wanglab/gogpt-training-data huggingface dataset:
Protein: Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Confluent 3Y1 cell-associated protein 1) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II) (O35049)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location (By similarity). Regulates the cell cycle by acting as a growth suppressor in confluent cells. Acts as a regulator of postnatal development and participates in bone and dentin mineralization. May be involved in IL-1-beta-induced JNK activation in hepatocytes. May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10823942}; Lipid-anchor {ECO:0000269|PubMed:10823942}. Cell membrane {ECO:0000269|PubMed:15059969}; Lipid-anchor {ECO:0000269|PubMed:15059969}. Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:10823942).
Interaction partners:
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Ceramide glucosyltransferase
- Ceramide synthase 5
- Ceramide kinase
- Ceramide synthase 6
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
Sequence:
MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLVASFIPTTYEKRQRADDPCYLQLFCTVLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKSPAGGAALLSEWKGTGAGKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGSDGARAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDSCIVRIGGEEGGRAQEADDPAPGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESLVKARAGQDSGGSGEPGSNSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHCYPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAIRCEQLDLLQDWLADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDINGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA
Protein: Syndetin (Coiled-coil domain-containing protein 132) (EARP/GARPII complex subunit VPS50) (Q96JG6)
Organism: Homo sapiens (Human)
Function: Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane. Within the EARP complex, required to tether the complex to recycling endosomes. Not involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).
Subcellular location: Recycling endosome {ECO:0000269|PubMed:25799061}. Membrane {ECO:0000250|UniProtKB:F1LSG8}. Note=Associates with membranes in an EIPR1-dependent manner. {ECO:0000250|UniProtKB:F1LSG8}.
Interaction partners:
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 54
- EARP and GARP complex-interacting protein 1
Sequence:
MQKIKSLMTRQGLKSPQESLSDLGAIESLRVPGKEEFRELREQPSDPQAEQELINSIEQVYFSVDSFDIVKYELEKLPPVLNLQELEAYRDKLKQQQAAVSKKVADLILEKQPAYVKELERVTSLQTGLQLAAVICTNGRRHLNIAKEGFTQASLGLLANQRKRQLLIGLLKSLRTIKTLQRTDVRLSEMLEEEDYPGAIQLCLECQKAASTFKHYSCISELNSKLQDTLEQIEEQLDVALSKICKNFDINHYTKVQQAYRLLGKTQTAMDQLHMHFTQAIHNTVFQVVLGYVELCAGNTDTKFQKLQYKDLCTHVTPDSYIPCLADLCKALWEVMLSYYRTMEWHEKHDNEDTASASEGSNMIGTEETNFDRGYIKKKLEHGLTRIWQDVQLKVKTYLLGTDLSIFKYDDFIFVLDIISRLMQVGEEFCGSKSEVLQESIRKQSVNYFKNYHRTRLDELRMFLENETWELCPVKSNFSILQLHEFKFMEQSRSPSVSPSKQPVSTSSKTVTLFEQYCSGGNPFEIQANHKDEETEDVLASNGYESDEQEKSAYQEYDSDSDVPEELKRDYVDEQTGDGPVKSVSRETLKSRKKSDYSLNKVNAPILTNTTLNVIRLVGKYMQMMNILKPIAFDVIHFMSQLFDYYLYAIYTFFGRNDSLESTGLGLSSSRLRTTLNRIQESLIDLEVSADPTATLTAAEERKEKVPSPHLSHLVVLTSGDTLYGLAERVVATESLVFLAEQFEFLQPHLDAVMPAVKKPFLQQFYSQTVSTASELRKPIYWIVAGKALDYEQMLLLMANVKWDVKEIMSQHNIYVDALLKEFEQFNRRLNEVSKRVRIPLPVSNILWEHCIRLANRTIVEGYANVKKCSNEGRALMQLDFQQFLMKLEKLTDIRPIPDKEFVETYIKAYYLTENDMERWIKEHREYSTKQLTNLVNVCLGSHINKKARQKLLAAIDDIDRPKR
Protein: Inter-alpha-trypsin inhibitor heavy chain 4 (Q5EBC0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Beta-2-glycoprotein 1
- Haptoglobin
- Alpha-1-antiproteinase
- Hemopexin
- Fibrinogen gamma chain
- Murinoglobulin-1
- Plasminogen
- Afamin
- Apolipoprotein A-II
- Protein AMBP
Sequence:
MKSPAPAHMWNIVLVLLSLLAVLPITTTEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADTVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYTAAVGRGESAGLVKTTGRKTEQFEVSVNVAPGSKTTFELIYQELLQRRLGMYELLLKVRPEQLVKHLQMDIYIFEPQGISTLETESTFMTQELANALTTSQNKTKAHIQFKPTLSQQRKSQNEQDTVLDGDFTVRYDVDRSSTGGTIQIENGYFVHHFAPEDLPTMAKNVLFVIDKSGSMAGKKIQQTREALIKILKDLSTQDQFNIIVFSGEANQWEQLLVQATEENLNRAVDYASKIPAQGGTNINKAVLSAVELLDKSNQAELLPSKSVSLIILLTDGEPTVGETNPKIIQKNTQEAINGRYSLFCLGFGFDVNYPFLEKLALDNGGLARRIYEDSDSALQLQDFYQEVANPLLSSVTFEYPSNAVEDVTRYNFQHHFKGSEMVVAGKLRDQGPDVLLAKVSGQMHLQNITFQTEASIAQQEKEFQGPKYIFHNFMERLWALLTIQQQLEQRISASGAELEALEAQVLNLSLKYNFVTPLTHMVVTKPEDQEQFQVAEKPTEVDGGVWSILSAVQRHFKTPTTGSKLLTSRLRGNRFQTLSRLGDGLVGSRQYMPPPGLPGPPGLPGPPGPPGHPHFASSIDYGRQPSLGRVLDLPSLSSQDPAGPSLAMLPKVVEQEGTTPEESPNPDHPRAPTIILPLPGSGVDQLCVDILHSEKPMKLFVDINQGLEVVGKYEKNIGFSWIEVTILKPHLQVHATPERLVVTRGRKNSEYKWKKTLFSVLPGLKMTMDKTGLLQLSGPDKVTISLLSLDDPQRGLMLLLNDTHHFSNDITGELGQFYQDIIWDDTKQTVRVLGIDYPATRELKLSYQDGFPGTEISCWTVKI
Protein: Candida glabrata strain CBS138 chromosome H complete sequence (Q6FSD6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- 3-ketodihydrosphingosine reductase TSC10
- sphingosine kinase
- sphingosine kinase
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Ceramide very long chain fatty acid hydroxylase
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MSVNGTLFEQSFNLKGGYDYMHTVSAPEIKLTPREDLTSYCSDGILALAAPVIAYWAQSAFFHIIDVFHLAEKYRIHPSEEIEKRNRATRLQVLREVIFQHIVQTVVGLIFLKFADESVTGFEQNEMWHWRQQAPGFIPDAAVYYAYMYGVSLIKLSLGFLFIDTWQYFWHRVMHLSPFMYKYFHSIHHELYVPYAYGALFNNPVEGFILDTLGTGIAMFLTGLTHREEAVLFTFATMKTIDDHCGYALPFDPFQIVFPNNAVYHDIHHQQFGLKTNFAQPFFTFWDNLFGTNFKGFEEYQKKQRRVTIDKYKEFLAKREAEKLEKIKNFSKKNENKKEK
Protein: D-erythrose-4-phosphate dehydrogenase (E4PDH) (EC 1.2.1.72) (P0A9B6)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate.
Subcellular location: Cytoplasm.
Interaction partners:
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Enolase
- Erythronate-4-phosphate dehydrogenase
- Transketolase 1
- Transketolase 2
- Phosphoenolpyruvate carboxykinase
- Ribose-phosphate pyrophosphokinase
- Transaldolase B
- Glucose-6-phosphate isomerase
Sequence:
MTVRVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNQDQLRAEHRIVSNASCTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFANRMLDTTLAMATVAFR
Protein: Liquid facets, isoform J (M9PEF2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRKQKDDMQVNVAGLRRNIKNLAHNYSDAQVKVREATSNDPWGPSAAIMSEIAELTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKENIFAIQTLREFVYFEEGKDQGTHVREKAKQLVTLLKDDERLKNERVKAQKAKERFAQNPSGFGSDGYIDGPSQRDLPPGWQEEPPKSVSELEMVRPQTAGEEELQLQLAMAMSREEAEQEEAKRRSDDVRLQLALSQSEQDFKDPNGRPIPAPKKEEQQSHLLDLLDISLGATSISSPPLGAAGGAPTAVVDPWAMPGPRAPSQLSDPWSGTSSPQVDPWNPSAAPRTILGAGVPMTSAPLGAGNDAWGARTQSPSVASGSSNEGWLQSNGNANQNGRGATPAGPPAEGWLIKSTAVGALGAAPINHAANNGSSSSDPWLAEPAASAAGGAAAVGLADPWAPGAASQTGAGALDDPWKALGTGAIKKQSPEFDEFDLITNRNKSEHSNSNASNNNNASLLDDMDPLSANYGNGGINSSMHPSTGATAKKSIKDAHSFLGENSALVNLDNLIKPIAPQTQTGNQPAYNPFSDNVVPPKTNLFQQQQPAVPSINQLKQQAPFSVSMNQDPWAPVMGGVSTTSQPQPNLQVYNNAYQSSSSTNILGKSNIPTNMNSSTSNSTIHSCYASPSPGVDGIRNMDIFTERPYYNSPTAPADDTYMYNSRDNNNINSNYGTPSLYSSFAASYSSALSDSLAETPGISVAPLGFVADTVMSFGPSSSSANCKLEQNNNMPWIKPEAATNPFLS
Protein: MAF bZIP transcription factor F (B0QY70)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVDPLSSKALKIKRELSENTPHLSDEALMGLSVRELNRHLRGLSAEEVTRLKQRRRTLKNRGYAASCRVKRVCQKEELQKQKSELEREVDKLARENAAMRLELDALRGKCEALQGFARSVAAAR
Protein: KIAA1683 protein (A0JP07)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTLQGRADLSGNQGNAAGRLATVHEPVVTQWAVHPPAPAHPSLLDKMEKAPPQPQHEGLKSKEHLPQQPAEGKTASRRVPRLRAVVESQAFKNILVDEMDMMHARAATLIQANWRGYWLRQKLISQMMAAKAIQEAWRRFNKRHILHSSKSLVKKTRAEEGDIPYHAPQQVRFQHPEENRLLSPPIMVNKETQFPSCDNLVLCRPQSSPLLQPPAAQGTPEPCVQGPHAARVRGLAFLPHQTVTIRFPCPVSLDAKCQPCLLTRTIRSTCLVHIEGDSVKTNASSQRHPPCLSQRPLAAPLTKASSQGHLPTELTKTPSLAHLDTCLSKMHSQTHLATGAVKVQSQAPLATCLTKTQSREQPITDITTCLIPAHQAADLSSNTHSQVLLTGSKVSNHACQRLGGLSAPPWAKPEDRQTQPQPHGHVPGKTTQGGPCPAACEVQGMLVPPMAPTGHSTCNVESWGDNGATRAQPSMPGQAVPCQEDTGPADAGVVGGQSWNRAWEPARGAASWDTWRNKAVVPPRRSGEPMVSMQAAEEIRILAVITIQAGVRGYLARRRIRLWHRGAMVIQATWRGYRVRRNLAHLCRATTTIQSAWRGYSTRRDQARHWQMLHPVTWVELGSRAGVMSDRSWFQDGRARTVSDHRCFQSCQAHACSVCHSLSSRIGSPPSVVMLVGSSPRTCHTCGRTQPTRVVQGMGQGTEGPGAVSWASAYQLAALSPRQPHRQDKAATAIQSAWRGFKIRQQMRQQQMAAKIVQATWRGHHTRSCLKNTEALLGPADPSASSRHMHWPGI
Protein: Uroporphyrinogen-III synthase, chloroplastic (AtUROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) (O48721)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, a precursor of tetrapyrroles such as chlorophyll, heme and phycobilins.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18042043}.
Interaction partners:
- Porphobilinogen deaminase, chloroplastic
- Uroporphyrinogen decarboxylase 2, chloroplastic
- Uroporphyrinogen decarboxylase 1, chloroplastic
- Coproporphyrinogen-III oxidase 1, chloroplastic
- S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase, chloroplastic
- Coproporphyrinogen-III oxidase 2, chloroplastic
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Chlorophyll synthase, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
Sequence:
MALLLLSHCSILSFQPPLSSSSSFHSSHIQSLSKPVFASPSPIRNSISSSVSSSSSSVSSSNSIPQVVVTRERGKNNQIIKALEKNGISSLELPLIQHARGPDFDRLASVLNDKSFDWIIITSPEAGSVFLEAWKTASSPEVQIGVVGAGTARVFEEAMKSADGLLHVAFTPSKATGKVLASELPEKVGKRSSVLYPASLKAGNDIVEGLSKRGFEVVRLNTYTTVPVQSVDTVLLQQALSAPVLSVASPSAVRAWLHLIQNEEQWSNYVACIGETTASAARRLGLKNVYYPEKPGLEGWVESIMEALGAHADSSNPSSRN
Protein: Transcription factor Iwr1 domain-containing protein (Q389Q7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRIKRSRCTASESGELVAPPLLRVRLDSSRGVRVGCDASNNTKNDALDAPPTPRASGSVEDECQRRVLFFRLLERGACGAAGDDKTYALANSAVLPSNTALSVERVWDAQGNLVMDCQVVGKKSGEVGVVPVSSIVGDVLVGPGDSVAIDSEGSWSVYILDKGAAADAVGEVNEEEGDKNMKEDDVFGFGNLRITDDDDGESTAVSCVKPYFAFRSERKRHREGTYHDYVLSFGESLANRSVAVNKAELLLYDALQKNYDDFLLDEQGAIDPELYLYPDHRKDDEYDSNAADFSANEYPDETSSSNSIRTDGMSTAGTYDDERCHRPRGVWGSSGFCGDSDVGDPLGSSWNDTDDGY
Protein: Cis-retinol/androgen dehydrogenase type 3 (Retinol dehydrogenase 9) (Q8K5C8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Beta,beta-carotene 15,15'-dioxygenase
- All-trans-retinol 13,14-reductase
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Retinal dehydrogenase 2
Sequence:
MWLFLVALVGLWTLLCFFRERQVVSYLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKERVGNRGLWGLVNNAGISIPSGPNEWMKKQDFAHVLDVNLLGLIEVTLSMLPLVRKARGRVINVASVLGRVSLCGGAYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNELDKRCNKDLSLVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTSLKPEKAL
Protein: Cyclin-dependent kinase inhibitor 1A (P21) (Q64315)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cyclin-dependent kinase 2
- G1/S-specific cyclin-D1
- Cyclin-dependent kinase 4
- G1/S-specific cyclin-E1
- cyclin-dependent kinase
- Cyclin-A2
- Cellular tumor antigen p53
- Cyclin-A1
- G1/S-specific cyclin-D3
- Cyclin E2
Sequence:
MSDPGDVRPVPHRSKVCRRLFGPVDSEQLSRDCDALMASCLQEARERWNFDFATETPLEGNYVWERVRSPGLPKIYLSPGSRRRDDLGGDKRPSTSSALLQGPGPAPEDHVALSLSCTLVSHAPERPEDSPGGTGTSQGRKRRQTSLTDFYHSKRRLVFCKRKP
Protein: F-box protein SKIP19 (F-box/LRR-repeat protein 20) (SKP1-interacting partner 19) (Q9M0U9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- F-box/LRR-repeat protein At1g67190
- F-box/kelch-repeat protein At3g24760
- F-box protein At5g52880
- F-box/kelch-repeat protein At2g24250
- SKP1-like protein 1B
- F-box/kelch-repeat protein At1g64840
- F-box protein At4g27050
- Putative F-box protein At1g47730
- F-box protein At1g30790
- F-box/kelch-repeat protein At3g04660
Sequence:
MASSSSPPAAMEVGESTNWTELPPELTSAILHRLGAIEILENAQKVCRSWRRVCKDPSMWRKIDMHNLGDLDDMDYNLEIMCRHAVDRSQGGLVDIGIWYFGTVDLLNYIAHRSSNLRSLRLIRCSQITDDGFVEAVVKLPLEELELSYCSFSVESLRVVGQCCLNMKTLKLNKHPQKENDDDALAIAETMPKLRHLQLCGNGLSDTGLNAILDNCSNLEHLDLRRCFNVNLVGDLQKRCFESVKVVRHPNDSIHDIDIGSSEDEDPYDFSDIDLMSGDDDFEGYYDFSGASDFSDYDQFDF
Protein: RE43027p (Q8IGR2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQLFQNYRDDERRIGEEYLSSLQDLNCNSKPLINMLTMLAEENINYAHIIVKVVEYYISQVAPEFKLPILYLIDSIVKNVKSSYVQLFGQCIVNIFLHAFESVQHSQSQVLEKVRERMYALRQTWNEVFPPSKMYALDVKVKRLDNNWPITAKQPTNKIHVNPAIHVNPDFLKPGLVPGMPGNPTITSDMEEILQAKTRELLELKKRKLELELEQTKKHLEEQERQLTQTTDAMVGAPIIMPAPTPAAICPPITDPGIAVHNQRAPGVMGNVGPVMHNMPVAPQLFANKPKVHPVNPALLNSVRQRDPRLARQMHAASSHPAAPARNDPRLEAKSSSSQKSSRSRSKSPVRNSSSRSGKSGSSSHSSSSSRERSESKSSTTSSSSSSSDVRHKGVTASSSNQPTVKRSGKITSKDSDRYVRNGSPLGSAKRKSSSPSSSPSKSKRSTSHKSSSSRGKTSSLRSRSRSPVFMDVDLRTGVRSKSPESRAVAPSSLPLAGASLPASAKAPKDLEKRKKQLLILISHLLANNQVWFDLEPRATDSLVENLEYINQNGGTRWLRLVEGRVIGTVCG
Protein: Speckle-type POZ protein (HIB homolog 1) (PDX-1 C-terminal-interacting factor 1) (Q6ZWS8)
Organism: Mus musculus (Mouse)
Function: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL (By similarity). In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15121856}. Nucleus speckle {ECO:0000269|PubMed:15121856}.
Interaction partners:
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Zinc finger protein GLI2
- Suppressor of fused homolog
- Zinc finger protein GLI1
- Speckle-type POZ protein-like
- Transcriptional activator GLI3
- Androgen receptor
- Katanin p60 ATPase-containing subunit A1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS
Protein: Zinc finger A20 and AN1 domain-containing stress-associated protein 3 (AtSAP3) (Q9ZNU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in environmental stress response.
Interaction partners:
- At3g13310
- Oligouridylate-binding protein 1B
- Chaperone DnaJ-domain superfamily protein
- AT-hook motif nuclear-localized protein 23
- At1g56300
- Oligouridylate-binding protein 1C
Sequence:
MAEEHRLQEPRLCANNCGFFGSTATQNLCSKCFRDLQHQEQNSSTAKHALTQSLAAVGAAASSSVSPPPPPPADSKEIVEAKSEKRAAAEPEEADGPPQDPKRCLTCRRRVGITGFRCRCGFVFCGTHRYAEQHECSFDFKRMGKDKIAKANPIVKADKLEKI
Protein: Peroxisomal membrane protein 11C (Peroxin-11C) (Peroxisomal biogenesis factor 11C) (Protein PEX11 homolog gamma) (PEX11-gamma) (Q96HA9)
Organism: Homo sapiens (Human)
Function: Promotes membrane protrusion and elongation on the peroxisomal surface.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:12417726, ECO:0000269|PubMed:12559946, ECO:0000269|PubMed:20826455}; Multi-pass membrane protein {ECO:0000269|PubMed:12417726, ECO:0000269|PubMed:12559946}.
Interaction partners:
- Peroxisomal membrane protein 11B
- Peroxisomal membrane protein 11A
- Peroxisomal membrane protein PEX13
- Peroxisomal biogenesis factor 19
- Peroxisome biogenesis factor 10
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX16
- Peroxisomal membrane protein PEX14
- Peroxisomal ATPase PEX6
- Peroxisomal targeting signal 2 receptor
Sequence:
MASLSGLASALESYRGRDRLIRVLGYCCQLVGGVLVEQCPARSEVGTRLLVVSTQLSHCRTILRLFDDLAMFVYTKQYGLGAQEEDAFVRCVSVLGNLADQLYYPCEHVAWAADARVLHVDSSRWWTLSTTLWALSLLLGVARSLWMLLKLRQRLRSPTAPFTSPLPRGKRRAMEAQMQSEALSLLSNLADLANAVHWLPRGVLWAGRFPPWLVGLMGTISSILSMYQAARAGGQAEATTP
Protein: RNA-binding region-containing protein 3 (RNA-binding motif protein 40) (RNA-binding protein 40) (U11/U12 small nuclear ribonucleoprotein 65 kDa protein) (U11/U12 snRNP 65 kDa protein) (U11/U12-65K) (Q96LT9)
Organism: Homo sapiens (Human)
Function: Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3'-stem-loop of m(7)G-capped U12 snRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14974681}.
Interaction partners:
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
- Small nuclear ribonucleoprotein G
- Zinc finger matrin-type protein 5
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Small nuclear ribonucleoprotein Sm D3
- Splicing factor 3B subunit 2
- Small nuclear ribonucleoprotein Sm D2
- Splicing factor 3B subunit 1
Sequence:
MAAPEQPLAISRGCTSSSSLSPPRGDRTLLVRHLPAELTAEEKEDLLKYFGAQSVRVLSDKGRLKHTAFATFPNEKAAIKALTRLHQLKLLGHTLVVEFAKEQDRVHSPCPTSGSEKKKRSDDPVEDDKEKKELGYLTVENGIAPNHGLTFPLNSCLKYMYPPPSSTILANIVNALASVPKFYVQVLHLMNKMNLPTPFGPITARPPMYEDYMPLHAPLPPTSPQPPEEPPLPDEDEELSSEESEYESTDDEDRQRMNKLMELANLQPKRPKTIKQRHVRKKRKIKDMLNTPLCPSHSSLHPVLLPSDVFDQPQPVGNKRIEFHISTDMPAAFKKDLEKEQNCEEKNHDLPATEVDASNIGFGKIFPKPNLDITEEIKEDSDEMPSECISRRELEKGRISREEMETLSVFRSYEPGEPNCRIYVKNLAKHVQEKDLKYIFGRYVDFSSETQRIMFDIRLMKEGRMKGQAFIGLPNEKAAAKALKEANGYVLFGKPMVVQFARSARPKQDPKEGKRKC
Protein: Flagellar hook-associated protein 2 (HAP2) (Filament cap protein) (Flagellar cap protein) (P24216)
Organism: Escherichia coli (strain K12)
Function: Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
Subcellular location: Secreted. Bacterial flagellum.
Interaction partners:
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 3
- Flagellar hook protein FlgE
- Flagellar hook-associated protein 1
- Flagellin
- Flagellar basal body rod protein FlgB
- Flagellar protein FliT
- Flagellar basal-body rod protein FlgC
- Basal-body rod modification protein FlgD
- Flagellar motor switch protein FliM
Sequence:
MASISSLGVGSGLDLSSILDSLTAAQKATLTPISNQQSSFTAKLSAYGTLKSALTTFQTANTALSKADLFSATSTTSSTTAFSATTAGNAIAGKYTISVTHLAQAQTLTTRTTRDDTKTAIATSDSKLTIQQGGDKDPITIDISAANSSLSGIRDAINNAKAGVSASIINVGNGEYRLSVTSNDTGLDNAMTLSVSGDDALQSFMGYDASASSNGMEVSVAAQNAQLTVNNVAIENSSNTISDALENITLNLNDVTTGNQTLTITQDTSKAQTAIKDWVNAYNSLIDTFSSLTKYTAVDAGADSQSSSNGALLGDSTLRTIQTQLKSMLSNTVSSSSYKTLAQIGITTDPSDGKLELDADKLTAALKKDASGVGALIVGDGKKTGITTTIGSNLTSWLSTTGIIKAATDGVSKTLNKLTKDYNAASDRIDAQVARYKEQFTQLDVLMTSLNSTSSYLTQQFENNSNSK
Protein: Tubulin polyglutamylase TTLL13 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 13) (A4Q9F6)
Organism: Mus musculus (Mouse)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates ATP-dependent polyglutamate side-chain elongation of the polyglutamylation reaction but not the initiation step. Preferentially modifies the alpha-tubulin tail over a beta-tail.
Interaction partners:
Sequence:
MEPNNCKTSESEEDDIEEEESEEECVREESTTPNSTQQALRKADYKEFENGVALSVVAKKIPKKILSATDTDDLEVGRRRRKRKRRPLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTVYWTDCSVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMQKLYPTEYNIFPRTWCLPADYGDFQAYGRQRKTRTYICKPDSGCQGRGIFITRTPKEIKPGEHMICQQYITKPFLIDGFKFDMRIYVLITSCDPLRIFMYEEGLARFATMPYVEPSHNNLEEVCMHLTNYAINKHNENFVRDDAVGSKRKLSTLNAWLREHSHDPQELWGDIEDIIIKTIISAHSVLRHNYRTCFPQYLCGGTCACFEILGFDILLDHKLKPWLLEVNHSPSFTTDSRLDREVKDALLCDAMNLVNLRGCDKKKVIEEDKRRVKERLFPCHQQPRETRREQFELSQAAMHDQERYEDSHLGGYRRIYPGPDSEKYAPFFKHNGSLFQETAASKAREECARQQLEEIRLKQEQQENPGTKKRKENKEQNQGESAGEKSRSRTATRVLATSLAYRNRNREKELLPVQLDTTQPQDIVEEEELERMKLLLQRENLIRSLGIVEQLTRMLYPSHRSHRKLHEYRPRFHQDGLSSQELQPVNLVPLVLLRGAASEQIPPHFLQPLRPHELIPRILGPLSSINPAIAQHSRYHLQPKNFNWIGDSAATGPCSLSMKKSGRHYISSSRVRLTSRKRRKAQHSTKTANGLQSLLIERLPTSSRLKSSGQDLCLQKAKNTETPRVLQHSKILWGSVKTKR
Protein: Small ribosomal subunit protein uS3m (28S ribosomal protein S24, mitochondrial) (MRP-S24) (S24mt) (bMRP-47) (bMRP47) (Q96EL2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS34
- Small ribosomal subunit protein uS11m
Sequence:
MAASVCSGLLGPRVLSWSRELPCAWRALHTSPVCAKNRAARVRVSKGDKPVTYEEAHAPHYIAHRKGWLSLHTGNLDGEDHAAERTVEDVFLRKFMWGTFPGCLADQLVLKRRGNQLEICAVVLRQLSPHKYYFLVGYSETLLSYFYKCPVRLHLQTVPSKVVYKYL
Protein: Homeobox protein knotted-1-like 4 (Protein KNAT4) (P48001)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein KNATM
- At4g32030
- At4g32050
- Armadillo repeat-containing protein LFR
Sequence:
MAFHNNHFNHFTDQQQHQPPPPPQQQQQQHFQESAPPNWLLRSDNNFLNLHTAASAAATSSDSPSSAAANQWLSRSSSFLQRGNTANNNNNETSGDVIEDVPGGEESMIGEKKEAERWQNARHKAEILSHPLYEQLLSAHVACLRIATPVDQLPRIDAQLAQSQNVVAKYSTLEAAQGLLAGDDKELDHFMTHYVLLLCSFKEQLQQHVRVHAMEAVMACWEIEQSLQSFTGVSPGEGTGATMSEDEDEQVESDAHLFDGSLDGLGFGPLVPTESERSLMERVRQELKHELKQGYKEKIVDIREEILRKRRAGKLPGDTTSVLKSWWQSHSKWPYPTEEDKARLVQETGLQLKQINNWFINQRKRNWHSNPSSSTVSKNKRRSNAGENSGRDR