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AAMP_HUMAN
ID   AAMP_HUMAN              Reviewed;         434 AA.
AC   Q13685; Q8WUJ9; Q96H92;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 179.
DE   RecName: Full=Angio-associated migratory cell protein;
GN   Name=AAMP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=7743515;
RA   Beckner M.E., Krutzsch H.C., Stracke M.L., Williams S.T., Gallardo J.A.,
RA   Liotta L.A.;
RT   "Identification of a new immunoglobulin superfamily protein expressed in
RT   blood vessels with a heparin-binding consensus sequence.";
RL   Cancer Res. 55:2140-2149(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Skin;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10329261; DOI=10.1006/mvre.1999.2144;
RA   Beckner M.E., Peterson V.A., Moul D.E.;
RT   "Angio-associated migratory cell protein is expressed as an extracellular
RT   protein by blood-vessel-associated mesenchymal cells.";
RL   Microvasc. Res. 57:347-352(1999).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18634987; DOI=10.1016/j.jacc.2008.03.055;
RA   Vogt F., Zernecke A., Beckner M., Krott N., Bosserhoff A.-K., Hoffmann R.,
RA   Zandvoort M.A.M.J., Jahnke T., Kelm M., Weber C., Blindt R.;
RT   "Blockade of angio-associated migratory cell protein inhibits smooth muscle
RT   cell migration and neointima formation in accelerated atherosclerosis.";
RL   J. Am. Coll. Cardiol. 52:302-311(2008).
RN   [6]
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., Buerckstuemmer T.,
RA   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Plays a role in angiogenesis and cell migration. In smooth
CC       muscle cell migration, may act through the RhoA pathway.
CC       {ECO:0000269|PubMed:10329261, ECO:0000269|PubMed:18634987}.
CC   -!- INTERACTION:
CC       Q13685; Q8WTP8-2: AEN; NbExp=4; IntAct=EBI-727274, EBI-12119298;
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in metastatic melanoma, liver, skin,
CC       kidney, heart, lung, lymph node, skeletal muscle and brain, and also in
CC       A2058 melanoma cells and activated T-cells (at protein level).
CC       Expressed in blood vessels. Strongly expressed in endothelial cells,
CC       cytotrophoblasts, and poorly differentiated. colon adenocarcinoma cells
CC       found in lymphatics. {ECO:0000269|PubMed:10329261,
CC       ECO:0000269|PubMed:7743515}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA68889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAG33036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/AAMPID533ch2q35.html";
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DR   EMBL; M95627; AAA68889.1; ALT_INIT; mRNA.
DR   EMBL; CR456755; CAG33036.1; ALT_INIT; mRNA.
DR   EMBL; BC008809; AAH08809.2; -; mRNA.
DR   EMBL; BC020244; AAH20244.1; -; mRNA.
DR   EMBL; BC039866; AAH39866.2; -; mRNA.
DR   CCDS; CCDS33378.1; -.
DR   PIR; I39383; I39383.
DR   RefSeq; NP_001078.2; NM_001087.4.
DR   AlphaFoldDB; Q13685; -.
DR   SMR; Q13685; -.
DR   BioGRID; 106532; 50.
DR   IntAct; Q13685; 19.
DR   MINT; Q13685; -.
DR   STRING; 9606.ENSP00000248450; -.
DR   GlyGen; Q13685; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13685; -.
DR   PhosphoSitePlus; Q13685; -.
DR   BioMuta; AAMP; -.
DR   DMDM; 62906874; -.
DR   EPD; Q13685; -.
DR   jPOST; Q13685; -.
DR   MassIVE; Q13685; -.
DR   MaxQB; Q13685; -.
DR   PaxDb; Q13685; -.
DR   PeptideAtlas; Q13685; -.
DR   PRIDE; Q13685; -.
DR   ProteomicsDB; 59660; -.
DR   Antibodypedia; 34259; 172 antibodies from 29 providers.
DR   DNASU; 14; -.
DR   Ensembl; ENST00000248450.9; ENSP00000248450.4; ENSG00000127837.10.
