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Reviewed, UniProtKB/Swiss-Prot Q3SXM5 (HSDL1_HUMAN)

Last modified July 7, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hydroxysteroid dehydrogenase-like protein 1
Gene names
Name: HSDL1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Tissue specificity

Highly expressed in testis and ovary. Also detected in thyroid, spinal cord, adrenal gland, heart, placenta, skeletal muscle and pancreas. Ref.1

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.

Caution

Although related to the SDR family, lacks the conserved active Tyr residue in position 218 which is replaced by a Phe, suggesting that it may lack oxidoreductase activity.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandNADP
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PITPNAQ001691EBI-1056703,EBI-1042490

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 330329Hydroxysteroid dehydrogenase-like protein 1
PRO_0000313671

Regions

Nucleotide binding67 – 9630NADP Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.5

Natural variations

Natural variant2481P → S: dbSNP rs11540436.
VAR_037693
Natural variant3271C → S: dbSNP rs4378600. Ref.2 Ref.3 Ref.4
VAR_037694

Experimental info

Sequence conflict11M → V in AAK15047. Ref.1
Sequence conflict11M → V in AAK16927. Ref.1
Sequence conflict2221K → R in AAI04220. Ref.4
Sequence conflict2221K → R in AAI06918. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q3SXM5-1 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 62034775E4E6151B

FASTA33037,018
        10         20         30         40         50         60 
MAAVDSFYLL YREIARSCNC YMEALALVGA WYTARKSITV ICDFYSLIRL HFIPRLGSRA 

        70         80         90        100        110        120 
DLIKQYGRWA VVSGATDGIG KAYAEELASR GLNIILISRN EEKLQVVAKD IADTYKVETD 

       130        140        150        160        170        180 
IIVADFSSGR EIYLPIREAL KDKDVGILVN NVGVFYPYPQ YFTQLSEDKL WDIINVNIAA 

       190        200        210        220        230        240 
ASLMVHVVLP GMVERKKGAI VTISSGSCCK PTPQLAAFSA SKAYLDHFSR ALQYEYASKG 

       250        260        270        280        290        300 
IFVQSLIPFY VATSMTAPSN FLHRCSWLVP SPKVYAHHAV STLGISKRTT GYWSHSIQFL 

       310        320        330 
FAQYMPEWLW VWGANILNRS LRKEALCCTA 

« Hide

References

« Hide 'large scale' references
[1]"A novel human hydroxysteroid dehydrogenase like 1 gene (HSDL1) is highly expressed in reproductive tissues."
Huang Y., Tang R., Dai J., Gu S., Zhao W., Cheng C., Xu M., Zhou Z., Ying K., Xi Y., Mao Y.
Mol. Biol. Rep. 28:185-191(2001) [PubMed: 12153137] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-327.
[3]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-327.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-327.
[5]Bienvenut W.V., Preisinger C., Kolch W.
Submitted (JUL-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12 AND 91-99, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Chronic myeloid leukemia cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF237684 mRNA. Translation: AAK15047.1. Different initiation.
AY028377 mRNA. Translation: AAK16927.1. Different initiation.
AK074878 mRNA. Translation: BAC11262.1.
CH471114 Genomic DNA. Translation: EAW95502.1.
BC104219 mRNA. Translation: AAI04220.1.
BC106917 mRNA. Translation: AAI06918.1.
BC104218 mRNA. Translation: AAI04219.1.
IPIIPI00171459.
UniGeneHs.555992

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ3SXM5. 1 interaction.

Proteomic databases

PRIDEQ3SXM5.

Genome annotation databases

EnsemblENSG00000103160. Homo sapiens. [Contig view]
KEGGhsa:83693.
UCSCuc002fhk.1. human.

Organism-specific databases

GeneCardsGC16M082714.
HGNCHGNC:16475. HSDL1.
PharmGKBPA134988345.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ3SXM5.

Gene expression databases

ArrayExpressQ3SXM5.
BgeeQ3SXM5.
CleanExHS_HSDL1.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio72659.

Entry information

Entry nameHSDL1_HUMAN
AccessionPrimary (citable) accession number: Q3SXM5
Secondary accession number(s): Q3SXM4, Q8NC98, Q9BY22
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 7, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents