wanglab/gogpt-training-data huggingface dataset:
Protein: Lipid A deacylase PagL (EC 3.1.1.77) (LPS 3-O-deacylase PagL) (Outer membrane enzyme PagL) (Q7WD07)
Organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Function: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety.
Subcellular location: Cell outer membrane {ECO:0000250|UniProtKB:Q9HVD1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9HVD1}.
Interaction partners:
Sequence:
MQFLKKNKPLFGIVTLALACATAQAQPTQGGVSLHYGIGDHYQRVTLNYETPTLWSHQFGGNWGRLDLTPELGASYWWADGSRSPGHVWQASAIPMFRWWTGERFYIEAGIGATVFSSTSFADKRIGSAFQFGDHIGLGFLLTPSNRIGLRYSHFSNAGIKEPNPGLDIVQLTYTYQF
Protein: Dickkopf-related protein 1 (Dickkopf-1) (Dkk-1) (hDkk-1) (SK) (O94907)
Organism: Homo sapiens (Human)
Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Kremen protein 1
- Kremen protein 2
- Low-density lipoprotein receptor-related protein 6
- Cytoskeleton-associated protein 4
- Protein Wnt-3a
- Proto-oncogene Wnt-1
- Catenin beta-1
- Sclerostin
- Dickkopf-related protein 3
Sequence:
MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH
Protein: Sodium-dependent serotonin transporter (SERT) (5HT transporter) (5HTT) (Solute carrier family 6 member 4) (Q9XT49)
Organism: Bos taurus (Bovine)
Function: Serotonin transporter whose primary function in the central nervous system involves the regulation of serotonergic signaling via transport of serotonin molecules from the synaptic cleft back into the pre-synaptic terminal for re-utilization. Plays a key role in mediating regulation of the availability of serotonin to other receptors of serotonergic systems. Terminates the action of serotonin and recycles it in a sodium-dependent manner.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P31645}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P31652}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000250|UniProtKB:Q60857}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q60857}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q60857}. Note=Could be part of recycling endosomes. Density of transporter molecules on the plasma membrane is itself regulated by STX1A. Density of transporter molecules on the plasma membrane is also regulated by serotonin (By similarity). Density of transporter molecules seems to be modulated by ITGAV:ITGB3 (By similarity). {ECO:0000250|UniProtKB:P31645, ECO:0000250|UniProtKB:P31652, ECO:0000250|UniProtKB:Q60857}.
Interaction partners:
- 5-hydroxytryptamine receptor 2A
- Synaptic vesicular amine transporter
- tryptophan 5-monooxygenase
- 5-hydroxytryptamine receptor 2B
- Tryptophan 5-hydroxylase 2
- Amine oxidase [flavin-containing] A
- 5-hydroxytryptamine receptor 1A
- 5-hydroxytryptamine receptor 1B
- Amine oxidase [flavin-containing] B
Sequence:
METTPLNSQKELSAYKDGEDCQENGVLQKGVPAPGDKAESGQISNGYSAVPNPGAGDDTQHSIPAATTALVAEVHPAERETWAKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELALGQYHRNGCISIWTKICPIFKGIGCAICLIAFYIASYYNTIIAWALYYLISSFTEQLPWTSCENSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGLSWQLVLCIMFIFTVIYFSIWKGVKTSGKVVWVTATFPYIILLILLVRGATLPGAWRGVLFYLKPNWQKLLETGVWVDAAAQIFFSLGPGFGVLLAFASYNKFHNNCYQDALVTSAVNCMTSFVSGFVIFTVLGYMAEMRKEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIVFFLMLITLGLDSTFAGLEGVITAVLDEFPHVWAKRREWFVLGVVITCFFGSLVTLTFGGAYVVKLLEEFATGPAVLTVALIEAVAVFWFYGINQFCSDVKEMLGFSPGWFWKICWVAISPLFLLFIICSFLMSPPQLRLFQYDYPRWSIILGYCIGTSSFICIPTYITYRLIVTPGTLKERIIKGITPETPTAIPCGDIRLNAV
Protein: Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)] (P14778)
Organism: Homo sapiens (Human)
Function: Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells.
Subcellular location: Membrane {ECO:0000269|PubMed:8142597}; Single-pass type I membrane protein {ECO:0000269|PubMed:8142597}. Cell membrane {ECO:0000305|PubMed:8142597}. Secreted {ECO:0000269|PubMed:8142597}.
Interaction partners:
- Interleukin-1 beta
- TNF receptor-associated factor 6
- Interleukin-1 alpha
- Interleukin-1 receptor-associated kinase 1
- Interleukin-1 receptor accessory protein
- Interleukin-1 receptor antagonist protein
- Myeloid differentiation primary response protein MyD88
- Interleukin-1 receptor type 2
- Interleukin-6
- Tumor necrosis factor
Sequence:
MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG
Protein: Protein numb (P16554)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required in determination of cell fate during sensory organ formation in embryos. Restricts developmental potential and promote maturation of intermediary neuronal progenitor (INP) cells probably acting as an antagonist of Notch signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:2752427}. Cytoplasm, cell cortex {ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:26481050}. Cytoplasm {ECO:0000269|PubMed:26481050}. Note=In larval brain, shows asymmetric localization and asymmetrically sized divisions in type II secondary neuroblasts. {ECO:0000269|PubMed:18342578}.
Interaction partners:
- Partner of numb
- AP-2 complex subunit alpha
- Neurogenic locus Notch protein
- FI04474p
- Atypical protein kinase C
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- Inscuteable
- Bazooka, isoform B
- non-specific serine/threonine protein kinase
- DE-cadherin
Sequence:
MGNSSSHTHEPLERGFTRGKFGDVKNGKSASFRFSKKSPKKMDRLRRSFRDSFRRRKDRVPESSKPHQWQADEEAVRSATCSFSVKYLGCVEVFESRGMQVCEEALKVLRQSRRRPVRGLLHVSGDGLRVVDDETKGLIVDQTIEKVSFCAPDRNHERGFSYICRDGTTRRWMCHGFLACKDSGERLSHAVGCAFAVCLERKQRRDKECGVTMTFDTKNSTFTRTGSFRQQTLTERLAMATVGTNERSVDGPGSAMPGPPAATVKPFNPFAIERPHATPNMLERQSSFRLSTIGSQSPFKRQMSLRINDLPSNADRQRAFLTAAAGNPMQTPLRSVSPIAEVSPAKSAGADPLSAAAVAADSVSQLCQELSQGLSLLTQTDALLAAGEDLNFNNNRSINQNIIAAEKQVQHVHSYAPPTAQVTPRVASTTPTYQTLHSQSPSRSEQSIETSTELPNAEQWLGHVVRSTSPAAPKRPTYLANVGRAQTLASGTGAAVGGGGPDDPFDAEWVANVAAAKQLSPDLPIPSTARSPLARHSTNPFISPPKAPAQSFQVQL
Protein: Aspartate--tRNA ligase, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (Cell proliferation-inducing gene 40 protein) (P14868)
Organism: Homo sapiens (Human)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}.
Interaction partners:
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Bifunctional glutamate/proline--tRNA ligase
- Eukaryotic translation elongation factor 1 epsilon-1
- Glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
Sequence:
MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP
Protein: Ropporin-1-like protein (AKAP-associated sperm protein) (Q9EQ00)
Organism: Mus musculus (Mouse)
Function: Important for male fertility. With ROPN1, involved in fibrous sheath integrity and sperm motility, plays a role in PKA-dependent signaling processes required for spermatozoa capacitation.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:23303679}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96C74}.
Interaction partners:
- Sperm surface protein Sp17
- A-kinase anchor protein 3
Sequence:
MPLPDTMFCAQQIHIPPELPDILKQFTKAAIRTQPADVLQWSAGYFSALSRGDPLPVKDRIEMPVATQKTDTGLTQGLLKVLHKQCSHKQYVELADLEKKWKNLCLPVEKLRTILELDPCEDKIEWIKFLALGCSSLGRTLNTAMKNVCEILTSDPEGGPARIPFETFAYVYQYLSGLDPELPAVETENYLTSLRLMSESRKNGMIGLSDFFVGKKII
Protein: Fc receptor-like A (Fc receptor homolog expressed in B-cells) (Fc receptor-like and mucin-like protein 1) (Fc receptor-like protein) (Fc receptor-related protein X) (FcRX) (Q920A9)
Organism: Mus musculus (Mouse)
Function: May be implicated in B-cell differentiation and lymphomagenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7L513}. Note=Seems not to be secreted. {ECO:0000250|UniProtKB:Q7L513}.
Interaction partners:
- B-lymphocyte antigen CD19
- Immunoglobulin mu Fc receptor
- 8hs20 protein
- B-lymphocyte antigen CD20
- B-cell antigen receptor complex-associated protein beta chain
- Tyrosine-protein kinase Blk
- B-cell antigen receptor complex-associated protein alpha chain
- Fc receptor-like protein 6
- POU domain class 2-associating factor 1
Sequence:
MKLSCTLTQWALYVCPAVLLATQMLLAASSETLKCEGLVSTEQGSCQAAAEEDEGDEDDGDMTQSSEAGFQFKGYTFSKPFHLSVSYDWLILQGPATLIFEGDTLVLHCRAWQDWPLTQVIFYREGSALGPPGPKSEFSITMVQKSDGGHYHCSGIFRSPGPGSREAASPVAITVQELFAAPVLKALPSSEPQEGGSVTLSCQTKLALQRSASRLLFSFYKDGRSLSVRGVSSELKIPKASEEHSGSYWCEAVTEDRQISKQSPQLEIWVQALQKPTASETPPTEALGPLPPPPASSAEQPRFSSPDPHLHHQMQLLLKQIQDVRALLGHLVMELRDLSVYLKPGTTKVADK
Protein: Pre-alpha-onocerin synthase LCC (EC 5.4.99.65) (A0A125SXN1)
Organism: Lycopodium clavatum (Stag's-horn clubmoss)
Function: Oxidosqualene cyclase involved in the biosynthesis of alpha-onocerin, a triterpenoid characterized by a symmetrical structure due to cyclizations at both termini of dioxidosqualene that inhibits acetylcholinesterase. Catalyzes the first half of the cyclization, exclusively from dioxidosqualene.
Interaction partners:
Sequence:
MWKLKIAEGSPGLDTLNDHVGRQIWCYEKDAGTPEEHAEVEEARAKFTEQRHEQRQSADILMKLQLLKENSFSPLPTQPKVDRFEDITEDAVQTTLRRALRFFAAIQAHDGHWPGDHAGLMFLTPCLVICLYVTGALNTVLSEAHRQEMRRYLYNHQNKDGGWGLNIESHSTMFCTVFSYVTLRLLEEGPHDGDEGAMESARLWILDHGGAIAIPSWGKFWLAVLGVFEWSGVHPMPPEIWFLPHFLPIHPGQMNIHGKLILLPMTYIYGRQFVGPITSLVKALRGEIFSTHYNTIDWQEARTMCAKEDRYYSTPFVQDLAFTFAKQCTEPLLRSWPGSLVRKKALERVIKWIHTEDKNFRYVGIGPLSKVSVMLCCWIEDPNSEAFKRHLLRVHDYLWLAEDGMKMQGYNGCQMWETVLGTQAVLSARMHDECNSMLRKAEDYISKTQIQEDGNLDTKLWYHKISKGGWPHSTRDHGWPISDCSAEGLKVALALADLPWAMTGSQISEENLFDCVNVILSLQNPDGGFSAFELKRAYPWAEKLLQSETFGDITIDYSWVECSSSCIQALVAFKKKYTTHRKEEICRAINRACRFIESIQRKDGSWYGYWAVCFTYGAWFGITGLVAAGKSFHESEAIRRACDFLLSKQLPSGGWGESYLSSENEEYTHLKHGRAHVVHTAWSLLALLASGQAERDPVPLHRAATILINSQLENGDYPQQEIVGAIHKTCMTTYTLFCNIFAIQALGEYRQKIFHS
Protein: Glycerol kinase (Glycerokinase) (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Q64516)
Organism: Mus musculus (Mouse)
Function: Key enzyme in the regulation of glycerol uptake and metabolism.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P32189}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:P32189}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P32189}. Note=Glycerol kinase activity is more cytosolic in some tissues. It probably represents the expression of isoforms lacking a transmembrane domain. {ECO:0000250|UniProtKB:P32189}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P32189}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:P32189}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P32189}.
Interaction partners:
- Monoglyceride lipase
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol-3-phosphate acyltransferase 4
- glycerol kinase
- Aldo-keto reductase family 1 member B1
- Aldo-keto reductase family 1 member A1
- Aldose reductase-related protein 2
Sequence:
MAAAKKAVLGPLVGAVDQGTSSTRFLVFNSKTAELLSHHQVEIKQEFPREGWVEQDPKEILQSVYECIEKTCEKLGQLNIDISNIKAIGVSNQRETTVVWDKVTGEPLYNAVVWLDLRTQSTVENLSKRIPGNNNFVKSKTGLPLSTYFSAVKLRWLLDNVKKVQEAVEENRALFGTIDSWLIWSLTGGIHGGVHCTDVTNASRTMLFNIHSLEWDKELCEFFGIPMEILPNVRSSSEIYGLMKISHSLKAGALEGVPISGCLGDQSAALVGQMCFQDGQAKNTYGTGCFLLCNTGHKCVFSEHGLLTTVAYKLGRDKPVYYALEGSVAIAGAVIRWLRDNLGIIKSSEEIEKLAKEVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKCHIAFAALEAVCFQTREILDAMNRDCGIPLSHLQVDGGMTSNKILMQLQADILYIPVVKPSMPETTALGAAMAAGAAEGVGVWSLEPEDLSAVTMERFEPQINAEESEIRYSTWKKAVMKSIGWVTTQSPESGDPSIFCSLPLGFFIVSSMVMLIGARYISGIP
Protein: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (TaPIN1) (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1) (Q4UG71)
Organism: Theileria annulata
Function: Peptidyl-prolyl cis/trans isomerase (PPIase) that acts as a key virulence factor by promoting host leukocyte transformation. Binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins. Promotes host leukocyte transformation by binding to phosphorylated host FBXW7, disrupting dimerization and promoting FBXW7 autoubiquitination and subsequent degradation. Degradation of host FBXW7, leads to stabilization of JUN, which promotes cell transformation.
Subcellular location: Secreted {ECO:0000305|PubMed:25624101}. Host cytoplasm {ECO:0000269|PubMed:25624101}. Host nucleus {ECO:0000269|PubMed:25624101}.
Interaction partners:
- Bacterial surface antigen
- indole-3-glycerol-phosphate synthase
- peptidylprolyl isomerase
- Serine/threonine protein kinase, putative
- RNaseP-like protein with Nifu domain, putative
- Acyl carrier protein
- Membrane insertase YidC/Oxa/ALB C-terminal domain-containing protein
Sequence:
MIRNFLNFLWNNTSLRFLIINTIIFAMDKVRCAHLLLKHTGSRNPVNRNTGMAVTRTKEEAVSEMKGYLEMLRKSDNLDQEFRRLATAKSECSSARKGGDLGFFDRNTMQKPFTEASFKLEVNEISDLVETDSGVHLIYRIA
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (F1QQA2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC5 isoform X1
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit
- RNA polymerase I and III subunit C.
- Polymerase
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MLQEEFGEMSPQQLAAPVDTVEEKWKLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMKANEKITSDADPMWYLKYLNIYVGMPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYTRGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPMEFSKLNECPLDPGGYFIVKGQEKVILIQEQLSKNRIIVDQDRKGTVGASVTSSTHEKKSRTNMIVKQGRFYLKHNTLSEDAPIAIIFKAMGVESDQEIVQMIGTEEHVMAAFAPSLEECQKAQIFTQTQALRYIGNKVRRQRMWGGPKKTKMEEARELLASTILTHVPVKEFNFRAKCIYLAVMVRRVILAQGDNKVDDRDYYGNKRLELAGQLLSLLFEDLFKKFNSELKKIADQIIPKQRAAQFDVVKHMRQDQITNGMVNAISTGNWSLKRFKMDRQGVTQVLSRLSFISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLCPSDTPEGEACGLVKNLALMTHITTDMEDGPIIKLAFNLGVEDVNLLCGEELSYPTVFLVFLNGNILGVIRDHQKLVYTFRLMRRAGFINEFVSISTNLTDRCVYISSDGGRLCRPYIIVKNGKPAVKNKHIEELSQGYRTFEDFLHESLVEYLDVNEENDCNIALYEHMISKDTTHLEIEPFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQRPMVKTKTIELIDFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLRRYTNQTFDKVMGPMLDAETRKPIWRHSILDADGICSPGEKVENKQVLVNKSMPTVTQTPLEGSAQPGQPQYREVPVSYKGATDSYIEKVMISSNAEDAFLVKILLRQTRRPEIGDKFSSRHGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGYPSRMTVGKLIELLAGKAGVLDGRFHYGTAFGGSKVKDVCEDLIRYGYNYQGKDYVTSGITGEPLEAYIYFGPVYYQKLKHMVLDKMHARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVCGQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLARYNE
Protein: Rhomboid-4 (EC 3.4.21.-) (Rhomboid-4, isoform B) (SD06923p) (Q9VYW6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Protein spitz
Sequence:
MPVKTVNRQQSQTPAQQLQLQQQRDVENGLYPTIPAERRSPPSRPQTLRQDTIDMEEIPLNQTNSQEPEDRRKMHEIFDKHDSDRDGLINTHELKELISDGYCRDIPAYIADQILKRSDQDNDGHLDFEEFYAMSLRHKWMVRNMLTRYCRYVVPPPKPLEGDEPDGAYEKQMSICPPPLTMVLFSIIEIIMFLVDVIHFQDDPNYQDRIGESTSGPAATLFIYNPYKRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPRIFLAGASGGVYALITAHIATIIMNYSEMEYAIVQLLAFLVFCFTDLGTSVYRHLTDQHDQIGYVAHLSGAVAGLLVGIGVLRNLEVRRWERILWWVAVIVYFALMTTGIIIHVFVPDYFPKQEYN
Protein: Photosynthetic reaction center H subunit (D2Z0P9)
Organism: Thermochromatium tepidum (Chromatium tepidum)
Interaction partners:
Sequence:
MSAGITHYIDAAQITIWAFWLFFFGLIIYLRREDKREGYPLDSDRTERSGGRVKVVGFPDLPDPKTFVLPHNGGTVVAPRVEAPVAVNATPFSPAPGSPLVPNGDPMLSGFGPAASPDRPKHCDLTFEGLPKIVPMRVAKEFSIAEGDPDPRGMTVVGLDGEVAGTVSDVWVDRSEPQIRYLEVEVAANKKKVLLPIGFSRFDKKARKVKVDAIKAAHFANVPTLSNPDQVTLYEEDKVCAYYAGGKLYATAERAGPLL
Protein: GPI transamidase component PIG-S homolog (Q10351)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the GPI transamidase complex. Involved in transfer of GPI to proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GPI-anchor transamidase
- GPI transamidase component gaa1
- GPI transamidase component PIG-T homolog
- GPI transamidase component GAB1 homolog
Sequence:
MSPCKWLTMFLKGCWGKIANMNHLDSCFPLRYIIGRKKASKLLCTMDSGLKSDSHEVERSNFQLNKPEKSLKRYALLSFYVIILLAIPVWWKTTHYERSSLPFEDMENAPSTVQTHLRFSPTFRILDDKGNNLTKEVQKVLEAEPQIYSYNLKVLEDDPVDYRIVLRESTDLQWFWDENNFIIDTPSKGPSELAILIVNCLWEAFSPQVMEVWSKFTRFSSTVEPSRAETKRTVQFSPQYRVLLSLLVGEGNHEPINWDIENAIQKYFNPLIEQLASLAKLNIETQIQYFVEDAEAYIKDDKFCTKHADLPNLVNNFEKYLSFSPHIREPTIHFVLYVPSPQIQPLWLENEDSNIIPTNSMLLPQWGSITTINFNVTEKKLLHDVDLKDYFRVISRDLLLLLGINDVPVSSLSATLADRLLRQRIAESCIEASDTLQNLAKLVHSMQSMAVPKEIQMYVKDTLLSLDMAYKALSQNNLNEALSYSNNAFSKSQEALFHPSMVTTIYFPDESKYGIYAPLFAPILIPLLISFIKEVKDMLRERKLHRVANVPKPN
Protein: 5'-AMP-activated protein kinase subunit gamma (AMPK gamma) (AMPK subunit gamma) (Regulatory protein CAT3) (Sucrose non-fermenting protein 4) (P12904)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.
Subcellular location: Nucleus {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:3049255}. Cytoplasm {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228}.
Interaction partners:
- SNF1 protein kinase subunit beta-3
- SNF1 protein kinase subunit beta-2
- Carbon catabolite-derepressing protein kinase
- SNF1 protein kinase subunit beta-1
- SNF1-activating kinase 1
- Regulatory protein MIG1
- Regulatory protein CAT8
- Serine/threonine-protein kinase TOR1
- Target of rapamycin complex 1 subunit KOG1
- Serine/threonine-protein kinase TOR2
Sequence:
MKPTQDSQEKVSIEQQLAVESIRKFLNSKTSYDVLPVSYRLIVLDTSLLVKKSLNVLLQNSIVSAPLWDSKTSRFAGLLTTTDFINVIQYYFSNPDKFELVDKLQLDGLKDIERALGVDQLDTASIHPSRPLFEACLKMLESRSGRIPLIDQDEETHREIVVSVLTQYRILKFVALNCRETHFLKIPIGDLNIITQDNMKSCQMTTPVIDVIQMLTQGRVSSVPIIDENGYLINVYEAYDVLGLIKGGIYNDLSLSVGEALMRRSDDFEGVYTCTKNDKLSTIMDNIRKARVHRFFVVDDVGRLVGVLTLSDILKYILLGSN
Protein: Small ribosomal subunit protein uS15 (40S ribosomal protein S13) (P62301)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62277}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL36
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS8
Sequence:
MGRMHAPGKGLSQSALPYRRSVPTWLKLTSDDVKEQIYKLAKKGLTPSQIGVILRDSHGVAQVRFVTGNKILRILKSKGLAPDLPEDLYHLIKKAVAVRKHLERNRKDKDAKFRLILIESRIHRLARYYKTKRVLPPNWKYESSTASALVA
Protein: Transmembrane protein 87A (Elkin1) (Q8NBN3)
Organism: Homo sapiens (Human)
Function: May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:32228863}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26157166, ECO:0000269|PubMed:32228863}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:32228863}; Multi-pass membrane protein {ECO:0000255}. Cell projection, ruffle {ECO:0000269|PubMed:32228863}.
Interaction partners:
Sequence:
MAAAAWLQVLPVILLLLGAHPSPLSFFSAGPATVAAADRSKWHIPIPSGKNYFSFGKILFRNTTIFLKFDGEPCDLSLNITWYLKSADCYNEIYNFKAEEVELYLEKLKEKRGLSGKYQTSSKLFQNCSELFKTQTFSGDFMHRLPLLGEKQEAKENGTNLTFIGDKTAMHEPLQTWQDAPYIFIVHIGISSSKESSKENSLSNLFTMTVEVKGPYEYLTLEDYPLMIFFMVMCIVYVLFGVLWLAWSACYWRDLLRIQFWIGAVIFLGMLEKAVFYAEFQNIRYKGESVQGALILAELLSAVKRSLARTLVIIVSLGYGIVKPRLGVTLHKVVVAGALYLLFSGMEGVLRVTGAQTDLASLAFIPLAFLDTALCWWIFISLTQTMKLLKLRRNIVKLSLYRHFTNTLILAVAASIVFIIWTTMKFRIVTCQSDWRELWVDDAIWRLLFSMILFVIMVLWRPSANNQRFAFSPLSEEEEEDEQKEPMLKESFEGMKMRSTKQEPNGNSKVNKAQEDDLKWVEENVPSSVTDVALPALLDSDEERMITHFERSKME
Protein: T. brucei spp.-specific protein (Q389B5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPCFLSVVRSRFMELRQEEPSSQQRSNFVPKSPNPSALMPLPGAGIQPICPQLPNANHAETERSAIQAGRHAFFATKFSSRPHTAVTARMSEGKSATLGYTFLLLWALLSPHLLIPPPKKQQCTCPTGPAQ