wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-21 receptor (IL-21 receptor) (IL-21R) (Novel interleukin receptor) (CD antigen CD360) (Q9HBE5)
Organism: Homo sapiens (Human)
Function: This is a receptor for interleukin-21.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-21
- Cytokine receptor common subunit gamma
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 3
- Interleukin-4
- Interleukin-7
- Tyrosine-protein kinase JAK3
- Interleukin-15
- Interleukin-2
- Interleukin-6
Sequence:
MPRGWAAPLLLLLLQGGWGCPDLVCYTDYLQTVICILEMWNLHPSTLTLTWQDQYEELKDEATSCSLHRSAHNATHATYTCHMDVFHFMADDIFSVNITDQSGNYSQECGSFLLAESIKPAPPFNVTVTFSGQYNISWRSDYEDPAFYMLKGKLQYELQYRNRGDPWAVSPRRKLISVDSRSVSLLPLEFRKDSSYELQVRAGPMPGSSYQGTWSEWSDPVIFQTQSEELKEGWNPHLLLLLLLVIVFIPAFWSLKTHPLWRLWKKIWAVPSPERFFMPLYKGCSGDFKKWVGAPFTGSSLELGPWSPEVPSTLEVYSCHPPRSPAKRLQLTELQEPAELVESDGVPKPSFWPTAQNSGGSAYSEERDRPYGLVSIDTVTVLDAEGPCTWPCSCEDDGYPALDLDAGLEPSPGLEDPLLDAGTTVLSCGCVSAGSPGLGGPLGSLLDRLKPPLADGEDWAGGLPWGGRSPGGVSESEAGSPLAGLDMDTFDSGFVGSDCSSPVECDFTSPGDEGPPRSYLRQWVVIPPPLSSPGPQAS
Protein: Ras-related protein Rap-1A (EC 3.6.5.2) (C21KG) (G-22K) (GTP-binding protein smg p21A) (Ras-related protein Krev-1) (P62834)
Organism: Homo sapiens (Human)
Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11359771}; Lipid-anchor {ECO:0000269|PubMed:11359771}. Cytoplasm {ECO:0000269|PubMed:11359771}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11359771}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Note=Recruited from early endosome to late endosome compartment after nerve growth factor (NGF) stimulation. Localized with RAPGEF2 at cell-cell junctions (By similarity). Colocalized with RAPGEF2 in the perinuclear region. {ECO:0000250}.
Interaction partners:
- Krev interaction trapped protein 1
- Ral guanine nucleotide dissociation stimulator
- RAF proto-oncogene serine/threonine-protein kinase
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Rap guanine nucleotide exchange factor 2
- Rap guanine nucleotide exchange factor 4
- RAS guanyl-releasing protein 2
- Ras association domain-containing protein 5
- Rap guanine nucleotide exchange factor 6
- Serine/threonine-protein kinase B-raf
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL
Protein: Glutathione S-transferase theta-3 (EC 2.5.1.18) (Q99L20)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows high activity towards 4-nitrobenzyl chloride (4-NBC). Also has lower activity towards 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP), cumene hydroperoxide, 1-chloro-2,4-dinitrobenzene (CDNB), 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), and ethacrynic acid.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S-transferase A3
- Glutathione S-transferase Mu 6
- Glutathione S-transferase Mu 1
- Glutathione S-transferase Mu 5
- Cytochrome P450 2C54
- Glutathione S-transferase Mu 2
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase A4
- Glutathione S-transferase Mu 4
Sequence:
MGLELYLDLMSQPCRAVYIFAKKNGIPFQLRTIELLKGQQYTDSFAQVNPLRKVPALKDGDFVLAESVAILLYLSRKYKAPDHWYPQDLQTRARVDEYLAWQHTALRSCCTRAMWQKMMFPVFLGQPVPPEMLASTLAELDGCLQVLEDKFLRNQAFLTGSHISVADLVAITELMHPVSAGCKIFESRPKLAAWRQRVEAEVGESLFQEAHEVVLKAKDMPPLMDPALKEKLKLSVQCLLH
Protein: Galectin-3 (Gal-3) (35 kDa lectin) (Carbohydrate-binding protein 35) (CBP 35) (Galactose-specific lectin 3) (IgE-binding protein) (Laminin-binding protein) (Lectin L-29) (Mac-2 antigen) (P08699)
Organism: Rattus norvegicus (Rat)
Function: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes (By similarity). Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P17931}. Nucleus {ECO:0000250|UniProtKB:P17931}. Secreted {ECO:0000250|UniProtKB:P17931}. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P17931}.
Interaction partners:
- Galectin-3-binding protein
- Mucin-1
- Receptor-type tyrosine-protein phosphatase C
- C-type lectin domain containing 7A
- Lymphocyte activation gene 3 protein
- Tripartite motif-containing 16
- Toll-like receptor 4
- Receptor protein-tyrosine kinase
- Toll-like receptor 2
- Low affinity immunoglobulin gamma Fc region receptor II
Sequence:
MADGFSLNDALAGSGNPNPQGWPGAWGNQPGAGGYPGASYPGAYPGQAPPGGYPGQAPPSAYPGPTGPSAYPGPTAPGAYPGPTAPGAFPGQPGGPGAYPSAPGAYPSAPGAYPATGPFGAPTGPLTVPYDMPLPGGVMPRMLITIIGTVKPNANSITLNFKKGNDIAFHFNPRFNENNRRVIVCNTKQDNNWGREERQSAFPFESGKPFKIQVLVEADHFKVAVNDVHLLQYNHRMKNLREISQLGIIGDITLTSASHAMI
Protein: IFITM2 protein (Interferon induced transmembrane protein 2 (1-8D)) (Q6IBB0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MNHIVQTFSPVNSGQPPNYEMLKEEQEVAMLGAPHNPAPPTSTVIHIRSETSVPDHVVWSLFNTLFMNTCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGIFMTILLVIIPVLVVQAQR
Protein: cDNA, FLJ92974, highly similar to Homo sapiens methylmalonic aciduria (cobalamin deficiency) type B(MMAB), mRNA (B2R6J3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVCGLGSRLGLGSRLGLQGCFGAARLLYPRFQSRGPQGVEDGDRPQPSSKTPRIPKIYTKTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFALELVTEKGHTFAEELQKIQCTLQDVGSALATPCSSAREAHLKYTTFKAGPILELEQWIDKYTSQLPPLTAFILPSGGKISSALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTLARYAAMKEGNQEKIYKKNDPSAESEGL
Protein: Outer dynein arm-docking complex subunit 4 (Tetratricopeptide repeat protein 25) (TPR repeat protein 25) (A5PK42)
Organism: Bos taurus (Bovine)
Function: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}.
Interaction partners:
- Outer dynein arm-docking complex subunit 2
- Outer dynein arm-docking complex subunit 3
- Outer dynein arm-docking complex subunit 1
- Calaxin
- Methyl-CpG-binding domain protein 1
- Tektin-1
- EF-hand domain-containing family member C2
- Cilia and flagella associated protein 45.
- Tektin bundle-interacting protein 1
- Tektin-3
Sequence:
MADPENEVLRSTFPSYMAEGERLYLCGEFAKAAHSFSNALHLQSGDKNCLVARSKCFLKMGELEKSLEDAEASLQGDPTFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPDREFKVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAESMRAQQKPHPVRQLIHHPKRESKRKGSLKSEKIVRQLLGELYVDKEYLEKLLLDEDLIKGTIKHGLTVEDLIMTGINYLETRSDFWRQQKPIYARERDRKLMQEKWLRDRKRRPSQTARYILKSLEDIDMLLTSGSAEGSLQKAEKVLKKVLEWNKEEVPNKDELVGNLYSCIGNAQIELGQMVAALQSHRKDLEIAKEYDLPDAKSRALDNIGRVFARVGKFQQAIDTWEEKIPLAKTTLEKTWLFHEIGRCYLELDQAWEAQSYGEKSQQCAEEEGDMEWQLNASVLVAQAQVKLRDFESAVNNFEKALERAKLVHNNEAQQAIINALDDANKGIIEELKKTNYREILKEKKEKENATMLDGQTRTAKEKETRKTKDEPEKVMKQWVQEQTEKQLEGVLSKETLGVTARQPEQRQREDPEKASWRKELGAKERGPGDTAKGQFGEAGRTEQNREETREIYRRPSELDQNLSDESSPRESEGLEKRLSKTDGGELEALGKTESGEIKEMEITENSEKIEKDEKEDEPIE
Protein: Myosin light chain kinase 3 (EC 2.7.11.18) (Cardiac-MyBP-C-associated Ca/CaM kinase) (Cardiac-MLCK) (E9PT87)
Organism: Rattus norvegicus (Rat)
Function: Calmodulin-dependent kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes. Increases cardiomyocyte contractility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17885681}.
Interaction partners:
- Calmodulin-like protein 4
- Calmodulin-1
- Myosin regulatory light chain RLC-A
- Myosin light polypeptide 6
- Calmodulin-like protein 3
- Myosin regulatory light polypeptide 9
- Myosin regulatory light chain 12B
- Myosin light chain 4
- Myosin light chain 3
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MSGVSEEDPEGLGPQGLPALGGACLVTVDKKLNVLTEKVDRLLHFQEDVTEKLQCVCQGMDHLEQGLHRLEASQELGLAGPGSTSPAAAQAAWPEVLELVRAVRQEGAQHGARLEALFKMVVAVDRAITLVGSTIQNSKVDDFILQGTVPWRKGSLADGPEENKEQAEVAGVKPKHVLNTGSVQAATSRALWEESQKQDTPVGTVEGLPLIIDTSLKGADLTQAGASLRQGVEALDPGQEPPPTEAESRLPALASEDTGTTLELSVAIDRISEVLTSLRMSQSAGEGTSSSKPDCSEPGPQPLGPLTTDSDIHSDEGLPRISVRMREMTTPEELFETQGGSPIGSAEAPGPGTVLEDQIPKGARPFPPLPKRSCNNGGASAEEATGPGAEPIRGPSLVTRDWRDEPVGTTDLQQGRDPGAVSPEPGKDHAAQGPGRTEAGRRVSSAAEAAIVVLDDSAAPPAPFEHRVVSIKDTLISTSYTVSQHEVLGGGRFGQVHRCTERSTGLALAAKIIKVKNIKDREDVKNEINIMNQLSHVNLIQLYDAFESKNSFTLIMEYVDGGELFDRITDEKYHLTELDVVLFTRQICEGVHYLHQHYILHLDLKPENILCVSQTGHQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYEFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNFIVNCSWDFDADTFKGLSEEAKDFVSRLLVKEKSCRMSATQCLKHEWLNHLIAKASGSNVRLRSQLLLQKYMAQRKWKKHFHVVTAVNRLRKFPTCP
Protein: Protein yippee-like 5 (Q65Z55)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Function: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (By similarity). Required for normal cell proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:20580816}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20580816}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20580816}. Midbody {ECO:0000269|PubMed:20580816}. Note=Deteted in nucleus and at the centrosome during interphase. During mitosis, detected on the mitotic spindle, at spindle poles and at the midbody. {ECO:0000269|PubMed:20580816}.
Interaction partners:
Sequence:
MGRIFLDHIGGTRLFSCANCDTILTNRSELISTRFTGATGRAFLFNKVVNLQYSEVQDRVMLTGRHMVRDVSCKNCNSKLGWIYEFATEDSQRYKEGRVILERALVRESEGFEEHVPSDNS
Protein: Alkaline ceramidase 3 (AlkCDase 3) (Alkaline CDase 3) (EC 3.5.1.-) (EC 3.5.1.23) (Alkaline dihydroceramidase SB89) (Alkaline phytoceramidase) (aPHC) (Q9NUN7)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum and Golgi ceramidase that catalyzes the hydrolysis of unsaturated long-chain C18:1-, C20:1- and C20:4-ceramides, dihydroceramides and phytoceramides into sphingoid bases like sphingosine and free fatty acids at alkaline pH. Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation. Controls the generation of sphingosine in erythrocytes, and thereby sphingosine-1-phosphate in plasma. Through the regulation of ceramides and sphingosine-1-phosphate homeostasis in the brain may play a role in neurons survival and function (By similarity). By regulating the levels of pro-inflammatory ceramides in immune cells and tissues, may modulate the inflammatory response (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11356846}; Multi-pass membrane protein {ECO:0000269|PubMed:11356846, ECO:0000269|PubMed:30575723}. Golgi apparatus membrane {ECO:0000269|PubMed:11356846}; Multi-pass membrane protein {ECO:0000269|PubMed:11356846, ECO:0000269|PubMed:30575723}.
Interaction partners:
- Neutral ceramidase
- Acid ceramidase
- Sphingosine kinase 1
- Sphingosine kinase 2
- Ceramide synthase 6
- Ceramide synthase 2
- Ceramide synthase 3
- Ceramide synthase 5
- Ceramide synthase 4
- Sphingolipid delta
Sequence:
MAPAADREGYWGPTTSTLDWCEENYSVTWYIAEFWNTVSNLIMIIPPMFGAVQSVRDGLEKRYIASYLALTVVGMGSWCFHMTLKYEMQLLDELPMIYSCCIFVYCMFECFKIKNSVNYHLLFTLVLFSLIVTTVYLKVKEPIFHQVMYGMLVFTLVLRSIYIVTWVYPWLRGLGYTSLGIFLLGFLFWNIDNIFCESLRNFRKKVPPIIGITTQFHAWWHILTGLGSYLHILFSLYTRTLYLRYRPKVKFLFGIWPVILFEPLRKH
Protein: Type IV secretion system protein VirD4 (Q2GIA7)
Organism: Anaplasma phagocytophilum (strain HZ)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Type IV secretion system protein VirB10
- Type IV secretion system protein
- Type IV secretion protein VirB8-1
- Type IV secretion system protein VirB9
- Type IV secretion system protein VirB9-2
- Type IV secretion system protein virB4
- Type IV secretion system protein VirB4-2
- Type IV secretion system protein VirB3
- DNA topoisomerase 1
- Type IV secretion system protein VirB6 family
Sequence:
MHSSNHIRNILVFFCGLFCLLEFCFYISGVLFVLLVWGVDYLDFNAINPSVSDFPMRLWPTIFQYISKWWGDPKLFGIANSLKLWGSFFAPIGLVCLVAWNLRHVLIDWRPFKKKESLHGDSRWASERDIRKIGLRSRRGILLGKDQRGYLVADGYQHALLFAPTGSGKGVGFVIPNLLFWEDSVIVHDVKLENYDLTSGWRKKIGQEVYVWNPAQPDGISHCYNPLDWISKKPGQMVDDVQKIANLIMPEQDFWYNEARSLFVGVVLYLLAVPEKVKSFGEVVRTMRSDDVVYNLAVVLDTIGKKIHPVAYMNIAAFLQKADKERSGVISTMNSSLELWANPLIDTATASSDFNIQDFKRKRVSVYVGVTPDNLTRLRPLMQVFYQQATEFLCRTLPSDDEPYGVLFLMDEFPTLGKMEQFQTGIAYFRGYRVRLFLIIQDTEQLKGIYEEAGMNSFLSNSTYRITFAANNIETANLISQLIGNKTVSQESLNRPKFLDLNPASRSLHISDTQRALLLPQEVIMLPKDEQILLIESTYPIKSRKIKYFEDKTFTRRLLKSTFIPTQEPYDPEKIRGGVEGEAGIVSEASENSEDLKALMGSSSAENPPERAEYGYEDDGDLVDREEFEDLYGIGEEPEDDLEDLDESDDYFHDEDDVLNDEDYDDPYEDDMELEGDGDWDENEAFEDELLDDEVVDDEFDSLEPEEDEDFEEDDSLEEEDEFGEDRPTDDNDSSNGRLK
Protein: At1g05070/T7A14_6 (Transmembrane protein, putative (DUF1068)) (Q94AB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At3g06530
- rRNA biogenesis protein RRP5
- Nucleolar-like protein
- Protein SLOW WALKER 1
- Nucleolar protein
- KRR1 small subunit processome component
- F18K10.11 protein
- Putative WD-repeat membrane protein
- Probable U3 small nucleolar RNA-associated protein 11
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
Sequence:
MARHTAALKIGLALLGLSMAGYILGPPLYWHLTEALAAVSASSCPSCPCECSTYSAVTIPKELSNASFADCAKHDPEVNEDTEKNYAELLTEELKLREAESLEKHKRADMGLLEAKKVTSSYQKEADKCNSGMETCEEAREKAELALAEQKKLTSRWEERARQKGWREGSTKPNVKSKSNVQVA
Protein: Sol narae, isoform C (EC 3.4.24.-) (B7YZP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSPLVLFTALLLVSSTICQGLPDLHKQMTPEQLQSVFHVDTHDAVPHYELVQLQHHENNHNRRRRSIGKGPKVNAALPPHHVKKDLSKNAYYSELKHEALASGGNHLFAPEVSAIKSHNVSFSAFGQHLNLSLRATQGLFKGAPHQLRMWTVGSEPNATHGLDLQEIVHEQHTSNDVGEVFQDEKNMAAILMRRHMETGDLIMEGSIGHDLVIKPLPHELSPNPEESHHIIYKREASAAEGQLSDFAFMEPDDLLASEKLERLQRRQRRSRRSAPSSPDFEDLNDEDEGALDGEPQVAESRTRSRRQAPYIIYPEVLVIVDYDGYRLHGGDNLQVKRYFISFWNGVDLRYRLLKGPRIRISIAGIIISRGRDATPYLERNRVGRDAIDSAAALTDMGKYLFRERRLPVYDIAVAITKLDMCRRTSAYGECNRGTAGFAYVGGACVVNKRLEKVNSVAIIEDTGGFSGIIVAAHEVGHLLGAVHDGSPPPSYLGGPGAQRCRWEDGYIMSDLRHTERGFRWSACTVQSFHHFLNGDTATCLHNAPHEDSALGRSLPGTLLSLDAQCRRDRGTYACFKDERVCAQLFCFDAQTGYCVAYRPAAEGSACGNGYHCLDGRCTPLPSNIIPDYGHNYRLVYNKIDNKKDAAEDVESSSEETESQEDETESVEDQDEGTTSSEEQEDNKIEQSSAAGGAAAQSTTTARSTTTTTVRTTSTTTTTAKPKSKSFGYLHRSLPERQWMQDNGVLVTTRISSSVSSSSSGSSSGEAAATSTRRPTTTTTTQTPNLFQIYTHELRKQIEYYLHMLQTQQHATKFQPEQQQQQSQQQQSIVEIPLVQKSLTNYSVTSSSSSTSNGAKQQPPSNKDENQRQQQQQQQAQQQLQDGLPDEENEATAGIQSNEAIERQKRKFPTTPTAATSAAQKSATPATPATSATSARPTPTTAKPITTSSFLDAYFKKLQALHDAGSASSSTTTTTTTSVSSSVSSATSSKQQHPQQQQQQQVQQIADGSHFLKRTPHRSSLKAYKTSSSSSNNSSSQTQQQQQQQQQQYATNYIGDTTNNQPAVLDNSGSASSTTETAKKPKIKTQKLIRRTRVMQTQTQTI
Protein: ACB domain-containing protein (Q57Y52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSAQFEAATEFVRSLPKDGPVQLTDAEKLQFYALFKQATEGPVTDPQPWAVQLEKRSKWDARKAISDMSKEDAMKKYVELLVEKTANTANPWKPPQ
Protein: Fumarate hydratase class II (Fumarase C) (EC 4.2.1.2) (Aerobic fumarase) (Iron-independent fumarase) (P05042)
Organism: Escherichia coli (strain K12)
Function: Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305}.
Interaction partners:
- Malate dehydrogenase
- Fumarate hydratase class I, aerobic
- Fumarate hydratase class I, anaerobic
- DNA gyrase subunit B
- NADP-dependent malic enzyme
- Succinate dehydrogenase flavoprotein subunit
- Protein RecA
- Citrate synthase
- Adenylate kinase
- NAD-dependent malic enzyme
Sequence:
MNTVRSEKDSMGAIDVPADKLWGAQTQRSLEHFRISTEKMPTSLIHALALTKRAAAKVNEDLGLLSEEKASAIRQAADEVLAGQHDDEFPLAIWQTGSGTQSNMNMNEVLANRASELLGGVRGMERKVHPNDDVNKSQSSNDVFPTAMHVAALLALRKQLIPQLKTLTQTLNEKSRAFADIVKIGRTHLQDATPLTLGQEISGWVAMLEHNLKHIEYSLPHVAELALGGTAVGTGLNTHPEYARRVADELAVITCAPFVTAPNKFEALATCDALVQAHGALKGLAASLMKIANDVRWLASGPRCGIGEISIPENEPGSSIMPGKVNPTQCEALTMLCCQVMGNDVAINMGGASGNFELNVFRPMVIHNFLQSVRLLADGMESFNKHCAVGIEPNRERINQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAALALGYLSEAEFDSWVRPEQMVGSMKAGR
Protein: dynamin GTPase (EC 3.6.5.5) (Q6P122)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGNRGMEDLIPLINKLQDAFSSIGQSCNLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLVNSKAEYAEFLHCKGRKFVDFDEVRMEIEAETDRITGSNKGISAVPINLRVYSPNVLNLTLIDLPGMTKVAVGDQPQDIEYQIRDMLMQFISKENCLILAVTPANMDLANSDALKISKEVDAQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQKDIDGRKDIRAALAAERKFFLSHPAYRHMAERMGTPYLQKTLNQQLTNHIRDTLPALRSKLQSQLLSLEKEVEEYKNFKPDDPARKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGVRTGLFTPDLAFEAIVKQQIVKLKEPCLKCVDLVVSELATLIHKGTEKLNSYPRLREETERIVTTHVRERESKTKEQVMLLIDIELSYINTNHEDFIGFANAQQRSAAVTKKRAVPNQVIRRGWLTINISIMKGGSKDYWFVLTAESLSWYKDEEEKEKKFMLPLDNLKLRDVEKSFMSNKHTFGIFNTEQRNVYKDLRQIELACATQEDVDSWKASFLRAGVYPEKDQVENGDVSADSLSMDPQLERQVETIRNLVDSYISIVNKSIRDLMPKTIMHLMINSAKEFIYSELLAYLYSSGDQNSLMEESAEQEQRRDEMLRMYNALKEALKIIGDISTSTITTPVPAPVDDTWIHTDPSPPSQRKPSGGSAPPPGRPPAVRGPTPGAPAQPPLNPSPAFGAPPVPSRPTTLEPAVAPPPQVPSRPARVPPTVPPGIPRRPPAAPNRPTIIRPTEPSLLD
Protein: Liprin-alpha 4 (Protein tyrosine phosphatase, receptor type, f polypeptide (PTPRF),-interacting protein (liprin), alpha 4) (B8QI36)
Organism: Mus musculus (Mouse)
Interaction partners:
- Receptor-type tyrosine-protein phosphatase F
- Liprin-beta-1
- Liprin-beta-2
- Regulating synaptic membrane exocytosis protein 1
- Peripheral plasma membrane protein CASK
- Protein lin-7 homolog C
Sequence:
MCEVMPTINEGDPLGPPHGADAEANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLGTARRDLIKSEELSSKHQRDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGIHSRSHVGSAADVRFSLSTATHAPPGLHRRYSALRDESAKDWKPSPLPGVLGATTPAFDSDPEISDVDEDEPGGLVGTQVDVISPGGHSDAQTLAMMLQEQLDAINQEIRMIQEEKESTELRAEEIETRVTSGSMEALNLTQLRKRGSIPTSLTALSLASASPPLSGRSTPKLTSRSAAQDLDRMGVMTLPSDLRKHRRKLLSPVSREENREDKATIKCETSPPSSPRTLRLEKLGHPGLSQEEGKSALEGQDSNPSSSNSSQDSLHKGAKRKGIKSSIGRLFGKKEKGRLIQLSRDATGHVLLTDSELSLQEPMVPAKLGTQAEKDRRLKKKHQLLEDARRKGMPFAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLTSPSAPPTSRTSSGNVWVTHEEMETLATSTKTDSEEGSWAQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELEKRREESQHEIKDVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQSTQARQVMEREFNNLLALGTDRKLDDGEEKVFRRAPSWRKRFRPRDHHSGGMLGTSAETLPAGFRVSTLGPLQPPPAPPKKIMPEAGTAGAQRLEPSTVRTYSC
Protein: LIM/homeobox protein Lhx4 (LIM homeobox protein 4) (P53776)
Organism: Mus musculus (Mouse)
Function: May play a critical role in the development of respiratory control mechanisms and in the normal growth and maturation of the lung. Binds preferentially to methylated DNA (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Insulin gene enhancer protein ISL-1
- LIM domain-binding protein 1
- Pituitary-specific positive transcription factor 1
- Insulin gene enhancer protein ISL-2
Sequence:
MMQSAAVPAEGAVKGLPEMLGVPMQQIPQCAGCNQHILDKFILKVLDRHWHSSCLKCADCQMQLADRCFSRAGSVYCKEDFFKRFGTKCTACQQGIPPTQVVRKAQDFVYHLHCFACIICNRQLATGDEFYLMEDGRLVCKEDYETAKQNDDSEAGAKRPRTTITAKQLETLKNAYKNSPKPARHVREQLSSETGLDMRVVQVWFQNRRAKEKRLKKDAGRHRWGQFYKSVKRSRGGSKQEKESSAEDCGVSDSELSFREDQILSELGHTNRIYGNVGDVTGGQLMNGSFSMDGTGQSYQDLRDGSPYGIPQSPSSISSLPSHAPLLNGLDYTVDSNLGIIAHAGQGVSQTLRAMAGGPTSDLSTGSSVGYPDFPTSPASWLDEMDHPPF
Protein: Sop-2-related protein 3 (Q11193)
Organism: Caenorhabditis elegans
Function: Probably acts synergistically with sop-2 to maintain the transcriptionally repressive state of homeotic genes in order to regulate various neurogenic identities. Specification of some neuronal identities also involves expression of non-Hox genes. Specifies dopaminergic and serotonergic neuronal cell fate, and regulates neurotransmitter choice and axon pathfinding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17215367}. Nucleus {ECO:0000269|PubMed:17215367}.
Interaction partners:
- SET domain-containing protein
- Late nodulin
- ELK transcription factor homolog
- Homeobox domain-containing protein
- Polycomb protein sop-2
Sequence:
MDTTNQSEDIKPCDSDLMESILMFDEPISDILAHNKLWISHARTRSNFFPQEGRHISNQHTEAATSLKMWMLSKNLVVIVKRKDDIFPCKILTRNPENLFVARFLESGKEKHIQVEYSDIIMTRSELEKALPLCQHLIPARNWDDFYIIRDFEKATPYFEQGLSALVKPGQQFELQLEDAPDFYVMATVVKNYRGFLLVEYQNFKRWIHMLSPYCHEIGWGKNEKQEYLKRGPYNRHMNVDLVAGLVKQSTNQKLGAVPEIVFRNNCPVPHRIPEYSACVYLDLDQKRFYFAHKVTTKTCRNNRHFFNISIGKNLVTSKQNNRPYEFHVYHPRILPYSVAKRMEVQIILPPDVKLLPDESNLDGYLRTYCNPCDKHKTSDRVQPSPKIAKKKNGPLLLDDTPDAMFRSRPLLGDNIGAHKEWTNFMNHIPDYKRKDLLKSMDTLKFCEIFRPTPTGALQLTAAEVTGQQECMLRLKVSGEDEPVYIHNADPHLYHLGACLDMELAINFHGEFFDEKPLKKNKNANNGFSSF
Protein: V-type proton ATPase subunit e 2 (V-ATPase subunit e 2) (Vacuolar proton pump subunit e 2) (Q2KIB5)
Organism: Bos taurus (Bovine)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5EB76}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase 116 kDa subunit a 1
- Ribonuclease kappa
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit E 1
- Renin receptor
- V-type proton ATPase subunit G 2
- V-type proton ATPase subunit C 1
- V-type proton ATPase catalytic subunit A
Sequence:
MTAHSFALPVVIFTTFWGLIGIAGPWFVPKGPNRGVIITMLVATAVCCYLFWLIAILAQLNPLFGPQLKNETIWYVRFLWE