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P14410 (SUIS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sucrase-isomaltase, intestinal

Cleaved into the following 2 chains:

  1. Sucrase
    EC=3.2.1.48
  2. Isomaltase
    EC=3.2.1.10
Gene names
Name:SI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1827 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

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.

Subunit structure

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

Subcellular location

Apical cell membrane; Single-pass type II membrane protein. Note: Brush border.

Tissue specificity

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. Ref.5

Post-translational modification

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

Sulfated By similarity.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

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.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Contains 2 P-type (trefoil) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 18271826Sucrase-isomaltase, intestinal
PRO_0000018551
Chain2 – 10071006Isomaltase
PRO_0000018552
Chain1008 – 1827820Sucrase
PRO_0000018553

Regions

Topological domain2 – 1211Cytoplasmic
Transmembrane13 – 3220Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 18271795Lumenal
Domain61 – 11050P-type 1
Domain932 – 97847P-type 2
Region110 – 1007898Isomaltase
Region1008 – 1827820Sucrase
Compositional bias43 – 6018Ser/Thr-rich

Sites

Active site5051Nucleophile; for isomaltase activity Ref.7
Active site6041For isomaltase activity Ref.7
Active site13941Nucleophile; for sucrase activity Ref.7
Active site13971For sucrase activity By similarity
Active site15001Proton donor; for isomaltase activity By similarity
Binding site2641Substrate
Binding site3881Substrate
Binding site5881Substrate
Binding site6621Substrate

Amino acid modifications

Modified residue71Phosphoserine; by PKA Ref.6
Modified residue2371Sulfotyrosine Potential
Modified residue2391Sulfotyrosine Potential
Modified residue3911Sulfotyrosine Potential
Modified residue4001Sulfotyrosine Potential
Modified residue6671Sulfotyrosine Potential
Modified residue7631Sulfotyrosine Potential
Modified residue7651Sulfotyrosine Potential
Glycosylation991N-linked (GlcNAc...) Ref.7
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Ref.7
Glycosylation8231N-linked (GlcNAc...) Potential
Glycosylation8551N-linked (GlcNAc...) Ref.7
Glycosylation9041N-linked (GlcNAc...) Ref.7
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation12351N-linked (GlcNAc...) Potential
Glycosylation13031N-linked (GlcNAc...) Potential
Glycosylation13401N-linked (GlcNAc...) Potential
Glycosylation13541N-linked (GlcNAc...) Potential
Glycosylation14031N-linked (GlcNAc...) Potential
Glycosylation15351N-linked (GlcNAc...) Potential
Glycosylation15721N-linked (GlcNAc...) Potential
Glycosylation16751N-linked (GlcNAc...) Potential
Glycosylation17481N-linked (GlcNAc...) Potential
Glycosylation17631N-linked (GlcNAc...) Potential
Glycosylation18151N-linked (GlcNAc...) Potential
Disulfide bond63 ↔ 94 Ref.7
Disulfide bond77 ↔ 93 Ref.7
Disulfide bond88 ↔ 106 Ref.7
Disulfide bond520 ↔ 545 Ref.7
Disulfide bond635 ↔ 646 Ref.7

Natural variations

Natural variant151V → F. Ref.3 Ref.5 Ref.11 Ref.12
Corresponds to variant rs9290264 [ dbSNP | Ensembl ].
VAR_025367
Natural variant1171Q → R in CSID; missorting of the enzyme to the basolateral membrane. Ref.10
VAR_025368
Natural variant2311T → A. Ref.1 Ref.3 Ref.4 Ref.11 Ref.12
Corresponds to variant rs9283633 [ dbSNP | Ensembl ].
VAR_025369
Natural variant3411L → P in CSID; causes loss of anchored SI from the membrane. Ref.9
VAR_025370
Natural variant5771V → G in CSID. Ref.12
Corresponds to variant rs121912615 [ dbSNP | Ensembl ].
VAR_025371
Natural variant5941S → P in CSID. Ref.12
VAR_025372
Natural variant6201L → P in CSID; SI accumulates predominantly in the ER. Ref.11
VAR_025373
Natural variant6941T → P in CSID. Ref.12
VAR_025374
Natural variant10731G → D in CSID. Ref.12
VAR_025375
Natural variant10981Q → P in CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi. Ref.8
VAR_007854
Natural variant12291C → Y in CSID. Ref.12
VAR_025376
Natural variant13671R → G in CSID. Ref.12
VAR_025377
Natural variant15231M → I. Ref.1 Ref.3 Ref.12
Corresponds to variant rs4855271 [ dbSNP | Ensembl ].
VAR_025378
Natural variant17451F → C in CSID. Ref.12
Corresponds to variant rs79717168 [ dbSNP | Ensembl ].
VAR_025379
Natural variant18021T → S.
Corresponds to variant rs9917722 [ dbSNP | Ensembl ].
VAR_034522

Experimental info

Sequence conflict3001N → D in AAI16453. Ref.3
Sequence conflict4601S → I in AAI15035. Ref.3
Sequence conflict4751P → S in AAI15035. Ref.3
Sequence conflict5481A → V in AAI16453. Ref.3
Sequence conflict5841F → L in AAI15035. Ref.3
Sequence conflict5881R → C in AAI15035. Ref.3
Sequence conflict6331D → A in AAI15035. Ref.3
Sequence conflict6871Q → R in AAI16453. Ref.3
Sequence conflict8841T → A in AAI15035. Ref.3
Sequence conflict10161S → E AA sequence Ref.5
Sequence conflict10221V → T AA sequence Ref.5
Sequence conflict11551A → V in AAI15035. Ref.3
Sequence conflict12031E → Q in CAA45140. Ref.1
Sequence conflict17821V → I in AAI15035. Ref.3
Sequence conflict18251N → S in AAI16453. Ref.3

Secondary structure

........................................................................................................................................................................ 1827
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14410 [UniParc].

Last modified January 11, 2011. Version 6.
Checksum: DCB93F068AEEF83E

FASTA1,827209,453
        10         20         30         40         50         60 
MARKKFSGLE ISLIVLFVIV TIIAIALIVV LATKTPAVDE ISDSTSTPAT TRVTTNPSDS 

        70         80         90        100        110        120 
GKCPNVLNDP VNVRINCIPE QFPTEGICAQ RGCCWRPWND SLIPWCFFVD NHGYNVQDMT 

       130        140        150        160        170        180 
TTSIGVEAKL NRIPSPTLFG NDINSVLFTT QNQTPNRFRF KITDPNNRRY EVPHQYVKEF 

       190        200        210        220        230        240 
TGPTVSDTLY DVKVAQNPFS IQVIRKSNGK TLFDTSIGPL VYSDQYLQIS TRLPSDYIYG 

       250        260        270        280        290        300 
IGEQVHKRFR HDLSWKTWPI FTRDQLPGDN NNNLYGHQTF FMCIEDTSGK SFGVFLMNSN 

       310        320        330        340        350        360 
AMEIFIQPTP IVTYRVTGGI LDFYILLGDT PEQVVQQYQQ LVGLPAMPAY WNLGFQLSRW 

       370        380        390        400        410        420 
NYKSLDVVKE VVRRNREAGI PFDTQVTDID YMEDKKDFTY DQVAFNGLPQ FVQDLHDHGQ 

       430        440        450        460        470        480 
KYVIILDPAI SIGRRANGTT YATYERGNTQ HVWINESDGS TPIIGEVWPG LTVYPDFTNP 

       490        500        510        520        530        540 
NCIDWWANEC SIFHQEVQYD GLWIDMNEVS SFIQGSTKGC NVNKLNYPPF TPDILDKLMY 

       550        560        570        580        590        600 
SKTICMDAVQ NWGKQYDVHS LYGYSMAIAT EQAVQKVFPN KRSFILTRST FAGSGRHAAH 

       610        620        630        640        650        660 
WLGDNTASWE QMEWSITGML EFSLFGIPLV GADICGFVAE TTEELCRRWM QLGAFYPFSR 

       670        680        690        700        710        720 
NHNSDGYEHQ DPAFFGQNSL LVKSSRQYLT IRYTLLPFLY TLFYKAHVFG ETVARPVLHE 

       730        740        750        760        770        780 
FYEDTNSWIE DTEFLWGPAL LITPVLKQGA DTVSAYIPDA IWYDYESGAK RPWRKQRVDM 

       790        800        810        820        830        840 
YLPADKIGLH LRGGYIIPIQ EPDVTTTASR KNPLGLIVAL GENNTAKGDF FWDDGETKDT 

       850        860        870        880        890        900 
IQNGNYILYT FSVSNNTLDI VCTHSSYQEG TTLAFQTVKI LGLTDSVTEV RVAENNQPMN 

       910        920        930        940        950        960 
AHSNFTYDAS NQVLLIADLK LNLGRNFSVQ WNQIFSENER FNCYPDADLA TEQKCTQRGC 

       970        980        990       1000       1010       1020 
VWRTGSSLSK APECYFPRQD NSYSVNSARY SSMGITADLQ LNTANARIKL PSDPISTLRV 

      1030       1040       1050       1060       1070       1080 
EVKYHKNDML QFKIYDPQKK RYEVPVPLNI PTTPISTYED RLYDVEIKEN PFGIQIRRRS 

      1090       1100       1110       1120       1130       1140 
SGRVIWDSWL PGFAFNDQFI QISTRLPSEY IYGFGEVEHT AFKRDLNWNT WGMFTRDQPP 

      1150       1160       1170       1180       1190       1200 
GYKLNSYGFH PYYMALEEEG NAHGVFLLNS NAMDVTFQPT PALTYRTVGG ILDFYMFLGP 

      1210       1220       1230       1240       1250       1260 
TPEVATKQYH EVIGHPVMPA YWALGFQLCR YGYANTSEVR ELYDAMVAAN IPYDVQYTDI 

      1270       1280       1290       1300       1310       1320 
DYMERQLDFT IGEAFQDLPQ FVDKIRGEGM RYIIILDPAI SGNETKTYPA FERGQQNDVF 

      1330       1340       1350       1360       1370       1380 
VKWPNTNDIC WAKVWPDLPN ITIDKTLTED EAVNASRAHV AFPDFFRTST AEWWAREIVD 

      1390       1400       1410       1420       1430       1440 
FYNEKMKFDG LWIDMNEPSS FVNGTTTNQC RNDELNYPPY FPELTKRTDG LHFRTICMEA 

      1450       1460       1470       1480       1490       1500 
EQILSDGTSV LHYDVHNLYG WSQMKPTHDA LQKTTGKRGI VISRSTYPTS GRWGGHWLGD 

      1510       1520       1530       1540       1550       1560 
NYARWDNMDK SIIGMMEFSL FGMSYTGADI CGFFNNSEYH LCTRWMQLGA FYPYSRNHNI 

      1570       1580       1590       1600       1610       1620 
ANTRRQDPAS WNETFAEMSR NILNIRYTLL PYFYTQMHEI HANGGTVIRP LLHEFFDEKP 

      1630       1640       1650       1660       1670       1680 
TWDIFKQFLW GPAFMVTPVL EPYVQTVNAY VPNARWFDYH TGKDIGVRGQ FQTFNASYDT 

      1690       1700       1710       1720       1730       1740 
INLHVRGGHI LPCQEPAQNT FYSRQKHMKL IVAADDNQMA QGSLFWDDGE SIDTYERDLY 

      1750       1760       1770       1780       1790       1800 
LSVQFNLNQT TLTSTILKRG YINKSETRLG SLHVWGKGTT PVNAVTLTYN GNKNSLPFNE 

      1810       1820 
DTTNMILRID LTTHNVTLEE PIEINWS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRUUHU. S36082.
RefSeqNP_001032.2. NM_001041.3.
UniGeneHs.429596.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LPOX-ray3.20A/B/C/D62-931[»]
3LPPX-ray2.15A/B/C/D62-931[»]
ProteinModelPortalP14410.
SMRP14410. Positions 62-931, 937-1818.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4998644.
STRING9606.ENSP00000264382.

Chemistry

BindingDBP14410.
ChEMBLCHEMBL2748.
DrugBankDB00284. Acarbose.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSiteP14410.

Polymorphism databases

DMDM317373594.

Proteomic databases

PaxDbP14410.
PRIDEP14410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264382; ENSP00000264382; ENSG00000090402.
GeneID6476.
KEGGhsa:6476.
UCSCuc003fei.3. human.

Organism-specific databases

CTD6476.
GeneCardsGC03M164696.
H-InvDBHIX0030867.
HGNCHGNC:10856. SI.
HPAHPA011897.
MIM222900. phenotype.
609845. gene.
neXtProtNX_P14410.
Orphanet306446. 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.
PharmGKBPA35758.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000067936.
HOVERGENHBG080721.
InParanoidP14410.
KOK01203.
OMAKYHKNDM.
OrthoDBEOG7FJGZS.
PhylomeDBP14410.
TreeFamTF314577.

Enzyme and pathway databases

BioCycMetaCyc:HS01688-MONOMER.
BRENDA3.2.1.10. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP14410.
BgeeP14410.
CleanExHS_SI.
GenevestigatorP14410.

Family and domain databases

Gene3D4.10.110.10. 2 hits.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PfamPF01055. Glyco_hydro_31. 2 hits.
PF00088. Trefoil. 2 hits.
[Graphical view]
SMARTSM00018. PD. 2 hits.
[Graphical view]
SUPFAMSSF51445. SSF51445. 4 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEPS00129. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP14410.
GenomeRNAi6476.
NextBio25157.
PROP14410.
SOURCESearch...

Entry information

Entry nameSUIS_HUMAN
AccessionPrimary (citable) accession number: P14410
Secondary accession number(s): A2RUC3, Q1JQ80, Q1RMC2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 151 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries