073G → D in CSID. 1 PublicationCorresponds to variant rs121912616dbSNPEnsembl.1
Natural variantiVAR_0078541098Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. 1 PublicationCorresponds to variant rs121912611dbSNPEnsembl.1
Natural variantiVAR_0253761229C → Y in CSID. 1 PublicationCorresponds to variant rs121912614dbSNPEnsembl.1
Natural variantiVAR_0253771367R → G in CSID. 1 PublicationCorresponds to variant rs143388292dbSNPEnsembl.1
Natural variantiVAR_0253781523M → I.3 PublicationsCorresponds to variant rs4855271dbSNPEnsembl.1
Natural variantiVAR_0253791745F → C in CSID. 1 PublicationCorresponds to variant rs79717168dbSNPEnsembl.1
Natural variantiVAR_0345221802T → S.Corresponds to variant rs9917722dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63597 mRNA. Translation: CAA45140.1.
AC092695 Genomic DNA. No translation available.
AC140119 Genomic DNA. No translation available.
AC144561 Genomic DNA. No translation available.
BC115034 mRNA. Translation: AAI15035.1.
BC116452 mRNA. Translation: AAI16453.1.
BC132834 mRNA. Translation: AAI32835.1.
BC132860 mRNA. Translation: AAI32861.1.
M22616 mRNA. Translation: AAA60551.1.
CCDSiCCDS3196.1.
PIRiS36082. UUHU.
RefSeqiNP_001032.2. NM_001041.3.
UniGeneiHs.429596.

Genome annotation databases

EnsembliENST00000264382; ENSP00000264382; ENSG00000090402.
GeneIDi6476.
KEGGihsa:6476.
UCSCiuc003fei.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63597 mRNA. Translation: CAA45140.1.
AC092695 Genomic DNA. No translation available.
AC140119 Genomic DNA. No translation available.
AC144561 Genomic DNA. No translation available.
BC115034 mRNA. Translation: AAI15035.1.
BC116452 mRNA. Translation: AAI16453.1.
BC132834 mRNA. Translation: AAI32835.1.
BC132860 mRNA. Translation: AAI32861.1.
M22616 mRNA. Translation: AAA60551.1.
CCDSiCCDS3196.1.
PIRiS36082. UUHU.
RefSeqiNP_001032.2. NM_001041.3.
UniGeneiHs.429596.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LPOX-ray3.20A/B/C/D62-931[»]
3LPPX-ray2.15A/B/C/D62-931[»]
ProteinModelPortaliP14410.
SMRiP14410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4998644.
STRINGi9606.ENSP00000264382.

Chemistry databases

BindingDBiP14410.
ChEMBLiCHEMBL2748.
DrugBankiDB00284. Acarbose.
DB00747. Scopolamine.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

PTM databases

iPTMnetiP14410.
PhosphoSitePlusiP14410.

Polymorphism and mutation databases

BioMutaiSI.
DMDMi317373594.

Proteomic databases

MaxQBiP14410.
PaxDbiP14410.
PeptideAtlasiP14410.
PRIDEiP14410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264382; ENSP00000264382; ENSG00000090402.
GeneIDi6476.
KEGGihsa:6476.
UCSCiuc003fei.3. human.

Organism-specific databases

CTDi6476.
DisGeNETi6476.
GeneCardsiSI.
H-InvDBHIX0030867.
HGNCiHGNC:10856. SI.
HPAiHPA011897.
MalaCardsiSI.
MIMi222900. phenotype.
609845. gene.
neXtProtiNX_P14410.
OpenTargetsiENSG00000090402.
Orphaneti306446. Congenital sucrase-isomaltase deficiency with minimal starch tolerance.
306474. Congenital sucrase-isomaltase deficiency with starch and lactose intolerance.
306436. Congenital sucrase-isomaltase deficiency with starch intolerance.
306462. Congenital sucrase-isomaltase deficiency without starch intolerance.
306486. Congenital sucrase-isomaltase deficiency without sucrose intolerance.
PharmGKBiPA35758.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1065. Eukaryota.
COG1501. LUCA.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiP14410.
KOiK01203.
OMAiDQLPGDN.
OrthoDBiEOG091G01E3.
PhylomeDBiP14410.
TreeFamiTF314577.

Enzyme and pathway databases

BioCyciMetaCyc:HS01688-MONOMER.
ZFISH:HS01688-MONOMER.
BRENDAi3.2.1.10. 2681.
3.2.1.48. 2681.
ReactomeiR-HSA-189085. Digestion of dietary carbohydrate.

Miscellaneous databases

ChiTaRSiSI. human.
EvolutionaryTraceiP14410.
GenomeRNAii6476.
PROiP14410.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090402.
CleanExiHS_SI.
ExpressionAtlasiP14410. baseline and differential.
GenevisibleiP14410. HS.

Family and domain databases

CDDicd00111. Trefoil. 2 hits.
Gene3Di4.10.110.10. 2 hits.
InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
IPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 2 hits.
PF16863. NtCtMGAM_N. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTiSM00018. PD. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 4 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 2 hits.
PS00707. GLYCOSYL_HYDROL_F31_2. 2 hits.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUIS_HUMAN
AccessioniPrimary (citable) accession number: P14410
Secondary accession number(s): A2RUC3, Q1JQ80, Q1RMC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 176 of the entry and version 6 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

Miscellaneous

There is a high degree of homology between the isomaltase and sucrase portions (41% of amino acid identity) indicating that this protein is evolved by partial gene duplication.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.