wanglab/gogpt-training-data huggingface dataset:
Protein: NUDIX hydrolase, conserved (Q38BD3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pab1p-dependent poly
- 5'-3' exoribonuclease 2
Sequence:
MAMGRVSVSSLPSNVSAWVEALQRALHLKVEDLHLPEHFHLKNLSTGCRFSHLNTPPTVGDKRESAVLVLLSPAAGMPPNTFQEMCVTLTKRTPHLRHHKGEMSFPGGRLDGEEQAAAAAQRETAEEIGIDSSLYEILGPLRPLAPLSGKSHVTPIVAVTQYSVTPLCHSPHEVDSIHYLHLSPLLLNSKQTHCRLLKYLPSSSGVPLHFPCFFTSPSQARYCDPVSPSPGLLQLSQEDGGHEPLLPNNFPGELVWGVTAFVMCELLVRLITALGGSGTALGCSPAIARDPEHPLGKR
Protein: Allograft inflammatory factor 1 (AIF-1) (Ionized calcium-binding adapter molecule 1) (O70200)
Organism: Mus musculus (Mouse)
Function: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10934045}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}; Peripheral membrane protein; Cytoplasmic side. Cell projection, phagocytic cup {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}. Note=Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis. {ECO:0000269|PubMed:10934045}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Glial fibrillary acidic protein
- RNA binding protein fox-1 homolog 3
- Interleukin-1 beta
- Macrosialin
- Complement C1q subcomponent subunit A
- Integrin alpha-M
- Tumor necrosis factor
- T-lymphocyte activation antigen CD86
- Macrophage colony-stimulating factor 1 receptor
Sequence:
MSQSRDLQGGKAFGLLKAQQEERLEGINKQFLDDPKYSNDEDLPSKLEAFKVKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKRLIREVSSGSEETFSYSDFLRMMLGKRSAILRMILMYEEKNKEHKRPTGPPAKKAISELP
Protein: Growth/differentiation factor 10 (GDF-10) (Bone morphogenetic protein 3B) (BMP-3B) (P97737)
Organism: Mus musculus (Mouse)
Function: Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway. Plays an inhibitory role in the process of adipogenesis.
Subcellular location: Secreted {ECO:0000269|PubMed:21712809}.
Interaction partners:
- Activin receptor type-1B
Sequence:
MAPGPARISLGSQLLPMVPLLLLLRGAGCGHRGPSWSSLPSAAAGLQGDRDSQQSPGDAAAALGPGAQDMVAIHMLRLYEKYNRRGAPPGGGNTVRSFRARLEMIDQKPVYFFNLTSMQDSEMILTAAFHFYSEPPRWPRAREVFCKPRAKNASCRLLTPGLPARLHLIFRSLSQNTATQGLLRGAMALTPPPRGLWQAKDISSIIKAARRDGELLLSAQLDTGEKDPGVPRPSSHMPYILVYANDLAISEPNSVAVSLQRYDPFPAGDFEPGAAPNSSADPRVRRAAQVSKPLQDNELPGLDERPAPALHAQNFHKHEFWSSPFRALKPRTGRKDRKKKDQDTFTAASSQVLDFDEKTMQKARRRQWDEPRVCSRRYLKVDFADIGWNEWIISPKSFDAYYCAGACEFPMPKIVRPSNHATIQSIVRAVGIVPGIPEPCCVPDKMNSLGVLFLDENRNAVLKVYPNMSVETCACR
Protein: Protein STRUBBELIG-RECEPTOR FAMILY 8 (Leucine-rich repeat receptor kinase-like protein SRF8) (Q6R2J8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome b561 and DOMON domain-containing protein At3g61750
Sequence:
MAIGDRAMFTVLLLFIASISGFSVVRCVTDPSDVQALQVLYTSLNSPSQLTNWKNGGGDPCGESWKGITCEGSAVVTIDISDLGVSGTLGYLLSDLKSLRKLDVSGNSIHDTLPYQLPPNLTSLNLARNNLSGNLPYSISAMGSLSYMNVSGNSLTMSIGDIFADHKSLATLDLSHNNFSGDLPSSLSTVSTLSVLYVQNNQLTGSIDVLSGLPLKTLNVANNHFNGSIPKELSSIQTLIYDGNSFDNVPASPQPERPGKKETPSGSKKPKIGSEEKSSDSGKGLSGGVVTGIVFGSLFVAGIIALVLYLCLHKKKRKVRGSTRASQRSLPLSGTPEVQEQRVKSVASVADLKSSPAEKVTVDRVMKNGSISRIRSPITASQYTVSSLQVATNSFSQENIIGEGSLGRVYRAEFPNGKIMAIKKIDNAALSLQEEDNFLEAVSNMSRLRHPNIVPLAGYCTEHGQRLLVYEYVGNGNLDDTLHTNDDRSMNLTWNARVKVALGTAKALEYLHEVCLPSIVHRNFKSANILLDEELNPHLSDSGLAALTPNTERQVSTQVVGSFGYSAPEFALSGIYTVKSDVYTFGVVMLELLTGRKPLDSSRTRAEQSLVRWATPQLHDIDALSKMVDPSLNGMYPAKSLSRFADIIALCIQPEPEFRPPMSEVVQQLVRLVQRASVVKRRSSDDTGFSYRTPEHEHVDISF
Protein: rRNA 2'-O-methyltransferase fibrillarin (EC 2.1.1.-) (Histone-glutamine methyltransferase) (P35551)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ105me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889}. Note=Fibrillar region of the nucleolus.
Interaction partners:
- Uncharacterized WD repeat-containing protein C2E1P5.05
- Nucleolar protein 56
- Nucleolar protein 58
- 13 kDa ribonucleoprotein-associated protein
- U3 small nucleolar RNA-associated protein 22
- H/ACA ribonucleoprotein complex subunit cbf5
- U3 small nucleolar RNA-associated protein 21 homolog
- Periodic tryptophan protein 2 homolog
- Probable U3 small nucleolar RNA-associated protein 7
- U3 small nucleolar ribonucleoprotein protein mpp10
Sequence:
MAYTPGSRGGRGGSRGGRGGFNGGRGGFGGGRGGARGGGRGGARGGRGGRGGARGGRGGSSGGRGGAKGGAKVIIEPHRHAGVFIARGKEDLLVTRNLVPGESVYNEKRISVDSPDGTKVEYRVWNPFRSKLAAGILGGLDNIYIKPGARVLYLGAANGTSVSHVADVVGPEGLVYAVEFSHRSGRDLLNMAKKRTNVIPIVEDARHVQKYRMLVGMVDVVFADVAQPDQARIVALNAAAFLKNEGGVVISVKASCIDSTADAAVVFAREVKKMQEEKIKPQEQLTLEPYERDHCIIVGKYLRHQ
Protein: Kinetoplastid kinetochore protein 5 (Q57XA1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVARLRQYEQRHKIPHQPVVREASSTSRVACGVATNNVSLFPSSASLSAKTSRSQSVKPSIHKIPSRSLSLVQSVSSKTSTRKEMASLTREAAEMLNPTHRLKGLASIDVPDELFHGVEFAPPPQCFRPAWSLIGTFKTDVHTLVSVDTYEGSVKWYQQSPKGGFHRMCASTSVITSVQMANAEGSPLGEYLVVINTSIRPSRITFGFKKSTDARKMVVLLTPPPHHA
Protein: Probable secretory pathway GDP dissociation inhibitor 1 (Q10305)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- GTP-binding protein ypt1
- GTP-binding protein ryh1
- GTP-binding protein ypt3
- GTP-binding protein ypt2
- GTP-binding protein ypt5
- Ypt/Rab-type GTPase ypt7
- Nuclear control of ATPase protein 2
- Ypt/Rab-type GTPase ypt71
- GTPase-activating protein gyp7
Sequence:
MDEEYDVIVLGTGLTECVLSGLLSVDGKKVLHIDRNDYYGADSASLNLTQLYALFRPGEQRPESLGRDRDWCVDLVPKFLMANGDLTNILIYTDVTRYIEFKQIAGSYVYRDGRIAKVPGNEMEALKSPLMSLFEKRRAKKFLEWVNNYREDDPSTYKDINIDRDSMESVFKKFGLQSGTQDFIGHAMALYLDDAYLKKPARETRERILLYASSIAKFGKSPYIYPLYGLGELPQGFARLSAIYGGTYMLNQPVDEIVYGDDGVAIGVRSGDQVAKAKQIIGDPSYFREKVRSVGRLVRAICILNHPIPNTDNLDSVQIIIPQNQVKRKHDIYIAGISSVHNVCPKGYYLAIISTIVETANPLSEIAPGLKLLGPVVESFSRVQEIYEPVTDGTKDQCYISKSVDATSHFETLTCDVRDIYKRMTGTDLVLKQRPKMEDQ
Protein: Cruzioseptin-10 (CZS-10) (C0HK08)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
GFLDVLKGVGKAALGAVTHHINNLVNQQ
Protein: Insulin-like growth factor-1 (R4HZM2)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
GAELVDALQFVCGDRGFYFSKPTGYGSSSRRLHHKGIVDECCFQSCDLRRLEMYCAPIKPPKSARSVR
Protein: Dynamin-1 (EC 3.6.5.5) (B-dynamin) (D100) (Dynamin I) (Dynamin, brain) (P21575)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis (By similarity).
Subcellular location: [Isoform 2]: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:9725914}. Note=Strongly associated with clathrin-coated vesicles at the plasma membrane. {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: [Isoform 6]: Golgi apparatus {ECO:0000269|PubMed:9725914}. Note=Diffuse cytoplasmic distribution. {ECO:0000269|PubMed:9725914}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05193}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q05193}. Cytoplasmic vesicle {ECO:0000305|PubMed:17257598}. Presynapse {ECO:0000269|PubMed:9238017}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q08DF4}. Note=Associated to the membrane in a helical polymer shape in a GTP bound state. Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation. {ECO:0000250|UniProtKB:Q05193}.
Interaction partners:
- Dynamin-3
- Myc box-dependent-interacting protein 1
- Amphiphysin
- Endophilin-A1
- Hematopoietic lineage cell-specific protein
- Dynamin-2
- Mitochondrial fission 1 protein
- Intersectin-1
- Sorting nexin
- Clathrin heavy chain 1
Sequence:
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDLAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSEKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL
Protein: Reticulon-4 receptor-like 2 (Nogo receptor-like 3) (Nogo-66 receptor homolog 1) (Nogo-66 receptor-related protein 2) (NgR2) (Q80WD1)
Organism: Rattus norvegicus (Rat)
Function: Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG. Plays a functionally redundant role in postnatal brain development. Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum. Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system (By similarity). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG. Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development. Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660, ECO:0000269|PubMed:19420245}; Lipid-anchor, GPI-anchor {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7M6Z0}. Perikaryon {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660}. Cell projection, axon {ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660}. Membrane raft {ECO:0000269|PubMed:15673660}. Note=Localized to the surface of neurons, including axons (PubMed:12694398, PubMed:15673660). Detected close to synapses, but is excluded from synapses (By similarity). {ECO:0000250|UniProtKB:Q7M6Z0, ECO:0000269|PubMed:12694398, ECO:0000269|PubMed:15673660}.
Interaction partners:
- Reticulon-4
- Myelin-associated glycoprotein
- Paired Ig-like receptor B
- Neutrophil immunoglobulin-like receptor 1
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
Sequence:
MLPGLRRLLQGPASACLLLTLLALPPVTPSCPMLCTCYSSPPTVSCQANNFSSVPLSLPPSTQRLFLQNNLIRSLRPGTFGPNLLTLWLFSNNLSTIYPGTFRHLQALEELDLGDNRHLRSLEPDTFQGLERLQSLHLYRCQLSSLPGNIFRGLVSLQYLYLQENSLLHLQDDLFADLANLSHLFLHGNRLRLLTEHVFRGLGSLDRLLLHGNRLQGVHRAAFHGLSRLTILYLFNNSLASLPGEALADLPALEFLRLNANPWACDCRARPLWAWFQRARVSSSDVTCATPPERQGRDLRTLRDTDFQACPPPTPTRPGSRARGNSSSNHLYGVAEAGAPPADPSTLYRDLPAEDSRGRQGGDAPTEDDYWGGYGGEDQRGEQTCPGAACQAPADSRGPVLSAGLRTPLLCLLLLAPHHL
Protein: Filamin-A-interacting protein 1 (FILIP) (Q9CS72)
Organism: Mus musculus (Mouse)
Function: By acting through a filamin-A/F-actin axis, it controls the start of neocortical cell migration from the ventricular zone. May be able to induce the degradation of filamin-A.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7Z7B0, ECO:0000250|UniProtKB:Q8K4T4}.
Interaction partners:
- Filamin-A
- Rho-related GTP-binding protein RhoD
Sequence:
MRSRNQGGESSSNGHVSCPKPSIISSDGGKGPSEDAKKNKANRKGEDDVMASGTVKRHLKPSGESEKKTKKPLELSKEDLIQLLSIMEGELQAREDVIHMLKTEKTKPEVLEAHYGSAEPEKVLRVLHRDAILAQEKSIGEDVYEKPISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITYKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLSQRIEELEETNKSLQKAEEELQELRDKIAKGECGNSSLMAEVESLRKRVLEMEGKDEEITKTEAQCRELKKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSRSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKVELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYSLTKERDELMGKLRSEEERSCELSCSVDLLKKRLDGIEEVEREINRGRLCKGSEFTCPEDNKIRELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQMAKNKAIEKGEAVSQEAELRHRFRMEEAKSRDLQAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEETKNKNMGREVLNLTKELELSKRYSRALRPSGNGRRMVDVPVASTGVQTEAVCGDAAEEETPAVFIRKSFQEENHIMSNLRQVGLKKPMERSSVLDRYPPAANELTMRKSWIPWMRKRENGPSAPQEKGPRPNQGTGHPGELVLAPKQGQPLHIRVTPDHENSTATLEITSPTSEEFFSSTTVIPTLGNQKPRITIIPSPNVMSQKPKSADPTLGPERAMSPVTITTISREKSPEGGRGAFADRPASPIQIMTVSTSAAPPEIAVSPDSQEVPMGRTILKVTPEKQTVPTPMRKYNANANIITTEDNKIHIHLGSQFKRSPGPAAAEGVSPVITVRPVNVTAEKEVSTGTVLRSPRNHLSSRPGANKVTSTITITPVTTSSTRGTQSVSGQDGSSQRPTPTRIPMSKGMKAGKPVVAAPGAGNLTKFQPRAETQSMKIELKKSAASSTASLGGGKG
Protein: RE62495p (Q8SYH2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MICPKRTSELLDLHLAPFKDKDPAWEIGVSKIAGRGVVATRSLKRGEIIFRDSPLLIGLAAHEEDSLNACSVCLKMLPDTRFMCRQGCGLPVCSLCAKKKQHKSDCDLFKSWGPNEPDVANSVVIRLLCVARAINLSKEQRDLIYCLQANLDNNHRTEVRNAAKCFKNFPTDKKLIEIMNRTVAVLRTNGFDKTTDRTNDNQEFNYRALYPLFGVVNHDCIPNAYYTFEEKTNNMIVRAAVDIPEGFEVTTTYTKLFTGNIARHLFLKMKKSFTCKCSRCSDPTEKGAFISGLYCRDTNCAGLVVPEITGLPHPNWNCLVCKQKSTHAQMMKSQDFASGAINAKVNSNSLRTLVQYLNEKSDSFIPSSNYVVIDAKMSVLQRLQQGREDCSEELAHNTRLRYSRDITQLMDKLGLGDSLLRTHLEELLRREEERRAKRLADEAEKQRKLAELQAKAAEADKLLEVLQKEQSEQSEQAEPAGTADPGTAPAAPPVATAELA
Protein: Interleukin-1 receptor type I (Interleukin-1 receptor-like protein) (Interleukin-1 receptor-like protein precursor) (Q8QFN4)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Interleukin-1
- Interleukin-1
- Interleukin 1 receptor accessory protein
- Interleukin-1
- Myeloid differentiation primary response protein MyD88
- Interleukin-1 receptor type 1-like
- Interleukin-1 receptor-associated kinase 1-like isoform X1
- Interleukin-1 receptor type 1-like
- TNF receptor-associated factor 6-like
- TNF receptor-associated factor 6-like
Sequence:
MLGEFYIRFLSMTLLLHVSHGQEHQGAIEVHHISAGHFFQLKCSDYDDAEDQTTVTWSRGGNQTLNMTSGVEVRGEVLWFLPTHTSHNGHYTCESKYPNGSWEMKFVLSVDPGPCPVPAENRTVSQGMSEVVFCRQQDVLGLDPTAHIRWFKDCSPVDKHGETIIEEDGPKRLRLVNATESHAGVYTCLVEFSLQGGNYTATHSTQLKVNKEKVPLKPQVTYPRKETVTVEPGSRVELVCSAFLGVGEGTESESFMFWTVDGRHTDHIEQLNVTKTTILPRSSGVYGRSTLSIYEVRPEFLNVTISCIALNALGQDVGFLWLQPANHSGFYTCLCLCLAFSMVILGVAMCCLFKVDLVLAYRRLRPLVSKKRAPDGKLYDAYVSYVHGDGLSRAEMFALQVLPEVLERRYGYTLFVSGRDDLPGEAIHDVTSETMRRSRRLIIILSAQSVSPLHPKMDPEDQLPLHQSPQDSPSYDQQIGLYDALIQNGLRVVLVEIDGKVDYTSLPKSLHYIRRKQGALRWRRPSSGKSSSTAHPNGHFWKCLRYHMPFKPKGDLKPQLTPGINCSIELY
Protein: Succinate-semialdehyde dehydrogenase [NADP(+)] GabD (SSDH) (EC 1.2.1.79) (Glutarate-semialdehyde dehydrogenase) (EC 1.2.1.-) (P25526)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth. Also catalyzes the conversion of glutarate semialdehyde to glutarate, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Interaction partners:
- 4-aminobutyrate aminotransferase GabT
- Glutarate 2-hydroxylase
- L-2-hydroxyglutarate dehydrogenase
- 4-aminobutyrate aminotransferase PuuE
- Succinate semialdehyde dehydrogenase [NAD
- Gamma-aminobutyric acid permease
- 3-sulfolactaldehyde reductase
- Fumarate reductase flavoprotein subunit
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase iron-sulfur subunit
Sequence:
MKLNDSNLFRQQALINGEWLDANNGEAIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERATILRNWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGVPAGVFNVVTGSAGAVGNELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLDNGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHERGGNFFQPTILVDVPANAKVSKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIGL
Protein: Cholesteryl ester transfer protein (Lipid transfer protein I) (P11597)
Organism: Homo sapiens (Human)
Function: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL. Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination.
Subcellular location: Secreted {ECO:0000269|PubMed:24293641, ECO:0000269|PubMed:3281933}. Note=Secreted in plasma. {ECO:0000269|PubMed:3281933}.
Interaction partners:
- Apolipoprotein B-100
- Apolipoprotein A-I
- Phosphatidylcholine-sterol acyltransferase
- Apolipoprotein C-I
- Apolipoprotein F
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein A-II
- Serum paraoxonase/arylesterase 1
- Hepatic triacylglycerol lipase
Sequence:
MLAATVLTLALLGNAHACSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITASYLESHHKGHFIYKNVSEDLPLPTFSPTLLGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPKISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIVTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESVQSFLQSMITAVGIPEVMSRLEVVFTALMNSKGVSLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLS
Protein: Macrodomain Ter protein (P0A8N0)
Organism: Escherichia coli (strain K12)
Function: Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01073, ECO:0000269|PubMed:18984159}. Note=Accumulates in the cell as a discrete focus that colocalizes with the Ter macrodomain.
Interaction partners:
- Cell division protein ZapB
- Chromosome partition protein MukB
- Cell division protein ZapA
- Chromosome partition protein MukE
- Negative modulator of initiation of replication
- Nucleoid occlusion factor SlmA
- Chromosome partition protein MukF
- DNA translocase FtsK
- Cell division protein FtsZ
- Acyl carrier protein
Sequence:
MKYQQLENLESGWKWKYLVKKHREGELITRYIEASAAQEAVDVLLSLENEPVLVNGWIDKHMNPELVNRMKQTIRARRKRHFNAEHQHTRKKSIDLEFIVWQRLAGLAQRRGKTLSETIVQLIEDAENKEKYANKMSSLKQDLQALLGKE
Protein: Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)] (P47990)
Organism: Gallus gallus (Chicken)
Function: Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.
Subcellular location: Peroxisome {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:6953967}.
Interaction partners:
- Uncharacterized protein.
- Purine nucleoside phosphorylase
- Guanine deaminase
- Arylamine N-acetyltransferase, pineal gland isozyme NAT-10
- Hypoxanthine-guanine phosphoribosyltransferase
- Thiopurine S-methyltransferase.
- Arylamine N-acetyltransferase, liver isozyme
- Arylamine N-acetyltransferase, pineal gland isozyme NAT-3
- Hypoxanthine phosphoribosyltransferase
- Glutathione peroxidase
Sequence:
MAPPETGDELVFFVNGKKVVEKDVDPETTLLTYLRRKLGLCGTKLGCGEGGCGACTVMISKYDPFQKKILHHTANACLFPICALHHVAVTTVEGIGNTKSRLHPAQERIAKSHGSQCGFCTPGIVMSMYTLLRNKPKPKMEDIEDAFQGNLCRCTGYRPILEGYRTFAVDSNCCGKAANGTGCCHSKGENSMNGGCCGGKANGPGCCMNEKENVTMMSSSLFDSSEFQPLDPTQEPIFPPELMTQRNKEQKQVCFKGERVMWIQPTTLQELVALKSQYPNAKLVVGNTEVGIEMRLKNMLYPVILAPAWIPEMNAVQQTETGITFGAACTLSSVEEVLRKAVAELPSYKTEIFQAALEQLRWFAGPQIRNVAALGGNIMTASPISDLNPVLMASGSKLTLISMEGKRTVMMDEKFFTGYRKTIVKPEEVLLSVEIPYSKEGEYFSAFKQAYRREDDIAIVTCGMRVLFQHGTSRVQEVKLSYGGMAPTTILALKTCRELAGRDWNEKLLQDACRLLAGEMDLSPSAPGGMVEFRRTLTLSFFFKFYLTVLQKLSKDQNGPNNLCEPVPPNYISATELFHKDPIASTQLFQEVPRGQLVEDTVGRPLVHLSAAKQACGEAVYCDDIPHYENELYLTLVTSTQAHAKILSIDASEAQSVPGFVCFVSAKDVPGSNITGIANDETVFAEDVVTCVGHIIGAVIADTQEHSRRAAKAVKIKYEELKPIVTIQEAIEQQSFIKPIKRIKKGDVNKGFEESDHILEGEMHIGGQEHFYLETHCTLAVPKGEDGEMELFVSTQNLMKTQEFTASALGVPSNRIVVRVKRMGGGFGGKETRNTILTTVVAVAAFKTGRPVRCMLDRDEDMLISGGRHPFLGRYKVGFMKNGKIKSLEVSYYSNGGNSADLSHGVMDRALLHLDNSYNIPNVSIMGFICKTNLSSNTAFRGFGGPQGMMIAECWMSDLARKCGLPPEEVRKINLYHEGDLTHFNQKLEGFTLRRCWDECLSSSNYHARKKLIEEFNKQNRWKKRGMCIIPTKFGISFTVPFLNQAGALVHVYTDGSVLLTHGGTEMGQGLHTKMIQVASRSLGIPTSKIYISETSTNTVPNTSPTAASVSADINGMAVHNACQTILKRLEPIKQSNLKGSWEDWIKTAYENCISLSATGFYRIPDVGYNFETNKGKPFHYFSYGVACSEVEIDCLTGDHKNIRTDIVMDVGTSLNPAIDIGQIEGAFVQGIGLFTMEELRYSPEGNLYTRGPGMYKIPAFGDIPTEFYVSLLRDCPNSKAIYSSKAVGEPPLFLSASVFYAIKDAIYSAREDSGVTEPFRLDSPATPERIRNACVDTFTKMCPSAEPGTFKPWSVRA
Protein: Xanthine permease XanQ (P67444)
Organism: Escherichia coli (strain K12)
Function: Specific, proton motive force-dependent high-affinity transporter for xanthine.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16096267}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine/hypoxanthine permease GhxQ
- Putative purine permease YbbY
- Adenine permease AdeQ
- Guanine deaminase
- Adenine permease AdeP
- Guanine/hypoxanthine permease GhxP
- Uric acid transporter UacT
- Uncharacterized protein YgfM
Sequence:
MSDINHAGSDLIFELEDRPPFHQALVGAITHLLAIFVPMVTPALIVGAALQLSAETTAYLVSMAMIASGIGTWLQVNRYGIVGSGLLSIQSVNFSFVTVMIALGSSMKSDGFHEELIMSSLLGVSFVGAFLVVGSSFILPYLRRVITPTVSGIVVLMIGLSLIKVGIIDFGGGFAAKSSGTFGNYEHLGVGLLVLIVVIGFNCCRSPLLRMGGIAIGLCVGYIASLCLGMVDFSSMRNLPLITIPHPFKYGFSFSFHQFLVVGTIYLLSVLEAVGDITATAMVSRRPIQGEEYQSRLKGGVLADGLVSVIASAVGSLPLTTFAQNNGVIQMTGVASRYVGRTIAVMLVILGLFPMIGGFFTTIPSAVLGGAMTLMFSMIAIAGIRIIITNGLKRRETLIVATSLGLGLGVSYDPEIFKILPASIYVLVENPICAGGLTAILLNIILPGGYRQENVLPGITSAEEMD
Protein: ATP-dependent RNA helicase abstrakt (DEAD box protein abstrakt) (EC 3.6.4.13) (Q9V3C0)
Organism: Drosophila melanogaster (Fruit fly)
Function: ATP-dependent RNA helicase. Is essential for the directed and fasciculated early outgrowth of the bolwig nerves, as well as for its navigation at later stages. Is required during post-transcriptional gene expression. Plays a role during morphogenetic process, apoptosis and the establishment of cell polarity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAHVKRYRRSSKSSEEGDLDNEDYVPYVPVKERKKQHMIKLGRIVQLVSETAQPKSSSENENEDDSQGAHDVETWGRKYNISLLDQHTELKKIAEAKKLSAVEKQLREEEKIMESIAQQKALMGVAELAKGIQYEQPIKTAWKPPRYIREMSEEEREAVRHELRILVEGETPSPPIRSFREMKFPKGILNGLAAKGIKNPTPIQVQGLPTVLAGRDLIGIAFTGSGKTLVFVLPVIMFALEQEYSLPFERNEGPYGLIICPSRELAKQTHEIIQHYSKHLQACGMPEIRSCLAMGGLPVSEALDVISRGVHIVVATPGRLMDMLDKKILTLDMCRYLCMDEADRMIDMGFEEDVRTIFSFFKGQRQTLLFSATMPKKIQNFARSALVKPVTINVGRAGAASMNVTQQVEYVKQEAKVVYLLDCLQKTAPPVLIFAEKKQDVDCIHEYLLLKGVEAVAIHGGKDQEERSRAVDAYRVGKKDVLVATDVASKGLDFPNVQHVINYDMPDDIENYVHRIGRTGRSNTKGLATTLINKTTEQSVLLDLKHLLIEGKQEVPDFLDELAPETEHQHLDLGDSHGCTYCGGLGHRITECPKLEAVQNKQASNIGRRDYLSNTAADY