DR   GeneID; 14; -.
DR   KEGG; hsa:14; -.
DR   MANE-Select; ENST00000248450.9; ENSP00000248450.4; NM_001087.5; NP_001078.2.
DR   UCSC; uc002vhk.4; human.
DR   CTD; 14; -.
DR   DisGeNET; 14; -.
DR   GeneCards; AAMP; -.
DR   HGNC; HGNC:18; AAMP.
DR   HPA; ENSG00000127837; Low tissue specificity.
DR   MIM; 603488; gene.
DR   neXtProt; NX_Q13685; -.
DR   OpenTargets; ENSG00000127837; -.
DR   PharmGKB; PA24365; -.
DR   VEuPathDB; HostDB:ENSG00000127837; -.
DR   eggNOG; KOG0296; Eukaryota.
DR   GeneTree; ENSGT00940000153648; -.
DR   HOGENOM; CLU_000288_57_9_1; -.
DR   InParanoid; Q13685; -.
DR   OMA; WMWKVPS; -.
DR   OrthoDB; 1025450at2759; -.
DR   PhylomeDB; Q13685; -.
DR   TreeFam; TF314543; -.
DR   PathwayCommons; Q13685; -.
DR   Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-HSA-177929; Signaling by EGFR.
DR   Reactome; R-HSA-194138; Signaling by VEGF.
DR   Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR   SignaLink; Q13685; -.
DR   BioGRID-ORCS; 14; 719 hits in 1093 CRISPR screens.
DR   ChiTaRS; AAMP; human.
DR   GeneWiki; AAMP_(gene); -.
DR   GenomeRNAi; 14; -.
DR   Pharos; Q13685; Tbio.
DR   PRO; PR:Q13685; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q13685; protein.
DR   Bgee; ENSG00000127837; Expressed in body of stomach and 198 other tissues.
DR   ExpressionAtlas; Q13685; baseline and differential.
DR   Genevisible; Q13685; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IDA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0014909; P:smooth muscle cell migration; IEP:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Angiogenesis; Cell membrane; Cytoplasm; Developmental protein;
KW   Differentiation; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..434
FT                   /note="Angio-associated migratory cell protein"
FT                   /id="PRO_0000050832"
FT   REPEAT          89..129
FT                   /note="WD 1"
FT   REPEAT          132..171
FT                   /note="WD 2"
FT   REPEAT          173..212
FT                   /note="WD 3"
FT   REPEAT          214..254
FT                   /note="WD 4"
FT   REPEAT          258..299
FT                   /note="WD 5"
FT   REPEAT          315..354
FT                   /note="WD 6"
FT   REPEAT          356..395
FT                   /note="WD 7"
FT   REPEAT          398..433
FT                   /note="WD 8"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..63
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VARIANT         250
FT                   /note="I -> V (in dbSNP:rs2305835)"
FT                   /id="VAR_037061"
SQ   SEQUENCE   434 AA;  46751 MW;  A7B8314442EBAF15 CRC64;
     MESESESGAA ADTPPLETLS FHGDEEIIEV VELDPGPPDP DDLAQEMEDV DFEEEEEEEG
     NEEGWVLEPQ EGVVGSMEGP DDSEVTFALH SASVFCVSLD PKTNTLAVTG GEDDKAFVWR
     LSDGELLFEC AGHKDSVTCA GFSHDSTLVA TGDMSGLLKV WQVDTKEEVW SFEAGDLEWM
     EWHPRAPVLL AGTADGNTWM WKVPNGDCKT FQGPNCPATC GRVLPDGKRA VVGYEDGTIR
     IWDLKQGSPI HVLKGTEGHQ GPLTCVAANQ DGSLILTGSV DCQAKLVSAT TGKVVGVFRP
     ETVASQPSLG EGEESESNSV ESLGFCSVMP LAAVGYLDGT LAIYDLATQT LRHQCQHQSG
     IVQLLWEAGT AVVYTCSLDG IVRLWDARTG RLLTDYRGHT AEILDFALSK DASLVVTTSG
     DHKAKVFCVQ RPDR
 
 
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