wanglab/gogpt-training-data huggingface dataset:
Protein: Solute carrier family 15 member 4 (Peptide/histidine transporter 1) (Q91W98)
Organism: Mus musculus (Mouse)
Function: Proton-coupled amino-acid transporter that mediates the transmembrane transport of L-histidine and some di- and tripeptides from inside the lysosome to the cytosol, and plays a key role in innate immune response. Able to transport a variety of di- and tripeptides, including carnosine and some peptidoglycans. Transporter activity is pH-dependent and maximized in the acidic lysosomal environment (By similarity). Involved in the detection of microbial pathogens by toll-like receptors (TLRs) and NOD-like receptors (NLRs), probably by mediating transport of bacterial peptidoglycans across the endolysosomal membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand, and L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (tri-DAP), the NOD1 ligand. Required for TLR7, TLR8 and TLR9-mediated type I interferon (IFN-I) productions in plasmacytoid dendritic cells (pDCs). Independently of its transporter activity, also promotes the recruitment of innate immune adapter TASL to endolysosome downstream of TLR7, TLR8 and TLR9: TASL recruitment leads to the specific recruitment and activation of IRF5 (By similarity). Required for isotype class switch recombination to IgG2c isotype in response to TLR9 stimulation. Required for mast cell secretory-granule homeostasis by limiting mast cell functions and inflammatory responses.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:21277849, ECO:0000269|PubMed:24695226, ECO:0000269|PubMed:29155995}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:24695226, ECO:0000269|PubMed:29784761}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:19570976}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEGERAPLLGSRRPAVSAASAVFAGRRAACGAVLLAELLERAAFYGVTANLVLFLNGAPFDWEGAQASQALLLFMGLTYLGSPFGGWLADARLGRARAILLSLALYLLGLLAFPLLAAPRSRSFLCGDPRPELVRNCSAPFPNGSASCPENAARRCAPATFAGLVLVGLGVATVKANITPFGADQVKDRGPEATRRFFNWFYWSINLGAILSLGGIAYIQQNVSFFTGYLIPTVCVAIAFLVFLCGQSVFITKPPDGSAFTDMFRILTYSCCSQRGGQRRSGEGLGVFQQSSKHSLFDSCKMSRGGPFTEDKVEDVKALVKIVPVFLALIPYWTVYFQMQTTYALQSLHLKIPEISSITTTHHTLPAAWLTMFDAVLILLLIPLKDKLVDPVLRRHGLLPSSLKRIAVGMFFVMCSAFAAGILESKRLDLVKEKTINQTIGGVVYHAADLPIWWQIPQYVLIGISEIFASIAGLEFAYSAAPKSMQSAIMGLFFFFSGIGSFVGSGLLALVSLKAIGWMSSHTDFGNINSCHLHYYFFLLAAIQGATLLLFLIVSVKYDRQRARTDGGPASTRT
Protein: Delta(7)-sterol-C5(6)-desaturase 1 (EC 1.14.19.20) (Delta(7)-sterol-C5-desaturase 1) (Delta-7-C-5 sterol desaturase 1) (Protein DWARF 7) (Protein STEROL 1) (Q39208)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of sitosterol and campesterol, a precursor of growth-promoting brassinosteroids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 7-dehydrocholesterol reductase
- Delta
- Probable 3-beta-hydroxysteroid-Delta
- Ergosterol biosynthetic protein 28
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 2-2
- Delta
- Sterol 14-demethylase
- Methylsterol monooxygenase 1-2
- Methylsterol monooxygenase 1-1
Sequence:
MAADNAYLMQFVDETSFYNRIVLSHLLPANLWEPLPHFLQTWLRNYLAGTLLYFISGFLWCFYIYYLKINVYLPKDAIPTIKAMRLQMFVAMKAMPWYTLLPTVSESMIERGWTKCFASIGEFGWILYFVYIAIYLVFVEFGIYWMHRELHDIKPLYKYLHATHHIYNKQNTLSPFAGLAFHPVDGILQAVPHVIALFIVPIHFTTHIGLLFMEAIWTANIHDCIHGNIWPVMGAGYHTIHHTTYKHNYGHYTIWMDWMFGSLRDPLLEEDDNKDSFKKAE
Protein: T. brucei spp.-specific protein (Q57U49)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTNEPSEAATAPTPADLRHISPSPPRVRPQSSADMTSQLSFPCAYAARVYHVCTENSFCHPQPPDDVKLPMRPHSSGATYLGWIRNSLSGRLTANCYGQTNICSSKGCGINCGNQTIQRSSSSLPCTTATHPANSPAAFEEGNGDDVRDASAPVRRTNFSLARRLRLRGPLHYQRVVDVVRRLRVEGHLSNKECDESFNRLQHNGTNPCAVTNGIQDGRGVHHNILNCSEAATSTMFSPGQTQRESNSLNHARNSNSEPTGGENTGNNQKTECTYNLPNCVTGVIDGDAEVLDATADSSVTSGASVVDIVVLSNADGGDTAVMKMTRDVVVVATDVGVGVGAGLSNDVTTANVEARRRISPSTASLEKERRGGDDVVDAVGTAVDRSAGSVKGHNFNCTEFLPFNVVEGELLRNRRALEQLVTIFEGTLHEIRSACVAEDDGDDVG
Protein: Ataxin-2 C-terminal domain-containing protein (Q586H3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEHSRRKEESPVWLNSSIHVWKTKNDINVVNLRDASEHLPALPSARAEERPPGNGGHRTSMERTGENNERTTEPTKQETLNEILALMHRASDQTRGSSKGTTADSNLSTNAGGKGPVTDSEGKASLFPEPKTSGIVDVEFVQGVNLPGGKNVSPPLHTQPPRDSMQTVALFHDPVWGAAAVSSGADVFDTGSESQGSAVTSLQVENVSGRYSKGDVNPPLMPAPAAPVTMIAPSAPLSYKVPGNVNETMFTPQAQPVAMTSSPSQLGYPQNIGLSTAGWAGAAPHPTGVAMRPVQFVSVPVPVMAHNAVMAVPQPYRMPYSVYQMQPQAPHPAQLQHQPVVYHTSPGQELHHIHQQKVLAPQDATPRPGTNIGATPFVPGGKSV
Protein: Cyclic di-GMP phosphodiesterase PA4781 (EC 3.1.4.-) (Q9HV27)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP. Hydrolyzes c-di-GMP to GMP in a two-step reaction, via the linear intermediate 5'-phosphoguanylyl(3'->5')guanosine (pGpG). In vitro, can use pGpG as an alternative substrate and hydrolyze it into GMP. Acts in regulation of motility, synthesis of virulence determinants and biofilm architecture. May act preferentially as a pGpG binding protein.
Interaction partners:
- diguanylate cyclase
- Diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- diguanylate cyclase
- GGDEF domain-containing protein
- Diguanylate cyclase TpbB
- Sensor domain-containing diguanylate cyclase
- histidine kinase
- histidine kinase
Sequence:
MESMLDRPEQELVLVVDDTPDNLLLMRELLEEQYRVRTAGSGPAGLRAAVEEPRPDLILLDVNMPGMDGYEVCRRLKADPLTRDIPLMFLTARADRDDEQQGLALGAVDYLGKPVSPPIVLARVRTHLQLKANADFLRDKSEYLELEVRRRTRQLQQLQDAVIEALATLGDLRDNPRSRHLPRIERYVRLLAEHLAAQRAFADELTPEAVDLLSKSALLHDIGKVAVPDRVLLNPGQLDAADTALLQGHTRAGRDALASAERRLGQPSGFLRFARQIAYSHHERWDGRGFPEGLAGERIPLAARIVALADRYDELTSRHAYRPPLAHAEAVLLIQAGAGSEFDPRLVEAFVAVADAFAEVARRYADSAEALDVEMQRLEQAVAESIELTAPPA
Protein: POZ-, AT hook-, and zinc finger-containing protein 1 (BTB/POZ domain zinc finger transcription factor) (Protein kinase A RI subunit alpha-associated protein) (Zinc finger and BTB domain-containing protein 19) (Zinc finger protein 278) (Zinc finger sarcoma gene protein) (Q9HBE1)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that plays a role in many biological processes such as embryogenesis, senescence, T-cell development or neurogenesis. Interacts with the TP53 protein to control genes that are important in proliferation and in the DNA-damage response. Mechanistically, the interaction inhibits the DNA binding and transcriptional activity of TP53/p53. Part of the transcriptional network modulating regulatory T-cell development and controls the generation of the regulatory T-cell pool under homeostatic conditions.
Subcellular location: Nucleus {ECO:0000269|PubMed:10713105}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF4
- RNA-binding protein EWS
- CD8 subunit beta
- Cellular tumor antigen p53
- Nuclear receptor corepressor 1
Sequence:
MERVNDASCGPSGCYTYQVSRHSTEMLHNLNQQRKNGGRFCDVLLRVGDESFPAHRAVLAACSEYFESVFSAQLGDGGAADGGPADVGGATAAPGGGAGGSRELEMHTISSKVFGDILDFAYTSRIVVRLESFPELMTAAKFLLMRSVIEICQEVIKQSNVQILVPPARADIMLFRPPGTSDLGFPLDMTNGAALAANSNGIAGSMQPEEEAARAAGAAIAGQASLPVLPGVDRLPMVAGPLSPQLLTSPFPSVASSAPPLTGKRGRGRPRKANLLDSMFGSPGGLREAGILPCGLCGKVFTDANRLRQHEAQHGVTSLQLGYIDLPPPRLGENGLPISEDPDGPRKRSRTRKQVACEICGKIFRDVYHLNRHKLSHSGEKPYSCPVCGLRFKRKDRMSYHVRSHDGSVGKPYICQSCGKGFSRPDHLNGHIKQVHTSERPHKCQTCNASFATRDRLRSHLACHEDKVPCQVCGKYLRAAYMADHLKKHSEGPSNFCSICNRGFSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGAAFHCARTYGNKEGQKCSHQDPIESSDSYGDLSDASDLKTPEKQSANGSFSCDMAVPKNKMESDGEKKYPCPECGSFFRSKSYLNKHIQKVHVRALGGPLGDLGPALGSPFSPQQNMSLLESFGFQIVQSAFASSLVDPEVDQQPMGPEGK
Protein: LD40224p (Q9VJZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO02273p1
- Anamorsin homolog
- BolA-like protein DDB_G0274169
- Glutaredoxin-2
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Glutaredoxin-2
- GH14121p
- Grain, isoform C
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- Iron-sulfur cluster assembly enzyme IscU
Sequence:
MPVVNVSAAEEYQKYINADKTTVALFAAEWAEQCGQVKDALEELAKITGEKLQFISLNAEQFPEISMKHQIEAVPTVIFFAKGSAVDRVDGVDIAAISAKSKKLAENASSAAATGQTLEERLKALINTAPLMIFMKGDRNGPRCGFSKQLIGIVNETNLPYETFDILGDEEVRQGLKTYSDWPTYPQVYVKGELIGGLDIIKELLANNELESTLKG
Protein: E3 ubiquitin-protein ligase WAV3 (EC 2.3.2.27) (Protein WAVY GROWTH 3) (RING-type E3 ubiquitin transferase WAV3) (Q9LTA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in the regulation of root growth. Acts as positive regulator of root gravitropism. Possesses E3 protein ligase activity in vitro.
