Full text data of SMAP2
SMAP2
(SMAP1L)
[Confidence: low (only semi-automatic identification from reviews)]
Stromal membrane-associated protein 2 (Stromal membrane-associated protein 1-like)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Stromal membrane-associated protein 2 (Stromal membrane-associated protein 1-like)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8WU79
ID SMAP2_HUMAN Reviewed; 429 AA.
AC Q8WU79; B2R7T1; B7Z5B5; B7Z8V2; D3DPV2; Q5QPL2; Q96C93; Q9NST2;
read moreAC Q9UJL8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Stromal membrane-associated protein 2;
DE AltName: Full=Stromal membrane-associated protein 1-like;
GN Name=SMAP2; Synonyms=SMAP1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Rhodes S., Huckle E.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Neutrophil, Thalamus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-132 IN COMPLEX WITH ZINC
RP IONS.
RG Structural genomics consortium (SGC);
RT "Structure of the GAP domain of SMAP1L (LOC64744) stromal membrane-
RT associated protein 1-like.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: GTPase activating protein that acts on ARF1. Can also
CC activate ARF6 (in vitro). May play a role in clathrin-dependent
CC retrograde transport from early endosomes to the trans-Golgi
CC network (By similarity).
CC -!- SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin
CC heavy chains (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci
CC throughout the cytoplasm and in juxtanuclear structures (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WU79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WU79-2; Sequence=VSP_018504;
CC Name=3;
CC IsoId=Q8WU79-3; Sequence=VSP_043789;
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
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DR EMBL; AL133206; CAB61580.1; -; mRNA.
DR EMBL; AL137764; CAB70912.1; -; mRNA.
DR EMBL; AK298702; BAH12851.1; -; mRNA.
DR EMBL; AK303975; BAH14088.1; -; mRNA.
DR EMBL; AK313105; BAG35928.1; -; mRNA.
DR EMBL; AK316218; BAH14589.1; -; mRNA.
DR EMBL; AL031985; CAI19853.1; -; Genomic_DNA.
DR EMBL; AL031985; CAI19854.1; -; Genomic_DNA.
DR EMBL; AL031985; CAI19855.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07220.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07222.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07221.1; -; Genomic_DNA.
DR EMBL; BC014512; AAH14512.1; -; mRNA.
DR EMBL; BC021133; AAH21133.1; -; mRNA.
DR RefSeq; NP_001185907.1; NM_001198978.1.
DR RefSeq; NP_001185908.1; NM_001198979.1.
DR RefSeq; NP_001185909.1; NM_001198980.1.
DR RefSeq; NP_073570.1; NM_022733.2.
DR UniGene; Hs.15200; -.
DR UniGene; Hs.602551; -.
DR PDB; 2IQJ; X-ray; 1.90 A; A/B=1-132.
DR PDBsum; 2IQJ; -.
DR ProteinModelPortal; Q8WU79; -.
DR SMR; Q8WU79; 10-132.
DR IntAct; Q8WU79; 3.
DR STRING; 9606.ENSP00000361803; -.
DR PhosphoSite; Q8WU79; -.
DR DMDM; 74760545; -.
DR PaxDb; Q8WU79; -.
DR PRIDE; Q8WU79; -.
DR DNASU; 64744; -.
DR Ensembl; ENST00000372708; ENSP00000361793; ENSG00000084070.
DR Ensembl; ENST00000372718; ENSP00000361803; ENSG00000084070.
DR Ensembl; ENST00000539317; ENSP00000442835; ENSG00000084070.
DR GeneID; 64744; -.
DR KEGG; hsa:64744; -.
DR UCSC; uc001cfj.3; human.
DR CTD; 64744; -.
DR GeneCards; GC01P040810; -.
DR HGNC; HGNC:25082; SMAP2.
DR HPA; HPA021466; -.
DR HPA; HPA024424; -.
DR neXtProt; NX_Q8WU79; -.
DR PharmGKB; PA162403939; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG055260; -.
DR InParanoid; Q8WU79; -.
DR KO; K12486; -.
DR OMA; DINALRX; -.
DR OrthoDB; EOG78M02F; -.
DR PhylomeDB; Q8WU79; -.
DR ChiTaRS; SMAP2; human.
DR EvolutionaryTrace; Q8WU79; -.
DR GenomeRNAi; 64744; -.
DR NextBio; 66687; -.
DR PRO; PR:Q8WU79; -.
DR ArrayExpress; Q8WU79; -.
DR Bgee; Q8WU79; -.
DR CleanEx; HS_SMAP2; -.
