wanglab/gogpt-training-data huggingface dataset:
Protein: Methionine aminopeptidase 2A (MAP 2A) (MetAP 2A) (EC 3.4.11.18) (Peptidase M) (Q9FV49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:11060042}.
Interaction partners:
- Methionine aminopeptidase 1B, chloroplastic
- Methionine aminopeptidase 1C, chloroplastic/mitochondrial
- Methionine aminopeptidase 1D, chloroplastic/mitochondrial
- Methionine aminopeptidase 1A
- Peptide deformylase 1B, chloroplastic/mitochondrial
- Peptide deformylase 1A, chloroplastic/mitochondrial
- Sphingolipid delta
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL23y
Sequence:
MAIGNPEVATMGKENTEAESSNGNESQLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTKKKKKKSKSKKKKSSLQQTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKNYDVGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISKGDDY
Protein: Pituitary adenylate cyclase-activating polypeptide type I receptor (PACAP type I receptor) (PACAP-R-1) (PACAP-R1) (P70205)
Organism: Mus musculus (Mouse)
Function: This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41586}.
Interaction partners:
- Pituitary adenylate cyclase-activating polypeptide
- VIP peptides
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-glucagon
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Pro-opiomelanocortin
- Guanine nucleotide-binding protein G
Sequence:
MARTLQLSLTALLLLPMAIAMHSDCIFKKEQAMCLERIQRANDLMGLNESSPGCPGMWDNITCWKPAQIGEMVLVSCPEVFRIFNPDQVWMTETIGDSGFADSNSLEITDMGVVGRNCTEDGWSEPFPHYFDACGFDDYEPESGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSSHCFVSTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWAVLRLYFDDAGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIIILVQKLQSPDMGGNESSIYFSCVQKCYCKPQRAQQHSCKMSELSTITLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFTMDFKHRHPSLASSGVNGGTQLSILSKSSSQLRMSSLPADNLAT
Protein: Homeobox protein engrailed-1 (Homeobox protein en-1) (Hu-En-1) (Q05925)
Organism: Homo sapiens (Human)
Function: Required for proper formation of the apical ectodermal ridge and correct dorsal-ventral patterning in the limb.
Subcellular location: Nucleus.
Interaction partners:
- Transducin-like enhancer protein 1
- Paired box protein Pax-2
- Proto-oncogene Wnt-1
- Fibroblast growth factor 8
- Hepatocyte nuclear factor 3-beta
- Paired box protein Pax-6
- TLE family member 5
Sequence:
MEEQQPEPKSQRDSALGAAAAATPGGLSLSLSPGASGSSGSGSDGDSVPVSPQPAPPSPPAAPCLPPLAHHPHLPPHPPPPPPQHLAAPAHQPQPAAQLHRTTNFFIDNILRPDFGCKKEQPPPQLLVAAAARGGAGGGGRVERDRGQTAAGRDPVHPLGTRAPGAASLLCAPDANCGPPDGSQPAAAGAGASKAGNPAAAAAAAAAAVAAAAAAAAAKPSDTGGGGSGGGAGSPGAQGTKYPEHGNPAILLMGSANGGPVVKTDSQQPLVWPAWVYCTRYSDRPSSGPRTRKLKKKKNEKEDKRPRTAFTAEQLQRLKAEFQANRYITEQRRQTLAQELSLNESQIKIWFQNKRAKIKKATGIKNGLALHLMAQGLYNHSTTTVQDKDESE
Protein: E3 ubiquitin-protein ligase MIB2 (EC 2.3.2.27) (Mind bomb homolog 2) (Novel zinc finger protein) (Novelzin) (Putative NF-kappa-B-activating protein 002N) (RING-type E3 ubiquitin transferase MIB2) (Skeletrophin) (Zinc finger ZZ type with ankyrin repeat domain protein 1) (Q96AX9)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14507647}. Endosome {ECO:0000269|PubMed:14507647}. Note=Colocalizes with endosomal compartments.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase CYLD
- B-cell lymphoma/leukemia 10
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor
- CASP8 and FADD-like apoptosis regulator
- Protein jagged-2
- TNF receptor-associated factor 2
- Ubiquitin-conjugating enzyme E2 D2
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- E3 ubiquitin-protein ligase NEURL1B
Sequence:
MDPDPQAGVQVGMRVVRGVDWKWGQQDGGEGGVGTVVELGRHGSPSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYDNAQIGVRHPNIICDCCKKHGLRGMRWKCRVCLDYDLCTQCYMHNKHELAHAFDRYETAHSRPVTLSPRQGLPRIPLRGIFQGAKVVRGPDWEWGSQDGGEGKPGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLKCVGEAAGGFYYKDHLPRLGKPAELQRRVSADSQPFQHGDKVKCLLDTDVLREMQEGHGGWNPRMAEFIGQTGTVHRITDRGDVRVQFNHETRWTFHPGALTKHHSFWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAVAGQRWTFSPSCLVAYRPEEDANLDVAERARENKSSLSVALDKLRAQKSDPEHPGRLVVEVALGNAARALDLLRRRPEQVDTKNQGRTALQVAAYLGQVELIRLLLQARAGVDLPDDEGNTALHYAALGNQPEATRVLLSAGCRADAINSTQSTALHVAVQRGFLEVVRALCERGCDVNLPDAHSDTPLHSAISAGTGASGIVEVLTEVPNIDVTATNSQGFTLLHHASLKGHALAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQILIREGRCDVNVRNRKLQSPLHLAVQQAHVGLVPLLVDAGCSVNAEDEEGDTALHVALQRHQLLPLVADGAGGDPGPLQLLSRLQASGLPGSAELTVGAAVACFLALEGADVSYTNHRGRSPLDLAAEGRVLKALQGCAQRFRERQAGGGAAPGPRQTLGTPNTVTNLHVGAAPGPEAAECLVCSELALLVLFSPCQHRTVCEECARRMKKCIRCQVVVSKKLRPDGSEVASAAPAPGPPRQLVEELQSRYRQMEERITCPICIDSHIRLVFQCGHGACAPCGSALSACPICRQPIRDRIQIFV
Protein: Protein X (HBx) (Peptide X) (pX) (P03165)
Organism: Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
Function: Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04074}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04074}. Host mitochondrion {ECO:0000255|HAMAP-Rule:MF_04074}. Note=Mainly cytoplasmic as only a fraction is detected in the nucleus. In cytoplasm, a minor fraction associates with mitochondria or proteasomes. {ECO:0000255|HAMAP-Rule:MF_04074}.
Interaction partners:
Sequence:
MAARLCCQLDPARDVLCLRPVGAESRGRPFSGSLGTLSSPSPSAVPTDHGAHLSLRGLPVCAFSSAGPCALRFTSARRMETTVNAHQILPKVLHKRTLGLSAMSTTDLEAYFKDCLFKDWEELGEEIRLKVFVLGGCRHKLVCAPAPCNFFTSA
Protein: DM10 domain-containing protein (Q387A9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- CFA20 domain-containing protein
Sequence:
MAYQQSRALKKEFSLPMVPGMTCGEEMLRRSYHRTQVHGRKYDTNTHIDGVPEDMSRFNLQTVSSISKYAPEMLPTATQTQKSDEQNVDLTGRVLRFYAYTKELVPESFVERERVRKFVFNVFLEDNTMSVVEDVADNSGIAMPASLKRHIVPLPDGSPITFANFRVGETITFYGRTYMVYDADKFTRDFYSQSGLELDPALPLPFDAYTELQNRPKKIYAVRTIAASDPTNLTLLPEQVRATQQFLKHDGEVLRCDCVWDDMEALHGTKHYLTLYYFLSDDSIALVEKDYPNSGRDPFPRFFRRQRVAKPKDGRFDPTSLGTLTFEDTSNRDYYTDADIRIGNCLHVFGRDVLIYDYDEYTQHHLLKKFGITSYDPIPGGKNPPAAPIGCHRREKTAQELEEVQMRKRAENRMREYGDVTVKFLMRLDNAKYEDEIRRFVLTVYPADDTISIFEPVIRNMGIVGGKFLQRQRSKRPNGEFYTAKDFFVGARLTINGFPFVILSSDERSLSYMETKHDEFIRSDINYVVRKLRAMLLSRKTGLVEAFREADKENSTGLKMDVFLDIMNRLKLDISEQELLSLLRYFDKQNESYVSYEEFMSRVMPEGVAVASDDRPWEVIDAQSAEEELAAFVVDPRIDEEKRLRAEQISLAARGAEEFLTLYDQRRQLVLKEFRAMTDYSPEGVIGAKEFKMCIRRKLFVQTIPDAALDALCDKLFPPEMPKLSLEELTRVFNGTSTLPRNMKDIKAGESK
Protein: Carboxypeptidase N catalytic chain (CPN) (EC 3.4.17.3) (Carboxypeptidase N polypeptide 1) (Carboxypeptidase N small subunit) (Q9EQV8)
Organism: Rattus norvegicus (Rat)
Function: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.
Subcellular location: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Carboxypeptidase N subunit 2
- Carboxypeptidase B2
Sequence:
MPDLPSAFLPLLLLSKFVTPVTFRHHRYDDLVRTLYKVHNQCPDITRLYNIGRSVKGRYLYVLEFSDYPGTHEPLEPEVKYVGNMHGNEVLGRELLLQLSEFLCEEFRNRNQRILRLIQDTRIHILPSMNPDGYEVAAAQGPNTSGYLVGRNNANGVDLNRNFPDLNTYFYYNSKYGGPNHHLPLPDNWKSQVEPETRAVIQWIRSLNFVLSANMHGGAVVANYPYDKSLEHRFRSPHRTSNSPTPDDELFQTLAKVYSYAHGWMHQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCNKFPRQEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLTGAVISVTGINHDVTSGEHGDYFRLLLPGTYSVTAKASGYEPKTVTVTVGPAGPTLVDFQLKRSTTQVHPVQKAPGRGQGSRAKQPRTSRKKDQAAKRHRGPA
Protein: Aldehyde dehydrogenase (EC 1.2.1.10, EC 1.2.1.3) (Aldehyde dehydrogenase, isoform B) (Q9VLC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Alcohol dehydrogenase
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Alcohol dehydrogenase class-3
- Acetyl-coenzyme A synthetase
- Probable methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- GH01837p)
- monoamine oxidase
- Uncharacterized protein
- MIP01391p)
- RH03309p)
Sequence:
MLRVLKTGALLRSQAKNFAAAVANYSSLPQPQTTPDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVKVAQKNS
Protein: Amino acid transporter (Q5BIC0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
Sequence:
MTRPKQDGGKFKAFMQENVLTMATVIGVFVGGLIGFIIKNSTGEWSKREIMYISFPGEIFLRMLKCLIVPLLVSSITSAIGGLDLSMSSKIATRAITYYFVTTISAVILGICLVTTLRPGQGAKIVETQTESIDKASKVLTPDTLMDLVRNMFTDNIIQSTMFQHRTEIYENTSISPAQPMENWEFKSAQREGSNVLGLVMFSVILGTTIGRMREKGQLLQDFFTTLSEAMMTITSWVIWISPLGVAFLIAAKIVEMESIAATIQSLGWYFITVMIGLFLHGFGTIAVIFFLGTRRLPYRYIAKLSQVLATAFGTGSSSATMPLTIKCLDNMGIDPRVTRFVIPVGATINMDGTALYEAVAALFIAQYREMSYSFGTIVAVSITATAASIGAAGIPQAGLVTMVMVLDTVGLEPKDVSLIIAVDWLLDRFRTTINVMCDALGTILVNHLSKNDLASVDRLNAEPHELLELGPNGHEMKE
Protein: Tuftelin (Enamelin) (P27628)
Organism: Bos taurus (Bovine)
Function: Involved in the mineralization and structural organization of enamel.
Subcellular location: Secreted {ECO:0000303|PubMed:1874744}. Note=Secreted at a very early stage of enamel formation, and tightly bound to the surface of the growing crystallites. {ECO:0000303|PubMed:1874744}.
Interaction partners:
- Amelogenin, X isoform
- Ameloblastin
- Tuftelin-interacting protein 11
- Amelotin
- Enamelin
- Odontogenic ameloblast-associated protein
Sequence:
MNGTRNWCTLVDVHPEGQTAGSVDVLRLTLQSELTGDELERIAQKAGRKTYAMVSSHSTSHSLASELVESNDGHEEIIKVYLKGRSGDKMIHEKNINQLKSEVQYIQEARNCLQKLREDISSKLDRDPGDSVHKQEIQVVLEKQNGLSEGPLTTYSSPPEVDTHINEDVESLRKTVQDLLVKLQEAEQQHQSDCSAFKVTLSQYQREAKQSQVALQRAEDRAEQKEAEVGELQRRLQGMETEYQAILAKVREGETALEELRSKNVDCQAEQEKAANLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDTTIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQNRAKTENLGSIRISKPPSPKPMPLIRVVET
Protein: Lipoyl synthase (EC 2.8.1.8) (Lip-syn) (LS) (Lipoate synthase) (Lipoic acid synthase) (Sulfur insertion protein LipA) (P60716)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for LipA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}.
Interaction partners:
- Octanoyltransferase
- Lipoate-protein ligase A
- Glycine cleavage system H protein
- Biotin synthase
- Iron-sulfur cluster assembly scaffold protein IscU
- Fe/S biogenesis protein NfuA
- Dihydrolipoyl dehydrogenase
- tRNA-2-methylthio-N
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Sequence:
MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLAQTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRALDILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGETNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAACGPFVRSSYHADLQAKGMEVK
Protein: Pregnancy-specific glycoprotein (Q62057)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MELSSELFSNGCTSWQRVLLTASLLTCWLLPTTARVTIESLPPQVYEGENVLLRVDNMPENLLVFGWYRGMTNLWQAIAQHWLYYYSVMVKGLNHSGREILYINGSLWIQNVTQEDTGYYTFQTISKRGEIVSNTSLYLHVYSSLFICVRPTTLISPTIELVPASVAAGGSILLLVHNIPKYLQSLFWYKGLIAFNKVEIARYRTAKNS
Protein: Ubiquitin conjugating enzyme E2 B (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme B) (UBC1) (Q94490)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in protein ubiquitination and degradation during development. Mediates protein ubiquitination at the mound and finger stage required for subsequent development and may be an essential component of the developmental transition between the induction of postaggregative gene expression and subsequent cell-type differentiation and morphogenesis. ubcB and ubpB differentially control ubiquitination/deubiquitination and degradation of mkkA protein in a cell-type-specific and temporally regulated manner.
Interaction partners:
- HECT-type E3 ubiquitin transferase
- Peroxisome biogenesis factor 10
- Signal peptidase complex catalytic subunit sec11
- Probable ubiquitin-conjugating enzyme E2 variant
- Peroxisomal targeting signal 1 receptor
- Ubiquitin-like domain-containing protein
- Anaphase-promoting complex subunit 11
- E1 ubiquitin-activating enzyme
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-like modifier-activating enzyme atg7
Sequence:
MAAHKRLQKEITDMLKTPPSWCSAHLVDDNLQKWKATVQGPEGSPFEKGVFSMDIDIPADYPFKPPTLKFTTKIYHPNIKTSDGAICAEVFSTWSPQLKILDVLTTIRSILTDPNPDNPLETEIAQQFKTDRNAFNKTAKEWTKKYAK
Protein: U4/U6 small nuclear ribonucleoprotein Prp31 (Pre-mRNA-processing factor 31) (Q7SXM7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in pre-mRNA splicing as component of the spliceosome. Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WWY3}. Nucleus speckle {ECO:0000250|UniProtKB:Q8WWY3}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q8WWY3}. Note=Predominantly found in speckles and in Cajal bodies. {ECO:0000250|UniProtKB:Q8WWY3}.
Interaction partners:
- Pre-mRNA-processing factor 8.
- Pre-mRNA-processing factor 6
- PRP3 pre-mRNA-processing factor 3 homolog
- Activating signal cointegrator 1 complex subunit 3
- U4/U6 small nuclear ribonucleoprotein Prp4
- U6 snRNA-associated Sm-like protein LSm8
- Elongation factor Tu GTP-binding domain-containing 2.
- Spliceosome-associated factor 1, recruiter of U4/U6.U5 tri-snRNP
- U6 snRNA-associated Sm-like protein LSm6
- Microfibril-associated protein 1.
Sequence:
MSLADELLADLEEAGEEDGLYPGGEEGESDGEPGERQVDGGLEDIPEEMEVDYSSTESVTSIAKLRHSKPFAEIMDKISHYVGNQRKNSEVSGPVEADPEYRLIVAANNLTVEIDNELNIIHKFVRDKYSKRFPELESLVPNALDYIRTVKELGNNLEKCKNNETLQQILTNATIMVVSVTASTTQGTMLGDDELQRLEEACDMALELNQSKHRIYEYVESRMSFIAPNLSIIVGASTAAKIMGVAGGLTNLSKMPACNLMLLGAQRRTLSGFSSTSLLPHTGYIYHCDVVQTLPPDLRRKAARLVSAKCTLASRVDSFHESADGKVGYDLKEEIERKFDKWQEPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKERLGLTEIRKHANRMTFAEIEDDAYQEDLGFSLGQLGKSGSGRVRQAQVNDSTKARISKSLQRTLQKQSMTYGGKSTVRDRSSGTSSSVAFTPLQGLEIVNPQAAEKKVAEANQKYFSNMAEFLKVKREKEDKV
Protein: Phospholipid:diacylglycerol acyltransferase (PDAT) (EC 2.3.1.158) (Pombe LRO1 homolog 1) (Triacylglycerol synthase) (TAG synthase) (O94680)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid. Plays a major role in triacylglycerol formation at log phase. Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Triacylglycerol lipase ptl3
- Probable diacylglycerol pyrophosphate phosphatase 1
- Nuclear elongation and deformation protein 1
- Triacylglycerol lipase ptl1
- Probable sterol O-acyltransferase 2
- Putative lipase atg15
- Putative phosphatidate cytidylyltransferase
- Uncharacterized acyltransferase C1851.02
- Probable sterol O-acyltransferase 1
Sequence:
MASSKKSKTHKKKKEVKSPIDLPNSKKPTRALSEQPSASETQSVSNKSRKSKFGKRLNFILGAILGICGAFFFAVGDDNAVFDPATLDKFGNMLGSSDLFDDIKGYLSYNVFKDAPFTTDKPSQSPSGNEVQVGLDMYNEGYRSDHPVIMVPGVISSGLESWSFNNCSIPYFRKRLWGSWSMLKAMFLDKQCWLEHLMLDKKTGLDPKGIKLRAAQGFEAADFFITGYWIWSKVIENLAAIGYEPNNMLSASYDWRLSYANLEERDKYFSKLKMFIEYSNIVHKKKVVLISHSMGSQVTYYFFKWVEAEGYGNGGPTWVNDHIEAFINISGSLIGAPKTVAALLSGEMKDTAQLNQFSVYGLEKFFSRSERAMMVRTMGGVSSMLPKGGDVVWGNASWAPDDLNQTNFSNGAIIRYREDIDKDHDEFDIDDALQFLKNVTDDDFKVMLAKNYSHGLAWTEKEVLKNNEMPSKWINPLETSLPYAPDMKIYCVHGVGKPTERGYYYTNNPEGQPVIDSSVNDGTKVENGIVMDDGDGTLPILALGLVCNKVWQTKRFNPANTSITNYEIKHEPAAFDLRGGPRSAEHVDILGHSELNEIILKVSSGHGDSVPNRYISDIQEIINEINLDKPRN
Protein: SPX domain-containing protein 6 (Protein SPX DOMAIN GENE 6) (OsSPX6) (Q8H398)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May be involved in maintaining cellular Pi homeostasis when plants are exposed to an external change in Pi.
Interaction partners:
Sequence:
MKFGKLLKRQIEQSLPEWRDKFVSYKELKRIVASISGSPADEAAFVAALAADIDKIDSFFLEQEEEFVIRHRELQEAIKKAAEAAAEVAGIRREIVDFHGEMVLLLSYSSINYIGVGKILKKHDKRTGGALAAPVAEAVRERRHFFKTETVSRMVRECEAMMAEAAVLPAEAAPEALAAAAEHGIFRNTVAALLTMEDVRRGSSTHGRHSLPPLTLPDSDWLRSFQPPSPIPIQ
Protein: Low density lipoprotein-related protein 6 (D0EWS1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MDGSNRQIIVQKQIYWPNGLTIDLDEQKLYWADAKLSFIHRANLDGTSREAVVEGSLTHPFALTLYDETLYWTDWQTRSIHACNKHSGEKHREILNGIYSPMDIQVLGQERQPNIQTPCSERNGGCSHLCLLSPIPPFYSCACPTGVKLKEDGKTCRPGAEQVLLLARRTDLRRISLDLPDFTDIVLQVNDIRHAIAIDYDPVEGYVYWTDDELRAIRRARIDGSDAQTLITNEINHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTSRRVLISENLDEPRAIVLDPINGYMYWTDWGELPKIERANLDGTDRVVLLNTSLGWPNGLAIDYIAGKLYWGDAKTDKIEVINVDGTNRMTILEDKLPHIFGFTLLGEYIYWTDWQRRSIERVHIANSTREVIVEQLPDLMGLKATKVMEAEGTNGCAENNGGCSHLCFHRPQGLSCACPMGLELLSDLRTCVVPEAFLLFTNRADIRSISLGTNSNDVPIPLTGVKEASALDFDVLENRIYWTDVSTKTISRAFMNGSSVEPVIEFGLDYPEGMAVDWMGRNLYWADTGTNRIEVARLDGQYRQVLVCKDLDNPRSLALDPANGYMYWTEWGGRPRIARAHMDGSNIVTLVDKVGRANGLTIDYIDQRLYWTDLDTCMIESTNMQSLQREIVADDLPHPFGLTQYRDYIYWTDWNLRSIERADKRSGLNRTVVQGHLEYVMDILVFHSSRQDGANDCSQNNGQCAHLCLASPSGAQCRCASHYTLEANGRNCSSPSSFLLFSQKSSISRMVLGEQSPDMILPIHVMKNLRAISFDPLERLVYWVDGRQNIRRSRDDGTQASTVMTPNSDHPKQPHDLSLDPYSRTVYWTCETTNTINIHRMDGHVIGEVLKDDVDKPRAIVVNAEKGYMYFTTVQERSAKIEGASLDGTERESLFTTSLIRPVALALDNKLGKLFWVDADLKRIESSDLSGANRIVLQDSNILQPVGLTVLGDHLYWIDKQQQMIERVDKLTGEKRTRIQGRLQYLTGIHAVQYMETDEFATHPCSRDNGGCSHICIAKGDGTPRCSCPMHLVLLQNLLSCGEPPTCSSEQFTCATGEIDCIPMAWRCDGIAECADNSDEMNCPICSKLQFQCDKGQCVDIQVRCNGEPDCADGSDEQDCETICLSNQFRCGNSQCILKKQQCDSFPDCTDESDERFCDFPPPPNDLPRHTSTIGPVIGIILSVFVMGGMCFVCQRVVCRHYKGPNGGFPHEYISGTPHVPLNFIAPTNSQHGKGISCGKSMMSSVSLMGSSSSGAPLYDRNHVTGASSSSSSSTKGAFYPQMLNPPPSPATDRSLYNAEVFYSSNSPSTTRSYRPYLMRGVAPPTTPCSTDVCDSDYTTSRWKSNKYYMDLNSDSDPYPPPPTPRSQYMSAEESCPPSPSTERSYFHLCPPPPSPCTDSS
Protein: Inositol polyphosphate 5-phosphatase K isoform X1 (Inositol polyphosphate-5-phosphatase Kb) (A0A2R8QKI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Si:ch211-160o17.2.
- Kinase
- Kinase
- Kinase
- Kinase
- Multiple inositol-polyphosphate phosphatase 1b
- Multiple inositol polyphosphate phosphatase 1
- Inositol-tetrakisphosphate 1-kinase
- Inositol-tetrakisphosphate 1-kinase
- Kinase
Sequence:
MSDTFDVPRMRSDSMSTMTSQSTSARFILRQRLAQLLTCLEDLSSDDEANEEVSRTLDEAFNLCGRYSNRESFRLHMVTWNVGTAEPPADVRSLLQLDSQPTTDLYVIGLQEVNATPVRYISDLIAEDTWSHLLMETLAPEGYIKVTSVRMQGLLLILFAKQVHLPFIRDIQSTYTRTGLFGYWGNKGGISVRFSFYGEMLCFLNCHLAAHMNYALQRMDEFEYILDTQEFDMFNTPQVLDHKVVFWFGDLNFRIADHGMHFLRSSINNSRFNLLWDRDQLSMLKKKEPILQEFEEGPLRFKPTYKFDRFSETYNTRAPRTWFGLTGKKRKPAWTDRILWRIKPKATEIEDEKSSTASSADDDEFSVKVTQDMYTCDVSYGVSDHKPVIGTFNLEMRKKVETPLVALTVEGIWSADEDAIFTYTILENFESSTFDWIGLYKIGFKSASDYSTFAWVKDDEVAANGEVVMVQMNKNELPLLAGDYVLGYFSTNMQTLIAFSPNFQILESKRAVMEGLVQENINGLEK