Interaction partners:
- Magnesium-chelatase subunit ChlI-2, chloroplastic
- Magnesium-chelatase subunit ChlI-1, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- Protein MODIFYING WALL LIGNIN-1
- Alpha/beta hydrolase domain-containing protein WAV2
- RING-H2 finger protein ATL10
- Homeobox protein LUMINIDEPENDENS
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Cyclin-T1-4
Sequence:
MGTGWRRAFCTTAPRNSDAAAPDLDKQRTGYNLTPSPSPRSCVKLAFLSGGSNPSTPRSTSSPSLRCRTADAQTPTAEQTSTPRSATKSPRLSLAAISNPSSPRSPLKLSLFRNSFKFRSTCGICLNSVKTGQGTAKYTAECSHAFHFPCIADYVRKQGKLVCPVCNSIWKDASLLVPHKNATESPLDDSVSVIQEKRVVVTSSPRAKPRPKQSDYSRFYDDDEPLLSPRFVTIPEADENCGGEEEDDVPQFKGFVVDPNPSFAVKTNEIPVNGRDFGNVQVSLLPEAAVVSVGCGYETRAVALRVKAPPPLTARGGVGRRLLDPSQRAPVDLVVVVDVGGTMNGAKLQMVKRAMRLVISSLGSADRLSIVAVVMTVPKRLLPLKRMTEHGKRSAGAVVDGLLCGQGSNTSEALKKASRVLEDRRERNPVASIVLLTDGQGQLSKVHTNQRSTITNVGSTRFAHIEIPVTEHGFGESGGCSNAPAEEAFAKCIGGLLSVVVQDLRIQIRVGSGSGPCEISAIYLCNGRPTLVSSGSGSVRLGDLYAGEERELLVELRVPSTATRAYQILSVRGLFKDPSTQEVVYGRDQSLRVPQAVRSSSSPRIERLRSLFIATRAVAESRRLVEYGECTSAYHLLTSARALLGQSGTVEAAEYIKVVEAELVEVQWRGQQLMEYQSQHQQQHNQRRRGSERETTTTMTLMDENGEPLTPASAWRAAEKLAKLAMMKKSDLHGFENARF
Protein: Transcription factor MYB104 (Myb-related protein 104) (AtMYB104) (Q9SM27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- At3g10595
- Serine/threonine-protein kinase PBL36
- Homeodomain-like superfamily protein
- Homeodomain-like superfamily protein
Sequence:
MIQDQANDLLAMKKTFTKSKWKPEEDRILKDYVIQYGDRTWTHVPKRTGLPHNPASCRFRWMNHLKPSLKKGPFTDEEEKRVLQLHAVLGNKWSQMAREFPGRTDNEIKNFWNARRMRLKGKGLPVYPDEVREQAIRTAAQYGVKVELLNAHYSQDSLMAGNVEKPQELNNLALNQCSPYYQSTLANVQPSRNRVMEPETTFPFTGGSAMNEQNPTLLCNPYVESTQEQLPDSHLFGNVTYSSPPMPLIHEVENLELPSFQGFDFHEEPSSFGAEQYNPMLNLEPHNTLVQSPLIGQTPTDFPSSFYDELLDELLESVVNGSLGEIPKTDTSSESQLFQSSLRSHTDATPDIANTTGYVGSNERNTTNDDDWIRLLLDEGFI
Protein: Copper-exporting P-type ATPase (EC 7.2.2.8) (Copper-exporting P-type ATPase A) (Copper-transporting PIB-type ATPase) (Cu(+) transport ATPase) (Cu(+)-ATPase LpCopA) (LpCopA) (Q5ZWR1)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Couples the hydrolysis of ATP with the export of copper.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:24317491}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Copper efflux ATPase
Sequence:
MKHDHHQGHTHSGKGHACHHEHNSPKTQQASSKMEGPIVYTCPMHPEIRQSAPGHCPLCGMALEPETVTVSEVVSPEYLDMRRRFWIALMLTIPVVILEMGGHGLKHFISGNGSSWIQLLLATPVVLWGGWPFFKRGWQSLKTGQLNMFTLIAMGIGVAWIYSMVAVLWPGVFPHAFRSQEGVVAVYFEAAAVITTLVLLGQVLELKAREQTGSAIRALLKLVPESAHRIKEDGSEEEVSLDNVAVGDLLRVRPGEKIPVDGEVQEGRSFVDESMVTGEPIPVAKEASAKVIGATINQTGSFVMKALHVGSDTMLARIVQMVSDAQRSRAPIQRLADTVSGWFVPAVILVAVLSFIVWALLGPQPALSYGLIAAVSVLIIACPCALGLATPMSIMVGVGKGAQSGVLIKNAEALERMEKVNTLVVDKTGTLTEGHPKLTRIVTDDFVEDNALALAAALEHQSEHPLANAIVHAAKEKGLSLGSVEAFEAPTGKGVVGQVDGHHVAIGNARLMQEHGGDNAPLFEKADELRGKGASVMFMAVDGKTVALLVVEDPIKSSTPETILELQQSGIEIVMLTGDSKRTAEAVAGTLGIKKVVAEIMPEDKSRIVSELKDKGLIVAMAGDGVNDAPALAKADIGIAMGTGTDVAIESAGVTLLHGDLRGIAKARRLSESTMSNIRQNLFFAFIYNVLGVPLAAGVLYPLTGLLLSPMIAAAAMALSSVSVIINALRLKRVTL
Protein: Periostin (D3ZAF5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Metalloendopeptidase
- Collagen alpha-1
- Lumican
- Collagen alpha-1
- Collagen alpha-2
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Fibronectin
- Integrin alpha-V
- Decorin
Sequence:
MVPLLPLSALLLLFLCDVDPANANSYYDKVLAHSRIRGRDQGPNVCALQQILGTKKKYFSSCKNWYQGAICGKKTTVLYECCPGYMRMEGMKGCPAVMPIDHVYGTLGIVGATTTQHYSDVSKLREEIEGKGSYTYFAPSNEAWDNLDSDIRRGLENNVNVELLNALHSHMVNKRMLTKDLKHGMVIPSMYNNLGLFINHYPNGVVTVNCARVIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDELSSFRAAAITSDLLESLGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSEAITGGAVFETMEGNTIEIGCEGDSISINGIKMVNKKDIVTKNGVIHLIDEVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASSLKPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLSDLYNGQILETIGGKQLRVFVYRTAICIENSCMVRGSKQGRNGAIHIFREIIQPAEKSLHEKLRQDKRFSIFLSLLEAADLKDLLTQPGDWTLFAPTNDAFKGMTNEEREILIGDKNALQNIILYHLTPGVYIGKGFEPGVTNILKTTQGSKIYVKGVNETLLVNELKSKESDIMTTNGVIHVVDKLLYPADIPVGNDQLLELLNKLIKYIQIKFVRGSTFKEIPMTVYTTKIITKLVEPKIKVIQGSLQPIIKTEGPAMTKIHIEGEPDFRLIKEGETVTEVIHGEPVIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLQKFLQKDTPAKKIQANKRVQGSRRRSREGRSQ
Protein: Extended synaptotagmin-1 (E-Syt1) (Membrane-bound C2 domain-containing protein) (Q9BSJ8)
Organism: Homo sapiens (Human)
Function: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29469807}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:29469807}; Peripheral membrane protein {ECO:0000269|PubMed:29469807}. Note=Localizes primarily to the endoplasmic reticulum (PubMed:29469807). Recruited to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels (PubMed:22250200, PubMed:29469807). {ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:29469807}.
Interaction partners:
- Extended synaptotagmin-2
- Extended synaptotagmin-3
- Stromal interaction molecule 1
- Derlin-2
- Coiled-coil domain-containing protein 112
- Oxysterol-binding protein 1
Sequence:
MERSPGEGPSPSPMDQPSAPSDPTDQPPAAHAKPDPGSGGQPAGPGAAGEALAVLTSFGRRLLVLIPVYLAGAVGLSVGFVLFGLALYLGWRRVRDEKERSLRAARQLLDDEEQLTAKTLYMSHRELPAWVSFPDVEKAEWLNKIVAQVWPFLGQYMEKLLAETVAPAVRGSNPHLQTFTFTRVELGEKPLRIIGVKVHPGQRKEQILLDLNISYVGDVQIDVEVKKYFCKAGVKGMQLHGVLRVILEPLIGDLPFVGAVSMFFIRRPTLDINWTGMTNLLDIPGLSSLSDTMIMDSIAAFLVLPNRLLVPLVPDLQDVAQLRSPLPRGIIRIHLLAARGLSSKDKYVKGLIEGKSDPYALVRLGTQTFCSRVIDEELNPQWGETYEVMVHEVPGQEIEVEVFDKDPDKDDFLGRMKLDVGKVLQASVLDDWFPLQGGQGQVHLRLEWLSLLSDAEKLEQVLQWNWGVSSRPDPPSAAILVVYLDRAQDLPLKKGNKEPNPMVQLSIQDVTQESKAVYSTNCPVWEEAFRFFLQDPQSQELDVQVKDDSRALTLGALTLPLARLLTAPELILDQWFQLSSSGPNSRLYMKLVMRILYLDSSEICFPTVPGCPGAWDVDSENPQRGSSVDAPPRPCHTTPDSQFGTEHVLRIHVLEAQDLIAKDRFLGGLVKGKSDPYVKLKLAGRSFRSHVVREDLNPRWNEVFEVIVTSVPGQELEVEVFDKDLDKDDFLGRCKVRLTTVLNSGFLDEWLTLEDVPSGRLHLRLERLTPRPTAAELEEVLQVNSLIQTQKSAELAAALLSIYMERAEDLPLRKGTKHLSPYATLTVGDSSHKTKTISQTSAPVWDESASFLIRKPHTESLELQVRGEGTGVLGSLSLPLSELLVADQLCLDRWFTLSSGQGQVLLRAQLGILVSQHSGVEAHSHSYSHSSSSLSEEPELSGGPPHITSSAPELRQRLTHVDSPLEAPAGPLGQVKLTLWYYSEERKLVSIVHGCRSLRQNGRDPPDPYVSLLLLPDKNRGTKRRTSQKKRTLSPEFNERFEWELPLDEAQRRKLDVSVKSNSSFMSRERELLGKVQLDLAETDLSQGVARWYDLMDNKDKGSS
Protein: Aklanonic acid methyltransferase DnrC (AAMT) (EC 2.1.1.288) (Q54818)
Organism: Streptomyces peucetius
Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the methyl esterification of aklanonic acid to yield aklanonic acid methyl ester.
Interaction partners:
Sequence:
MQDSSYKEQVTQAFDQSSSTYDRLGVEFFTPMGRPLVEISEPVTGERVLDIGCGRGACLFPAAEKVGPQGRVHGIDIAPGMIEEARKEAAERGLRNIALDVMDAETPELPARSFDLVMGSYSVIFLPDAVGALARYAGILDHGGRIAFTSPVFRAGTFPFLPPEFTPLIPQALLEHLPEQWRPEALVRRFNSWLERAEDLLRTLERCGYTSVAVTDEPVRMTALSSEAWVDWSHTQGMRLLWQNLPQAQRTELRARLVEGLDKLSDATGALAIDVPVRFVTARVAH
Protein: Metallothionein-3 (MT-3) (GIFB) (GIF) (Growth inhibitory factor) (Metallothionein-III) (MT-III) (P25713)
Organism: Homo sapiens (Human)
Function: Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro.
