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Q9Y3M8 (STA13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
StAR-related lipid transfer protein 13
Alternative name(s):
46H23.2
Deleted in liver cancer 2 protein
Short name=DLC-2
Rho GTPase-activating protein
START domain-containing protein 13
Short name=StARD13
Gene names
Name:STARD13
Synonyms:DLC2, GT650
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1113 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GTPase-activating protein for RhoA, and perhaps for Cdc42. May be involved in regulation of cytoskeletal reorganization, cell proliferation and cell motility. Acts a tumor suppressor in hepatocellular carcinoma cells. Ref.2 Ref.3

Subunit structure

Homodimer. Interacts with TAX1BP1. Ref.2 Ref.10

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Lipid droplet Ref.3 Ref.8.

Tissue specificity

Ubiquitously expressed. Underexpressed in hepatocellular carcinoma cells and some breast cancer cell lines. Ref.1 Ref.2

Sequence similarities

Contains 1 Rho-GAP domain.

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 START domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAX1BP1Q86VP12EBI-465487,EBI-529518

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y3M8-1)

Also known as: DLC2alpha;

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: Q9Y3M8-2)

Also known as: DLC2beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: MFSQVPRTPA...RHQLVTKIQQ → MLEPSSVLHA...SRVNHTFQRR
Isoform 3 (identifier: Q9Y3M8-3)

Also known as: DLC2gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
Isoform 4 (identifier: Q9Y3M8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: MFSQVPRTPA...RHQLVTKIQQ → MSTGTQPKTKVLSDKRPKERV
Isoform 5 (identifier: Q9Y3M8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: MFSQVPRTPA...RHQLVTKIQQ → MLEPSSVLHA...SRVNHTFQRR
     695-695: V → E
     696-1113: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11131113StAR-related lipid transfer protein 13
PRO_0000220679

Regions

Domain55 – 12268SAM
Domain663 – 868206Rho-GAP
Domain899 – 1107209START

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue1331Phosphoserine By similarity

Natural variations

Alternative sequence1 – 118118Missing in isoform 3.
VSP_017353
Alternative sequence1 – 5656MFSQV…TKIQQ → MLEPSSVLHANVNQAPLWCL VLRWCRECKDTVCGGKQKSR VNHTFQRR in isoform 2 and isoform 5.
VSP_017354
Alternative sequence1 – 5656MFSQV…TKIQQ → MSTGTQPKTKVLSDKRPKER V in isoform 4.
VSP_017355
Alternative sequence6951V → E in isoform 5.
VSP_017356
Alternative sequence696 – 1113418Missing in isoform 5.
VSP_017357
Natural variant1751T → M.
Corresponds to variant rs9568878 [ dbSNP | Ensembl ].
VAR_037494
Natural variant2501K → R.
Corresponds to variant rs3742321 [ dbSNP | Ensembl ].
VAR_022098
Natural variant3831R → P.
Corresponds to variant rs34425674 [ dbSNP | Ensembl ].
VAR_037495
Natural variant7981N → S.
Corresponds to variant rs35144435 [ dbSNP | Ensembl ].
VAR_037496

Experimental info

Mutagenesis6991R → A: Loss of RhoGAP activity. Ref.1
Mutagenesis7361K → E: Loss of RhoGAP activity. Ref.3
Mutagenesis7401R → E: Loss of RhoGAP activity. Ref.3
Sequence conflict1431K → R in AAQ72791. Ref.2
Sequence conflict3971I → V in AAQ72791. Ref.2
Sequence conflict10971I → T in AAQ72791. Ref.2

Secondary structure

................................................ 1113
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (DLC2alpha) [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 314F809C23E6E1E4

FASTA1,113124,967
        10         20         30         40         50         60 
MFSQVPRTPA SGCYYLNSMT PEGQEMYLRF DQTTRRSPYR MSRILARHQL VTKIQQEIEA 

        70         80         90        100        110        120 
KEACDWLRAA GFPQYAQLYE DSQFPINIVA VKNDHDFLEK DLVEPLCRRL NTLNKCASMK 

       130        140        150        160        170        180 
LDVNFQRKKG DDSDEEDLCI SNKWTFQRTS RRWSRVDDLY TLLPRGDRNG SPGGTGMRNT 

       190        200        210        220        230        240 
TSSESVLTDL SEPEVCSIHS ESSGGSDSRS QPGQCCTDNP VMLDAPLVSS SLPQPPRDVL 

