wanglab/gogpt-training-data huggingface dataset:
Protein: Condensin complex subunit 2 (Barren homolog protein 1) (Chromosome-associated protein H) (hCAP-H) (Non-SMC condensin I complex subunit H) (XCAP-H homolog) (Q15003)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size.
Subcellular location: Nucleus {ECO:0000269|PubMed:11694586}. Cytoplasm {ECO:0000269|PubMed:11694586}. Chromosome {ECO:0000269|PubMed:11694586}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Condensin complex subunit 3
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 1
- Condensin-2 complex subunit D3
- Condensin-2 complex subunit G2
- Chromosome-associated kinesin KIF4A
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Condensin-2 complex subunit H2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
Sequence:
MGPPGPALPATMNNSSSETRGHPHSASSPSERVFPMPLPRKAPLNIPGTPVLEDFPQNDDEKERLQRRRSRVFDLQFSTDSPRLLASPSSRSIDISATIPKFTNTQITEHYSTCIKLSTENKITTKNAFGLHLIDFMSEILKQKDTEPTNFKVAAGTLDASTKIYAVRVDAVHADVYRVLGGLGKDAPSLEEVEGHVADGSATEMGTTKKAVKPKKKHLHRTIEQNINNLNVSEADRKCEIDPMFQKTAASFDECSTAGVFLSTLHCQDYRSELLFPSDVQTLSTGEPLELPELGCVEMTDLKAPLQQCAEDRQICPSLAGFQFTQWDSETHNESVSALVDKFKKNDQVFDINAEVDESDCGDFPDGSLGDDFDANDEPDHTAVGDHEEFRSWKEPCQVQSCQEEMISLGDGDIRTMCPLLSMKPGEYSYFSPRTMSMWAGPDHWRFRPRRKQDAPSQSENKKKSTKKDFEIDFEDDIDFDVYFRKTKAATILTKSTLENQNWRATTLPTDFNYNVDTLVQLHLKPGTRLLKMAQGHRVETEHYEEIEDYDYNNPNDTSNFCPGLQAADSDDEDLDDLFVGPVGNSDLSPYPCHPPKTAQQNGDTPEAQGLDITTYGESNLVAEPQKVNKIEIHYAKTAKKMDMKKLKQSMWSLLTALSGKEADAEANHREAGKEAALAEVADEKMLSGLTKDLQRSLPPVMAQNLSIPLAFACLLHLANEKNLKLEGTEDLSDVLVRQGD
Protein: Spermidine export protein MdtJ (P69212)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the excretion of spermidine. Can also confer resistance to deoxycholate and SDS.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Spermidine export protein MdtI
- Guanidinium exporter
- Multidrug transporter EmrE
Sequence:
MYIYWILLGLAIATEITGTLSMKWASVSEGNGGFILMLVMISLSYIFLSFAVKKIALGVAYALWEGIGILFITLFSVLLFDESLSLMKIAGLTTLVAGIVLIKSGTRKARKPELEVNHGAV
Protein: Dipeptidyl-peptidase 5 (EC 3.4.14.-) (Dipeptidyl-peptidase V) (DPP V) (DppV) (Q9P778)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Secreted {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor brr2
- Sorting nexin C1711.11
Sequence:
MHSLFKQLVFFLVMTLTAADKAAFDAESMLEAPRRSAVVSNPLGNLGIFIESNYSFADHKYNSGIYLLNESTRNHQELLVHGKSNKALTWITDSAFLYAREDNSSSSSILLFDVNNRSERIIYNHNSSISDIRIGEKNNHYRIVFSSVDNSLVKGPSNVHVYDHLFVRHWDRWNTGSRNTLYFIELDKKTENSNYFEISSEKAIDLLKETGLESPVEPFGGLSDFDSNYDKLVFVAKDPKLNPATQTKTVVYEINLNTRNLKSLSTAKGACSSPRLAKDGNHIAWLEMQTPQYESDQNQIMVYESESGAKKHIARHWDRSPSSIEWGVFKGGEPGLFAIAENYGKQILFFVSIFHHQVIPMTEEHSVSSISVPKSSSLWLTKSSLINPPYYAKINVETLNESVLLENNVGLSPTSYEEIWFPGTHGHRIHAWIVKPESFDKSKKYPVAVLIHGGPQGSWTDSWSTRWNPAVFANAGFIVFALDPTGSTGYGQRFTDSIALDWGGKPYKDIELGVEYIKNHLSYADSEKMVALGASYGGYMINWIQGHPLGRQFRALVCHDGVFNTLNTFYNTEELYFSIHDFGGTPWENRVIYERWNPSNFVNYWATPELVIHSSKDYRLTESEGIAAFNVLQYKGIPSRLLVFEDENHWVIKPDNSLRWHKEVLSWILHYTKDCNANEDETF
Protein: Oryzalexin E synthase (EC 1.14.14.122) (Cytochrome P450 76M6) (Q6Z5I7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Enzyme of the diterpenoid metabolism involved in the biosynthesis of the oryzalexin class of phytoalexins. Can use ent-sandaracopimaradien and syn-stemodene as substrates, but no activity with syn-stemoden-19-oic acid. Hydroxylates 3-alpha-hydroxy-ent-sandaracopimaradiene at C-9-beta, resulting in a 3-alpha,9-beta-diol corresponding to oryzalexins E.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ent-sandaracopimaradiene 3-hydroxylase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- 4-coumarate--CoA ligase
Sequence:
MEKLKSELWMTAVATCMSLLLYLTILRRRHASGGRSLALPPGPTPLPLIGNLLCLGGIFHQTLAKLARVHGPVMTLKLGLTTAVVVSSAEAAREAYTKHDQRLAARPVPDAFRANGFSERSIVFSPSSDPQWKNLRGIHATHIFSPRALAALRGIRERKVRDIVGYIRTVAGEEMCVREVVHNGVLNLISTSFFSMDMADVRSESARGLRGLIEDIIATVAGPNVSDFFPFLRQLDLQGLRRQTGSHLGIVFGLLDDIIDRRMAETRDHPDKQRHGDFLDALISLASAGKIPRYHITYLLFDVFAAGADTMTTTVEWAMAELLRNPRVMAKVRAEVTDALGGRESFDEGDAASLTYLQCVFKEAMRLHPVGSILVPHLAVQDGVEIGGYAVPKGTTVIFNAWAIMRDPAAWESPDQFLPERFLHKEESSSPPLELRGKDYEYIPFGSGRRLCPGLPLAERAVPFILASLLHAFEWRLPDGMSPDDMDMTEKFATANVLATPLKAVPVASHTS
Protein: DUF222 domain-containing protein (Q8NRW3)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- HNH nuclease domain-containing protein
- HNH nuclease domain-containing protein
- HNH nuclease domain-containing protein
- HNH nuclease domain-containing protein
- HNH domain-containing protein
Sequence:
MSITTHVQALTTALNAIDNHLASMLDHGVTPDQYKAIEPDLIALEHTINHHATIAAQTTALAERTNAAQSIGSTHLIDYLTTTFGLSKARAHHRINLAHSLYPIPKPNSGSGNGGNGGNPDGGPDGGDSGDDDSGDDDPDPEPDKPEDGKPDSDKPRRPRISAEKHAIITDELARLNPNTTPSAEELRNQALSQAIWRTPEDLRTWLRHQVTTANKNNPNPITAMKRRYLSVGKPDADNMVRISGLVPAATAALITANTAPLTKRGNLVDLPAAEDMRTRGQRHADALHHIMEIYNHGIVTPARGGTASIIISMTTDDLDEINHANSSGESLLNNLYPTNTGYSLNLAEIMNLIAAKYDFAVLLDGETGQPLNVNRMQRSANLTQRIALFASELVCSAPNCDRPQLECEVHHLDPWMRGGLTNLVNLTHQCFNHHPRNDDSRSGVNGKGFMDRDPATGRVGHYPVGGEGPVFNRSAAADRSGGAWARRKHHGPPPTPPDPPDPPGPEPDPGDEGRLF
Protein: Interleukin-2 receptor subunit alpha (IL-2 receptor subunit alpha) (IL-2-RA) (IL-2R subunit alpha) (IL2-RA) (CD antigen CD25) (P26897)
Organism: Rattus norvegicus (Rat)
Function: Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-2
- Interleukin-2 receptor subunit beta
- Interleukin 2 receptor, gamma, isoform CRA_a.
- Tyrosine-protein kinase JAK3
- Interferon gamma
- Tyrosine-protein kinase
- Signal transducer and activator of transcription 5A
- Interleukin-15
- Signal transducer and activator of transcription 5B
- Interleukin-10
Sequence:
MEPHLLMLGFLSFTIVPGCWAELCLYDPPEVPNATFKALSYKNGTILNCECKRGFRRLNELVYMACLGNSWSNNCQCTSNSHDNSREQVTPQPEGQKEQQTTDTQKSTQSVYQENLAGHCREPPPWRHEDTKRIYHFVEGQIVLYTCIQGYKALQRGPAISICKTVCGEIRWTHPQLTCVDEKEHHQFLASEESQGSRNSFPESEASCPTPNTDFSQLTEATTTMETFVFTKEYQVAVASCIFLLLSILLLSGFTWQHRWRKSRRTI
Protein: Centrosomal protein 55 kDa (Q54G01)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNNINNDPFKTPKFKRPLTVDKYPLNKINNTNNNNNNNNNNFTNHQPQQQSQPQQQQNVNNNDIETPTQNENITIINEIEKEKFKKQIEELIKEIQIIKQETENDWRIKENELRNEIQSITKQYDNLKEFSNTQDQLIKNQYFEIEKQSQKSYQQSMEVERLLKKSQSQEQQIITLLETTDKNKRFSSDLLIKNAQLNERILELENRITKYEDGTISITDNEKQIRQQLSDYKLKLQDLHQQNQRLQATQREQSNQKSKSEQTLQTTLSEKLNEINALSLQIDFLELKLQNSETKLAESINILNEYDQTIKNFEDTQKQKDQEFNQILQINENLKLQIHETEFKYRQLLNENSNINNNNNNQSILFQAKKEIKSISQELIYIKELLKMIDSTIILPKNLKQRQSSSIFDNLENYNNTPPPDPNDLLSMMKFIREELYSINLSINKKCSELLQIHNSNQEFNINPSNCSFQ
Protein: Disease resistance protein (TIR-NBS-LRR class) family (F4JNL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTNSSQSRKPQVFISFRGKAQRKTLVSFIKSKLEEISEINVFMDEYEIRGRPITTLFERIRESSIALVIFSDKYPESRWCLDELVEIKKQMETGSIVPFPIFYKVKAESVKNQTGHFRNVLLKTEEDVRKKVDRSNIRSILETEDMIWGWRQALVSVGGRMGFSYNHKCDNDFVNDIVVQIKKMLADLSPSPRNGLKIIERPQMHPQEEVTSLLQALNLKKSDLEDLIHINGVVSHGTDRLVFLDLISLQNPILADRLIELVQAGRNLLVLLGSLEYYNKGFTFKRIFLPKKSQQLPGYTVVAESNDNLRNHEVSYSDTVLTCFSFLCNILKRSEMKIDPLSQRVFIGLGEKHLGKFLVSSLKEELESNQILVYVEDETKSRIKESGVAVVFFSKKYPNSEKCLDELVEIKKLMDAGKIDPLPVFYSLKDEPVKNLKGYFLNRLLKIENEVRKNIKTRDDKSILDTEAKIWGWRDALSSIASRPGLSYELSTDDVFVSDIVTKVNELFASRERKKTEAATTVVKTLDADDLFYSRTSFLQAIDRDITDFESFTDIPNGLVLLRLKGHTNLVFLKLSSHENLLQVLYLLSLDFNKRGGEAESIVTSASGSIVAASSMFQPLDNSIRIDLNRQKYAT
Protein: Putative magnesium transporter YhiD (P0AFV2)
Organism: Escherichia coli (strain K12)
Function: Could be involved in magnesium uptake.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein HdeD
- Transcriptional regulator GadE
- HTH-type transcriptional regulator DctR
- Glutamate decarboxylase alpha
- Outer membrane protein Slp
- Acid stress chaperone HdeB
- Acid stress chaperone HdeA
- Multidrug resistance protein MdtE
- Glutamate decarboxylase beta
- Glutamate/gamma-aminobutyrate antiporter
Sequence:
MTAEFIIRLILAAIACGAIGMERQMRGKGAGLRTHVLIGMGSALFMIVSKYGFADVLSLDHVGLDPSRIAAQVVTGVGFIGAGNILVRNQNIVGLTTAADIWVTAAIGMVIGSGMYELGIYGSVMTLLVLEVFHQLTFRLMNKNYHLQLTLVNGNTVSMLDWFKQQKIKTDLVSLQENEDHEVVAIDIQLHATTSIEDLLRLLKGMAGVKGVSIS
Protein: Transcription factor Sp9 (P0CG40)
Organism: Homo sapiens (Human)
Function: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Acrosomal protein SP-10
- Lipase member N
Sequence:
MATSILGEEPRFGTTPLAMLAATCNKIGNTSPLTTLPESSAFAKGGFHPWKRSSSSCNLGSSLSGFAVATGGRGSGGLAGGSGAANSAFCLASTSPTSSAFSSDYGGLFSNSAAAAAAAAGVSPQEAGGQSAFISKVHTTAADGLYPRVGMAHPYESWYKSGFHSTLAAGEVTNGAASSWWDVHSSPGSWLEVQNPAGGLQSSLHSGAPQASLHSQLGTYNPDFSSLTHSAFSSTGLGSSAAAASHLLSTSQHLLAQDGFKPVLPSYSDSSAAVAAAAASAMISGAAAAAAGGSSARSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRSDHLSKHIKTHNGGGGGKKGSDSDTDASNLETPRSESPDLILHDSGVSAARAAAAAAAAAAAAAAAASAGGKEAASGPNDS
Protein: Archaemetzincin (EC 3.4.-.-) (Q8TXW1)
Organism: Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Function: Probable zinc metalloprotease whose natural substrate is unknown. Does not show endo- or exopeptidase activity against resorufin labeled casein, p-nitroanilide (pNA), amidomethylcoumarin (AMC) (one to three amino acids in length), and hippuryl-aminoacid substrates.
Interaction partners:
- Acetyltransferase
- Uncharacterized protein
Sequence:
MKLCLVAFDGRIPMLSSIVDRFEEHVSEYLGEVKVKKKRAKLPEHAYSKVRGQYLARALLDTLRGMKGEYDRVLGLTSEDLYAPGLNFVFGQARCPGREAVVSVARLLDPDPELYLERVVKELTHELGHTFGLGHCPDRNCVMSFSSSLLEVDRKSPNFCRRCTELLQRNLKRGG
Protein: Glutamate receptor 1.1 (AtGLR1) (Ligand-gated ion channel 1.1) (Q9M8W7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glutamate-gated receptor that probably acts as non-selective cation channel. Can transport sodium, potassium, and calcium ions. Functions as a carbon and nitrogen regulator and/or sensor that regulates carbon and nitrogen metabolism and distinct physiological process such as germination through the control of acid abscisic (ABA) biosynthesis. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells. Seems required for the regulation of the abscisic acid (ABA) signaling pathway that modulates many aspects of plant physiology such as seed germination and response to drought (e.g. stomata opening).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Probable pectin methyltransferase QUA2
- Uncharacterized protein
Sequence:
MEILFSISILALLFSGVVAAPSDDDVFEEVRVGLVVDLSSIQGKILETSFNLALSDFYGINNGYRTRVSVLVRDSQGDPIIALAAATDLLKNAKAEAIVGAQSLQEAKLLATISEKAKVPVISTFLPNTLSLKKYDNFIQWTHDTTSEAKGITSLIQDFSCKSVVVIYEDADDWSESLQILVENFQDKGIYIARSASFAVSSSGENHMMNQLRKLKVSRASVFVVHMSEILVSRLFQCVEKLGLMEEAFAWILTARTMNYLEHFAITRSMQGVIGFKSYIPVSEEVKNFTSRLRKRMGDDTETEHSSVIIGLRAHDIACILANAVEKFSVSGKVEASSNVSADLLDTIRHSRFKGLSGDIQISDNKFISETFEIVNIGREKQRRIGLWSGGSFSQRRQIVWPGRSRKIPRHRVLAEKGEKKVLRVLVTAGNKVPHLVSVRPDPETGVNTVSGFCVEVFKTCIAPFNYELEFIPYRGNNDNLAYLLSTQRDKYDAAVGDITITSNRSLYVDFTLPYTDIGIGILTVKKKSQGMWTFFDPFEKSLWLASGAFFVLTGIVVWLVERSVNPEFQGSWGQQLSMMLWFGFSTIVFAHREKLQKMSSRFLVIVWVFVVLILTSSYSANLTSTKTISRMQLNHQMVFGGSTTSMTAKLGSINAVEAYAQLLRDGTLNHVINEIPYLSILIGNYPNDFVMTDRVTNTNGFGFMFQKGSDLVPKVSREIAKLRSLGMLKDMEKKWFQKLDSLNVHSNTEEVASTNDDDEASKRFTFRELRGLFIIAGAAHVLVLALHLFHTRQEVSRLCTKLQSFYK
Protein: EKC/KEOPS complex subunit SPAP27G11.07c (EC 3.6.-.-) (Atypical serine/threonine protein kinase BUD32 homolog) (EC 2.7.11.1) (Q9P7N1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53323}. Nucleus {ECO:0000250|UniProtKB:P53323}. Chromosome, telomere {ECO:0000250|UniProtKB:P53323}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- EKC/KEOPS complex subunit cgi121
- EKC/KEOPS complex subunit SPAC4H3.13
- Threonylcarbamoyl-AMP synthase
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- 18S rRNA aminocarboxypropyltransferase
- EKC/KEOPS complex subunit gon7
Sequence:
MSEKPDLRQRCSDIYREIKEKKLTVVKQGAEAITIKTEFYPGEVCLLKCRPAKRWRHPILDQKLSRKRCLVEARLLAKCHYVGIKCPMLYFIDANRGQIYMEWIDGPCVRDYIREICECEIEKKLIPLMKRIGSEVAKMHKNDIVHGDLTTSNMMLESHNNPVPIFIDFGLGSVSESEEDKAVDIYVLERALSSTLPESESLFHHVLDSYAQSWKQSKATLRRFEEVRMRGRKRTMIG
Protein: Hyaluronidase-1 (Hyal-1) (EC 3.2.1.35) (Hyaluronoglucosaminidase-1) (Lung carcinoma protein 1) (LuCa-1) (Q12794)
Organism: Homo sapiens (Human)
Function: May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth.
Subcellular location: Secreted {ECO:0000269|PubMed:9223416}. Lysosome {ECO:0000269|PubMed:9223416}.
Interaction partners:
- Alpha-L-iduronidase
- Beta-glucuronidase
- Arylsulfatase B
- Hyaluronan synthase 2
- CD44 antigen
- Hyaluronan synthase 1
- Macrophage-stimulating protein receptor
Sequence:
MAAHLLPICALFLTLLDMAQGFRGPLLPNRPFTTVWNANTQWCLERHGVDVDVSVFDVVANPGQTFRGPDMTIFYSSQLGTYPYYTPTGEPVFGGLPQNASLIAHLARTFQDILAAIPAPDFSGLAVIDWEAWRPRWAFNWDTKDIYRQRSRALVQAQHPDWPAPQVEAVAQDQFQGAARAWMAGTLQLGRALRPRGLWGFYGFPDCYNYDFLSPNYTGQCPSGIRAQNDQLGWLWGQSRALYPSIYMPAVLEGTGKSQMYVQHRVAEAFRVAVAAGDPNLPVLPYVQIFYDTTNHFLPLDELEHSLGESAAQGAAGVVLWVSWENTRTKESCQAIKEYMDTTLGPFILNVTSGALLCSQALCSGHGRCVRRTSHPKALLLLNPASFSIQLTPGGGPLSLRGALSLEDQAQMAVEFKCRCYPGWQAPWCERKSMW
Protein: fumarate hydratase (EC 4.2.1.2) (Q8IRQ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASQEFRVESDTFGELKVPADKYYGAQTMRSQINFPIGGATERMPKPVVQAMGILKKAAAEVNKEFGLDSKVSEAISKAADDVISGKLYDDHFPLVIWQTGSGTQSNMNVNEVISNRAIELLGGKLGSKTPVHPNDHVNKSQSSNDTFPTAIHISVALELNNNLKPAIKTLHDALRAKSEEFKDIIKIGRTHTMDAVPLTLGQEFSGYAQQLAYAQERIDACLPRVYELALGGTAVGTGLNTRKGFAEKCAAKIAELTSLPFVTAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRFLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCESLTMLSAQVMGNQVAVTIGGSNGHFELNVFKPLIVSNVLRSIRLLSDGSRTFTANCVNGIQANRENIAKIMNESLMLVTALNPHIGYDKAAKIAKTAHKNGTTLKEEAINLGYLTEQQFNDWVRPEQMLGPK
Protein: Tcfcp2 protein (Transcription factor CP2) (G3V969)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU01313}.
Interaction partners:
Sequence:
MAWALKLPLADEVIESGLVQDFDASLSGIGQELGAGAYSMSDVLALPIFKQEESSLPPENENEILPFQYVLCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKLGELPEINGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGVIDPRANPTQLNTVEFLWDPAKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENENGEYTEHLHSASCQIKVFKPKGADRKQKIDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVSNSPSPGFNSSHSSFSLGEGNGSPNHQPEPPPPVTDNLLPTTTPQEAQQWLHRNRFSTFTRLFTNFSGADLLKLTRDDVIQICGPADGIRLFNALKGRMVRPRLTIYVCQESLQLREQPQQPQPQQKQEDGDSNVYHAIYLEELTAVELTEKIAQLFSISPQQISQIYKQGPTGIHVLISDEMVQNFQEEACFILDTMEAETSDSYHVILK
Protein: Sorting nexin-19 (Q6P4T1)
Organism: Mus musculus (Mouse)
Function: Plays a role in intracellular vesicle trafficking and exocytosis. May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).
Subcellular location: Early endosome membrane {ECO:0000305|PubMed:25148684}; Peripheral membrane protein {ECO:0000269|PubMed:25148684}; Cytoplasmic side {ECO:0000269|PubMed:25148684}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25148684}; Peripheral membrane protein {ECO:0000269|PubMed:25148684}; Cytoplasmic side {ECO:0000269|PubMed:25148684}.
Interaction partners:
Sequence:
MKAQTVSPTQGTISESSYVHSNLWSSRKLMIVGVLVGWLLVIHLLVNMWLLILLCASLVALGGWLGSTAILGASGQLHLERFITITTCPPCPEAERQLEQEINRTIQMIIRDFVLSWYRSVSHEPAFEAEMEAAMKGLVQELRRRMSIVDSHALTQRVLTLCGCHLQSYIQAKEATAKEQSCPVQPSQLWDAYCQVTAPHPAMSCPTTEVTYARGIVNLILKELVPKPHLETRTGRHVVVEVITCNVILPLISKLSDPDWIHLILVSIFSKYRHDAAQGTKPPCSSSVLEQPSVPTSLPLIVEVESLPVGKASSPATAPVHLTSSEPAPSPEIEEGHEAVEGDLPGMLEEKKVGNSSSHFLQPDIRGPLFLCEDSELESPLSELSKETILLMTPGNFLSDRIQDALCALDDSGALEPKDGEGSECMEGAEAEEAPGTDTETGMLVSVLNCPEIQIDTADKEVEQGDDTSLTALLEEPEKPCPLRPSCLDKDLASGVCSLEPAMPPVPLSSSPPGPLSSATFSFESLSSPDGPVVIQNLRITGTITAREHSGTGFHPYTLYTVKYETVLNGENSSGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIKNVKGPKKLFPDLPFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALNTDARIAFVKKPFMVSRIDKMVVSAIVDTLKTAFPRSEPQSPTEELSEAENESKPQTEGKKASKSRLRFSSSKIAPALSIAEAQDKILYCLQEGNSESEVLSMSGMESFIEKQTKLLRIQPAEVPDKDPQQVPKEYVDSGLLDKAVVAQELNKSGPGTETELADTAFDLILLLLMEQWKWLCTESMQKFLHIIFGTLVQRWLEVQVANLTCPQRWAQYLHLLRESIWPGGVLPKFPRPGRTQAQKAATEKQALQSLMDLLPDFLVEILGVNKCRLSWSLVLESFQQPLINRHLIYCLGDIILELLDLSASVEECAPATSASDSPGSLKKMAVST
Protein: Feruloyl esterase C (EC 3.1.1.73) (Ferulic acid esterase C) (FAEC) (Q5B2G3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against paranitrophenyl-acetate, methyl ferulate and wheat arabinoxylan.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Xylanolytic transcriptional activator xlnR
- Probable D-xylulose reductase A
- Probable feruloyl esterase B
Sequence:
MLRAVLLPTLLAFGAFTPVHGANSPGCGKQPTLTNGVNQINGREYVLKIPDGYDPSKPHHLIFGLHWRGGNMYNVVNGDSIQPWYGLEARAQGSAIFVAPNGLNAGWANTNGEDVAFIDAIMEQVEDDLCVDQASRFATGFSWGGGMSYALACARAAEFRAVSVLSGGLISGCDGGNDPIAYLGIHGINDPVLPLDGGVTLANTFVSNNGCQPTDIGQPASGSGGSVRTDFSGCSHPVSFIAYDGGHDGAPLGVGSSLAPDATWEFFMAA
Protein: Cytochrome b-c1 complex catalytic subunit, mitochondrial (EC 7.1.1.8) (Complex III catalytic subunit) (A0A1D8PHA3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome b
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- NAD-dependent epimerase/dehydratase domain-containing protein
- NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
- Fesur1p
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit Va
- Cytochrome c oxidase subunit 6, mitochondrial
Sequence:
MFRTAYKTMNQSMVQKFIAGGVGVTGLTASYLLYQDSMTADAMTAAEHGLHPPAYNWPHNGMFETFDHASIRRGFQVYREVCAACHSLDRIAWRNLVGVSHTTSEAKAMAEELEYDDEPDDEGKPRKRPGKLADYIPGPYENEQAARAANQGAYPPDLSLIVKARHGGSDYIFSLLTGYPDEPPAGVVLPEGSNYNPYFPGGAIAMGRVLFDDLVEYEDGTPATTSQMAKDVSTFLNWASEPEHDDRKKWGLKALVVLSSLYLLSIWVKRFKWTPIKNRKFRFDPPKK
Protein: Glycogen debranching enzyme (EC 2.4.1.25) (EC 3.2.1.33) (Glycogen debrancher) (F8VPN4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Glycogen phosphorylase, muscle form
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, brain form
- Phosphoglucomutase-1
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogenin-1
- Alpha-amylase 1
- Pancreatic alpha-amylase 2a5
- Sucrase-isomaltase, intestinal
Sequence:
MEHSKQIRILLLNEMEKLEKTLFRLEQGFELQFRLGPTLQGKAVTVYTNYPLPGEAFNREKFRSLDWENPTEREDDSDKYCKLHLQQSGSFQYYFLQGNEKSGGGYIVVDPILRIGVDNHVLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLADQLELNPDFSRPSKRYTWSDVGQLVEKLKREWNILCITDVVYNHTATNSKWILEHPESAYNLVNSPHLKPAWVLDRALWHFSCDVADGKYREKGVPALIENDQHMNCIRKIIWEDIFPRIQLWEFFQVDVHKAVEQFRRLLSQENRRVTKSEPKEHLKIIQDPEYRRRGCAVDMDTALATFIPHDNGPAAIEECCNWFRKRLEELNSEKHHLTSCHQEQAVNCLLGNVFYERLAGHGPKLGPVTRKYPLVTRYFTFPFGEMALSAEEALIHLPDKACFLMAHNGWVMGDDPLRNFAEPGSDVYLRRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATHFQGVRLDNCHSTPLHVAEYMLDAARKLQPNLYVVAELFTGSEELDNIFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEPVGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTVVSMACCASGSTRGYDELVPHQISVVAEERFYTKWNPGASPADTGDVNVHSGIIAARCAINRLHQELGAKGFIQVYVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEARTIERNTKPYKKDENSINGMPNMTVELREHIQLHESKIVRQAGVATKGPNEYIQEIEFENLSPGSVIIFRVSLDPHAQVAVGILRNHLTQFSSHFKSGSLAVDNADPILKIPFASIASKLTLAELNQVLYRCESEEQEDGGGCYDIPNWSSLKYAGLQGLMSVLAEIRPKNDLGHPFCENLRSGDWMIDYVSGRLISRSGSIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLDVAWKQMSSFVQNGSTFVKHLSLGSVQMCGVGKCPCLPLLSPSLLDVPCRLNEITKEKEQCCASLAAGLPHFSSGLFRCWGRDTFIALRGMLLVTGRYLEARNIILAFASTLRHGLIPNLLGEGTYARYNCRDAVWWWLQCIQDYCRTVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPLFEVIQEAMQRHMQGIQFRERNAGPQIDRNMKDEGFNITAGIDEETGFVYGGNRFNCGTWMDKMGESDRARNRGIPATPRDGSAVEIVGLCKSAVRWLLELSKKNIFPYHEVRVKRHGKVVAVSYDEWNRKIQNNFEKLFHVSEDPSDPNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPNFTIAMVVAPELFTAEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGVYDNALDNDNYNLARGFNYHQGPEWLWPIGYFLRAKLYFSKMMGPETAAKTVFLVKNVLSRHYVHLERSPWKGLPELTNENGQYCPFSCETQAWSMAVVLETLYDL