Interaction partners:
- Metallothionein
- Metallothionein 1H-like protein 1
Sequence:
MDPETCPCPSGGSCTCADSCKCEGCKCTSCKKSCCSCCPAECEKCAKDCVCKGGEAAEAEAEKCSCCQ
Protein: MICOS complex subunit Mic10-like protein (DUF543) (F4I1E5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- MICOS complex subunit MIC60, mitochondrial
- Mitochondrial import receptor subunit TOM40-1
- Mitochondrial Rho GTPase 1
- Peroxisomal and mitochondrial division factor 2
Sequence:
METTKSNSSESDVNAKWDACLDLTARRFVYSSLGGAFAGLLFFRSPVTRWASIAFGAGIGIGSAYTDCSRVFDASSSTSATLLAAPKSTETSVSQVSRNLLRGKYDLEEWQQKSEDNEEAWSVVLYTDVKIVNDPLIFFVLKNLMFFYLRNNSSGLICLPLLFLHSSNNLLTYRLSYRF
Protein: Multidrug resistance protein MdtC (Multidrug transporter MdtC) (P76399)
Organism: Escherichia coli (strain K12)
Function: The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Multidrug resistance protein MdtB
- Multidrug resistance protein MdtA
- Signal transduction histidine-protein kinase BaeS
- Putative multidrug resistance protein MdtD
- Outer membrane protein TolC
- Periplasmic chaperone Spy
- Transcriptional regulatory protein BaeR
- Probable aminoglycoside efflux pump
- Multidrug efflux pump subunit AcrA
- Multidrug export protein EmrB
Sequence:
MKFFALFIYRPVATILLSVAITLCGILGFRMLPVAPLPQVDFPVIIVSASLPGASPETMASSVATPLERSLGRIAGVSEMTSSSSLGSTRIILQFDFDRDINGAARDVQAAINAAQSLLPSGMPSRPTYRKANPSDAPIMILTLTSDTYSQGELYDFASTQLAPTISQIDGVGDVDVGGSSLPAVRVGLNPQALFNQGVSLDDVRTAVSNANVRKPQGALEDGTHRWQIQTNDELKTAAEYQPLIIHYNNGGAVRLGDVATVTDSVQDVRNAGMTNAKPAILLMIRKLPEANIIQTVDSIRAKLPELQETIPAAIDLQIAQDRSPTIRASLEEVEQTLIISVALVILVVFLFLRSGRATIIPAVSVPVSLIGTFAAMYLCGFSLNNLSLMALTIATGFVVDDAIVVLENIARHLEAGMKPLQAALQGTREVGFTVLSMSLSLVAVFLPLLLMGGLPGRLLREFAVTLSVAIGISLLVSLTLTPMMCGWMLKASKPREQKRLRGFGRMLVALQQGYGKSLKWVLNHTRLVGVVLLGTIALNIWLYISIPKTFFPEQDTGVLMGGIQADQSISFQAMRGKLQDFMKIIRDDPAVDNVTGFTGGSRVNSGMMFITLKPRDERSETAQQIIDRLRVKLAKEPGANLFLMAVQDIRVGGRQSNASYQYTLLSDDLAALREWEPKIRKKLATLPELADVNSDQQDNGAEMNLVYDRDTMARLGIDVQAANSLLNNAFGQRQISTIYQPMNQYKVVMEVDPRYTQDISALEKMFVINNEGKAIPLSYFAKWQPANAPLSVNHQGLSAASTISFNLPTGKSLSDASAAIDRAMTQLGVPSTVRGSFAGTAQVFQETMNSQVILIIAAIATVYIVLGILYESYVHPLTILSTLPSAGVGALLALELFNAPFSLIALIGIMLLIGIVKKNAIMMVDFALEAQRHGNLTPQEAIFQACLLRFRPIMMTTLAALFGALPLVLSGGDGSELRQPLGITIVGGLVMSQLLTLYTTPVVYLFFDRLRLRFSRKPKQTVTE
Protein: Membrane-associated progesterone receptor component 1 (mPR) (Q17QC0)
Organism: Bos taurus (Bovine)
Function: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00264}; Extracellular side {ECO:0000250|UniProtKB:O55022}. Secreted {ECO:0000250|UniProtKB:O00264}.
Interaction partners:
- Sigma intracellular receptor 2
- Progesterone receptor
- Cytochrome b5
- Insulin-induced gene 1 protein
- Ferrochelatase, mitochondrial
- Cytochrome b5
- SERPINE1 mRNA binding protein 1
- PAQR8 protein
- Progestin and adipoQ receptor family member 7
Sequence:
MAAEDVAATGADTSELESGGLLQEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKDGEEPTVYSDKEEPKDESTRKND
Protein: Zinc transporter ZIP2 (6A1) (Eti-1) (Solute carrier family 39 member 2) (Zrt- and Irt-like protein 2) (ZIP-2) (hZIP2) (Q9NP94)
Organism: Homo sapiens (Human)
Function: Mediates zinc uptake. Zinc uptake may be mediated by a Zn(2+)-HCO(3)(-) symport mechanism and can function in the presence of albumin. May also transport other divalent cations. May be important in contact inhibition of normal epithelial cells and loss of its expression may play a role in tumorigenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10681536, ECO:0000269|PubMed:30914478}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Zinc transporter ZIP11
- Zinc transporter ZIP4
- Zinc transporter ZIP9
- Zinc transporter ZIP12
- Zinc transporter SLC39A7
Sequence:
MEQLLGIKLGCLFALLALTLGCGLTPICFKWFQIDAARGHHRLVLRLLGCISAGVFLGAGFMHMTAEALEEIESQIQKFMVQNRSASERNSSGDADSAHMEYPYGELIISLGFFFVFFLESLALQCCPGAAGGSTVQDEEWGGAHIFELHSHGHLPSPSKGPLRALVLLLSLSFHSVFEGLAVGLQPTVAATVQLCLAVLAHKGLVVFGVGMRLVHLGTSSRWAVFSILLLALMSPLGLAVGLAVTGGDSEGGRGLAQAVLEGVAAGTFLYVTFLEILPRELASPEAPLAKWSCVAAGFAFMAFIALWA
Protein: Basigin (Glycoprotein CE9) (OX-47 antigen) (CD antigen CD147) (P26453)
Organism: Rattus norvegicus (Rat)
Function: Essential for normal retinal maturation and development (By similarity). Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors (By similarity). In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors (By similarity).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000303|PubMed:11719518}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P18572}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P18572}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:11719518}; Single-pass type I membrane protein {ECO:0000303|PubMed:11719518}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000303|PubMed:11719518}. Basolateral cell membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000303|PubMed:11719518}.
Interaction partners:
- Monocarboxylate transporter 1
- 5-hydroxytryptamine receptor 1A
- Monocarboxylate transporter 4
- CD44 antigen
- 5-hydroxytryptamine receptor 2B
- Peptidyl-prolyl cis-trans isomerase A
- 5-hydroxytryptamine receptor 1B
- 5-hydroxytryptamine receptor 1D
- 5-hydroxytryptamine receptor 2C
- 5-hydroxytryptamine receptor 2A
Sequence:
MAAALLLALAFTFLSGQGACAAAGFLKAPMSQEQWAGGSVVLHCEAVGSPMPEIQWWFEGNEPNDSCSQLWDGARLDRVHIHATYRQHAASTLSVDGLAAEDTGTYECRASSDPDRNHLTRPPRVKWVRAQASVVVLEPGTIVTSVQEVDSKTQLTCFLNSSGIDIVGHRWMRGGKVLQEDTLPDLQMKYTVDADDRSGEYSCIFLPEPVGRGNINVEGPPRIKVGKKSEHASEGEFVKLICKSEASHPPVDEWVWFKTSDTGDQTISNGTEANSKYVIISTPELSELIISDLDMNVDPGTYVCNATNSQGSARETISLRVRSRLAALWPFLGIVAEVLVLVTIIFIYEKRRKPDQTLDEDDPGAAPLKGSGSHLNDKDKNVRQRNAT