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Protein

Serine hydrolase-like protein

Gene

SERHL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Putative serine hydrolase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Sequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

ESTHERihuman-SERHL. AlphaBeta_hydrolase.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine hydrolase-like protein (EC:3.1.-.-)
Short name:
SHL
Gene namesi
Name:SERHL
Synonyms:SERHL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:14408. SERHL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi21362940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Serine hydrolase-like proteinPRO_0000097665Add
BLAST

Proteomic databases

PaxDbiQ9NQF3.
PRIDEiQ9NQF3.

Expressioni

Gene expression databases

CleanExiHS_SERHL.
HS_SERHL2.

Organism-specific databases

HPAiHPA047904.

Interactioni

Protein-protein interaction databases

IntActiQ9NQF3. 1 interaction.
STRINGi9606.ENSP00000331376.

Structurei

3D structure databases

ProteinModelPortaliQ9NQF3.
SMRiQ9NQF3. Positions 26-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiKOG1454. Eukaryota.
COG0596. LUCA.
HOVERGENiHBG093937.
InParanoidiQ9NQF3.
PhylomeDBiQ9NQF3.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9NQF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENAAPGLI SELKLAVPWG HIAAKAWGSL QGPPVLCLHG WLDNASSFDR
60 70 80 90 100
LIPLLPQDFY YVAMDFGGHG LSSHYSPGVP YYLQTFVSEI RRVVAALKWN
110 120 130 140 150
RFSILGHSFG GVVGGMFFCT FPEMVDKLIL LDTPLFLLES DEMENLLTYK
160 170 180 190 200
RRAIEHVLQV EASQEPSHVF SLKQLLQRQR TALTSSAGSC VRIPSGSCRP

MSC
Length:203
Mass (Da):22,471
Last modified:October 1, 2000 - v1
Checksum:i7451E5712595097E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31E → K.
Corresponds to variant rs3213549 [ dbSNP | Ensembl ].
VAR_056985

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL365513 mRNA. Translation: CAB97209.1.
AL022316 Genomic DNA. No translation available.
BC093888 mRNA. Translation: AAH93888.1.
UniGeneiHs.360940.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL365513 mRNA. Translation: CAB97209.1.
AL022316 Genomic DNA. No translation available.
BC093888 mRNA. Translation: AAH93888.1.
UniGeneiHs.360940.

3D structure databases

ProteinModelPortaliQ9NQF3.
SMRiQ9NQF3. Positions 26-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9NQF3. 1 interaction.
STRINGi9606.ENSP00000331376.

Protein family/group databases

ESTHERihuman-SERHL. AlphaBeta_hydrolase.

Polymorphism and mutation databases

DMDMi21362940.

Proteomic databases

PaxDbiQ9NQF3.
PRIDEiQ9NQF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiSERHL.
H-InvDBHIX0016542.
HGNCiHGNC:14408. SERHL.
HPAiHPA047904.
neXtProtiNX_Q9NQF3.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1454. Eukaryota.
COG0596. LUCA.
HOVERGENiHBG093937.
InParanoidiQ9NQF3.
PhylomeDBiQ9NQF3.

Miscellaneous databases

ChiTaRSiSERHL. human.
PROiQ9NQF3.

Gene expression databases

CleanExiHS_SERHL.
HS_SERHL2.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [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].
    Tissue: Brain.

Entry informationi

Entry nameiSERHL_HUMAN
AccessioniPrimary (citable) accession number: Q9NQF3
Secondary accession number(s): Q5JZ95, Q9UH21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2000
Last modified: January 20, 2016
This is version 104 of the entry and version 1 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

This gene may have been partially duplicated (see SERHL2).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.