wanglab/gogpt-training-data huggingface dataset:
Protein: BTB/POZ domain-containing protein At1g50280 (Q8RXR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Protein NAP1
- Protein ABIL1
- Dirigent protein 16
- Dirigent protein 18
- Protein PIR
- Actin-related protein 2/3 complex subunit 3
- At4g14145
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
Sequence:
MSPLNDLKINLNGQYTFFLNQNVISKYSGSLRKMIKQSKKKRNKKKRIITIEINDFPGGPDGFELVSRFCYHNGEILIDVSNVSTLYCCSVFLGMSEKFCFSNLFLQTEKFLEEVFYGSWSDIVSCLKNCEQVFFQADSYGLVDKLIFAALNKISQNSDDFSSSSLSSFASSLSPEMAKNTSESDGRYISRSVACGRSNEWWFEDMTNLSPKIILKLVMIIGAYKTNIKSLVLTRFLLHYLKTKLQTKSRTTTELMRNKLEYSDLADTAVRGVISAGTRTFSCRKLFWILRVLSSFSLSRESRIGLETLIGEMLEQATLDDLLISARGSRESGFYNVDLVIRLLKVFVKNREEEEEESRERNMKEIGKLIDKYLREISPDQNLKVPKFLGVAESLPDSARDCFDGVYRAIDIYLQSHPNLTPQDRTEICRCLNYKKLTMETCKQLARNPKIPPEIAIEALKSRCGNQEHTTSDVKVANKSFSCRYSEEKKKPVVLHLEITEKLAERLKTKGGYNLKVMDSFREGL
Protein: Cysteine/serine-rich nuclear protein 1b (Zgc:66340) (Q6PFK3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGVLKRKYEEVEEDPCYSSSSPSSLSSSAYSEWDSDGESCYSDTLDSTPSNPSSPATSLNTTSILKKAKRTRQGNVQFDQVTVFFFPRCQGFTSVPSRGGCTLGMMQRHSAQRRYTLAEFAIAQRHLRREKLKNRMREEKLEALKLKLTKNGTQESEEAEKLTVDDIPEDEIDLSGVNVDDGSFLHPYPSKKRYAILKAAGVKKIDREEKRQLHELRTSREDCGCDCQGFCEPETCSCSLAGIKCQMDHSSFPCGCTKDGCGNTQGRIEFNSSRVHTHYIHTIMKLELEKRLEEHTTETPPENHPDSSSLNQPAEISSTPDMPTFHFNSELLSTGENSCSSDMTDSSSSSGQSEDSESVENVPSEQSPLDVDENGLTRILSFSDTDNEDCSIRERNDNCDYQQKKSEGSMGYGIFSTEDDKLSTQEHVSWSL
Protein: Protein PIMREG (CALM-interactor expressed in thymus and spleen) (PICALM-interacting mitotic regulator) (Regulator of chromosome segregation protein 1) (Q9BSJ6)
Organism: Homo sapiens (Human)
Function: During mitosis, may play a role in the control of metaphase-to-anaphase transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:16491119, ECO:0000269|PubMed:19383357}. Nucleus, nucleolus {ECO:0000269|PubMed:19383357}. Note=Partially localizes to the nucleolus. {ECO:0000269|PubMed:19383357}.
Interaction partners:
- Histone H3-like centromeric protein A
- Cell division cycle-associated protein 3
- Kinesin-like protein KIF20A
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- G2/mitotic-specific cyclin-B2
- Cyclin-dependent kinase 1
- Aurora kinase B
- Cell division cycle protein 20 homolog
- Disks large-associated protein 5
- Tudor domain-containing protein 7
Sequence:
MASRWQNMGTSVRRRSLQHQEQLEDSKELQPVVSHQETSVGALGSLCRQFQRRLPLRAVNLNLRAGPSWKRLETPEPGQQGLQAAARSAKSALGAVSQRIQESCQSGTKWLVETQVKARRRKRGAQKGSGSPTHSLSQKSTRLSGAAPAHSAADPWEKEHHRLSVRMGSHAHPLRRSRREAAFRSPYSSTEPLCSPSESDSDLEPVGAGIQHLQKLSQELDEAIMAEERKQALSDRQGFILKDVYASP
Protein: Protein phosphatase 1 regulatory subunit 13 like (K7EN03)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSEAFQSARDFLDMNFQSLAMKHMDLKQMELDTAAAKVDELTKQLESLWSDSPAPPGPQAGPPSRPPRYSSSSIPEPFGSRGSPRKAATDGADTPFGRSESAPTLHPYSPLSPKGRPSSPRTPLYLQ
Protein: Villin-1 (Q0DKN3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Ca(2+)-independent actin-binding protein. Binds actin microfilaments (MFs). Involved in actin filament bundling, severing and capping. Caps the barbed end of actin filaments and protects them from disassembly. Promotes VLN3-mediated MF severing.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O81644}.
Interaction partners:
- Os03g0225600 protein
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 8
- Os11g0157701 protein
- Expressed protein
Sequence:
MKGVDDAFLGVGDKPGLDIWCIMGSNLIAIEKSLHGKFYTGNTYIILSTVELKSGVRQHNVHYWVGEEAKEEDCLTASDKAIELDVALGSNTVQYRETQGEESDKFLSYFKPCIIPIQGSLSSHMRIYGDKSKDTTMFRCEGEHVARVTEVPFSRSSLDHKAVFVVDTESKIFLFSGCNSSMQTRAKALDVVKHLKENRHCGRCEIATIEDGKLVGDSDAGDFWNLFGGYAPIPRDVQDTVMTELMTTSSKKLFWINKRNLVPVETNLLEREMLNSDRNYILDCGTEVFLWMGMTTLVSERRTSVTALEDYVRCEGRQSNARSVILTEGHETVEFKMHFQHWPKNAVPKLYEAGREKVAAIFKHQGYDVTEIPEDKPRHFISCNGSLKVWLVDNGSVTLLCTEEQEQLYNGDCYIIRYSYIEDGKDYHLFFAWSGLNSINEDRVAAASLMSGMIDSVKGHAVVAQVFEGREPEMFFLVFKSLIIFKGGRSMAYKNFVSQRSDANGWYQKNGVALFRVQGLKHDCIRAIQVDLAASSLNSSHCYILQAGGSFFTWLGSLSSPSDHNLLDRMMDKLCPLKQSLLVREGSEPDRFWEALGGRSEYLREKQVKDWPADPHLYTCHFEQGLFKAKEVFSFSQDDLVTEEILILDCVEELHIWVGHQSGVLSKEQALDIGKMFLQAGIHQDGRRPIDTTMYIVTEGDEPRFFTSFFNWDYSKQTMLGNSFERKLAILKGISQKLETPERSLRKSSSSSLPRRSPGTSSSEPTTPEQRAAARTFASASTGKLLRERSPAALSPSLSTPSPSPRSRSSASSSPASWNSTPSTVARRLFPPSLHASAEAVATGTPRRR
Protein: Der GTPase-activating protein YihI (GAP) (P0A8H6)
Organism: Escherichia coli (strain K12)
Function: A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function, negatively regulating cell growth, probably via ribosome assembly. Stimulates the GTPase activity of Der; a construct missing the first 45 residues is even more stimulatory. Does not stimulate 2 other GTPases (ObgE and Era). Overexpression inhibits cell growth; precursor 16S rRNA accumulates, the 23S rRNA is 6-7 bases longer than usual, and 50S ribosomal subunits are improperly assembled, leading to 45S subunits lacking proteins L9, L18 and L25. Overexpression of Der in the same cells suppresses the 50S subunit assembly defect, corroborating that YihI and Der interact.
Interaction partners:
- GTPase Der
- Protein Syd
- Uncharacterized protein YigA
- UPF0208 membrane protein YfbV
- Oxygen-independent coproporphyrinogen III oxidase
- Negative modulator of initiation of replication
- Inner membrane protein YejM
- Nucleoid-associated protein YejK
- Regulator of ribonuclease activity B
- Met repressor
Sequence:
MKPSSSNSRSKGHAKARRKTREELDQEARDRKRQKKRRGHAPGSRAAGGNTTSGSKGQNAPKDPRIGSKTPIPLGVTEKVTKQHKPKSEKPMLSPQAELELLETDERLDALLERLEAGETLSAEEQSWVDAKLDRIDELMQKLGLSYDDDEEEEEDEKQEDMMRLLRGN
Protein: Vesicle transport through interaction with t-SNAREs homolog 1B (Vesicle transport v-SNARE protein Vti1-like 1) (Vti1-rp1) (Q9UEU0)
Organism: Homo sapiens (Human)
Function: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:18033301}; Single-pass type IV membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18033301, ECO:0000269|PubMed:23217709}; Single-pass type IV membrane protein {ECO:0000269|PubMed:23217709}. Lysosome membrane {ECO:0000269|PubMed:18033301, ECO:0000269|PubMed:23217709}. Cytoplasmic granule {ECO:0000269|PubMed:23217709}. Recycling endosome membrane {ECO:0000269|PubMed:18033301}; Single-pass type IV membrane protein {ECO:0000255}.
Interaction partners:
- Synaptobrevin homolog YKT6
- Syntaxin-7
- Syntaxin-6
- Clathrin interactor 1
- Vesicle-associated membrane protein 8
- Syntaxin-8
- Vesicle-associated membrane protein 4
- Syntaxin-5
- Vesicle-associated membrane protein 7
- Alpha-soluble NSF attachment protein
Sequence:
MASSAASSEHFEKLHEIFRGLHEDLQGVPERLLGTAGTEEKKKLIRDFDEKQQEANETLAEMEEELRYAPLSFRNPMMSKLRNYRKDLAKLHREVRSTPLTATPGGRGDMKYGIYAVENEHMNRLQSQRAMLLQGTESLNRATQSIERSHRIATETDQIGSEIIEELGEQRDQLERTKSRLVNTSENLSKSRKILRSMSRKVTTNKLLLSIIILLELAILGGLVYYKFFRSH
Protein: NAD-capped RNA hydrolase NudC (DeNADding enzyme NudC) (EC 3.6.1.-) (NADH pyrophosphatase) (EC 3.6.1.22) (P9WIX5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Interaction partners:
- Nicotinate phosphoribosyltransferase pncB1
- CinA-like protein
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- NAD-dependent protein deacylase
- Glutamine-dependent NAD
- Nicotinate phosphoribosyltransferase pncB2
- Probable nicotinate-nucleotide adenylyltransferase
- Probable soluble pyridine nucleotide transhydrogenase
- NAD kinase
- Possible transcriptional regulatory protein NadR
Sequence:
MTNVSGVDFQLRSVPLLSRVGADRADRLRTDMEAAAAGWPGAALLRVDSRNRVLVANGRVLLGAAIELADKPPPEAVFLGRVEGGRHVWAVRAALQPIADPDIPAEAVDLRGLGRIMDDTSSQLVSSASALLNWHDNARFSALDGAPTKPARAGWSRVNPITGHEEFPRIDPAVICLVHDGADRAVLARQAAWPERMFSLLAGFVEAGESFEVCVAREIREEIGLTVRDVRYLGSQQWPFPRSLMVGFHALGDPDEEFSFSDGEIAEAAWFTRDEVRAALAAGDWSSASESKLLLPGSISIARVIIESWAACE
Protein: GTPase-activating protein GYP7 (GAP for YPT7) (P48365)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTPase-activating protein (GAP) that most effectively accelerates the intrinsic GTPase activity of Ypt/Rab-type GTPase YPT7 involved in vacuole docking and fusion. It is also active, but to a lesser extent, on YPT31, YPT32, YPT1, YPT6 and SEC4. Provides a catalytic arginine (arginine finger) in trans to accelerate the GTP hydrolysis rate of the substrate GTPase (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ypt/Rab-type GTPase YPT7
- Autophagy-related protein 8
- GTPase-activating protein GYP8
- GTPase-activating protein GYP6
- GTPase-activating protein GYP2
- GTPase-activating protein GYP5
- Rab GDP-dissociation inhibitor
- Mitochondrial fission 1 protein
- Casein kinase I homolog 3
- GTPase-activating protein GYP3
Sequence:
MSKILFCKSKVFLHPTSDARDNIAGFLLLTLEANKLSHQAILQYIPESGLSTLEISKLLKHEAKVGTCPTSTPFVIENSINFSNLVNTSLGQAFEISLSQIYCIQFRPPSPNGWYVGSLVIYPLTEQFTGFQPPVLFFHDQLCPSTTDKLKRLRKSMNPFDDSDELYWGGVDLRNKINELMELKKSNLEPEFWLVNPSLNDLRNFVSKDLLESYNNSKKDTTELATAGVKLNEKFQEWKWNVMSKIADVTTKSTNFIDSWLTNNSPIQKSQIDNEYLQKLLNNEKVKQIEQDYDSARVYLANWSLGVKQEAERYQKQNKLFDSYRNNIFNDLNLTDELSDTEINNALQRQFPLTEAKWNSLWDENDGRLRVTVNEVKDFIFHGGLENDSLRGKVWGFLLEIYPWDSSQDERVQIDQTLAAEYDQLKLTWSKDFLQFDDEDEEEYWNDQLFRISKDVRRCDRNLEIFQYNTIDGLPPPPQQLPANENNSTSPESANDESDDADDGVRNPHLIHLQNILITYNVYNTNLGYVQGMTDLLSPIYVIMKEEWKTFWCFTHFMDIMERNFLRDQSGIHEQMLTLVELVQLMLPELSEHLNKCDSGNLFFCFRMLLVWFKREFEMEDIMHIWENFWTFYYSSQFQLFFMLAILQKNSQAILQHLNQFDQILKFFNELNGKLDWNDLMVRAELLFKKFEKMMHVMERDLQNVSSSSSSSSTGVLPCQSERLTLLLSKKPIIRHEGQRSKNSVK
Protein: Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphate O-acyltransferase MBOAT2) (EC 2.3.1.51) (1-acylglycerophosphocholine O-acyltransferase MBOAT2) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine MBOAT2 O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidic acid acyltransferase) (LPAAT) (Lyso-PA acyltransferase) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 2) (O-acyltransferase domain-containing protein 2) (Q6ZWT7)
Organism: Homo sapiens (Human)
Function: Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophospholipid leading to the production of a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. Catalyzes preferentially the acylation of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) and lysophosphatidic acid (LPA) and to a lesser extend lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS). Prefers oleoyl-CoA as the acyl donor. May be involved in chondrocyte differentiation (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8R3I2}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Lysophospholipid acyltransferase LPCAT4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- Glycerol-3-phosphate acyltransferase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase delta
- Lysocardiolipin acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
- Ethanolaminephosphotransferase 1
- Phosphatidate cytidylyltransferase 2
Sequence:
MATTSTTGSTLLQPLSNAVQLPIDQVNFVVCQLFALLAAIWFRTYLHSSKTSSFIRHVVATLLGLYLALFCFGWYALHFLVQSGISYCIMIIIGVENMHNYCFVFALGYLTVCQVTRVYIFDYGQYSADFSGPMMIITQKITSLACEIHDGMFRKDEELTSSQRDLAVRRMPSLLEYLSYNCNFMGILAGPLCSYKDYITFIEGRSYHITQSGENGKEETQYERTEPSPNTAVVQKLLVCGLSLLFHLTICTTLPVEYNIDEHFQATASWPTKIIYLYISLLAARPKYYFAWTLADAINNAAGFGFRGYDENGAARWDLISNLRIQQIEMSTSFKMFLDNWNIQTALWLKRVCYERTSFSPTIQTFILSAIWHGVYPGYYLTFLTGVLMTLAARAMRNNFRHYFIEPSQLKLFYDVITWIVTQVAISYTVVPFVLLSIKPSLTFYSSWYYCLHILGILVLLLLPVKKTQRRKNTHENIQLSQSKKFDEGENSLGQNSFSTTNNVCNQNQEIASRHSSLKQ
Protein: IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 (Q9XWG9)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ubiquitin-like domain-containing protein
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL31
- Calmodulin
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL38
Sequence:
MLTTSGYPNGSLRSSLDDSPQDPEESETFLLGMVTGDGLGKMFNARYRNIKEKKAAKMTYRAMIYNCLERPTGWKCFLYHFSVFLIVLICLILSVLSTVEEHSHFAAELLYILEIVLVVFFSVEFIVRLWSAGCRSKYIGVYGRLKFVRKPITLIDLVVVICSLFVICFGTEGQVFAASAMRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDHIGVDGRQAFTSYADALWWGVITMTTIGYGDVVPQTWLGRIVASCFSIFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAATLIQCLWRCHAAEKKVSATWNAHIDPLAHETKETHHWNGKKHASSMDSNNLTRKRQLFKKQSSLVNTFRRKGSPSTDVEMGELQQERLLRHERNSDTDDEKRIYRVGADIEIDYETEEPTTPTRPQGHISHVCELTDAHRNAIRAIRRVKYFVARRRFQQARKPYDVRDVIEQYSQGHLNMMVRIKELQRRLDQTLGKPGQYDGKGSRKGHPVTIGSRLSRLELQMSSLDRKVESSNRTLNALYRLMADRNSLTISPSPPALISRPVSPAACLSPRDQLSPTSISSQRSGSPGWQ
Protein: Heparan sulfate glucosamine 3-O-sulfotransferase 6 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 6) (3-OST-6) (Heparan sulfate 3-O-sulfotransferase 6) (h3-OST-6) (Q96QI5)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes Simplex Virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to anticoagulant heparan sulfate.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MAGSGGLGGGAGGGQGAGAGQGAALRASRAPMLLVALVLGAYCLCALPGRCPPAARAPAPAPAPSEPSSSVHRPGAPGLPLASGPGRRRFPQALIVGVKKGGTRALLEFLRLHPDVRALGSEPHFFDRCYERGLAWYRSLMPRTLDGQITMEKTPSYFVTREAPRRIHAMSPDTKLIVVVRNPVTRAISDYAQTLSKTPGLPSFRALAFRHGLGPVDTAWSAVRIGLYAQHLDHWLRYFPLSHFLFVSGERLVSDPAGEVGRVQDFLGLKRVVTDKHFYFNATKGFPCLKKAQGGSRPRCLGKSKGRPHPRVPQALVRRLQEFYRPFNRRFYQMTGQDFGWG
Protein: Mitochondrial ornithine transporter 1 (Solute carrier family 25 member 15) (Q9Y619)
Organism: Homo sapiens (Human)
Function: Mitochondrial ornithine-citrulline antiporter (Probable). Catalyzes the exchange between cytosolic ornithine and mitochondrial citrulline plus an H(+), the proton compensates the positive charge of ornithine thus leading to an electroneutral transport. Plays a crucial role in the urea cycle, by connecting the cytosolic and the intramitochondrial reactions of the urea cycle (Probable). Lysine and arginine are also transported by the antiport mechanism (Probable). In addition, catalyzes an electroneutral exchange of ornithine or lysine for H(+), a reaction driven by the pH gradient across the inner membrane (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q12375}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:10369256}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Mitochondrial carrier homolog 1
- N-acetylglutamate synthase, mitochondrial
Sequence:
MKSNPAIQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGLTDCCLKTYSQVGFRGFYKGTSPALIANIAENSVLFMCYGFCQQVVRKVAGLDKQAKLSDLQNAAAGSFASAFAALVLCPTELVKCRLQTMYEMETSGKIAKSQNTVWSVIKSILRKDGPLGFYHGLSSTLLREVPGYFFFFGGYELSRSFFASGRSKDELGPVPLMLSGGVGGICLWLAVYPVDCIKSRIQVLSMSGKQAGFIRTFINVVKNEGITALYSGLKPTMIRAFPANGALFLAYEYSRKLMMNQLEAY
Protein: UDP-N-acetylglucosamine transferase subunit ALG14 (Q54G73)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- OTU domain-containing protein
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- GDP-Man:Man
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
Sequence:
MTKSVFVTVGTTKFDDLIDKIDSPKLFNILLKYGFNKMIIQIGNYSGTIENSLPFDENNNNNNKTNSKTTTSTTTTAKFESLYFDYKPSLSEFMKNSDLIISHAGSGSILESLENNKPCICVVNDKLMDNHQKELADKLSNLSYILSTNPTSLYETIETKLDEYLKNRIYLDKSIHQKAQQQFATSLSNQFKLINNNEDDNTKTSSSSSTTTTTTTTNSKKKFKTMVVLGSGGHTTEMFYLLKKVDKNKFNPITYVLADSDKRSEDKIKIEDTSSPIIKKIPRSRNVGQSFFNSIFTTLIALFYSMLLVFKEKPDCLLCNGPGTCVPLAVCVLLLRWLRIGKGSKIIYIESLARVNDLSLSGKILQHISDWFVVQWPELLSKTDSSNVSCINLFFETF
Protein: Large ribosomal subunit protein uL1m (39S ribosomal protein L1, mitochondrial) (L1mt) (MRP-L1) (Q99N96)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL11m
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL17m
Sequence:
MAAAVRCLRRVLIHHQRHCLCKMASQASLYPCSVNSLLHNRHFAAAAAAATKPARKIKKGAKEKTSDEKPVDDIEKIKSYTYMESDPEDDVYLKRLYPRRIYEVEKAIHLLKKFQVLDFTNPKQGVYLDLTLDMALGKKKTVEPFASVIALPHLFSSEVNKVAVFTANASEIKIAEENGAAFAGGTDLVKKIMDDEVVVDFYVAVPEIMGELNPLRKKLKKRFPKATRNSIGRDIPKMLELFKTAHEIMVDEERQNFLSTKIATLDMPSDQIAANLQAVINEVCKHRPLNLGPFVVRAFLRSSTSEGLLLKTDSLLPKEAKTTEAETEETQTAEAA
Protein: Eukaryotic translation initiation factor 5A (eIF-5A) (Q387H6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping (By similarity). Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation. Required for cell growth during both bloodstream (BF) and insect procyclic (PF) life cycle stages and for survival of the bloodstream form.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26082486}. Note=Localizes to the cytoplasm in the procyclic insect (PF) life cycle stage. {ECO:0000269|PubMed:26082486}.
Interaction partners:
- Small ribosomal subunit protein uS5
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S18, putative
- Large ribosomal subunit protein uL5
- Ribosomal protein
- 40S ribosomal protein S15a, putative
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L17, putative
- 40S ribosomal protein S23, putative
Sequence:
MSDDEGQFAEGGAQVGSLTYPMQAGALKKGGYICINGRPCKVIDLSVSKTGKHGHAKVSIVALDIFTGNKMEDQAPSTHNVEVPFVKTATYSVLDIQEDREDPSKPAHLSLMDDEGETRDNLDMPPNAELAGQIKEQFDAGKDVLVVVVSAMGIDQILSFKNAAER
Protein: Mediator of RNA polymerase II transcription subunit 29 (Mediator complex subunit 29) (Q9XUS2)
Organism: Caenorhabditis elegans
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes (By similarity). Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery (By similarity). Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors (By similarity). Involved in development of gonad and seam cells. Plays a role in temporal regulation of seam cell division, probably acting as a part of the Mediator complex.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- MeDiaTor
- Mediator of RNA polymerase II transcription subunit 1.2
- Putative transcription factor sel-7
- Cdc-42 Related Protein
- Chromatin-remodeling complex ATPase chain isw-1
- Actin-related protein 2/3 complex subunit
- Major sperm protein
- Transcription initiation factor TFIID subunit 11
- Conserved oligomeric Golgi complex subunit 3
- CTCHY-type domain-containing protein
Sequence:
MSGQGPPPSMTPQQQHMLMQQQQQQQMMRQQQMQQQQMQQQRQQQIQQQAQQPYQRARTPQMVPQGGSPGGAHLQMHPHLQPQGQMQPRSPLVGAQLQAPSSVPTAANPTTPQMMQQQMGMNQPMSLPPTHVSRPGSVAPPSSVPVNLQHTSGAPGLPGSQMEHQYPMHLQPQQQTLSRPGSQQSQHIQQPGSIQRPGSVLAPGSIPPGGPASQTGPQSIQVFGPGSVQPPGSTQAPSSVQPASTFNPGSIQAPASQQPPASVQPPPSAASGSTVAGAQSSKEPLKPNEEQIRMVQDPVDLVRNLVQKDLRNSLVEMNKRGAELVRQKQEGEVNEDGKAQYSRATNDFHAVCDEIDRTLTTVLETAKQLSKLDKVFFDRSSRDLDGEVMVNSVQNFVDNTEIVQRMFDDTIGSVTSSMESMRRRQKKWEDQHKNDDVEMME
Protein: TOM1-like protein 9 (Q8L860)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might contribute to the loading of the ESCRT machinery.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22639582}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Protein ELC-like
- Protein ELC
- non-specific serine/threonine protein kinase
- Syntaxin-21
- Vacuolar protein sorting-associated protein 60.1
Sequence:
MVNAMVERATSEMLIGPDWAMNLEICDMLNSDPAQAKDVVKGIKKRIGSRNPKAQLLALTLLETIVKNCGDMVHMHVAEKGVIHEMVRIVKKKPDFHVKEKILVLIDTWQEAFGGPRARYPQYYAGYQELLRAGAVFPQRSERSAPVFTPPQTQPLTSYPPNLRNAGPGNDVPEPSAEPEFPTLSLSEIQNAKGIMDVLAEMLSALEPGNKEDLKQEVMVDLVEQCRTYKQRVVHLVNSTSDESLLCQGLALNDDLQRVLTNYEAIASGLPGTSSQIEKPKSETGKSLVDVDGPLIDTGDSSNQANGATSSSGNGVLNQLALPAPPVTNGSANSKIDLLSGDDLALVPVGPPQPASPVASDQNALALIDMFSDNTNNPSPATAPSGNPAQNIPLNPQGHQQPNSQAGEAGLQQSNGFAPQVGYSQFEQPSYGQGVSSPWSSQPAQQPVQPSYGAQDSTAFPPPPWEAQLQDYSPSAESGSPFSPGMHPTQTAFTHAQPVNNNNPYPQIPQTGPPVNNNSPYAQMPQTGQAVANISPYPQIPQNGVYMPNQPNQALGSGYQPQQQQQQQMMMAQYYAQQQQLQQQQQQQAYGNQMGGYGYGYNQQQQGSSPYLDQQMYGLSMRDQTSHQVASSSSTTSYLPPMKPKNKPEDKLFGDLVDISKFKPTKPTSGRAGTM
Protein: Uncharacterized protein (Q383S5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMRRTPPVARVVVSSFLREPSERKSFKETLAECDANGIDMASSLTSDFALLQSKLFKYRVVRLGDELQYVCRHPLGSLPSLPALVVHIILLTTVFFLFRNLGRFSSTALVKPPVALPGEGDS
Protein: Integral membrane protein GPR137 (Transmembrane 7 superfamily member 1-like 1 protein) (Q96N19)
Organism: Homo sapiens (Human)
Function: Lysosomal integral membrane protein that may regulate MTORC1 complex translocation to lysosomes. May play a role in autophagy.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:31036939}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MESNLSGLVPAAGLVPALPPAVTLGLTAAYTTLYALLFFSVYAQLWLVLLYGHKRLSYQTVFLALCLLWAALRTTLFSFYFRDTPRANRLGPLPFWLLYCCPVCLQFFTLTLMNLYFAQVVFKAKVKRRPEMSRGLLAVRGAFVGASLLFLLVNVLCAVLSHRRRAQPWALLLVRVLVSDSLFVICALSLAACLCLVARRAPSTSIYLEAKGTSVCQAAAMGGAMVLLYASRACYNLTALALAPQSRLDTFDYDWYNVSDQADLVNDLGNKGYLVFGLILFVWELLPTTLLVGFFRVHRPPQDLSTSHILNGQVFASRSYFFDRAGHCEDEGCSWEHSRGESTRCQDQAATTTVSTPPHRRDPPPSPTEYPGPSPPHPRPLCQVCLPLLAQDPGGRGYPLLWPAPCCSCHSELVPSP