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P14410

- SUIS_HUMAN

UniProt

P14410 - SUIS_HUMAN

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Protein

Sucrase-isomaltase, intestinal

Gene

SI

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei264 – 2641Substrate
Binding sitei388 – 3881Substrate
Active sitei505 – 5051Nucleophile; for isomaltase activity1 PublicationPROSITE-ProRule annotation
Binding sitei588 – 5881Substrate
Active sitei604 – 6041For isomaltase activity1 Publication
Binding sitei662 – 6621Substrate
Active sitei1394 – 13941Nucleophile; for sucrase activity1 PublicationPROSITE-ProRule annotation
Active sitei1397 – 13971For sucrase activityBy similarity
Active sitei1500 – 15001Proton donor; for isomaltase activityBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: Reactome
  2. carbohydrate binding Source: InterPro
  3. oligo-1,6-glucosidase activity Source: UniProtKB-EC
  4. sucrose alpha-glucosidase activity Source: Reactome

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. polysaccharide digestion Source: Reactome
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS01688-MONOMER.
BRENDAi3.2.1.10. 2681.
ReactomeiREACT_9472. 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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10856. SI.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1211CytoplasmicAdd
BLAST
Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 18271795LumenalAdd
BLAST

GO - Cellular componenti

  1. brush border Source: ProtInc
  2. extracellular vesicular exosome Source: UniProtKB
  3. Golgi apparatus Source: ProtInc
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital sucrase-isomaltase deficiency (CSID) [MIM:222900]: Autosomal 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.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171Q → R in CSID; missorting of the enzyme to the basolateral membrane. 1 Publication
VAR_025368
Natural varianti341 – 3411L → P in CSID; causes loss of anchored SI from the membrane. 1 Publication
VAR_025370
Natural varianti577 – 5771V → G in CSID. 1 Publication
Corresponds to variant rs121912615 [ dbSNP | Ensembl ].
VAR_025371
Natural varianti594 – 5941S → P in CSID. 1 Publication
VAR_025372
Natural varianti620 – 6201L → P in CSID; SI accumulates predominantly in the ER. 1 Publication
VAR_025373
Natural varianti694 – 6941T → P in CSID. 1 Publication
VAR_025374
Natural varianti1073 – 10731G → D in CSID. 1 Publication
VAR_025375
Natural varianti1098 – 10981Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. 1 Publication
VAR_007854
Natural varianti1229 – 12291C → Y in CSID. 1 Publication
VAR_025376
Natural varianti1367 – 13671R → G in CSID. 1 Publication
VAR_025377
Natural varianti1745 – 17451F → C in CSID. 1 Publication
Corresponds to variant rs79717168 [ dbSNP | Ensembl ].
VAR_025379

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi222900. phenotype.
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 18271826Sucrase-isomaltase, intestinalPRO_0000018551Add
BLAST
Chaini2 – 10071006IsomaltasePRO_0000018552Add
BLAST
Chaini1008 – 1827820SucrasePRO_0000018553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by PKA1 Publication
Disulfide bondi63 ↔ 941 PublicationPROSITE-ProRule annotation
Disulfide bondi77 ↔ 931 PublicationPROSITE-ProRule annotation
Disulfide bondi88 ↔ 1061 PublicationPROSITE-ProRule annotation
Glycosylationi99 – 991N-linked (GlcNAc...)1 Publication
Modified residuei237 – 2371SulfotyrosineSequence Analysis
Modified residuei239 – 2391SulfotyrosineSequence Analysis
Modified residuei391 – 3911SulfotyrosineSequence Analysis
Modified residuei400 – 4001SulfotyrosineSequence Analysis
Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi455 – 4551N-linked (GlcNAc...)1 Publication
Disulfide bondi520 ↔ 5451 PublicationPROSITE-ProRule annotation
Disulfide bondi635 ↔ 6461 PublicationPROSITE-ProRule annotation
Modified residuei667 – 6671SulfotyrosineSequence Analysis
Modified residuei763 – 7631SulfotyrosineSequence Analysis
Modified residuei765 – 7651SulfotyrosineSequence Analysis
Glycosylationi823 – 8231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi855 – 8551N-linked (GlcNAc...)1 Publication
Glycosylationi904 – 9041N-linked (GlcNAc...)1 Publication
Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1235 – 12351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1303 – 13031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1403 – 14031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1535 – 15351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1572 – 15721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1675 – 16751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1748 – 17481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1815 – 18151N-linked (GlcNAc...)Sequence Analysis

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.
PRIDEiP14410.

PTM databases

PhosphoSiteiP14410.

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

BgeeiP14410.
CleanExiHS_SI.
ExpressionAtlasiP14410. baseline and differential.
GenevestigatoriP14410.

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.

Structurei

Secondary structure

1
1827
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 684Combined sources
Helixi71 – 733Combined sources
Beta strandi75 – 773Combined sources
Helixi85 – 917Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi114 – 1218Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi144 – 15411Combined sources
Beta strandi157 – 1637Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi189 – 1957Combined sources
Turni196 – 1994Combined sources
Beta strandi200 – 2056Combined sources
Turni206 – 2094Combined sources
Beta strandi210 – 2145Combined sources
Helixi215 – 2173Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi226 – 2327Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi238 – 2447Combined sources
Beta strandi247 – 2504Combined sources
Beta strandi254 – 2618Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi302 – 3076Combined sources
Turni308 – 3103Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi321 – 33010Combined sources
Helixi331 – 34212Combined sources
Helixi350 – 3534Combined sources
Helixi365 – 37713Combined sources
Beta strandi384 – 3874Combined sources
Helixi389 – 3913Combined sources
Helixi393 – 3953Combined sources
Turni402 – 4076Combined sources
Helixi408 – 41710Combined sources
Beta strandi421 – 4266Combined sources
Helixi442 – 4509Combined sources
Beta strandi459 – 4624Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi470 – 4734Combined sources
Helixi480 – 49617Combined sources
Beta strandi500 – 5045Combined sources
Turni507 – 5093Combined sources
Beta strandi512 – 5154Combined sources
Turni524 – 5263Combined sources
Helixi535 – 5373Combined sources
Turni539 – 5424Combined sources
Helixi555 – 5584Combined sources
Helixi559 – 5613Combined sources
Helixi562 – 57716Combined sources
Beta strandi585 – 5884Combined sources
Helixi594 – 5963Combined sources
Beta strandi599 – 6013Combined sources
Beta strandi606 – 6083Combined sources
Helixi609 – 62416Combined sources
Beta strandi629 – 6313Combined sources
Beta strandi637 – 6393Combined sources
Helixi643 – 65311Combined sources
Beta strandi656 – 6583Combined sources
Helixi672 – 6754Combined sources
Helixi680 – 69415Combined sources
Helixi696 – 70914Combined sources
Beta strandi713 – 7153Combined sources
Helixi718 – 7214Combined sources
Helixi725 – 7295Combined sources
Beta strandi732 – 7365Combined sources
Turni737 – 7393Combined sources
Beta strandi740 – 7434Combined sources
Beta strandi751 – 7577Combined sources
Beta strandi762 – 7643Combined sources
Turni765 – 7673Combined sources
Beta strandi775 – 7817Combined sources
Beta strandi788 – 7925Combined sources
Beta strandi795 – 8006Combined sources
Helixi806 – 8094Combined sources
Beta strandi814 – 8196Combined sources
Beta strandi824 – 8329Combined sources
Beta strandi835 – 8373Combined sources
Helixi840 – 8434Combined sources
Beta strandi846 – 8549Combined sources
Beta strandi857 – 8659Combined sources
Helixi868 – 8725Combined sources
Beta strandi874 – 8829Combined sources
Beta strandi890 – 8945Combined sources
Beta strandi900 – 9023Combined sources
Beta strandi905 – 9084Combined sources
Turni909 – 9124Combined sources
Beta strandi913 – 9164Combined sources
Beta strandi927 – 9304Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LPOX-ray3.20A/B/C/D62-931[»]
3LPPX-ray2.15A/B/C/D62-931[»]
ProteinModelPortaliP14410.
SMRiP14410. Positions 62-931, 937-1818.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 11050P-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini932 – 97847P-type 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 1007898IsomaltaseAdd
BLAST
Regioni1008 – 1827820SucraseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 6018Ser/Thr-richAdd
BLAST

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

eggNOGiCOG1501.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000067936.
HOVERGENiHBG080721.
InParanoidiP14410.
KOiK01203.
OMAiKYHKNDM.
OrthoDBiEOG7FJGZS.
PhylomeDBiP14410.
TreeFamiTF314577.

Family and domain databases

Gene3Di4.10.110.10. 2 hits.
InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001N → D in AAI16453. (PubMed:15489334)Curated
Sequence conflicti460 – 4601S → I in AAI15035. (PubMed:15489334)Curated
Sequence conflicti475 – 4751P → S in AAI15035. (PubMed:15489334)Curated
Sequence conflicti548 – 5481A → V in AAI16453. (PubMed:15489334)Curated
Sequence conflicti584 – 5841F → L in AAI15035. (PubMed:15489334)Curated
Sequence conflicti588 – 5881R → C in AAI15035. (PubMed:15489334)Curated
Sequence conflicti633 – 6331D → A in AAI15035. (PubMed:15489334)Curated
Sequence conflicti687 – 6871Q → R in AAI16453. (PubMed:15489334)Curated
Sequence conflicti884 – 8841T → A in AAI15035. (PubMed:15489334)Curated
Sequence conflicti1016 – 10161S → E AA sequence (PubMed:1677636)Curated
Sequence conflicti1022 – 10221V → T AA sequence (PubMed:1677636)Curated
Sequence conflicti1155 – 11551A → V in AAI15035. (PubMed:15489334)Curated
Sequence conflicti1203 – 12031E → Q in CAA45140. (PubMed:1353958)Curated
Sequence conflicti1782 – 17821V → I in AAI15035. (PubMed:15489334)Curated
Sequence conflicti1825 – 18251N → S in AAI16453. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151V → F.4 Publications
Corresponds to variant rs9290264 [ dbSNP | Ensembl ].
VAR_025367
Natural varianti117 – 1171Q → R in CSID; missorting of the enzyme to the basolateral membrane. 1 Publication
VAR_025368
Natural varianti231 – 2311T → A.5 Publications
Corresponds to variant rs9283633 [ dbSNP | Ensembl ].
VAR_025369
Natural varianti341 – 3411L → P in CSID; causes loss of anchored SI from the membrane. 1 Publication
VAR_025370
Natural varianti577 – 5771V → G in CSID. 1 Publication
Corresponds to variant rs121912615 [ dbSNP | Ensembl ].
VAR_025371
Natural varianti594 – 5941S → P in CSID. 1 Publication
VAR_025372
Natural varianti620 – 6201L → P in CSID; SI accumulates predominantly in the ER. 1 Publication
VAR_025373
Natural varianti694 – 6941T → P in CSID. 1 Publication
VAR_025374
Natural varianti1073 – 10731G → D in CSID. 1 Publication
VAR_025375
Natural varianti1098 – 10981Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. 1 Publication
VAR_007854
Natural varianti1229 – 12291C → Y in CSID. 1 Publication
VAR_025376
Natural varianti1367 – 13671R → G in CSID. 1 Publication
VAR_025377
Natural varianti1523 – 15231M → I.3 Publications
Corresponds to variant rs4855271 [ dbSNP | Ensembl ].
VAR_025378
Natural varianti1745 – 17451F → C in CSID. 1 Publication
Corresponds to variant rs79717168 [ dbSNP | Ensembl ].
VAR_025379
Natural varianti1802 – 18021T → S.
Corresponds to variant rs9917722 [ dbSNP | Ensembl ].
VAR_034522

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.

Polymorphism databases

DMDMi317373594.

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 .
CCDSi CCDS3196.1.
PIRi S36082. UUHU.
RefSeqi NP_001032.2. NM_001041.3.
UniGenei Hs.429596.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LPO X-ray 3.20 A/B/C/D 62-931 [» ]
3LPP X-ray 2.15 A/B/C/D 62-931 [» ]
ProteinModelPortali P14410.
SMRi P14410. Positions 62-931, 937-1818.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4998644.
STRINGi 9606.ENSP00000264382.

Chemistry

BindingDBi P14410.
ChEMBLi CHEMBL2748.
DrugBanki DB00284. Acarbose.
DB00747. Scopolamine.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSitei P14410.

Polymorphism databases

DMDMi 317373594.

Proteomic databases

MaxQBi P14410.
PaxDbi P14410.
PRIDEi P14410.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264382 ; ENSP00000264382 ; ENSG00000090402 .
GeneIDi 6476.
KEGGi hsa:6476.
UCSCi uc003fei.3. human.