DR Genevestigator; Q8WU79; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR InterPro; IPR001164; ArfGAP.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW GTPase activation; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 429 Stromal membrane-associated protein 2.
FT /FTId=PRO_0000235841.
FT DOMAIN 13 137 Arf-GAP.
FT ZN_FING 28 51 C4-type.
FT REGION 163 232 Interaction with clathrin heavy chains
FT (By similarity).
FT REGION 340 429 Interaction with PICALM (By similarity).
FT COMPBIAS 279 411 Met-rich.
FT MOD_RES 219 219 Phosphoserine.
FT MOD_RES 225 225 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine (By similarity).
FT VAR_SEQ 1 80 Missing (in isoform 3).
FT /FTId=VSP_043789.
FT VAR_SEQ 1 33 MTGKSVKDVDRYQAVLANLLLEEDNKFCADCQS -> MIF
FT (in isoform 2).
FT /FTId=VSP_018504.
FT VARIANT 289 289 A -> T (in dbSNP:rs34845213).
FT /FTId=VAR_048327.
FT HELIX 13 19
FT HELIX 23 26
FT TURN 29 31
FT STRAND 38 40
FT TURN 41 44
FT STRAND 45 47
FT HELIX 49 58
FT TURN 60 62
FT STRAND 65 67
FT TURN 68 70
FT HELIX 75 82
FT HELIX 85 93
FT TURN 94 96
FT HELIX 107 118
SQ SEQUENCE 429 AA; 46786 MW; C2787BECAE37D6BD CRC64;
MTGKSVKDVD RYQAVLANLL LEEDNKFCAD CQSKGPRWAS WNIGVFICIR CAGIHRNLGV
HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAYLPET FRRPQIDPAV EGFIRDKYEK
KKYMDRSLDI NAFRKEKDDK WKRGSEPVPE KKLEPVVFEK VKMPQKKEDP QLPRKSSPKS
TAPVMDLLGL DAPVACSIAN SKTSNTLEKD LDLLASVPSP SSSGSRKVVG SMPTAGSAGS
VPENLNLFPE PGSKSEEIGK KQLSKDSILS LYGSQTPQMP TQAMFMAPAQ MAYPTAYPSF
PGVTPPNSIM GSMMPPPVGM VAQPGASGMV APMAMPAGYM GGMQASMMGV PNGMMTTQQA
GYMAGMAAMP QTVYGVQPAQ QLQWNLTQMT QQMAGMNFYG ANGMMNYGQS MSGGNGQAAN
QTLSPQMWK
//
ID SMAP2_HUMAN Reviewed; 429 AA.
AC Q8WU79; B2R7T1; B7Z5B5; B7Z8V2; D3DPV2; Q5QPL2; Q96C93; Q9NST2;
read moreAC Q9UJL8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Stromal membrane-associated protein 2;
DE AltName: Full=Stromal membrane-associated protein 1-like;
GN Name=SMAP2; Synonyms=SMAP1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Rhodes S., Huckle E.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Neutrophil, Thalamus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-132 IN COMPLEX WITH ZINC
RP IONS.
RG Structural genomics consortium (SGC);
RT "Structure of the GAP domain of SMAP1L (LOC64744) stromal membrane-
RT associated protein 1-like.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: GTPase activating protein that acts on ARF1. Can also
CC activate ARF6 (in vitro). May play a role in clathrin-dependent
CC retrograde transport from early endosomes to the trans-Golgi
CC network (By similarity).
CC -!- SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin
CC heavy chains (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci
CC throughout the cytoplasm and in juxtanuclear structures (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WU79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WU79-2; Sequence=VSP_018504;
CC Name=3;
CC IsoId=Q8WU79-3; Sequence=VSP_043789;
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
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DR EMBL; AL133206; CAB61580.1; -; mRNA.
DR EMBL; AL137764; CAB70912.1; -; mRNA.
DR EMBL; AK298702; BAH12851.1; -; mRNA.
DR EMBL; AK303975; BAH14088.1; -; mRNA.
DR EMBL; AK313105; BAG35928.1; -; mRNA.
DR EMBL; AK316218; BAH14589.1; -; mRNA.
DR EMBL; AL031985; CAI19853.1; -; Genomic_DNA.
DR EMBL; AL031985; CAI19854.1; -; Genomic_DNA.
DR EMBL; AL031985; CAI19855.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07220.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07222.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07221.1; -; Genomic_DNA.
DR EMBL; BC014512; AAH14512.1; -; mRNA.
DR EMBL; BC021133; AAH21133.1; -; mRNA.
DR RefSeq; NP_001185907.1; NM_001198978.1.
DR RefSeq; NP_001185908.1; NM_001198979.1.
DR RefSeq; NP_001185909.1; NM_001198980.1.
DR RefSeq; NP_073570.1; NM_022733.2.
DR UniGene; Hs.15200; -.
DR UniGene; Hs.602551; -.
DR PDB; 2IQJ; X-ray; 1.90 A; A/B=1-132.
DR PDBsum; 2IQJ; -.
DR ProteinModelPortal; Q8WU79; -.
DR SMR; Q8WU79; 10-132.
DR IntAct; Q8WU79; 3.
DR STRING; 9606.ENSP00000361803; -.
DR PhosphoSite; Q8WU79; -.
DR DMDM; 74760545; -.
DR PaxDb; Q8WU79; -.
DR PRIDE; Q8WU79; -.
DR DNASU; 64744; -.
DR Ensembl; ENST00000372708; ENSP00000361793; ENSG00000084070.
DR Ensembl; ENST00000372718; ENSP00000361803; ENSG00000084070.
DR Ensembl; ENST00000539317; ENSP00000442835; ENSG00000084070.
DR GeneID; 64744; -.
DR KEGG; hsa:64744; -.
DR UCSC; uc001cfj.3; human.
DR CTD; 64744; -.
DR GeneCards; GC01P040810; -.
DR HGNC; HGNC:25082; SMAP2.
DR HPA; HPA021466; -.
DR HPA; HPA024424; -.
DR neXtProt; NX_Q8WU79; -.
DR PharmGKB; PA162403939; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG055260; -.
DR InParanoid; Q8WU79; -.
DR KO; K12486; -.
DR OMA; DINALRX; -.
DR OrthoDB; EOG78M02F; -.
DR PhylomeDB; Q8WU79; -.
DR ChiTaRS; SMAP2; human.
DR EvolutionaryTrace; Q8WU79; -.
DR GenomeRNAi; 64744; -.
DR NextBio; 66687; -.
DR PRO; PR:Q8WU79; -.
DR ArrayExpress; Q8WU79; -.
DR Bgee; Q8WU79; -.
DR CleanEx; HS_SMAP2; -.
DR Genevestigator; Q8WU79; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR InterPro; IPR001164; ArfGAP.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW GTPase activation; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 429 Stromal membrane-associated protein 2.
FT /FTId=PRO_0000235841.
FT DOMAIN 13 137 Arf-GAP.
FT ZN_FING 28 51 C4-type.
FT REGION 163 232 Interaction with clathrin heavy chains
FT (By similarity).
FT REGION 340 429 Interaction with PICALM (By similarity).
FT COMPBIAS 279 411 Met-rich.
FT MOD_RES 219 219 Phosphoserine.
FT MOD_RES 225 225 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine (By similarity).
FT VAR_SEQ 1 80 Missing (in isoform 3).
FT /FTId=VSP_043789.
FT VAR_SEQ 1 33 MTGKSVKDVDRYQAVLANLLLEEDNKFCADCQS -> MIF
FT (in isoform 2).
FT /FTId=VSP_018504.
FT VARIANT 289 289 A -> T (in dbSNP:rs34845213).
FT /FTId=VAR_048327.
FT HELIX 13 19
FT HELIX 23 26
FT TURN 29 31
FT STRAND 38 40
FT TURN 41 44
FT STRAND 45 47
FT HELIX 49 58
FT TURN 60 62
FT STRAND 65 67
FT TURN 68 70
FT HELIX 75 82
FT HELIX 85 93
FT TURN 94 96
FT HELIX 107 118
SQ SEQUENCE 429 AA; 46786 MW; C2787BECAE37D6BD CRC64;
MTGKSVKDVD RYQAVLANLL LEEDNKFCAD CQSKGPRWAS WNIGVFICIR CAGIHRNLGV
HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAYLPET FRRPQIDPAV EGFIRDKYEK
KKYMDRSLDI NAFRKEKDDK WKRGSEPVPE KKLEPVVFEK VKMPQKKEDP QLPRKSSPKS
TAPVMDLLGL DAPVACSIAN SKTSNTLEKD LDLLASVPSP SSSGSRKVVG SMPTAGSAGS
VPENLNLFPE PGSKSEEIGK KQLSKDSILS LYGSQTPQMP TQAMFMAPAQ MAYPTAYPSF
PGVTPPNSIM GSMMPPPVGM VAQPGASGMV APMAMPAGYM GGMQASMMGV PNGMMTTQQA
GYMAGMAAMP QTVYGVQPAQ QLQWNLTQMT QQMAGMNFYG ANGMMNYGQS MSGGNGQAAN
QTLSPQMWK
//