Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y3M8

- STA13_HUMAN

UniProt

Q9Y3M8 - STA13_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

StAR-related lipid transfer protein 13

Gene

STARD13

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. lipid binding Source: InterPro

GO - Biological processi

  1. regulation of small GTPase mediated signal transduction Source: Reactome
  2. small GTPase mediated signal transduction Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:STARD13
Synonyms:DLC2, GT650
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:19164. STARD13.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. lipid particle Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi699 – 6991R → A: Loss of RhoGAP activity. 1 Publication
Mutagenesisi736 – 7361K → E: Loss of RhoGAP activity. 1 Publication
Mutagenesisi740 – 7401R → E: Loss of RhoGAP activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA38806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11131113StAR-related lipid transfer protein 13PRO_0000220679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei133 – 1331PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y3M8.
PaxDbiQ9Y3M8.
PRIDEiQ9Y3M8.

PTM databases

PhosphoSiteiQ9Y3M8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y3M8.
ExpressionAtlasiQ9Y3M8. baseline and differential.
GenevestigatoriQ9Y3M8.

Organism-specific databases

HPAiHPA039535.

Interactioni

Subunit structurei

Homodimer. Interacts with TAX1BP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TAX1BP1Q86VP12EBI-465487,EBI-529518

Protein-protein interaction databases

BioGridi124744. 12 interactions.
IntActiQ9Y3M8. 10 interactions.
MINTiMINT-1194865.

Structurei

Secondary structure

1
1113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 6914Combined sources
Helixi73 – 775Combined sources
Turni78 – 825Combined sources
Helixi88 – 925Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 11715Combined sources
Helixi913 – 92412Combined sources
Beta strandi929 – 9313Combined sources
Beta strandi934 – 9363Combined sources
Beta strandi938 – 9425Combined sources
Beta strandi952 – 96110Combined sources
Helixi963 – 97210Combined sources
Helixi974 – 9763Combined sources
Beta strandi985 – 9917Combined sources
Beta strandi994 – 10018Combined sources
Beta strandi1004 – 10063Combined sources
Beta strandi1010 – 102011Combined sources
Helixi1023 – 10253Combined sources
Beta strandi1027 – 10337Combined sources
Beta strandi1043 – 10464Combined sources
Beta strandi1049 – 105810Combined sources
Beta strandi1064 – 10729Combined sources
Beta strandi1075 – 10773Combined sources
Turni1079 – 10846Combined sources
Helixi1085 – 109915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H80NMR-A56-120[»]
2JW2NMR-A56-120[»]
2PSOX-ray2.80A/B/C903-1113[»]
ProteinModelPortaliQ9Y3M8.
SMRiQ9Y3M8. Positions 50-120, 655-863, 907-1104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3M8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 12268SAMAdd
BLAST
Domaini663 – 868206Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini899 – 1107209STARTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 START domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236923.
GeneTreeiENSGT00760000119123.
HOVERGENiHBG055955.
InParanoidiQ9Y3M8.
OMAiFVQWKVV.
OrthoDBiEOG7CG6Z8.
PhylomeDBiQ9Y3M8.
TreeFamiTF314044.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y3M8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MFSQVPRTPA SGCYYLNSMT PEGQEMYLRF DQTTRRSPYR MSRILARHQL
60 70 80 90 100
VTKIQQEIEA KEACDWLRAA GFPQYAQLYE DSQFPINIVA VKNDHDFLEK
110 120 130 140 150
DLVEPLCRRL NTLNKCASMK LDVNFQRKKG DDSDEEDLCI SNKWTFQRTS
160 170 180 190 200
RRWSRVDDLY TLLPRGDRNG SPGGTGMRNT TSSESVLTDL SEPEVCSIHS
210 220 230 240 250
ESSGGSDSRS QPGQCCTDNP VMLDAPLVSS SLPQPPRDVL NHPFHPKNEK
260 270 280 290 300
PTRARAKSFL KRMETLRGKG AHGRHKGSGR TGGLVISGPM LQQEPESFKA
310 320 330 340 350
MQCIQIPNGD LQNSPPPACR KGLPCSGKSS GESSPSEHSS SGVSTPCLKE
360 370 380 390 400
RKCHEANKRG GMYLEDLDVL AGTALPDAGD QSRMHEFHSQ ENLVVHIPKD
410 420 430 440 450
HKPGTFPKAL SIESLSPTDS SNGVNWRTGS ISLGREQVPG AREPRLMASC
460 470 480 490 500
HRASRVSIYD NVPGSHLYAS TGDLLDLEKD DLFPHLDDIL QHVNGLQEVV
510 520 530 540 550
DDWSKDVLPE LQTHDTLVGE PGLSTFPSPN QITLDFEGNS VSEGRTTPSD
560 570 580 590 600
VERDVTSLNE SEPPGVRDRR DSGVGASLTR PNRRLRWNSF QLSHQPRPAP
610 620 630 640 650
ASPHISSQTA SQLSLLQRFS LLRLTAIMEK HSMSNKHGWT WSVPKFMKRM
660 670 680 690 700
KVPDYKDKAV FGVPLIVHVQ RTGQPLPQSI QQALRYLRSN CLDQVGLFRK
710 720 730 740 750
SGVKSRIHAL RQMNENFPEN VNYEDQSAYD VADMVKQFFR DLPEPLFTNK
760 770 780 790 800
LSETFLHIYQ YVSKEQRLQA VQAAILLLAD ENREVLQTLL CFLNDVVNLV
810 820 830 840 850
EENQMTPMNL AVCLAPSLFH LNLLKKESSP RVIQKKYATG KPDQKDLNEN
860 870 880 890 900
LAAAQGLAHM IMECDRLFEV PHELVAQSRN SYVEAEIHVP TLEELGTQLE
910 920 930 940 950
ESGATFHTYL NHLIQGLQKE AKEKFKGWVT CSSTDNTDLA FKKVGDGNPL
960 970 980 990 1000
KLWKASVEVE APPSVVLNRV LRERHLWDED FVQWKVVETL DRQTEIYQYV
1010 1020 1030 1040 1050
LNSMAPHPSR DFVVLRTWKT DLPKGMCTLV SLSVEHEEAQ LLGGVRAVVM
1060 1070 1080 1090 1100
DSQYLIEPCG SGKSRLTHIC RIDLKGHSPE WYSKGFGHLC AAEVARIRNS
1110
FQPLIAEGPE TKI
Length:1,113
Mass (Da):124,967
Last modified:March 7, 2006 - v2
Checksum:i314F809C23E6E1E4
GO
Isoform 2 (identifier: Q9Y3M8-2) [UniParc]FASTAAdd to Basket

Also known as: DLC2beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: MFSQVPRTPA...RHQLVTKIQQ → MLEPSSVLHA...SRVNHTFQRR

Show »
Length:1,105
Mass (Da):123,893
Checksum:iC447ADE6F7AAF9D8
GO
Isoform 3 (identifier: Q9Y3M8-3) [UniParc]FASTAAdd to Basket

Also known as: DLC2gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.

Show »
Length:995
Mass (Da):111,192
Checksum:i3F608FA94A4EF8BF
GO
Isoform 4 (identifier: Q9Y3M8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: MFSQVPRTPA...RHQLVTKIQQ → MSTGTQPKTKVLSDKRPKERV

Show »
Length:1,078
Mass (Da):120,684
Checksum:i1B108966B3EDC44D
GO
Isoform 5 (identifier: Q9Y3M8-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:687
Mass (Da):76,367
Checksum:i4E1B65EA0FDCB836
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431K → R in AAQ72791. (PubMed:14697242)Curated
Sequence conflicti397 – 3971I → V in AAQ72791. (PubMed:14697242)Curated
Sequence conflicti1097 – 10971I → T in AAQ72791. (PubMed:14697242)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751T → M.
Corresponds to variant rs9568878 [ dbSNP | Ensembl ].
VAR_037494
Natural varianti250 – 2501K → R.
Corresponds to variant rs3742321 [ dbSNP | Ensembl ].
VAR_022098
Natural varianti383 – 3831R → P.
Corresponds to variant rs34425674 [ dbSNP | Ensembl ].
VAR_037495
Natural varianti798 – 7981N → S.
Corresponds to variant rs35144435 [ dbSNP | Ensembl ].
VAR_037496

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 3. 2 PublicationsVSP_017353Add
BLAST
Alternative sequencei1 – 5656MFSQV…TKIQQ → MLEPSSVLHANVNQAPLWCL VLRWCRECKDTVCGGKQKSR VNHTFQRR in isoform 2 and isoform 5. 2 PublicationsVSP_017354Add
BLAST
Alternative sequencei1 – 5656MFSQV…TKIQQ → MSTGTQPKTKVLSDKRPKER V in isoform 4. 1 PublicationVSP_017355Add
BLAST
Alternative sequencei695 – 6951V → E in isoform 5. 1 PublicationVSP_017356
Alternative sequencei696 – 1113418Missing in isoform 5. 1 PublicationVSP_017357Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9348.1. [Q9Y3M8-1]
CCDS9349.1. [Q9Y3M8-2]
CCDS9350.1. [Q9Y3M8-3]
PIRiH59432.
RefSeqiNP_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]
UniGeneiHs.156551.
Hs.507704.
Hs.721224.

Genome annotation databases

EnsembliENST00000255486; ENSP00000255486; ENSG00000133121. [Q9Y3M8-2]
ENST00000336934; ENSP00000338785; ENSG00000133121. [Q9Y3M8-1]
ENST00000399365; ENSP00000382300; ENSG00000133121. [Q9Y3M8-3]
GeneIDi90627.
KEGGihsa:90627.
UCSCiuc001uuu.3. human. [Q9Y3M8-2]
uc001uuv.3. human. [Q9Y3M8-1]
uc021rhz.1. human. [Q9Y3M8-5]

Polymorphism databases

DMDMi90185285.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS9348.1. [Q9Y3M8-1 ]
CCDS9349.1. [Q9Y3M8-2 ]
CCDS9350.1. [Q9Y3M8-3 ]
PIRi H59432.
RefSeqi NP_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 ]
UniGenei Hs.156551.
Hs.507704.
Hs.721224.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2H80 NMR - A 56-120 [» ]
2JW2 NMR - A 56-120 [» ]
2PSO X-ray 2.80 A/B/C 903-1113 [» ]
ProteinModelPortali Q9Y3M8.
SMRi Q9Y3M8. Positions 50-120, 655-863, 907-1104.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124744. 12 interactions.
IntActi Q9Y3M8. 10 interactions.
MINTi MINT-1194865.

PTM databases

PhosphoSitei Q9Y3M8.

Polymorphism databases

DMDMi 90185285.

Proteomic databases

MaxQBi Q9Y3M8.
PaxDbi Q9Y3M8.
PRIDEi Q9Y3M8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255486 ; ENSP00000255486 ; ENSG00000133121 . [Q9Y3M8-2 ]
ENST00000336934 ; ENSP00000338785 ; ENSG00000133121 . [Q9Y3M8-1 ]
ENST00000399365 ; ENSP00000382300 ; ENSG00000133121 . [Q9Y3M8-3 ]
GeneIDi 90627.
KEGGi hsa:90627.
UCSCi uc001uuu.3. human. [Q9Y3M8-2 ]
uc001uuv.3. human. [Q9Y3M8-1 ]
uc021rhz.1. human. [Q9Y3M8-5 ]

Organism-specific databases

CTDi 90627.
GeneCardsi GC13M033677.
H-InvDB HIX0171887.
HGNCi HGNC:19164. STARD13.
HPAi HPA039535.
MIMi 609866. gene.
neXtProti NX_Q9Y3M8.
PharmGKBi PA38806.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236923.
GeneTreei ENSGT00760000119123.
HOVERGENi HBG055955.
InParanoidi Q9Y3M8.
OMAi FVQWKVV.
OrthoDBi EOG7CG6Z8.
PhylomeDBi Q9Y3M8.
TreeFami TF314044.

Enzyme and pathway databases

Reactomei REACT_11051. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSi STARD13. human.
EvolutionaryTracei Q9Y3M8.
GeneWikii STARD13.
GenomeRNAii 90627.
NextBioi 76872.
PROi Q9Y3M8.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y3M8.
ExpressionAtlasi Q9Y3M8. baseline and differential.
Genevestigatori Q9Y3M8.

Family and domain databases

Gene3Di 1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProi IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view ]
Pfami PF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view ]
SMARTi SM00324. RhoGAP. 1 hit.
SM00234. START. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEi PS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.

Entry informationi

Entry nameiSTA13_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3M8
Secondary accession number(s): A2A309
, A2A310, Q5HYH1, Q5TAE3, Q6UN61, Q86TP6, Q86WQ3, Q86XT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 124 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3