Organism-specific databases

CTDi 6476.
GeneCardsi GC03M164696.
H-InvDB HIX0030867.
HGNCi HGNC:10856. SI.
HPAi HPA011897.
MIMi 222900. phenotype.
609845. gene.
neXtProti NX_P14410.
Orphaneti 306446. 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.
PharmGKBi PA35758.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1501.
GeneTreei ENSGT00760000119229.
HOGENOMi HOG000067936.
HOVERGENi HBG080721.
InParanoidi P14410.
KOi K01203.
OMAi KYHKNDM.
OrthoDBi EOG7FJGZS.
PhylomeDBi P14410.
TreeFami TF314577.

Enzyme and pathway databases

BioCyci MetaCyc:HS01688-MONOMER.
BRENDAi 3.2.1.10. 2681.
Reactomei REACT_9472. Digestion of dietary carbohydrate.

Miscellaneous databases

ChiTaRSi SI. human.
EvolutionaryTracei P14410.
GenomeRNAii 6476.
NextBioi 25157.
PROi P14410.
SOURCEi Search...

Gene expression databases

Bgeei P14410.
CleanExi HS_SI.
ExpressionAtlasi P14410. baseline and differential.
Genevestigatori P14410.

Family and domain databases

Gene3Di 4.10.110.10. 2 hits.
InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view ]
Pfami PF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view ]
SMARTi SM00018. PD. 2 hits.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 4 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEi PS00129. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase."
    Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N., Edwards Y., Swallow D., Rousset M.
    Biochem. J. 285:915-923(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-231 AND ILE-1523.
    Tissue: Intestine.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [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], VARIANTS PHE-15; ALA-231 AND ILE-1523.
  4. "Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3."
    Green F., Edwards Y., Hauri H.-P., Povey S., Ho M.W., Pinto M., Swallow D.
    Gene 57:101-110(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-679, VARIANT ALA-231.
  5. "Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon."
    Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S.
    Gastroenterology 101:618-625(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20 AND 1008-1024, TISSUE SPECIFICITY, VARIANT PHE-15.
  6. "Phosphorylation of the N-terminal intracellular tail of sucrase-isomaltase by cAMP-dependent protein kinase."
    Keller P., Semenza G., Shaltiel S.
    Eur. J. Biochem. 233:963-968(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-7.
  7. "Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains."
    Sim L., Willemsma C., Mohan S., Naim H.Y., Pinto B.M., Rose D.R.
    J. Biol. Chem. 285:17763-17770(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 62-931 ALONE AND IN COMPLEX WITH INHIBITOR, GLYCOSYLATION AT ASN-99; ASN-455; ASN-855 AND ASN-904, FUNCTION, ACTIVE SITE, SUBSTRATE-BINDING SITES, DISULFIDE BONDS.
  8. "Congenital sucrase-isomaltase deficiency: identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment."
    Ouwendijk J., Moolenaar C.E.C., Peters W.J., Hollenberg C.P., Ginsel L.A., Fransen J.A.M., Naim H.Y.
    J. Clin. Invest. 97:633-641(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSID PRO-1098.
  9. "Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme."
    Jacob R., Zimmer K.P., Schmitz J., Naim H.Y.
    J. Clin. Invest. 106:281-287(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSID PRO-341, CHARACTERIZATION OF VARIANT CSID PRO-341.
  10. "Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder."
    Spodsberg N., Jacob R., Alfalah M., Zimmer K.P., Naim H.Y.
    J. Biol. Chem. 276:23506-23510(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSID ARG-117, CHARACTERIZATION OF VARIANT CSID ARG-117.
  11. "Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum."
    Ritz V., Alfalah M., Zimmer K.P., Schmitz J., Jacob R., Naim H.Y.
    Gastroenterology 125:1678-1685(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PHE-15 AND ALA-231, VARIANT CSID PRO-620.
  12. "Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption."
    Sander P., Alfalah M., Keiser M., Korponay-Szabo I., Kovacs J.B., Leeb T., Naim H.Y.
    Hum. Mutat. 27:119-119(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CSID GLY-577; PRO-594; PRO-694; ASP-1073; TYR-1229; GLY-1367 AND CYS-1745, VARIANTS PHE-15; ALA-231 AND ILE-1523.

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 26, 2014
This is version 158 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

External Data

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