wanglab/gogpt-training-data huggingface dataset:
Protein: Anaphase-promoting complex subunit CDC26 (Anaphase-promoting complex subunit 12) (APC12) (Cell division cycle protein 26 homolog) (Q8NHZ8)
Organism: Homo sapiens (Human)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 15
- Anaphase-promoting complex subunit 13
- Cell division cycle protein 16 homolog
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 16
- Anaphase-promoting complex subunit 2
Sequence:
MLRRKPTRLELKLDDIEEFENIRKDLETRKKQKEDVEVVGGSDGEGAIGLSSDPKSREQMINDRIGYKPQPKPNNRSSQFGSLEF
Protein: Antigenic protein SchS21 (21 kDa secretory protein) (Alkaline exodeoxyribonuclease) (EC 3.1.11.-) (SchS21) (allergen Sta c 3.0101) (C7E9W0)
Organism: Stachybotrys chartarum (Toxic black mold) (Stilbospora chartarum)
Function: Has exodeoxyribonuclease activity with lambda-DNA and salmon testes dsDNA. No activity with circular plasmid DNA. The physiological role of this enzyme may be to degrade environmental DNA, and thus mobilize nitrogen for uptake.
Subcellular location: Secreted {ECO:0000269|PubMed:22424314}.
Interaction partners:
Sequence:
ASVTFWTLDNVDRTLVFTGNPGSAAIETITVGPAENTTVEFPGSWVGNWYAYPTDAEDVPGMLGEVQFGGWNGLTYFDVSAIVNPTDHDNVKQMWPAESRKPMSGCEVFPCDNAYWLPDDIQTKVTHEVDLWTTLGAGSTGLTF
Protein: Large ribosomal subunit protein eL37z (60S ribosomal protein L37-1) (Q8LFH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to the 23S rRNA.
Interaction partners:
- Large ribosomal subunit protein eL21x/eL21w
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS28x
- Large ribosomal subunit protein uL5y/uL5x/uL5w
- Large ribosomal subunit protein eL27z
- Large ribosomal subunit protein uL24c
- At1g43860
- Small ribosomal subunit protein eS28z/eS28y
Sequence:
MGKGTGSFGKRRNKSHTLCVRCGRRSFHIQKSRCSACAYPAARKRTYNWSVKAIRRKTTGTGRMRYLRNVPRRFKTCFREGTQATPRNKAAASSS
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Streptococcal surface enolase) (SEN) (Q5XD01)
Organism: Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:9603964}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:9603964}. Secreted, cell wall {ECO:0000269|PubMed:9603964}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface (PubMed:9603964). Once secreted, it remains attached to the cell surface (PubMed:9603964). {ECO:0000269|PubMed:9603964}.
Interaction partners:
Sequence:
MSIITDVYAREVLDSRGNPTLEVEVYTESGAFGRGMVPSGASTGEHEAVELRDGDKSRYLGLGTQKAVDNVNNIIAKAIIGYDVRDQQAIDRAMIALDGTPNKGKLGANAILGVSIAVARAAADYLEVPLYTYLGGFNTKVLPTPMMNIINGGSHSDAPIAFQEFMIMPVGAPTFKEGLRWGAEVFHALKKILKERGLVTAVGDEGGFAPKFEGTEDGVETILKAIEAAGYEAGENGIMIGFDCASSEFYDKERKVYDYTKFEGEGAAVRTSAEQVDYLEELVNKYPIITIEDGMDENDWDGWKVLTERLGKRVQLVGDDFFVTNTEYLARGIKENAANSILIKVNQIGTLTETFEAIEMAKEAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDQLGEVAQYKGIKSFYNLKK
Protein: F-box/LRR-repeat protein 2 (F-box and leucine-rich repeat protein 2) (Q8BH16)
Organism: Mus musculus (Mouse)
Function: Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin (By similarity). This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin (By similarity). Through CCND2 and CCND3 degradation induces cell-cycle arrest in G(0) (By similarity). SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy (By similarity). PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant. The SCF(FBXL2) complex acts as a regulator of inflammation by mediating ubiquitination and degradation of TRAF proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5 and TRAF6). The SCF(FBXL2) complex acts as a negative regulator of the NLRP3 inflammasome by mediating ubiquitination and degradation of NLRP3 (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9UKC9}; Lipid-anchor {ECO:0000250|UniProtKB:Q9UKC9}.
Interaction partners:
- S-phase kinase-associated protein 1
- Phosphatidylinositol 3-kinase regulatory subunit beta
- F-box only protein 3
- G1/S-specific cyclin-D3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- E3 ubiquitin-protein ligase MARCHF7
Sequence:
MVFSNSDDGLINKKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRVDLFNFQTDVEGRVVENISKRCGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDLTSCVSVTNSSLKGISEGCRNLEYLNLSWCDQITKEGIEALVRGCRGLKALLLRGCTQLEDEALKHIQNHCHELVSLNLQSCSRITDDGVVQICRGCHRLQALCLSGCSNLTDASLTALGLNCPRLQVLEAARCSHLTDAGFTLLARNCHELEKMDLEECVLITDSTLVQLSIHCPKLQALSLSHCELITDEGILHLSSSTCGHERLRVLELDNCLLVTDASLEHLENCRGLERLELYDCQQVTRAGIKRMRAQLPHVKVHAYFAPVTPPPAVAGSGHRLCRCCVIL
Protein: Copal-8-ol diphosphate hydratase TPSSA3, chloroplastic (8-hydroxycopalyl diphosphate synthase) (EC 4.2.1.133) (13-labden-8,15-diol pyrophosphate synthase TPSSA3) (SsLPS) (Diterpene synthase 1, chloroplastic) (SscTPS1) (Diterpene synthase Sa3) (SsTpsSa3) (G8GJ95)
Organism: Salvia sclarea (Clary sage)
Function: Involved in the biosynthesis of labdane-type diterpenoid including sclareol, a diterpene-diol that is used as fragrance and flavoring, and has anticancer effects (able to kill leukemic and colon cancer cells by apoptosis) (Probable). Sclareol can also be used as synthesis precursor of ambergris substitution fragance products such as ambrox (Probable). Terpene synthase that produces 8-hydroxycopalyl diphosphate from geranylgeranyl diphosphate (GGPP).
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:G8GJ96}.
Interaction partners:
Sequence:
MTSVNLSRAPAAITRRRLQLQPEFHAECSWLKSSSKHAPLTLSCQIRPKQLSQIAELRVTSLDASQASEKDISLVQTPHKVEVNEKIEESIEYVQNLLMTSGDGRISVSPYDTAVIALIKDLKGRDAPQFPSCLEWIAHHQLADGSWGDEFFCIYDRILNTLACVVALKSWNLHSDIIEKGVTYIKENVHKLKGANVEHRTAGFELVVPTFMQMATDLGIQDLPYDHPLIKEIADTKQQRLKEIPKDLVYQMPTNLLYSLEGLGDLEWERLLKLQSGNGSFLTSPSSTAAVLMHTKDEKCLKYIENALKNCDGGAPHTYPVDIFSRLWAIDRLQRLGISRFFQHEIKYFLDHIESVWEETGVFSGRYTKFSDIDDTSMGVRLLKMHGYDVDPNVLKHFKQQDGKFSCYIGQSVESASPMYNLYRAAQLRFPGEEVLEEATKFAFNFLQEMLVKDRLQERWVISDHLFDEIKLGLKMPWYATLPRVEAAYYLDHYAGSGDVWIGKSFYRMPEISNDTYKELAILDFNRCQTQHQLEWIHMQEWYDRCSLSEFGISKRELLRSYFLAAATIFEPERTQERLLWAKTRILSKMITSFVNISGTTLSLDYNFNGLDEIISSANEDQGLAGTLLATFHQLLDGFDIYTLHQLKHVWSQWFMKVQQGEGSGGEDAVLLANTLNICAGLNEDVLSNNEYTALSTLTNKICNRLAQIQDNKILQVVDGSIKDKELEQDMQALVKLVLQENGGAVDRNIRHTFLSVSKTFYYDAYHDDETTDLHIFKVLFRPVV
Protein: E3 ubiquitin-protein ligase Praja-2 (Praja2) (EC 2.3.2.27) (RING finger protein 131) (RING-type E3 ubiquitin transferase Praja-2) (O43164)
Organism: Homo sapiens (Human)
Function: Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes. Through the ubiquitination of MFHAS1, positively regulates the TLR2 signaling pathway that leads to the activation of the downstream p38 and JNK MAP kinases and promotes the polarization of macrophages toward the pro-inflammatory M1 phenotype. Plays a role in ciliogenesis by ubiquitinating OFD1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21423175}; Peripheral membrane protein {ECO:0000269|PubMed:21423175}. Golgi apparatus membrane {ECO:0000269|PubMed:21423175}; Peripheral membrane protein {ECO:0000269|PubMed:21423175}. Synapse {ECO:0000250|UniProtKB:Q63364}. Postsynaptic density {ECO:0000250|UniProtKB:Q63364}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:33934390}. Note=Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus (PubMed:21423175). Expressed in the postsynaptic density region of synapses (By similarity). Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane (PubMed:21423175). {ECO:0000250|UniProtKB:Q63364, ECO:0000269|PubMed:21423175}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D2
- Melanoma-associated antigen D1
- Malignant fibrous histiocytoma-amplified sequence 1
Sequence:
MSQYTEKEPAAMDQESGKAVWPKPAGGYQTITGRRYGRRHAYVSFKPCMTRHERSLGRAGDDYEVLELDDVPKENSSGSSPLDQVDSSLPSEPIFEKSETEIPTCGSALNQTTESSQSFVAVHHSEEGRDTLGSSTNLHNHSEGEYIPGACSASSVQNGIALVHTDSYDPDGKHGEDNDHLQLSAEVVEGSRYQESLGNTVFELENREAEAYTGLSPPVPSFNCEVRDEFEELDSVPLVKSSAGDTEFVHQNSQEIQRSSQDEMVSTKQQNNTSQERQTEHSPEDAACGPGHICSEQNTNDREKNHGSSPEQVVRPKVRKLISSSQVDQETGFNRHEAKQRSVQRWREALEVEESGSDDLLIKCEEYDGEHDCMFLDPPYSRVITQRETENNQMTSESGATAGRQEVDNTFWNGCGDYYQLYDKDEDSSECSDGEWSASLPHRFSGTEKDQSSSDESWETLPGKDENEPELQSDSSGPEEENQELSLQEGEQTSLEEGEIPWLQYNEVNESSSDEGNEPANEFAQPAFMLDGNNNLEDDSSVSEDLDVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDGLPETLVLEDHTAIGQEQCCPICCSEYIKDDIATELPCHHFFHKPCVSIWLQKSGTCPVCRRHFPPAVIEASAAPSSEPDPDAPPSNDSIAEAP
Protein: MOB kinase activator 3B (Mob1 homolog 2b) (Mps one binder kinase activator-like 2B) (MOB kinase activator-like 2B) (Q86TA1)
Organism: Homo sapiens (Human)
Function: Modulates LATS1 expression in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis.
Interaction partners:
Sequence:
MSIALKQVFNKDKTFRPKRKFEPGTQRFELHKRAQASLNSGVDLKAAVQLPSGEDQNDWVAVHVVDFFNRINLIYGTICEFCTERTCPVMSGGPKYEYRWQDDLKYKKPTALPAPQYMNLLMDWIEVQINNEEIFPTCVGVPFPKNFLQICKKILCRLFRVFVHVYIHHFDRVIVMGAEAHVNTCYKHFYYFVTEMNLIDRKELEPLKEMTSRMCH
Protein: Poly(A) binding protein cytoplasmic 1 (H0YAW6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQ
Protein: Urease accessory protein UreG (P18319)
Organism: Klebsiella aerogenes (Enterobacter aerogenes)
Function: Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01389, ECO:0000269|PubMed:9209019}.
Interaction partners:
Sequence:
MNSYKHPLRVGVGGPVGSGKTALLEALCKAMRDTWQLAVVTNDIYTKEDQRILTEAGALAPERIVGVETGGCPHTAIREDASMNLAAVEALSEKFGNLDLIFVESGGDNLSATFSPELADLTIYVIDVAEGEKIPRKGGPGITKSDFLVINKTDLAPYVGASLEVMASDTQRMRGDRPWTFTNLKQGDGLSTIIAFLEDKGMLGK
Protein: Receptor protein-tyrosine kinase (EC 2.7.10.1) (E7CXR8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MRPSGTARTKLLLLLAALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAVLSNYGTNKTGLRELPMRNLQEILIGAVRFSNNPILCNMETIQWRDIVQDVFLSNMSMDVQRHLTGCPKCDPSCPNGSCWGRGEENCQKLTKIICAQQCSRRCRGRSPSDCCHNQCAAGCTGPRESDCLVCHRFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEEDGVSKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGFLLIQAWPENWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKLFGTPNQKTKIMNNRAEKDCKATNHVCNPLCSSEGCWGPEPTDCVSCQNVSRGRECVDKCNILEGEPREFVENSECIQCHPECLPQTMNITCTGRGPDNCIKCAHYVDGPHCVKTCPSGIMGENNTLVWKFADANNVCHLCHANCTYGCAGPGLKGCQQPEGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMEEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSLSANSNSSTVACINRNGSCRVKEDAFLQRYSSDPTSVLTEDNIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLHPAPGRDLHYQNPHSNAVSNPEYLNTAQPTCLSSGFDSSALWIQKGSHQMSLDNPDYQQDFFPKEAKPNGIFKGPTAENAEYLRVAPPSSEFIGA
Protein: Leucine-rich repeat (LRR) family protein (F4K217)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MASRCELLLICVFSLLIAFAHSKTLKRDVKALNEIKASLGWRVVYSWVGDDPCGDGDLPPWSGVTCSTQGDYRVVTELEVYAVSIVGPFPIAVTNLLDLTRLDLHNNKLTGPIPPQIGRLKRLKVLYDPILFRVNLALTNLRWNKLQDVIPPEIGELKRLTHLYLSFNSFKGEIPKELAALPELRYLYLQENRLIGRIPAELGTLQNLRHLDVGNNHLVGTIRELIRFDGSFPALRNLYLNNNYLSGGIPAQLSNLTNLEIVYLSYNKFIGNIPFAIAHIPKLTYLYLDHNQFTGRIPDAFYKHPFLKEMYIEGNMFKSGVNPIGTHKVLEVSDADFAV
Protein: SIRP-beta B-type (Signal-regulatory protein beta 1A) (Q6F5F2)
Organism: Mus musculus (Mouse)
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Tyrosine-protein kinase SYK
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Leukocyte surface antigen CD47
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Predicted gene 5150
- Low affinity immunoglobulin gamma Fc region receptor III-A
Sequence:
MLLLDAWTHIPHSVLLLILLLGFKGAAVRELKVIQPVKSFFVGAGGSATLNCTVTSLLPVGPIRWYRGVGQSRLLIYPFTGEHSPRITNVSDVTKRNNMDFSIRISNVTPADSGTYYCVKFQRGSSEPDIEIQSGGGTELLVLAKPSSPMVSGPAARAVPQQTVTFTCRSHGFFPRNLTLKWFKNGDEISHLETSVEPEETSVSYRVSSTVQVVLEPRDVRSQIICEVDHVTLDRAPLRGIAHISEFIQVPPTLEIRQQPTMVWNVINVTCQIQKFYPPSFQLTWLENGNISRREVPFTLIVNKDGTYNWISCLLVNISALEENMVVTCKVEHDEQAEVIETHTVLVTEHQRVKELKTAGIAKIPVAVLLGSKILLLIAATVIYMHKKQNA
Protein: Actin-related protein 2 (Actin-like protein 2) (Actin-like protein C) (P53489)
Organism: Caenorhabditis elegans
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5
- Probable actin-related protein 2/3 complex subunit 3
- Probable actin-related protein 2/3 complex subunit 4
- Probable actin-related protein 2/3 complex subunit 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit
- CRIB domain-containing protein
- Probable actin-related protein 2/3 complex subunit 5
- SPIN90/Ldb17 leucine-rich domain-containing protein
- ADF-H domain-containing protein
Sequence:
MDSQGRKVIVVDNGTGFVKCGYAGTNFPAHIFPSMVGRPIVRSTQRVGNIEIKDLMVGEECSQLRQMLDINYPMDNGIVRNWDDMAHVWDHTFGPEKLDIDPKECKLLLTEPPLNPNSNREKMFQVMFEQYGFNSIYVAVQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFALHHLTRRLDIAGRDITKYLIKLLLQRGYNFNHSADFETVRQMKEKLCYIAYDVEQEERLALETTVLSQQYTLPDGRVIRLGGERFEAPEILFQPHLINVEKAGLSELLFGCIQASDIDTRLDFYKHIVLSGGTTMYPGLPSRLEKELKQLYLDRVLHGNTDAFQKFKIRIEAPPSRKHMVFLGGAVLANLMKDRDQDFWVSKKEYEEGGIARCMAKLGIKA
Protein: Deoxymugineic acid synthase 1-A (TaDMAS1) (EC 1.1.1.285) (W5DYE3)
Organism: Triticum aestivum (Wheat)
Function: Catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Dihydrodipicolinate reductase N-terminal domain-containing protein
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxy-tetrahydrodipicolinate reductase
- Serine aminopeptidase S33 domain-containing protein
Sequence:
MGAGDKTAAGMPRIGMGTAVQGPKPDPIRRAVLRAIEVGYRHFDTAAHYETEAPIGEAAAEAVRSGAVASRDDLFITSKLWCSDAHRDRVVPALRQTLRNLQMEYVDLYLVHWPVSMKPGRFKAPFTAEDFVPFDMRAVWEAMEECHRLGLAKAIGVANFSCKKLETLLSFATIPPTVNQVEVNPVWQQRKLREFCRGKGIQLCAYSPLGAKGTHWGSDAVMDAGVLQEIAASRGKSVAQVCLRWVYEQGDCLIVKSFDEARMRENLDVDGWELTEEEHRRIAEIPQRKINLGKRYVSEHGPYKSLEELWDGEI
Protein: Lipopolysaccharide heptosyltransferase 2 (EC 2.4.99.24) (ADP-heptose:lipopolysaccharide heptosyltransferase II) (ADP-heptose:LPS heptosyltransferase II) (Heptosyltransferase II) (P37692)
Organism: Escherichia coli (strain K12)
Interaction partners:
- ADP-L-glycero-D-manno-heptose-6-epimerase
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Lipopolysaccharide heptosyltransferase 1
- Bifunctional protein HldE
- Lipopolysaccharide core heptose
- O-antigen ligase
- Phosphoheptose isomerase
- Lipopolysaccharide glucosyltransferase WaaG
- 3-deoxy-D-manno-octulosonic acid transferase
- Lipopolysaccharide glucosyltransferase WaaO
Sequence:
MKILVIGPSWVGDMMMSQSLYRTLQARYPQAIIDVMAPAWCRPLLSRMPEVNEAIPMPLGHGALEIGERRKLGHSLREKRYDRAYVLPNSFKSALVPFFAGIPHRTGWRGEMRYGLLNDVRVLDKEAWPLMVERYIALAYDKGIMRTAQDLPQPLLWPQLQVSEGEKSYTCNQFSLSSERPMIGFCPGAEFGPAKRWPHYHYAELAKQLIDEGYQVVLFGSAKDHEAGNEILAALNTEQQAWCRNLAGETQLDQAVILIAACKAIVTNDSGLMHVAAALNRPLVALYGPSSPDFTPPLSHKARVIRLITGYHKVRKGDAAEGYHQSLIDITPQRVLEELNALLLQEEA
Protein: Ribosomal RNA-processing protein 14 (Ribosome biogenesis protein RRP14) (P36080)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in ribosome biogenesis and cell polarity. Required for the synthesis of both 40S and 60S ribosomal subunits and may also play some direct role in correct positioning of the mitotic spindle during mitosis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17804645}.
Interaction partners:
- rRNA-processing protein EBP2
- Ribosome biogenesis protein SSF1
- Ribosomal RNA-processing protein 1
- Ribosome production factor 1
- Ribosome biogenesis protein 15
- Ribosomal RNA-processing protein 15
- Ribosome biogenesis protein BRX1
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein RLP7
- Ribosome biogenesis protein NSA1
Sequence:
MSNSLEERLRANSSAFDGLLALIPAKYYYDEKSQEQWKAKKKTKEQSKNDKLKKLDPEQRDDETSSTLEVMKKKEKDAKPVVLPGEKFKHMKMQKQKEATSKVEGDSDLNVEVNDPMIIAPDEDEEEEEDIKVIFDDEGNEIPLESKKDTTEPDRSVEKKSITEEEKLQRKKNLEALRSKLQAKISDMKSKRKAPGSREAILAQRKRKEELKKRKRLESEQEQDQDEIASDSDMEDIDSDLENNSKKRFKKGKKDSEINADGVMFQNIIFDDGARATSDLQRLRKAGRTKGPAKNDVKSHLKLLEAKKNKMEAKDELEQIKQKEKEKWQKAMLQAEGIKIRDDEKLLRKAIKRKEAQKRKSAIEWSERKRVVEDTISERQKRREENLRIRKDNKGKKRNKQEKMKRKYVGSAVPKKRAGFEGRLKTGKKKGGPK
Protein: FI22004p1 (Q9W0D6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Eukaryotic translation release factor 3, isoform A
Sequence:
MSVIIRLQNLPWTANARDIRNFFSGLSIPEGGVHIIGGEMGDAFIAFSTDEDARCAMLKDREKLMEIQVRLLLSSRAEMQKVIETARKAASAQAPVSVPVPMPVVVPVTAAKVAGPAAPLPPIIGGLNTFLGQGQVKGVATGTVPSFLTYQQQAGITLSDVTGRRSRSRSSSSDDSDRERERDRQRERERGRKRRSDRLDKSQERELKMVAGGGALPSPWAQPPQNQLPAVGLGLNMGLNLNLPQIPSLQSYTTSTTTTNVTNNYNLEPSATSVQLLTALQQVSSGSAAPAQPSKSESEPIAFASVNPYAQMYPQLFQQQQMLLQQQQTQAKVSPTMGGSPGGGSTPQVVADTCYIRMSGMCQNTSYSDIRKYFQGMYIPHNGIKIMMVNGSRTGVAYVEFSRVSSAQKAVQRNNTMFRDRLIQIVPVGDDEFEMAEERASRQGQDGSRSHGNHNGGDRGERGGGAPVPVPRPVTNVLYIEDLPQTTTEQDIMKMFSASYTVVDILLSPSPKNRRESVAFVLFAREAEADSALQDTSKHYIGFRQLRVRSSSEEDMQNAKEKQRRANEQLLKEEADQREELLKDQQRRQKQQQQENENIQANRFAADPRRRQAEDQQQQQQMNMGPNFNSNMSPNMMAPFVNGGNMPFHMPPLQQNGVNNFPFNMNNNYNYNGNSNGNGPNYPNDNGGAGVIQRPRQEDVFVRVHNCEYATRANDLGELFSLEHLRIEHIEQLFNERNQSSGEFIVEFSDPASCKLAIREFHNRRFRGRGLRVVAITPQEIADRMKKPFMDYLPGGNGPRKAETNNANDGAGGNKASAQPSRRRGPSRFDKPQEQPSQQQDRPLSLEREDNSSTSSNAPVKQHFNPFARPDPPLSSSSLSPSNQGQVKPTSPVPVPTSIIPDKFNRPGCVVAMRNVPFKAELKDIMRFFSDYKLSPDDIIRRFNDEGKPTGDTRVAFESPSEARSAFESRRKKQIFNRTVYLDII
Protein: ElaC ribonuclease Z 1 (K7EIJ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMDVTFLGTGAAYPSPTRGASAVVLRCEGECWLFDCGEGTQTQLMKSQLKAGRITKIFITHLHGDHFFGLPGLLCTISLQSGSMVSKQPIEIYGPVGLRDFIWRTMELSHTELVFHYVVHELVPTADQCPAEELKEFAHVNRADSPPKEEQGRTILLDSEENSYLLFDDEQFVVKAFRLFHRIPSFGFSVVEKKRPGKLNAQKLKDLGKCFFVFCFFPPSHQ
Protein: Brivido-3, isoform B (Q9W4X5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKVKKTHWAMFAITVGIIIGCMICIAVFAGFQHEDVKFKTMLVSIVIVLIFQFLIGDPIKFVILSIDRALWPPRIYIPPRCDKDEMDEKEERRDFLKQRLINKRANLMLTSRYRNYKLNDQYKMIAHDLFIYGPYFLCLMCLVLVTRDQTLYHNTRIITDLFMYNHTDYTGLQEVYFLNQLFDFIESTLVLAFNSNSTESGSPGWAHAEQSVLLGVMRLRQLRVSNPQVGLGPPKFSDTYYMPDWQLPYRKLHYSDKYWRIYEPWIPIKMGFEFLDALLMNFDHVGSLNSYPELAGYVSLLARSAANSMKVIDYLSENHWLTLNTSAVFIDFTLYNVDVNLFSICTLRVEKTPFGGIVPDVQVDSAKLLENVDQMPYTGLLALLIYVLVFIQFAQTLAVKLWYEPHLLKSVWNKLDLFIFMVNVLVVVLVVLRESLVASMMKKVEGASKMEFIDFRRPSRMHQLTTITIGFLICITTLRLWRVLQFASVFKLFTRTLYLAWSAVASTAIAIVIFLIGFCFAVVTINGNYSSNFNKLVKSMVMCMCYSFGFSAQVKPSELFHGGKWLGILCYGVLAFVIIVLLINVFVSLINDYFTVAKTIRDSERENRITFFEFLVVEFSGVLGRFRKLPCWRRNYVRNGRTVAENVSRKLDSMDRQRLMRRRLRQGRHHLTLIRMFLFDEYVEWPQEQQKQPEAQDPDPNLGPDGSPPQDKRQDEAEA
Protein: Endothelin-1 receptor (Endothelin receptor type A) (ET-A) (ET-AR) (P26684)
Organism: Rattus norvegicus (Rat)
Function: Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Endothelin-3
- Endothelin-1
- Endothelin-2
- Angiotensinogen
- Endothelin receptor type B
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Kininogen-1
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-13
Sequence:
MGVLCFLASFWLALVGGAIADNAERYSANLSSHVEDFTPFPGTEFNFLGTTLQPPNLALPSNGSMHGYCPQQTKITTAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLITAIEIVSIWILSFILAIPEAIGFVMVPFEYKGEQHRTCMLNATTKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYDEMDKNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCHQSKSLMTSVPMNGTSIQWKNQEQNHNTERSSHKDSMN
Protein: Ribosomal RNA-processing protein 43 (Q8MPG3)
Organism: Trypanosoma brucei
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MSLPPATGAVELASFQQHVHQFLVQNKRLDGRPLDALREPHILRDSKGGDGLLASTLYTDNTGMCLNCTVSGVFGPPPSDQPDEGRLTVDVAAPFFQSHSTDQVAAALREVARFVRSTIISCMDLTELNIINGEACWVLQVELVILNADGGLRAAALHAVVAAIHNMLLPRSRLPNGDEVESRRLRFHTIPVAVTIGVYKLGASGVRFLMDTNAAEESVVDGLLTVVLSDENGIITFVQSGSYSISSLLLTGAVNEFALRSAALRAAILKPSVAAAKINGSKNSVTDPHPLKEG