wanglab/gogpt-training-data huggingface dataset:
Protein: Selenocysteine lyase (EC 4.4.1.16) (H7C277)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
XEQVAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAEFGQKRIHLNSQFPGTQRLPNTCNFSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQGFFSQNALAFGHTSHVDICIGVIFSGITFLMCGFTVQGTT
Protein: GTP-binding nuclear protein Ran (EC 3.6.5.-) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein) (P52301)
Organism: Xenopus laevis (African clawed frog)
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins (By similarity). RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis (By similarity). In concert with nemp1a/b, required for proper eye development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000269|PubMed:8413630}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
Interaction partners:
Sequence:
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEQDLQNAQATALPDEDDDL
Protein: Sodium-coupled neutral amino acid transporter 5 (Solute carrier family 38 member 5) (System N transporter 2) (A2VCW5)
Organism: Rattus norvegicus (Rat)
Function: Symporter that cotransports neutral amino acids and sodium ions, coupled to an H(+) antiporter activity. Releases L-glutamine and glycine from astroglial cells and may participate in the glutamate/GABA-glutamine cycle and the NMDA receptors activation. In addition contributes significantly to L-glutamine uptake in retina, namely in ganglion and Mueller cells and, therefore participates in the retinal glutamate-glutamine cycle. The transport activity is pH sensitive, Li(+) tolerant, bidirectional and associated with large uncoupled fluxes of protons. The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+). May have particular importance for modulation of net hepatic glutamine flux.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15390093, ECO:0000269|PubMed:22821889}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at astroglial membrane. {ECO:0000269|PubMed:22821889}.
Interaction partners:
- Sodium-coupled neutral amino acid transporter 3
- Neutral amino acid transporter B
Sequence:
MAISCAVGMEMQEPKMNGTLSTGAAAGYRQEREGFLPTTHGPAPGRKPVQFLDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCASVVGIRAYEQLGQRAFGPAGKVVVAIIICLHNVGAMSSYLFIIKSELPLVIGTFLHMDPEGDWFLKGNLLIILVSLLIILPLALMKHLGYLGYTSSLSLTCMLFFLISVIYKKFQLGCVVSHNDTVVESEPAPLQAFNSSCEAKLFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCCPTQRRMQAVANMSIGAMFIMYGLTATFGYLTFYSTVKAEMLEMYTQEDLLILCVRLAVLLAVTLTVPVVLFPIRRALQQLLFPSKAFSWPRHVAIALILLILVNILVICVPTIRDIFGFIGSTSAPSLIFILPSVFYLRIVPADMEPLFSWPKIQALCFGVLGVLFMAISLGFMFANWATGQSRMSGH
Protein: U3 small nucleolar RNA-associated protein 11 (U3 snoRNA-associated protein 11) (U three protein 11) (P34247)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase NEP1
- rRNA 2'-O-methyltransferase fibrillarin
- U3 small nucleolar RNA-associated protein 5
- U3 small nucleolar RNA-associated protein 12
- U3 small nucleolar RNA-associated protein 7
- U3 small nucleolar RNA-associated protein 10
- U3 small nucleolar RNA-associated protein 14
- Something about silencing protein 10
- U3 small nucleolar RNA-associated protein 9
- U3 small nucleolar ribonucleoprotein protein IMP4
Sequence:
MAKLVHDVQKKQHRERSQLTSRSRYGFLEKHKDYVKRAQDFHRKQSTLKVLREKAKERNPDEYYHAMHSRKTDAKGLLISSRHGDEEDESLSMDQVKLLKTQDSNYVRTLRQIELKKLEKGAKQLMFKSSGNHTIFVDSREKMNEFTPEKFFNTTSEMVNRSENRLTKDQLAQDISNNRNASSIMPKESLDKKKLKKFKQVKQHLQRETQLKQVQQRMDAQRELLKKGSKKKIVDSSGKISFKWKKQRKR
Protein: Spermidine N(1)-acetyltransferase (SAT) (EC 2.3.1.57) (Spermidine/spermine N(1)-acetyltransferase) (SSAT) (Q9KL03)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can use polyamines such as spermine and N(1)-acetylspermine, but not putrescine or cadaverine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphate acetyltransferase
- Transcriptional regulator
- Pyruvate-flavoredoxin oxidoreductase
- Bifunctional chorismate mutase/prephenate dehydratase
- Glutamate synthase large chain
- Glutamate synthase large chain
- Putative mannose-1-phosphate guanylyltransferase
Sequence:
MNSQLTLRALERGDLRFIHNLNNNRNIMSYWFEEPYESFDELEELYNKHIHDNAERRFVVEDAQKNLIGLVELIEINYIHRSAEFQIIIAPEHQGKGFARTLINRALDYSFTILNLHKIYLHVAVENPKAVHLYEECGFVEEGHLVEEFFINGRYQDVKRMYILQSKYLNRSE
Protein: At1g24210 (Paired amphipathic helix (PAH2) superfamily protein) (Q8LCT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MVGRRVSPALTKDDAHSYIIAVKETFHDEPTKYQEFIKLLNGVCDHRVDKYSVIARVEELMKDHQDLLLGFSVFLPPVSVEDFINKLKTRFQSLDTHVVGAIRGLMKMFKEGKMSVKEVQEEVIDVLFYHEDLIEDFLRFFTKNPVSTASLLLQL
Protein: Alpha-soluble NSF attachment protein (SNAP-alpha) (N-ethylmaleimide-sensitive factor attachment protein) (Q23983)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Also between the endosome and phagosome.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:17151602}. Membrane {ECO:0000269|PubMed:17151602}; Peripheral membrane protein {ECO:0000269|PubMed:17151602}.
Interaction partners:
- LD27967p
- Syntaxin-1A
- Syntaxin-5
- LD34211p
- LD23667p
- Protein sly1 homolog
- Secretory 22, isoform B
- Synaptosomal-associated protein
- LD03592p
- Synaptosomal-associated protein 25
Sequence:
MGDNEQKALQLMAEAEKKLTQQKGFLGSLFGGSNKVEDAIECYQRAGNMFKMSKNWTKAGECFCEAATLHARAGSRHDAGTCYVDASNCYKKVDVESAVNCLMKSIDIYTDMGRFTMAAKHHQSIAEMYESDPNNLAKSIQHYEQAADYFKGEESVSSANKCMLKVAQYAAQLEDYEKAISIYEQVAASSLESSLLKYSAKEYFFRAALCHLSVDLLNAQHAIEKYAQQYPAFQDSREFKLIKVLCENLEEQNIEGFTEAVKDYDSISRLDQWYTTILLRIKKAADEDPDLR
Protein: Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase (D4A8A0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Dihydroorotate dehydrogenase
- Argininosuccinate synthase
- Amidophosphoribosyltransferase
- Ornithine transcarbamylase, mitochondrial
- Glutamine synthetase
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- Asparagine synthetase
- Glutamine--fructose-6-phosphate aminotransferase 2
- Glutamine--fructose-6-phosphate aminotransferase 1
Sequence:
MAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRIFAVDCGLKYNQIRCLCQLGAEVTVVPWNHELDSRKYDGLFLSNGPGDPASYPGVVSTLNRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLETVRDTVAGNAEGRTVRERLAQRLCPPELPIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGILLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDVELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHRGRPLPQDLLHQAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVESVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQPPPPTPTTTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKPPRKVAESELIGTPDGPCYPVPPVPRQASPQNLGSSGLLHPQMSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSSQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
Protein: C-terminal binding protein 1 (H0Y8U5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
Protein: Phosphonoacetate hydrolase (EC 3.11.1.2) (Q51782)
Organism: Pseudomonas fluorescens
Function: Specifically hydrolyzes phosphonoacetate. Does not have activity on other organophosphonates or acetates.
Interaction partners:
Sequence:
MTQLISVNSRSYRLSSAPTIVICVDGCEQEYINQAIQAGQAPFLAELTGFGTVLTGDCVVPSFTNPNNLSIVTGAPPSVHGICGNFFFDQETQEEVLMNDAKYLRAPTILAEMAKAGQLVAVVTAKDKLRNLLGHQLKGICFSAEKADQVNLEEHGVENILARVGMPVPSVYSADLSEFVFAAGLSLLTNERPDFMYLSTTDYVQHKHAPGTPEANAFYAMMDSYFKRYHEQGAIVAITADHGMNAKTDAIGRPNILFLQDLLDAQYGAQRTRVLLPITDPYVVHHGALGSYATVYLRDAVPQRDAIDFLAGIAGVEAVLTRSQACQRFELPEDRIGDLVVLGERLTVLGSAADKHDLSGLTVPLRSHGGVSEQKVPLIFNRKLVGLDSPGRLRNFDIIDLALNHLA
Protein: Zinc finger FYVE domain-containing protein 1 (Double FYVE-containing protein 1) (SR3) (Tandem FYVE fingers-1) (Q9HBF4)
Organism: Homo sapiens (Human)
Function: Plays a role in the formation of lipid droplets (LDs) which are storage organelles at the center of lipid and energy homeostasis. Regulates the morphology, size and distribution of LDs. Mediates the formation of endoplasmic reticulum-lipid droplets (ER-LD) contacts by forming a complex with RAB18 and ZW10. Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through FYVE-type zinc finger.
Subcellular location: Golgi apparatus, Golgi stack {ECO:0000269|PubMed:11256955}. Golgi apparatus {ECO:0000269|PubMed:11024279, ECO:0000269|PubMed:11739631, ECO:0000269|PubMed:25876663}. Endoplasmic reticulum {ECO:0000269|PubMed:11024279, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:25876663, ECO:0000269|PubMed:30970241}. Lipid droplet {ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035}. Preautophagosomal structure {ECO:0000269|PubMed:25876663, ECO:0000269|PubMed:31293035, ECO:0000269|PubMed:33499712}. Mitochondrion {ECO:0000269|PubMed:25876663}. Note=Resides predominantly in the cisternal stacks of the Golgi (PubMed:11256955). Colocalizes with TRIM13 on the perinuclear endoplasmic reticulum (PubMed:22178386). During starvation conditions, localizes to omegasomes which are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures (PubMed:25876663, PubMed:31293035). Localizes to lipid droplets in the presence of oleic acid (PubMed:30970241, PubMed:31293035). {ECO:0000269|PubMed:11256955, ECO:0000269|PubMed:22178386, ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31293035}.
Interaction partners:
- WD repeat domain phosphoinositide-interacting protein 2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- WD repeat domain phosphoinositide-interacting protein 1
- Beclin 1-associated autophagy-related key regulator
- Beclin-1
- Autophagy protein 5
- Serine/threonine-protein kinase ULK1
- Ubiquitin-like protein ATG12
- Calcium-binding and coiled-coil domain-containing protein 2
- Zinc finger protein ZPR1
Sequence:
MSAQTSPAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKPGHVPYCDLCKGLSGHLPGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYNVSNLQESLEAEEMDEETKRKKMTEKVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGREVFKTSPTQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHFTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEVPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGVGCKKSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYERGEEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDGFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNKCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDNCYEARNVQLAVTEAQVDDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSIKLSKHHCRACGQGFCDECSHDRRAVPSRGWDHPVRVCFNCNKKPGDL
Protein: Bifunctional protein HldE [Includes: D-beta-D-heptose 7-phosphate kinase (EC 2.7.1.167) (D-beta-D-heptose 7-phosphotransferase) (D-glycero-beta-D-manno-heptose-7-phosphate kinase); D-beta-D-heptose 1-phosphate adenylyltransferase (EC 2.7.7.70) (D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase)] (P76658)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Interaction partners:
- Phosphoheptose isomerase
- D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- ADP-L-glycero-D-manno-heptose-6-epimerase
- Lipopolysaccharide heptosyltransferase 2
- Lipopolysaccharide heptosyltransferase 1
- Lipopolysaccharide heptosyltransferase 3
- DnaA initiator-associating protein DiaA
- Lipopolysaccharide glucosyltransferase WaaG
- Lipopolysaccharide core heptose
- 3-deoxy-D-manno-octulosonic acid transferase
Sequence:
MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVNTIEERPGGAANVAMNIASLGANARLVGLTGIDDAARALSKSLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPQPLHERINQALSSIGALVLSDYAKGALASVQQMIQLARKAGVPVLIDPKGTDFERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGMSLLQPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGTSTVSPIELENAVRGRADTGFGVMTEEELKLAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGDSRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEEIAGSKEVWANGGEVLVLNFEDGCSTTNIIKKIQQDKKG
Protein: Small ribosomal subunit protein mS41 (Q389L3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- 30S ribosomal protein S8, putative
- Uncharacterized protein
- Trans-sialidase
- Ribosomal protein S23 mitochondrial conserved domain-containing protein
Sequence:
MLKRTLTVLDQTYGPHKSYKYTYMPDPRKLAPIETTQRSEIVPQSIRPPTSYVPNHETFLERADIHRLRPTSDFKASFKDWNDLFTCDKRQLRVRGIPRMTRDAIRTAVQAFQNGNPPERFDTKEEWLYYKQFKTVDYSYRVIPELPEKYRPHQSGIDQAPLPDYREINKMPQWAECEERRQSKKTV
Protein: Osteopontin (Q9I832)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLTLLCLCFISITAAWPVSKSKQHAISASSEEKYDPRSHHTHRYHQDHVDSQSQEHLQQTQNDLASLQQTHYSSEENADVPEQPDFPDVPSKSQETVDDDDDDDNDSNDTDESDEVFTDFPTEAPVAPFNRGDNAGRGDSVAYGFRAKAHVVKASKIRKAARKLIEDDATTEDGDSQPAGLWWPKESREQNSRELPQHQSVENDSRPKFDSREVDGGDSKASAGVDSRESQGSVPAVDASNQTLESAEDAEDRHSIENNEVTR
Protein: WD repeat-containing protein WRAP73 (WD repeat-containing protein 8) (WD repeat-containing protein antisense to TP73 gene) (Q9P2S5)
Organism: Homo sapiens (Human)
Function: The SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome. Required for the centrosomal localization of SSX2IP and normal mitotic bipolar spindle morphology. Required for the targeting of centriole satellite proteins to centrosomes such as of PCM1, SSX2IP, CEP290 and PIBF1/CEP90. Required for ciliogenesis and involved in the removal of the CEP97:CCP110 complex from the mother centriole. Involved in ciliary vesicle formation at the mother centriole and required for the docking of vesicles to the basal body during ciliogenesis; may promote docking of RAB8A- and ARL13B-containing vesicles.
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:26545777, ECO:0000269|PubMed:26675238}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26675238}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:26675238}. Note=Enriched in the proximal end of the mother centriole (PubMed:26545777). During ciliogenesis also associated with the basal body of the adjacent centriole (PubMed:26675238). {ECO:0000269|PubMed:26545777, ECO:0000269|PubMed:26675238}.
Interaction partners:
- Afadin- and alpha-actinin-binding protein
- Multiple epidermal growth factor-like domains protein 6
- Centrosomal protein of 135 kDa
- Zinc finger and BTB domain-containing protein 40
Sequence:
MNFSEVFKLSSLLCKFSPDGKYLASCVQYRLVVRDVNTLQILQLYTCLDQIQHIEWSADSLFILCAMYKRGLVQVWSLEQPEWHCKIDEGSAGLVASCWSPDGRHILNTTEFHLRITVWSLCTKSVSYIKYPKACLQGITFTRDGRYMALAERRDCKDYVSIFVCSDWQLLRHFDTDTQDLTGIEWAPNGCVLAVWDTCLEYKILLYSLDGRLLSTYSAYEWSLGIKSVAWSPSSQFLAVGSYDGKVRILNHVTWKMITEFGHPAAINDPKIVVYKEAEKSPQLGLGCLSFPPPRAGAGPLPSSESKYEIASVPVSLQTLKPVTDRANPKIGIGMLAFSPDSYFLATRNDNIPNAVWVWDIQKLRLFAVLEQLSPVRAFQWDPQQPRLAICTGGSRLYLWSPAGCMSVQVPGEGDFAVLSLCWHLSGDSMALLSKDHFCLCFLETEAVVGTACRQLGGHT
Protein: Proteasome subunit beta inpE (EC 3.4.25.1) (Fellutamide B biosynthesis cluster protein E) (Inp cluster protein E) (Q5B7I7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Proteasome subunit beta type-6; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor. In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB. The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB. The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu. Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B. InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA. The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides. The MFS efflux transporter inpD may contribute to fellutamide resistance as well.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000305}.
