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Q92502 (STAR8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
StAR-related lipid transfer protein 8
Alternative name(s):
Deleted in liver cancer 3 protein
Short name=DLC-3
START domain-containing protein 8
Short name=StARD8
START-GAP3
Gene names
Name:STARD8
Synonyms:DLC3, KIAA0189
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accelerates GTPase activity of RHOA and CDC42, but not RAC1. Stimulates the hydrolysis of phosphatidylinositol 4,5-bisphosphate by PLCD1. Ref.7

Subunit structure

Binds both the SH2 and PTB domains of TNS1.

Subcellular location

Cell junctionfocal adhesion Ref.7.

Tissue specificity

Widely expressed with highest levels in kidney, lung and placenta. Ref.8

Sequence similarities

Contains 1 Rho-GAP domain.

Contains 1 START domain.

Sequence caution

The sequence BAA11506.2 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92502-1)

Also known as: DLC3beta;

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: Q92502-2)

Also known as: DLC3alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPLLDVFWSC...SLGALCRRLM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10231023StAR-related lipid transfer protein 8
PRO_0000220676

Regions

Domain573 – 777205Rho-GAP
Domain809 – 1017209START
Compositional bias24 – 274Poly-Glu
Compositional bias338 – 3425Poly-Glu

Amino acid modifications

Modified residue2381Phosphoserine By similarity
Modified residue4811Phosphoserine By similarity

Natural variations

Alternative sequence11M → MPLLDVFWSCFRKVKCFPLL QVKKNAEAEAKRACEWLQAT GFPQYVQLFEEGSFPLDIGS VKKNHGFLDEDSLGALCRRL M in isoform 2.
VSP_032984
Natural variant1881G → S in a breast cancer sample; somatic mutation. Ref.10
VAR_036588
Natural variant2421E → K in a breast cancer sample; somatic mutation. Ref.10
VAR_036589
Natural variant3271R → Q.
Corresponds to variant rs55962426 [ dbSNP | Ensembl ].
VAR_061816

Experimental info

Mutagenesis6081R → E: No effect on cell morphology when overexpressed. Ref.7
Sequence conflict4661P → S in BAA11506. Ref.1
Isoform 2:
Sequence conflict711D → G in CAH18253. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (DLC3beta) [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: F93804B352450DE2

FASTA1,023112,601
        10         20         30         40         50         60 
MTLNNCASMK LEVHFQSKQN EDSEEEEQCT ISSHWAFQQE SKCWSPMGSS DLLAPPSPGL 

        70         80         90        100        110        120 
PATSSCESVL TELSATSLPV ITVSLPPEPA DLPLPGRAPS SSDRPLLSPT QGQEGPQDKA 

       130        140        150        160        170        180 
KKRHRNRSFL KHLESLRRKE KSGSQQAEPK HSPATSEKVS KASSFRSCRG FLSAGFYRAK 

       190        200        210        220        230        240 
NWAATSAGGS GANTRKAWEA WPVASFRHPQ WTHRGDCLVH VPGDHKPGTF PRSLSIESLC 

       250        260        270        280        290        300 
PEDGHRLADW QPGRRWGCEG RRGSCGSTGS HASTYDNLPE LYPAEPVMVG AEAEDEDDEE 

       310        320        330        340        350        360 
SGGSYAHLDD ILQHVWGLQQ RVELWSRAMY PDLGPGDEEE EEATSSVEIA TVEVKCQAEA 

       370        380        390        400        410        420 
LSQMEVPAHG ESPAWAQAEV QPAVLAPAQA PAEAEPVAQE EAEAPAPAPA PAPAQDSEQE 

       430        440        450        460        470        480 
AHSGGEPTFA SSLSVEEGHS ISDTVASSSE LDSSGNSMNE AEAAGPLAGL QASMPRERRD 

       490        500        510        520        530        540 
SGVGASLTRP CRKLRWHSFQ NSHRPSLNSE SLEINRQFAG QINLLHKGSL LRLTAFMEKY 

       550        560        570        580        590        600 
TVPHKQGWVW SMPKFMRRNK TPDYRGQHVF GVPPLIHVQR TGQPLPQSIQ QAMRYLRSQC 

       610        620        630        640        650        660 
LDQVGIFRKS GVKSRIQNLR QMNETSPDNV CYEGQSAYDV ADLLKQYFRD LPEPIFTSKL 

       670        680        690        700        710        720 
TTTFLQIYQL LPKDQWLAAA QAATLLLPDE NREVLQTLLY FLSDIASAEE NQMTAGNLAV 

       730        740        750        760        770        780 
CLAPSIFHLN VSKKDSPSPR IKSKRSLIGR PGPRDLSDNM AATQGLSHMI SDCKKLFQVP 

       790        800        810        820        830        840 
QDMVLQLCSS YSAAELSPPG PALAELRQAQ AAGVSLSLYM EENIQDLLRD AAERFKGWMS 

       850        860        870        880        890        900 
VPGPQHTELA CRKAPDGHPL RLWKASTEVA APPAVVLHRV LRERALWDED LLRAQVLEAL 

       910        920        930        940        950        960 
MPGVELYHYV TDSMAPHPCR DFVVLRMWRS DLPRGGCLLV SQSLDPEQPV PESGVRALML 

       970        980        990       1000       1010       1020 
TSQYLMEPCG LGRSRLTHIC RADLRGRSPD WYNKVFGHLC AMEVAKIRDS FPTLQAAGPE 


TKL 

« Hide

Isoform 2 (DLC3alpha) [UniParc].

Checksum: 2BA1262D4C925551
Show »

FASTA1,103121,749

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"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 2).
Tissue: Endometrial tumor.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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 1).
Tissue: Uterus.
[7]"START-GAP3/DLC3 is a GAP for RhoA and Cdc42 and is localized in focal adhesions regulating cell morphology."
Kawai K., Kiyota M., Seike J., Deki Y., Yagisawa H.
Biochem. Biophys. Res. Commun. 364:783-789(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-608.
[8]"Deleted in liver cancer 3 (DLC-3), a novel Rho GTPase-activating protein, is downregulated in cancer and inhibits tumor cell growth."
Durkin M.E., Ullmannova V., Guan M., Popescu N.C.
Oncogene 26:4580-4589(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Oncogenic inhibition by a deleted in liver cancer gene requires cooperation between tensin binding and Rho-specific GTPase-activating protein activities."
Qian X., Li G., Asmussen H.K., Asnaghi L., Vass W.C., Braverman R., Yamada K.M., Popescu N.C., Papageorge A.G., Lowy D.R.
Proc. Natl. Acad. Sci. U.S.A. 104:9012-9017(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNS1.
[10]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-188 AND LYS-242.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D80011 mRNA. Translation: BAA11506.2. Different initiation.
AK291747 mRNA. Translation: BAF84436.1.
CR749411 mRNA. Translation: CAH18253.1.
AL360076 Genomic DNA. Translation: CAI41586.1.
CH471132 Genomic DNA. Translation: EAX05374.1.
CH471132 Genomic DNA. Translation: EAX05375.1.
BC035587 mRNA. Translation: AAH35587.1.
IPIIPI00293887.
IPI00742801.
PIRB59430.
RefSeqNP_001135975.1. NM_001142503.2.
NP_001135976.1. NM_001142504.2.
NP_055540.2. NM_014725.4.
UniGeneHs.95140.

3D structure databases

ProteinModelPortalQ92502.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000363727.

PTM databases

PhosphoSiteQ92502.

Polymorphism databases

DMDM90110072.

Proteomic databases

PaxDbQ92502.
PRIDEQ92502.

Protocols and materials databases

DNASU9754.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252336; ENSP00000252336; ENSG00000130052.
ENST00000374597; ENSP00000363725; ENSG00000130052.
ENST00000374599; ENSP00000363727; ENSG00000130052.
GeneID9754.
KEGGhsa:9754.
UCSCuc004dxa.3. human.
uc004dxb.3. human.

Organism-specific databases

CTD9754.
GeneCardsGC0XP067867.
HGNCHGNC:19161. STARD8.
MIM300689. gene.
neXtProtNX_Q92502.
PharmGKBPA38804.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236923.
HOGENOMHOG000039960.
HOVERGENHBG055955.
InParanoidQ92502.
OMARKAPDGH.
OrthoDBEOG4JDH7M.
PhylomeDBQ92502.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ92502.
BgeeQ92502.
CleanExHS_STARD8.
GenevestigatorQ92502.
GermOnlineENSG00000130052. Homo sapiens.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamPF00620. RhoGAP. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTSM00324. RhoGAP. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMSSF48350. Rho_GAP. 1 hit.
PROSITEPS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9754.
NextBio36716.
SOURCESearch...

Entry information

Entry nameSTAR8_HUMAN
AccessionPrimary (citable) accession number: Q92502
Secondary accession number(s): A8K6T2 expand/collapse secondary AC list , D3DVT9, Q5JST0, Q68DG7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 21, 2006
Last modified: May 1, 2013
This is version 106 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 X

Human chromosome X: 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

SIMILARITY comments

Index of protein domains and families