       250        260        270        280        290        300 
NHPFHPKNEK PTRARAKSFL KRMETLRGKG AHGRHKGSGR TGGLVISGPM LQQEPESFKA 

       310        320        330        340        350        360 
MQCIQIPNGD LQNSPPPACR KGLPCSGKSS GESSPSEHSS SGVSTPCLKE RKCHEANKRG 

       370        380        390        400        410        420 
GMYLEDLDVL AGTALPDAGD QSRMHEFHSQ ENLVVHIPKD HKPGTFPKAL SIESLSPTDS 

       430        440        450        460        470        480 
SNGVNWRTGS ISLGREQVPG AREPRLMASC HRASRVSIYD NVPGSHLYAS TGDLLDLEKD 

       490        500        510        520        530        540 
DLFPHLDDIL QHVNGLQEVV DDWSKDVLPE LQTHDTLVGE PGLSTFPSPN QITLDFEGNS 

       550        560        570        580        590        600 
VSEGRTTPSD VERDVTSLNE SEPPGVRDRR DSGVGASLTR PNRRLRWNSF QLSHQPRPAP 

       610        620        630        640        650        660 
ASPHISSQTA SQLSLLQRFS LLRLTAIMEK HSMSNKHGWT WSVPKFMKRM KVPDYKDKAV 

       670        680        690        700        710        720 
FGVPLIVHVQ RTGQPLPQSI QQALRYLRSN CLDQVGLFRK SGVKSRIHAL RQMNENFPEN 

       730        740        750        760        770        780 
VNYEDQSAYD VADMVKQFFR DLPEPLFTNK LSETFLHIYQ YVSKEQRLQA VQAAILLLAD 

       790        800        810        820        830        840 
ENREVLQTLL CFLNDVVNLV EENQMTPMNL AVCLAPSLFH LNLLKKESSP RVIQKKYATG 

       850        860        870        880        890        900 
KPDQKDLNEN LAAAQGLAHM IMECDRLFEV PHELVAQSRN SYVEAEIHVP TLEELGTQLE 

       910        920        930        940        950        960 
ESGATFHTYL NHLIQGLQKE AKEKFKGWVT CSSTDNTDLA FKKVGDGNPL KLWKASVEVE 

       970        980        990       1000       1010       1020 
APPSVVLNRV LRERHLWDED FVQWKVVETL DRQTEIYQYV LNSMAPHPSR DFVVLRTWKT 

      1030       1040       1050       1060       1070       1080 
DLPKGMCTLV SLSVEHEEAQ LLGGVRAVVM DSQYLIEPCG SGKSRLTHIC RIDLKGHSPE 

      1090       1100       1110 
WYSKGFGHLC AAEVARIRNS FQPLIAEGPE TKI 

« Hide

Isoform 2 (DLC2beta) [UniParc].

Checksum: C447ADE6F7AAF9D8
Show »

FASTA1,105123,893
Isoform 3 (DLC2gamma) [UniParc].

Checksum: 3F608FA94A4EF8BF
Show »

FASTA995111,192
Isoform 4 [UniParc].

Checksum: 1B108966B3EDC44D
Show »

FASTA1,078120,684
Isoform 5 [UniParc].

Checksum: 4E1B65EA0FDCB836
Show »