Interaction partners:
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome component Pup3, putative
- Proteasome subunit beta
- proteasome endopeptidase complex
Sequence:
MAKETRFYPYTSNGGATLGVSGPDFAILAGDTRSTAGYNINTRYEPKVFTIQDARDRSIVISVIGFAADGRALKERLDAIVAMYKYQHGKNIGLRACAQRVSTMLYEKRFFPYQLQTMVAGIDADGQGAIYYYDPAGCIEKRSHCAAGEASSLMLPFLDSQAPRLQPLSLQTAQQLVRDAYTGATERHIEVGDHLQMLVVTREGVSEQLVDLKKD
Protein: Musculoskeletal embryonic nuclear protein 1 (Q76MS9)
Organism: Gallus gallus (Chicken)
Function: May be involved in the development and regeneration of the musculoskeletal system.
Subcellular location: Nucleus {ECO:0000269|PubMed:23528857}.
Interaction partners:
- Leiomodin-2
Sequence:
MSQPDPVKKKRPPVKEEDLKGARGNLSKNQEIKSKTYQVMKQCEQMGSAAPSIFSRARTGSETVFEKSKDEPPKSVFG
Protein: UPF0587 protein YCR090C (P25654)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Cystine transporter
Sequence:
MPLFLVLKATLSENVTKVSIENTNESRAEFAFDLQCTSCRELHDSKVIINTFEEYAMPASKGTASFLMKCKFCSKELSVNLCAFEDEYLTDQSDDKWAKIKDVRKKHGLSKVKEDSFIPLSLDCRGCELIKFYPDTITFEVSLSSGKVMSCQLEDNEWYDYDDNLGEEVTMTDFSSSIIKGK
Protein: Translocator protein 2 (E2RDM9)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Cholesterol-binding protein involved in the redistribution of cholesterol from lipid droplets to the endoplasmic reticulum. Required to meet cholesterol demands during erythropoietic differentiation. May play a role in transport processes at the plasma membrane of erythrocytes, including regulating VDAC-mediated ATP export, and import of the heme precursors protoporphyrin IX and 5-aminolevulinic acid (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5TGU0}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:32358067}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane and intracellular membranes in developing and mature erythrocytes. {ECO:0000250|UniProtKB:Q5TGU0}.
Interaction partners:
- Uncharacterized protein.
- Steroidogenic acute regulatory protein
Sequence:
MQPQGAIFVALPHLGPILVSLLTRHRMIRWYDIPKKPPWCPPHKVLLAGWITIYFVMGYASYLVWKDLGGGFGRPLALPLGLYAVQLAVSWAVLIFFFAAHAHGLALLHMLLLYGLVVSTALIWHPINKLAAVLLLPYLAWLTVTASIAYHLWRDSLCPNHHQPLPMGEKRD
Protein: Pentatricopeptide repeat-containing protein (Q389C8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRDVLASFIEASAARGAWESALAAWNTALFTNSREVSSNHTLLLTRVLAQYSRWREAVAVATSAETALCSRQLAARRVALLATIKAGSWREACQQVLSVRRYLENSAAIGPSVGYTEEAEISKELYLVVELIEQDLLQGIPTEQRGLWDPVVGCLRGKVERHPPKQAGELRRCIPDVENTTRSDEYQMRCGSDADHVTNNEELVHILRKPKERNSWCGALRLLLDMQHPNAASVNIVITILKSQGREAEVLRVVNDFMVSRKIQPTAITVKAVSEAANTMRSLPLCISILDNPSMRGKLTAQSAVPMVLALQRLAEWKRCLEWWSSVPPPTTLSGEGTTDYNSGGVPNLRRHLKLSSYVAVCLAGGGCWLDALAALHYAAPYDPPLAILFSLRALRVAGNWEAAVTLLHKNCSVWKGSKVTLQVLDVVTEQNAESWIPPHVVHMLRGLFRS
Protein: Proteasome inhibitor PI31 subunit (A0A140VJT2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MAGLEVLFASAAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSELLPAGWNNNKDLYVLRYEYKDGSRKLLVKAITVESSMILNVLEYGSQQVADLTLNLDDYIDAEHLGDFHRTYKNSEELRSRIVSGIITPIHEQWEKANVSSPHREFPPATAREVDPLRIPPHHPHTSRQPPWCDPLGPFVVGGEDLDPFGPRRGGMIVDPLRSGFPRALIDPSSGLPNRLPPGAVPPGARFDPFGPIGTSPPGPNPDHLPPPGYDDMYL