wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (E2) (P11961)
Organism: Geobacillus stearothermophilus (Bacillus stearothermophilus)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Interaction partners:
Sequence:
MAFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLDAPGYENMTFKGQEQEEAKKEEKTETVSKEEKVDAVAPNAPAAEAEAGPNRRVIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGAKPAPAAAEEKAAPAAAKPATTEGEFPETREKMSGIRRAIAKAMVHSKHTAPHVTLMDEADVTKLVAHRKKFKAIAAEKGIKLTFLPYVVKALVSALREYPVLNTSIDDETEEIIQKHYYNIGIAADTDRGLLVPVIKHADRKPIFALAQEINELAEKARDGKLTPGEMKGASCTITNIGSAGGQWFTPVINHPEVAILGIGRIAEKPIVRDGEIVAAPMLALSLSFDHRMIDGATAQKALNHIKRLLSDPELLLMEA
Protein: TPR domain protein (A0A0H2UQR2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MLQALEEQDLTKAEHYFAKALENDSSDLLYELATYLEGIGFYPQAKEIYLKIVEDFPEVHLNLAAIASEDGQIEEAFTYLEEIQADSDWYVSSLALKADLYQLEGLTDVAREKLLEALTYSEDSLLILGLAELDSELENYQAAIQAYAQLDNRSIYEQTGISTYQRIGFAYAQLGKFETATEFLEKALELEYDDLTAFELASLYFDQEEYQKATLYFKQLDTISPDFEGYEYGYSQALHKEHQVQEALRIAKQGLEKNPFETRLLLAASQFSYELHDASGAENYLLTAKEDAEDTEEILLRLATIYLEQERYEDILELQSEEPENLLTKWMIARSYQEMDDLDTAYEYYQELTGDLKDNPEFLEHYIYLLRELGHFEEAKVHAHTYLKLVPDDVQMQELFERL
Protein: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase S (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase S) (Glucuronosyltransferase S) (GlcAT-S) (UDP-glucuronosyltransferase S) (DmGlcAT-BSI) (Q9VLA1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Enzyme has a broad specificity.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSSARLLESQTSDEDNEDIERRPHQSHSRSCSNNTTPTHPPHPMVRKGGVARRICLIGGALFLLLVALCYLTLSGDTRLGGSEDSEEGSHHGLDSMNFRPLNETVHICSESYEDRRQFMQDKPQSDYVQLPVIYFVTPTYPRREQIPELTRLAHTLLHIPRLHWLVADDQEKCNDYMDTLLYRFGMPFTHMVSPMPSKFRNEKPAPRGVANRRAALQWIRQHNLTNGILYFGDDDNTYDLRLFSEIRKTQRVSMFPVGLIADYGVSGPVVRKGKVVAFLDSWVAGRRWPVDMAGFAVNLEYMAQYPYVNMPYKPGYEEDLFLRSIGLQMNLIEPRGNNCTEILVWHTQTKSKKLGMVRLESKYLDDRSNLGALLHNLKLMGVTSTTESEGRNALISKNGRENPHSKILS
Protein: NPC intracellular cholesterol transporter 1 isoform X1 (Niemann-Pick disease, type C1) (A0A2R8Q2J0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- NPC intracellular cholesterol transporter 2
- NPC intracellular cholesterol transporter 2
- Sterol regulatory element-binding protein 2
- Insulin-induced gene protein
- Sterol regulatory element-binding transcription factor 1.
- Insulin-induced gene 1 protein
Sequence:
MLLLGRNHIFRLLLATVLLSHWVHGQHCIWYGECGNSPNVPEKKLNCNYTGPAVPLPNEGQELLQELCPRLVYADNRVCCDTQQLNTLKSNIQIPLQYLSRCPACFFNFMTLFCELTCSPRQSQFISVKDFLKEKNQTSVGNVTYYITQTFADAMFNACRDVQAPSSNIKALGLLCGRDASVCTPQIWIQYMFSISNGQVPFGIEPIFTDVPVQGMTPMNNRTFNCSQSLDDGSEPCSCQDCSEVCGPTPVPPPIPPPWIILGLDAMSFIMWCSYIAFLLIFFGVVLGAWCYRRSVVTSEYGPILDSNQPHSLNSDGTDLIDEASCCETVGERFENSLRLVFSRWGSLCVRQPLTIILSSLVLICICSAGLSYMRITTNPVELWSAPSSRARQEKNYFDQHFGPFFRTEQLIITTPWTEEGGFSTITGDIIPFSPILNLSLLHQVLDLQLEIENLIAEYKGENVTLKDICVSPLSPYNDNCTILSVLNYFQNSHEVLDHEFQDEFFLYNDYHTHLLYCASSPTSLDDTSRLHDPCMGTFGGPVFPWLVLGGYEDSAYNNATALVITFPVTNYLNDTEKLGKALAWEKEFIRFMKNYENPNLTVSFSSERSIEDEIDRESNSDVSTIVISYIIMFVYISVALGRINSCRTLLVDSKISLGIAGILIVLSSVACSLGIFSYIGIPLTLIVIEVIPFLVLAVGVDNIFIIVQTYQRDERMPEEELHQQIGRILGDVAPSMFLSSFSETVAFFLGALSTMPAVRTFSLFAGLAIFIDFLLQISCFVSLLGLDIKRQEANRMDILCCVKLSDGQEEKSEGWLFRFFKKIYAPFILKDWVRPLVVAVFVGMLSFSIAVVNKVEIGLEQTLSMPDDSYVLNYFGNLSKYLHTGPPVYFVVEDGHDYKTFEGQNAVCGGVGCNNDSLVQQIYTASLMSNYTRISNVPSSWLDDYFDWVKPQSTCCRYYNSTGAFCNASVVDKSCVHCRPMTSSGKQRPNGTEFMHFLPMFLSDNPNIKCGKGGHAAYGTAVDLKDNNTDVGATYFMSYHTILKNSSDFINAMKMARELTDNITQTLSTHDKSYKVFPYSVFYVFYEQYLTIVDDTALNLGVSLSAIFIVTAVLLGFELWSAVLVCFTIAMILINMFGVMWLWSISLNAVSLVNLVMSCGISVEFCSHIVRAFSISTRSSRVERAEEALAHMGSSVFSGITLTKFGGILILALSKSQIFQIFYFRMYLAIVLLGAAHGLIFLPVLLSYAGKSLSPRTFMICLEAVVHLKHLKTRHH
Protein: 2-methylcitrate dehydratase 2 (2-MC dehydratase) (EC 4.2.1.79) (Aconitate hydratase) (ACN) (Aconitase) (EC 4.2.1.3) (Q8NSL3)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer 2-methyl-aconitate. Could also catalyze the dehydration of citrate and the hydration of cis-aconitate (By similarity).
Interaction partners:
- Probable 2-methylisocitrate lyase 2
- 2-methylcitrate synthase 2
- H+/gluconate symporter and related permeases
- ABC-type dipeptide/oligopeptide/nickel transport systems, periplasmic components
- Large ribosomal subunit protein uL24
- Probable 2-methylisocitrate lyase 1
- HTH-type transcriptional regulator RamB
Sequence:
MINHEVRTHRSAEEFPYEEHLAHKIARVAADPVEVAADTQEMIINRIIDNASVQAASVLRRPVSSARAMAQVRPVTDGRGASVFGLPGRYAAEWAALANGTAVRELDFHDTFLAAEYSHPGDNIPPILAAAQQAGKGGKDLIRGIATGYEIQVNLVRGMCLHEHKIDHVAHLGPSAAAGIGTLLDLDVDTIYQAIGQALHTTTATRQSRKGAISSWKAFAPAFAGKMSIEAVDRAMRGEGAPSPIWEGEDGVIAWLLSGLDHIYTIPLPAEGEAKRAILDTYTKEHSAEYQSQAPIDLARSMGEKLAAQGLDLRDVDSIVLHTSHHTHYVIGTGSNDPQKFDPDASRETLDHSIMYIFAVALEDRAWHHERSYAPERAHRRETIELWNKISTVEDPEWTRRYHSVDPAEKAFGARAVITFKDGTVVEDELAVADAHPLGARPFAREQYIQKFRTLAEGVVSEKEQDRFLDAAQRTHELEDLSELNIELDADILAKAPVIPEGLF
Protein: Bacterial surface antigen (D15) domain-containing protein (Q55DS3)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Translocase of outer mitochondrial membrane
Sequence:
MDDDDIKIKFVNIKSENVFLIETYFKGFEKLPRRDWERGLEYIVGQMENDHVVTKGDFEIDPQTNEITVISKERGISFGVSANTDKTSSTRFQLANPFGKGGLVGFEFSAGLYKNNNGSVSYTDRFGNTLSLLKSSQDPVIKDRNFKIDETTLSYSFQKNSNKFSIFAGDSTVSVLNKNKNKEHLANTGLAFKTGISHIYSSNLRSKSINRLFKIQNELAFPILSSCSFFKSNITYSLDFPLYEQLKFRGDFITGGIFNFSKDSMIPISERFFNGRHYNFEGFVDSSLTEKGRSPYLGSSFFFTFRTALLHKIKDNASVMAYHCIGNTVLPLDSNETTFKSTALKLFSTNSIRSSIGLGISVDMGSADIECSLVKPLFFNSQDELNNFAFGINIKI
Protein: Methyltransferase N6AMT1 (HemK methyltransferase family member 2) (M.HsaHemK2P) (Lysine N-methyltransferase 9) (EC 2.1.1.-) (Methylarsonite methyltransferase N6AMT1) (EC 2.1.1.-) (Protein N(5)-glutamine methyltransferase) (EC 2.1.1.-) (Q9Y5N5)
Organism: Homo sapiens (Human)
Function: Methyltransferase that can methylate proteins and, to a lower extent, arsenic. Catalytic subunit of a heterodimer with TRMT112, which monomethylates 'Lys-12' of histone H4 (H4K12me1), a modification present at the promoters of numerous genes encoding cell cycle regulators. Catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly-Gln-Xaa-Xaa-Xaa-Arg motif. Methylates ETF1 on 'Gln-185'; ETF1 needs to be complexed to ERF3 in its GTP-bound form to be efficiently methylated. May also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid. It however only plays a limited role in arsenic metabolism compared with AS3MT.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6SKR2}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Histone H4
- Peptide chain release factor 1, mitochondrial
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Ferrochelatase, mitochondrial
- Eukaryotic peptide chain release factor subunit 1
- MTRF1L release factor glutamine methyltransferase
- tRNA
- Peptide chain release factor 1-like, mitochondrial
- Mitochondrial translation release factor in rescue
Sequence:
MAGENFATPFHGHVGRGAFSDVYEPAEDTFLLLDALEAAAAELAGVEICLEVGSGSGVVSAFLASMIGPQALYMCTDINPEAAACTLETARCNKVHIQPVITDLVKGLLPRLTEKVDLLVFNPPYVVTPPQEVGSHGIEAAWAGGRNGREVMDRFFPLVPDLLSPRGLFYLVTIKENNPEEILKIMKTKGLQGTTALSRQAGQETLSVLKFTKS
Protein: Progranulin (PGRN) (Acrogranin) (Epithelin precursor) (Glycoprotein of 88 Kda) (GP88) (Glycoprotein 88) (Granulin precursor) (PC cell-derived growth factor) (PCDGF) (Proepithelin) (PEPI) [Cleaved into: Paragranulin; Granulin-1 (Granulin G); Granulin-2 (Granulin F); Granulin-3 (Epithelin-2) (Granulin B); Granulin-4 (Epithelin-1) (Granulin A); Granulin-5 (Granulin C); Granulin-6 (Granulin D); Granulin-7 (Granulin E)] (P28799)
Organism: Homo sapiens (Human)
Function: Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation. Regulates protein trafficking to lysosomes and, also the activity of lysosomal enzymes. Facilitates also the acidification of lysosomes, causing degradation of mature CTSD by CTSB. In addition, functions as wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases. Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity.
Subcellular location: Secreted {ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:26370502}. Lysosome {ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:26370502, ECO:0000269|PubMed:28073925, ECO:0000269|PubMed:28541286, ECO:0000269|PubMed:28743268}. Note=Endocytosed by SORT1 and delivred to lysosomes (PubMed:21092856, PubMed:28073925). Targeted to lysosome by PSAP via M6PR and LRP1, in both biosynthetic and endocytic pathways (PubMed:26370502, PubMed:28073925). Co-localized with GBA1 in the intracellular trafficking compartments until to lysosome (By similarity). {ECO:0000250|UniProtKB:P28798, ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:26370502, ECO:0000269|PubMed:28073925}.
Interaction partners:
- Sortilin
- TAR DNA-binding protein 43
- Antileukoproteinase
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Transmembrane protein 106B
- Guanine nucleotide exchange factor C9orf72
- Microtubule-associated protein tau
- Cathepsin D
- Prosaposin
- Charged multivesicular body protein 2b
Sequence:
MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL
Protein: Phosphatase and actin regulator 1 (P62024)
Organism: Rattus norvegicus (Rat)
Function: Binds actin monomers (G actin) and plays a role in multiple processes including the regulation of actin cytoskeleton dynamics, actin stress fibers formation, cell motility and survival, formation of tubules by endothelial cells, and regulation of PPP1CA activity (By similarity). Involved in the regulation of cortical neuron migration and dendrite arborization (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15107502}. Synapse {ECO:0000269|PubMed:15107502}. Nucleus {ECO:0000250}. Note=Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import (By similarity). Enriched at synapses. {ECO:0000250}.
Interaction partners:
- WD repeat-containing protein 37
- Armadillo repeat-containing protein 8
Sequence:
MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQARRATLLLPPTLMAASSEDDIDRRPIRRVRSKSDTPYLAEARISFNLGAAEEVERLAAMRSDSLVPGTHTPPIRRRSKFANLGRIFKPWKWRKKKSEKFKHTSAALERKISMRQSREELIKRGVLKEIYDKDGELSISNEDDSLTNGQSLSSSQLSLPALSEMEPVPMPRDPCSYEVLQASDIMDGPDPGAPVKLPCLPVKLSPPLPPKKVLICMPVGGPELSLASYAAQKSSQQAVAQHHHTVLPSQMQHQLQYGSHGQHLPSSTGTLPMHPSGCRMIDELNKTLAMTMQRLESSEQRVPCSTSYHSSGLHSSDGVTKAGPLGLPEIRQVPTVVIECDDNKENVPHEPDYEDSSCLYAREEEEEEEDEDDDASLYTSSLAMKVCRKDSLAIKLSNRPSKRELEEKNILPRQTDEERLELRQQIGTKLTRRLSQRPTAEELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELRERKILIRFSDYVEVADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRFHRP
Protein: POP7 homolog, ribonuclease P/MRP subunit (C9JYM0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MAENREPRGAVEAELDPVEYTLRKRLPSRLPRRPNDIYVNMKTDFKAQLARCQKLLDGGARGQNACSEIYIHGLGLAINRAINIALQLQAGSFGSLQVAANTSTVELVDELEPETDTREPLTRIRNNSAIHIRVFRV
Protein: ATP-dependent translocase ABCB1 (ATP-binding cassette sub-family B member 1B) (Multidrug resistance protein 1B) (EC 7.6.2.2) (P-glycoprotein 1) (Phospholipid transporter ABCB1) (EC 7.6.2.1) (CD antigen CD243) (P06795)
Organism: Mus musculus (Mouse)
Function: Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P08183}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000250|UniProtKB:P08183}. Cytoplasm {ECO:0000250|UniProtKB:P08183}. Note=ABCB1 localization is influenced by C1orf115 expression levels (plasma membrane versus cytoplasm). {ECO:0000250|UniProtKB:P08183}.
Interaction partners:
- ATP-dependent translocase ABCB1
- Phosphatidylcholine translocator ABCB4
- CD44 antigen
Sequence:
MEFEENLKGRADKNFSKMGKKSKKEKKEKKPAVGVFGMFRYADWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFSTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQERRLSMKEAVDEDVPLVSFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAGAKRS
Protein: Testicular spindle-associated protein SHCBP1L (SHC SH2 domain-binding protein 1-like protein) (Q3TTP0)
Organism: Mus musculus (Mouse)
Function: Testis-specific spindle-associated factor that plays a role in spermatogenesis. In association with HSPA2, participates in the maintenance of spindle integrity during meiosis in male germ cells.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24557841}. Note=Colocalizes with alpha tubulin during meiosis (PubMed:24557841). Colocalizes with HSPA2 at spindle during the meiosis process (PubMed:24557841). {ECO:0000269|PubMed:24557841}.
Interaction partners:
- Calcium-binding and spermatid-specific protein 1
Sequence:
MESDATTSEPKASVGSDSSPAEQTVLATLRDSVAAPTRGFMSPVRSVVASPRPVKGKAARRRLQLPPVTQAETCDEEPVPAVPEDQEEAQPLPPIYASPMRGMWRSEKVALYCDQVLQGSKAEDAEEAMSRYLLEKLKAKDRWLGVWKSNPELFFEKYEEASIPFVGILVEVTCKPRQNLSSCFKVTVSVAEPFSSNIANIPRDLVDEVLGELEYSAPLLEVYPVDGQDADVRDIALALEVVRFFYDFLWRDWDDEENCENYTALIEERINLWCDIQDGTIPGPIAQRFKKTLEKYKNKRVELIEYQSNIKEDPSAAEAVECWKKYYEIVMLCGLLKMWEDLRLRVHGPFFPRILRRRKGKRDFGKTITHIVAKVMTTDMVKNLSSDTLLQQHNDLNLALDSCYSGDIVVIFPGEYQASNLALLTDDITIKGVGKREEIMITSEPSHDSFVVSKADNVKLMQLSLIQQGTVDGIVVVESGHLTLENCLLKCEGTGVCVLTGASLTITNSEITGAQGAGVELYPGSIAILEGNEIHHCNNLRTSDSSKSTLGGVNMKVLPAPKLKMTNNHIYNNNGYGVSILQPSEQFFIVAEAALNKGAASGDKKDDKMLSKVMQTLNVEMNNNRIEANLKGDIRIVTG
Protein: Golgi matrix protein 130 kD (Q9W289)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Grasp65
- Syntaxin-5
- Golgi SNAP receptor complex member 1
- General vesicular transport factor p115
- FI01544p
- Golgi microtubule-associated protein, isoform D
- Golgin-245
- Protein transport protein SEC23
- Golgin-84
- Serine/threonine-protein kinase polo
Sequence:
MPDDTQDAKAQKLAAARKKLKEYQQRASNNNGQPGAEEPVAATTQSHSSTVSISSNLSERSDSEINVNGGGAGGTQPPEQSALPTAASYFAQNESEHNGGLADASSLQAIQVIIAEKAQLNAELTKVRLACRERELELEELRILKDQNQLRLEQLQQHCQDQQSTGEQQRQQYAQLQAQLLQSQAQIKDQQSHLNELEAQLKQSNQHQEELQQQLSQKSNELEMAQLKLRQLSDESSVTTDNRVESLVQTQYMYEQQIRDLQAMVGQLTQDKEQAAGQYQNYVQHQSGEIAKLNERNTELSEVLNSLRERERQLVEHVGALERDIQKNISLQAQFKEASQVQPSKEETSEQKALKDELAVLKEQIENFEFERHEFQLKIKSQDDQLQLKNSALDELEKQLERLQAEQPDQSKLLATMESDKVAASRALTQNVEMKNQLDELQQRFVQLTNDKAELVIRLDSEEFANREIRQNYNSMEQKLQANEERFKFKDEEMIRLSHENVELQRQQLMLQQQLDRLRHYEAKAYHAGEETEKENGADAPENEAEEAKEVGLLHNHSHDHSHQHSDGHCHDNDHDHSHEHNHHNAGDHGHPHDHPHDHTHDHSHSHPHDHQHDHPHDHGQNHAHRQAAETLPTAEAVERLQSRFTTLISQVADLTEEKHSLEHLVLQLQSETETIGEYIALYQTQRRMLKQREYEKAAQMRLLQAEREQLREKIEALNKLVVSLGVELPADAAQAKQPEAAAGSEHTPGEGENSQQIINKIQDIISEIKENTEQPSHNHAGDHLNCCMGKFEVV
Protein: Capreomycidine synthase (EC 4.2.1.145) (Viomycin biosynthesis protein C) (Q84CG1)
Organism: Streptomyces vinaceus
Function: Involved in the biosynthesis of capreomycidine, an unusual amino acid used by non-ribosomal peptide synthases (NRPS) to make the tuberactinomycin class of peptide antibiotic such as viomycin and capreomycin. Catalyzes the dehydration of the C3 hydroxyl of (3S)-hydroxy-(2S)-arginine and the intramolecular cyclization to yield (2S,3R)-capreomycidine.
Interaction partners:
Sequence:
MTGPLGAGPQALPAAPLEDWLRERYFQAKTDISSSGVHNYTFGELRALDPALLGTRELDQLMFRDGPSLGDERLRAAVAARVRPGPGHVVMTTHGSSEALYLAFAALVRPGDEVVVATPAYHSLSGLATAAGASLRPWPLRPENGFAPDLDDLRAVLSDRTRLVVVNFPHNPSGACVDPRGRTELLDLVANSQAVLLWDGAFTDLVHDHPPLAEPSQDLDRVLSFGTLSKAYGLPGLRVGWCVVPQDLVSELVRIRDYLTLSLSPLVERVAAVAVEHADALITPRLTEARHNRRRVLEWAAASEGAIDCPVPRGGVTAFPRFTAHTDVTDLCERLLARHGVLVVPGRVFGQADRMRIGFSCPRPELERGLAAISEELGTHARGRRRGTG
Protein: NorD protein (Q51665)
Organism: Paracoccus denitrificans
Interaction partners:
Sequence:
MGLDLEPWEPEETVGKIWHVWASSFGAPQAFEDQAVALSEVSGRLAVLFRALGGGAAVEIRPAAVQASHHRIGWLRRLGTPAETVPHASFDGEILRLPERLSVLPSRQANGALFLWLAACAAHGSLAPAQGDPLFRDLVRLGAAQRAVEATLQDAPGLTGLYDDLAELVLSLRPVAPLPPAEAVVEALARHLLGDPAPLPPLARDWLAMLDDPQVKAPRDYRPMRPVPLWPDLALPETTLAAAPGDAPDGIAADPANARMFRARRRQSDQPQRRDSLILHKFEALLSWADLMNLNRHVDDDDQDDAKKAAEDQEELGLGQVSKAPATRLRLHLDLAPEDADLEAVAGIRTYPEWDARRGRYLAHHVRVLENRAPEHDEALTPDPRAQTRIRAVPRQFEALRPGRLITTGHRDGDELDAELTVRAAADLRATGQGSDRIWRQSRPLARNLAVSILLDVSRSTESAVTGRAVIEIEREALAALAWGLDACGDRFAINAFSSLKRDRVFLSACKDFDEPMGAAIERRIAGLRPRFYTRLGAGIRHASAGLSAQASSRRLLLVITDGKPNDLDHYEGRHGIEDSAMAVREARRAGHAVHGITVDRDAKSWFPRIFGQGGFSLIPHPDRLLAALPVIYRQLVA
Protein: Transcription factor SPATULA (Basic helix-loop-helix protein 24) (AtbHLH24) (bHLH 24) (Transcription factor EN 99) (bHLH transcription factor bHLH024) (Q9FUA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that plays a role in floral organogenesis. Promotes the growth of carpel margins and of pollen tract tissues derived from them.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcriptional adapter ADA2a
Sequence:
MISQREEREEKKQRVMGDKKLISSSSSSSVYDTRINHHLHHPPSSSDEISQFLRHIFDRSSPLPSYYSPATTTTTASLIGVHGSGDPHADNSRSLVSHHPPSDSVLMSKRVGDFSEVLIGGGSGSAAACFGFSGGGNNNNVQGNSSGTRVSSSSVGASGNETDEYDCESEEGGEAVVDEAPSSKSGPSSRSSSKRCRAAEVHNLSEKRRRSRINEKMKALQSLIPNSNKTDKASMLDEAIEYLKQLQLQVQMLTMRNGINLHPLCLPGTTLHPLQLSQIRPPEATNDPLLNHTNQFASTSNAPEMINTVASSYALEPSIRSHFGPFPLLTSPVEMSREGGLTHPRLNIGHSNANITGEQALFDGQPDLKDRIT
Protein: Inhibitory synaptic factor 1 (InSyn1) (Q2T9L4)
Organism: Homo sapiens (Human)
Function: Component of the protein machinery at the inhibitory synapses, probably acting as a scaffold. Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. This synaptic inhibition is fundamental for the functioning of the central nervous system, shaping and orchestrating the flow of information through neuronal networks to generate a precise neural code.
Subcellular location: Postsynaptic density {ECO:0000250|UniProtKB:Q8CD60}.
Interaction partners:
- Gephyrin
- Inhibitory synaptic factor 2A
Sequence:
MNIRGAPDLGQPSDDPSSGGERERIRQRMKMVIGQLEGILRELKEVAKELREVVSQIDKLTSDFDFELEPDDWTTATVSSTSSSDKAGMGGPFDLGHLDFMTADILSDSWEFCSFLDVSTPSDSVDGPESTRPGAGPDYRLMNGGTPIPNGPRVETPDSSSEEAFGAGPTVKSQLPQRTPGTRERVRFSDKVLYHALCCDDEEGDGEQEVEEEEVGLPPEPAHTEAHAGPHKPSPAPYKSRRSPLTSRHSGSTLAPEQTRRVTRNSSTQTVSDKSTQTVLPYTATRQKARGKN
Protein: Protein BCCIP homolog (O64885)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ribosome production factor 2 homolog
- AT5g04600/T32M21_200
- Probable rRNA-processing protein EBP2 homolog
- Ribosome assembly factor mrt4
- Putative U3 small nucleolar ribonucleoprotein
- Ribosome biogenesis protein BRX1 homolog 2
- Ribosome biogenesis protein WDR12 homolog
Sequence:
MPRRPSSGRRVLKHQPLTFSPFMRLLSFASMARRDLSHPEDCQCSDEDISFDEKQKIPNLPRKGKEEQVSDSSDEEDSQEDVQADFEFFDPKPTDFHGVKILLQNYLDDKEWDLSSFVDCILEQTTVGTVVKVADDEDESVFALVTALNMARDKDNKCFRELKEFLRKVCSEKNIANNLEMLLEKKAQDVGLLVSQRVMNLPPQLLPPLYDGLFDEVSWAIEDEPTEKLRRSFRFKSYLLVTKIYKLKNPKQRKPRHGEEDIEDTVFLKPEDELFLELSSWSFTFPMRSQLVTSQEMKNYQLMGLVMAVEANKIPKFRQMLNSLID
Protein: proteasome endopeptidase complex (EC 3.4.25.1) (Q5B698)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome component Pre6, putative
- proteasome endopeptidase complex
- Proteasome subunit alpha type
- Proteasome subunit beta
- Proteasome component Pup3, putative
- Proteasome subunit alpha type
- Proteasome subunit alpha type
Sequence:
MDQLVRQYTRSPHQNEFYSEQEQHDLTESLPPLSLKFALPPVANQSAFLRAMTDDHSNPNCPIKLAHGTTTLAFRFQGGIIVCTDSRATAGNWIASQTVKKVIPVSRLSRGEDKPGSAPVPGLLGTMAGGAADCQYWLRYLSQQCTLHEIRHKRRITVAAASKILANLTYAYKGYGLSMGTMLAGVTPQEGPALYYIDSDGTRLPGNLFCVGSGQTFAYGVLDANYRYDLTEEEALELGRRSILAAMHRDAYSGGFINLYHVKEEGWVHHGFDDMNPIFWKTKLEKGEFSNVTSAL
Protein: Iron-sulfur assembly protein 1 (P78859)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the assembly of mitochondrial and cytoplasmic iron-sulfur proteins. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Iron-sulfur assembly protein 2
- Iron sulfur cluster assembly protein 1, mitochondrial
- NifU-like protein C1709.19c
- Iron-sulfur cluster assembly factor IBA57
- Iron-sulfur clusters transporter atm1, mitochondrial
- Monothiol glutaredoxin-5
- Fe
- Probable cysteine desulfurase, mitochondrial
- Monothiol glutaredoxin-4
- Aconitate hydratase, mitochondrial
Sequence:
MLSCLSKPALRCRSVNRLQFLRKLSLQEIQTLKTQHQYLGRTRLDVETPSLKPSAAGSGSTAPKPVTEREIASTRFMPRKNVIKLTPLAVEHLKKMQSSASMKGKMLRIGVKQKGCAGQAYSLEYIEKPDKFDEIVKQDGISIIVARRALLQIIGSVMDYRDDDLQSRFIFSNPNVKSTCGCGESFSTLK