FASTA68776,367

References

« Hide 'large scale' references
[1]"Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma."
Ching Y.-P., Wong C.-M., Chan S.-F., Leung T.H.-Y., Ng D.-C., Jin D.-Y., Ng I.O.
J. Biol. Chem. 278:10824-10830(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF ARG-699.
[2]"Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins."
Nagaraja G.M., Kandpal R.P.
Biochem. Biophys. Res. Commun. 313:654-665(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TAX1BP1.
[3]"Deleted in liver cancer 2 (DLC2) suppresses cell transformation by means of inhibition of RhoA activity."
Leung T.H.-Y., Ching Y.-P., Yam J.W.P., Wong C.-M., Yau T.-O., Jin D.-Y., Ng I.O.
Proc. Natl. Acad. Sci. U.S.A. 102:15207-15212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-736 AND ARG-740.
[4]Rhodes S.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Uterus.
[6]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 5).
Tissue: Skin.
[8]"Mitochondrial targeting of growth suppressor protein DLC2 through the START domain."
Ng D.C.-H., Chan S.-F., Kok K.H., Yam J.W.P., Ching Y.-P., Ng I.O., Jin D.-Y.
FEBS Lett. 580:191-198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Solution structures, dynamics, and lipid-binding of the sterile alpha-motif domain of the deleted in liver cancer 2."
Li H., Fung K.-L., Jin D.-Y., Chung S.S.M., Ching Y.-P., Ng I.O., Sze K.-H., Ko B.C.B., Sun H.
Proteins 67:1154-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 56-120, SUBUNIT, INTERACTION WITH MEMBRANE PHOSPHOLIPIDS.
[11]"The crystal structure of human STARD13 (DLC2) lipid transfer and protein localization domain."
Structural genomics consortium (SGC)
Submitted (MAY-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-1113.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY082589 mRNA. Translation: AAL91648.1.
AY366448 mRNA. Translation: AAQ72791.1.
AY082590 mRNA. Translation: AAL91649.1.
AY082591 mRNA. Translation: AAL91650.1.
AL049801 mRNA. Translation: CAB42562.1.
BX647695 mRNA. Translation: CAI46026.1.
Z84483 Genomic DNA. Translation: CAC94774.1.
AL627232, AL139187 Genomic DNA. Translation: CAM17900.1.
AL139187, AL627232 Genomic DNA. Translation: CAM23625.1.
AL139187 Genomic DNA. Translation: CAM23626.1.
BC046563 mRNA. Translation: AAH46563.1.
CCDSCCDS9348.1. [Q9Y3M8-1]
CCDS9349.1. [Q9Y3M8-2]
CCDS9350.1. [Q9Y3M8-3]
PIRH59432.
RefSeqNP_001230395.1. NM_001243466.1. [Q9Y3M8-5]
NP_001230403.1. NM_001243474.1.
NP_001230405.1. NM_001243476.2.
NP_443083.1. NM_052851.2. [Q9Y3M8-3]
NP_821074.1. NM_178006.3. [Q9Y3M8-1]
NP_821075.1. NM_178007.2. [Q9Y3M8-2]
XP_006719951.1. XM_006719888.1. [Q9Y3M8-3]
XP_006719952.1. XM_006719889.1. [Q9Y3M8-3]
UniGeneHs.507704.
Hs.721224.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H80NMR-A56-120[»]
2JW2NMR-A56-120[»]
2PSOX-ray2.80A/B/C903-1113[»]
ProteinModelPortalQ9Y3M8.
SMRQ9Y3M8. Positions 50-120, 655-863, 907-1104.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124744. 12 interactions.
IntActQ9Y3M8. 10 interactions.
MINTMINT-1194865.

PTM databases

PhosphoSiteQ9Y3M8.

Polymorphism databases

DMDM90185285.

Proteomic databases

MaxQBQ9Y3M8.
PaxDbQ9Y3M8.
PRIDEQ9Y3M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255486; ENSP00000255486; ENSG00000133121. [Q9Y3M8-2]
ENST00000336934; ENSP00000338785; ENSG00000133121. [Q9Y3M8-1]
ENST00000399365; ENSP00000382300; ENSG00000133121. [Q9Y3M8-3]
GeneID90627.
KEGGhsa:90627.
UCSCuc001uuu.3. human. [Q9Y3M8-2]
uc001uuv.3. human. [Q9Y3M8-1]
uc021rhz.1. human. [Q9Y3M8-5]

Organism-specific databases

CTD90627.
GeneCardsGC13M033677.
H-InvDBHIX0171887.
HGNCHGNC:19164. STARD13.
HPAHPA039535.
MIM609866. gene.
neXtProtNX_Q9Y3M8.
PharmGKBPA38806.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236923.
HOVERGENHBG055955.
InParanoidQ9Y3M8.
OMAFVQWKVV.
OrthoDBEOG7CG6Z8.
PhylomeDBQ9Y3M8.
TreeFamTF314044.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9Y3M8.
BgeeQ9Y3M8.
GenevestigatorQ9Y3M8.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamPF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTARD13. human.
EvolutionaryTraceQ9Y3M8.
GeneWikiSTARD13.
GenomeRNAi90627.
NextBio76872.
PROQ9Y3M8.
SOURCESearch...

Entry information

Entry nameSTA13_HUMAN
AccessionPrimary (citable) accession number: Q9Y3M8
Secondary accession number(s): A2A309 expand/collapse secondary AC list , A2A310, Q5HYH1, Q5TAE3, Q6UN61, Q86TP6, Q86WQ3, Q86XT1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 120 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM