Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q96I15 (SCLY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenocysteine lyase

Short name=hSCL
EC=4.4.1.16
Gene names
Name:SCLY
Synonyms:SCL
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium By similarity.

Catalytic activity

L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasmcytosol By similarity.

Induction

Up-regulated in acute glomerulonephritis. Regulated by JUN/AP-1. Ref.5

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.

Sequence caution

The sequence BAA91659.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandPyridoxal phosphate
   Molecular functionLyase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular amino acid metabolic process

Traceable author statement. Source: ProtInc

   Cellular componentcytosol

Traceable author statement. Source: ProtInc

   Molecular functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

selenocysteine lyase activity

Traceable author statement. Source: ProtInc

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96I15-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96I15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     308-445: AAELVTQNCE...QAVAQLEDQA → VSPGELEEMS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Selenocysteine lyase
PRO_0000317012

Sites

Active site3881S-selanylcysteine intermediate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6
Modified residue2591N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence308 – 445138AAELV…LEDQA → VSPGELEEMS in isoform 2.
VSP_030854
Natural variant521K → E.
Corresponds to variant rs7597367 [ dbSNP | Ensembl ].
VAR_038464
Natural variant1751A → T. Ref.3
Corresponds to variant rs3210400 [ dbSNP | Ensembl ].
VAR_038465
Natural variant2761F → S.
Corresponds to variant rs35637307 [ dbSNP | Ensembl ].
VAR_038466

Experimental info

Sequence conflict421L → V in AAF36816. Ref.1

Secondary structure

............................................................... 445
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: D26F3FCFB8B165D2

FASTA44548,149
        10         20         30         40         50         60 
MEAAVAPGRD APAPAASQPS GCGKHNSPER KVYMDYNATT PLEPEVIQAM TKAMWEAWGN 

        70         80         90        100        110        120 
PSSPYSAGRK AKDIINAARE SLAKMIGGKP QDIIFTSGGT ESNNLVIHSV VKHFHANQTS 

       130        140        150        160        170        180 
KGHTGGHHSP VKGAKPHFIT SSVEHDSIRL PLEHLVEEQV AAVTFVPVSK VSGQAEVDDI 

       190        200        210        220        230        240 
LAAVRPTTRL VTIMLANNET GIVMPVPEIS QRIKALNQER VAAGLPPILV HTDAAQALGK 

       250        260        270        280        290        300 
QRVDVEDLGV DFLTIVGHKF YGPRIGALYI RGLGEFTPLY PMLFGGGQER NFRPGTENTP 

       310        320        330        340        350        360 
MIAGLGKAAE LVTQNCEAYE AHMRDVRDYL EERLEAEFGQ KRIHLNSQFP GTQRLPNTCN 

       370        380        390        400        410        420 
FSIRGPRLQG HVVLAQCRVL MASVGAACHS DHGDQPSPVL LSYGVPFDVA RNALRLSVGR 

       430        440 
STTRAEVDLV VQDLKQAVAQ LEDQA 

« Hide

Isoform 2 [UniParc].

Checksum: A831471CE76E5B11
Show »

FASTA31733,957

References

« Hide 'large scale' references
[1]"cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis."
Mihara H., Kurihara T., Watanabe T., Yoshimura T., Esaki N.
J. Biol. Chem. 275:6195-6200(2000) [PubMed: 10692412] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-175.
Tissue: Brain.
[4]"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] OF 189-445.
Tissue: Teratocarcinoma.
[5]"Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1."
Jafari C., Panzer U., Steinmetz O.M., Zahner G., Stahl R.A., Harendza S.
Cell. Mol. Biol. Lett. 11:424-437(2006) [PubMed: 16874457] [Abstract]
Cited for: INDUCTION BY JUN.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure of human selenocysteine lyase."
Structural genomics consortium (SGC)
Submitted (JUL-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-445 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF175767 mRNA. Translation: AAF36816.1.
AC016757 Genomic DNA. Translation: AAY24333.1.
AC016776 Genomic DNA. Translation: AAY24221.1.
BC000586 mRNA. Translation: AAH00586.2.
BC007891 mRNA. Translation: AAH07891.1.
AK001377 mRNA. Translation: BAA91659.1. Different initiation.
IPIIPI00101652.
IPI00884890.
RefSeqNP_057594.4. NM_016510.5.
UniGeneHs.709612.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GZCX-ray2.10A/B8-445[»]
3GZDX-ray1.80A/B/C/D8-445[»]
ProteinModelPortalQ96I15.
SMRQ96I15. Positions 29-444.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96I15. 1 interaction.
STRINGQ96I15.

PTM databases

PhosphoSiteQ96I15.

Polymorphism databases

DMDM167016561.

Proteomic databases

PRIDEQ96I15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254663; ENSP00000254663; ENSG00000132330.
GeneID51540.
KEGGhsa:51540.
UCSCuc002vxm.2. human.
uc002vxn.2. human.

Organism-specific databases

CTD51540.
GeneCardsGC02P238985.
H-InvDBHIX0114427.
HIX0200260.
HGNCHGNC:18161. SCLY.
MIM611056. gene.
neXtProtNX_Q96I15.
PharmGKBPA134979359.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00530000063513.
HOGENOMHBG635316.
HOVERGENHBG003708.
InParanoidQ96I15.
OMALEPEVIQ.
OrthoDBEOG4XH004.
PhylomeDBQ96I15.

Gene expression databases

ArrayExpressQ96I15.
BgeeQ96I15.
CleanExHS_SCLY.
GenevestigatorQ96I15.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR016454. Cysteine_dSase_NifS.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK01763.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF005572. NifS. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio55309.
SOURCESearch...

Entry information

Entry nameSCLY_HUMAN
AccessionPrimary (citable) accession number: Q96I15
Secondary accession number(s): B9A068 expand/collapse secondary AC list , Q53SN1, Q53SN8, Q7L670, Q9NVT7, Q9NZR7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 86 of the entry and version 2 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

Human chromosome 2

Human chromosome 2: 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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families