ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8IUX7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AEBP1_HUMAN
Primary accession number Q8IUX7
Secondary accession numbers Q14113 Q59ER7 Q6ZSC7 Q7KZ79
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 55)
Name and origin of the protein
Protein name Adipocyte enhancer-binding protein 1 [Precursor]
Synonyms AE-binding protein 1
Aortic carboxypeptidase-like protein
Gene name
Name: AEBP1
Synonyms: ACLP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Aortic smooth muscle;
DOI=10.1074/jbc.273.25.15654; PubMed=9624159 [NCBI, ExPASy, EBI, Israel, Japan]
Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T., Perrella M.A., Blanar M.A., Haber E., Lee M.-E.;
"Aortic carboxypeptidase-like protein, a novel protein with discoidin and carboxypeptidase-like domains, is up-regulated during vascular smooth muscle cell differentiation.";
J. Biol. Chem. 273:15654-15660(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-1133.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1083423; PubMed=12690205 [NCBI, ExPASy, EBI, Israel, Japan]
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 314-1158 (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Cancellous bone;
DOI=10.1006/bbrc.1996.1675; PubMed=8920928 [NCBI, ExPASy, EBI, Israel, Japan]
Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K., Okubo K.;
"A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its expression in a differentiating osteoblastic cell line.";
Biochem. Biophys. Res. Commun. 228:411-414(1996).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-922, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF053944; AAC25585.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK127541; BAC87026.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209744; BAD92981.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH236960; EAL23768.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471128; EAW61119.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038588; AAH38588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D86479; BAA13094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00745313; -.
IPI00894097; -.
PIR JC5256; JC5256.
RefSeq NP_001120.3; -.
UniGene Hs.439463
3D structure databases
HSSP Q90240; 1H8L. [HSSP ENTRY / PDB]
ModBase Q8IUX7.
Protein family/group databases
MEROPS M14.951; -.
PTM databases
PhosphoSite Q8IUX7; -.
Organism-specific databases
GeneCards GC07P044110; -.
HGNC HGNC:303; AEBP1.
GenAtlas AEBP1.
HPA CAB009966; -.
MIM 602981; gene. [NCBI / EBI]
PharmGKB PA24604; -.
Gene expression databases
Bgee Q8IUX7; -.
CleanEx HS_AEBP1; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004181; Molecular function: metallocarboxypeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0007155; Biological process: cell adhesion (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR014766; CarboxyPept_regulatory.
IPR000421; Coagulation_factor_5/8-type_C.
IPR000834; Peptidase_M14.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.1120; CarboxyPept_regulatory; 1.
Pfam PF00754; F5_F8_type_C; 1.
PF00246; Peptidase_M14; 1.
Pfam graphical view of domain structure.
PRINTS PR00765; CRBOXYPTASEA.
SMART SM00231; FA58C; 1.
SM00631; Zn_pept; 1.
SMART graphical view of domain structure.
PROSITE PS00132; CARBOXYPEPT_ZN_1; 1.
PS01285; FA58C_1; 1.
PS01286; FA58C_2; 1.
PS50022; FA58C_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q8IUX7; -.
Genome annotation databases
Ensembl ENSG00000106624; Homo sapiens. [Contig view]
GeneID 165; -.
KEGG hsa:165; -.
Phylogenomic databases
HOVERGEN Q8IUX7; -.
OMA Q8IUX7; LEEEWAP.
Other
NextBio 665; -.
SOURCE AEBP1; Homo sapiens.
ProtoNet Q8IUX7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; DNA-binding; Glycoprotein; Nucleus; Polymorphism; Repressor; Secreted; Signal; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     25  25     Potential. 
CHAIN   26   1158  1133     Adipocyte enhancer-binding protein 1. PRO_0000333189
DOMAIN   383    540  158     F5/8 type C. 
REGION   390    555  166     Required for DNA-binding and interaction with NFKBIA (By similarity). 
REGION   421    624  204     Interaction with MAPK1 and MAPK3 (By similarity). 
REGION   555    985  431     Interaction with PTEN (By similarity). 
REGION   941   1158  218     Required for transcriptional repression (By similarity). 
REGION   1006   1158  153     Interaction with MAPK1 and MAPK3 (By similarity). 
COMPBIAS   47    326  280     Pro-rich. 
COMPBIAS   1079   1136  58     Glu-rich. 
CARBOHYD   528    528        N-linked (GlcNAc...). 
CARBOHYD   922    922        N-linked (GlcNAc...). 
VAR_SEQ   1    457        Missing (in isoform 2). VSP_033467
VAR_SEQ   458    495        ITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEM -> MRKWWAPCPGSWLCSHCLGEGWALRGAGSTALRPASPQ (in isoform 2). VSP_033468
VAR_SEQ   543    544        AP -> ARECGGLAGALSGGGVLGWASRHPAKDNPASLAA (in isoform 2). VSP_033469
VARIANT   273    273  1     P -> T (in dbSNP:rs2537188 [NCBI]). VAR_043118 
VARIANT   648    648  1     D -> E (in dbSNP:rs11770649 [NCBI]). VAR_043119 
VARIANT   1001   1001  1     P -> L (in dbSNP:rs4724285 [NCBI]). VAR_043120 
VARIANT   1133   1133  1     K -> E (in dbSNP:rs13928 [NCBI]). VAR_043121 
VARIANT   1148   1148  1     V -> I (in dbSNP:rs13898 [NCBI]). VAR_043122 
CONFLICT   145    145        K -> E (in Ref. 1; AAC25585). 
CONFLICT   218    218        R -> Q (in Ref. 1; AAC25585). 
CONFLICT   569    569        D -> G (in Ref. 2; BAC87026). 
CONFLICT   715    715        R -> G (in Ref. 2; BAC87026). 
CONFLICT   884    884        S -> G (in Ref. 2; BAC87026). 
CONFLICT   1079   1079        E -> G (in Ref. 3; BAD92981). 
Sequence information
Length: 1158 AA [This is the length of the unprocessed precursor] Molecular weight: 130929 Da [This is the MW of the unprocessed precursor] CRC64: 1D7F4A20451646AE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAVRGAPLL SCLLALLALC PGGRPQTVLT DDEIEEFLEG FLSELEPEPR EDDVEAPPPP 

        70         80         90        100        110        120 
EPTPRVRKAQ AGGKPGKRPG TAAEVPPEKT KDKGKKGKKD KGPKVPKESL EGSPRPPKKG 

       130        140        150        160        170        180 
KEKPPKATKK PKEKPPKATK KPKEKPPKAT KKPKEKPPKA TKKPPSGKRP PILAPSETLE 

       190        200        210        220        230        240 
WPLPPPPSPG PEELPQEGGA PLSNNWQNPG EETHVEAREH QPEPEEETEQ PTLDYNDQIE 

       250        260        270        280        290        300 
REDYEDFEYI RRQKQPRPPP SRRRRPERVW PEPPEEKAPA PAPEERIEPP VKPLLPPLPP 

       310        320        330        340        350        360 
DYGDGYVIPN YDDMDYYFGP PPPQKPDAER QTDEEKEELK KPKKEDSSPK EETDKWAVEK 

       370        380        390        400        410        420 
GKDHKEPRKG EELEEEWTPT EKVKCPPIGM ESHRIEDNQI RASSMLRHGL GAQRGRLNMQ 

       430        440        450        460        470        480 
TGATEDDYYD GAWCAEDDAR TQWIEVDTRR TTRFTGVITQ GRDSSIHDDF VTTFFVGFSN 

       490        500        510        520        530        540 
DSQTWVMYTN GYEEMTFHGN VDKDTPVLSE LPEPVVARFI RIYPLTWNGS LCMRLEVLGC 

       550        560        570        580        590        600 
SVAPVYSYYA QNEVVATDDL DFRHHSYKDM RQLMKVVNEE CPTITRTYSL GKSSRGLKIY 

       610        620        630        640        650        660 
AMEISDNPGE HELGEPEFRY TAGIHGNEVL GRELLLLLMQ YLCREYRDGN PRVRSLVQDT 

       670        680        690        700        710        720 
RIHLVPSLNP DGYEVAAQMG SEFGNWALGL WTEEGFDIFE DFPDLNSVLW GAEERKWVPY 

       730        740        750        760        770        780 
RVPNNNLPIP ERYLSPDATV STEVRAIIAW MEKNPFVLGA NLNGGERLVS YPYDMARTPT 

       790        800        810        820        830        840 
QEQLLAAAMA AARGEDEDEV SEAQETPDHA IFRWLAISFA SAHLTLTEPY RGGCQAQDYT 

       850        860        870        880        890        900 
GGMGIVNGAK WNPRTGTIND FSYLHTNCLE LSFYLGCDKF PHESELPREW ENNKEALLTF 

       910        920        930        940        950        960 
MEQVHRGIKG VVTDEQGIPI ANATISVSGI NHGVKTASGG DYWRILNPGE YRVTAHAEGY 

       970        980        990       1000       1010       1020 
TPSAKTCNVD YDIGATQCNF ILARSNWKRI REIMAMNGNR PIPHIDPSRP MTPQQRRLQQ 

      1030       1040       1050       1060       1070       1080 
RRLQHRLRLR AQMRLRRLNA TTTLGPHTVP PTLPPAPATT LSTTIEPWGL IPPTTAGWEE 

      1090       1100       1110       1120       1130       1140 
SETETYTEVV TEFGTEVEPE FGTKVEPEFE TQLEPEFETQ LEPEFEEEEE EEKEEEIATG 

      1150 
QAFPFTTVET YTVNFGDF 

Q8IUX7 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!