wanglab/gogpt-training-data huggingface dataset:
Protein: GTP 3',8-cyclase (EC 4.1.99.22) (Molybdenum cofactor biosynthesis protein A) (Q72EJ8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Cyclic pyranopterin monophosphate synthase
- Molybdopterin molybdenumtransferase
- Formate dehydrogenase accessory protein FdhD, putative
- Probable molybdenum cofactor guanylyltransferase
- Molybdopterin molybdenumtransferase
- Molybdopterin adenylyltransferase
- Riboflavin biosynthesis protein RibBA
- GTP cyclohydrolase FolE2
- Adenylate cyclase
- Anaerobic ribonucleoside-triphosphate reductase, putative
Sequence:
MNHYDDRPASSLVDLHGRRVRYLRLSVTDRCNLRCLYCWGGGGMRFIPHDDILRYEEMARLVDVAVESGVEKVRLTGGEPLVRKNVLHLVELVRKKHPAIDLRITTNGTLLESHVAGLRDLGVSTVNVSLDTFRREVFHEVTGRDFLPQVMAGMEAVLAAGLSLKVNAVALRGVNDGELATFVDFARNHRVDVRFIEFMPMGCGTRWNDANFWPADDILARVHDLADLRPVVPDKGGRGPARLFDIVGGQGRFGVITPMSDHFCGDCNRLRVTSDGRLRTCLFADREYRLRPLLRHPKLGVEAVRRVIALANRRKPLGFRLLERMRPGLAVAERRMTAIGG
Protein: RNA-binding protein MRN1 (Multicopy suppressor of RSC-NHP6 synthetic lethality protein 1) (Post-transcriptional regulator of 69 kDa) (Q08925)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein that binds specific categories of mRNAs, including those that contain upstream open reading frames (uORFs) and internal ribosome entry sites (IRES). Probably involved in translational regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Heterogeneous nuclear rnp K-like protein 2
- mRNA-binding protein PUF2
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- Protein SCP160
- Uncharacterized protein YBL081W
- Protein JSN1
Sequence:
MVVSYNNNNNNNNNNNNNNISNNNNNNNMFPPFPSSDDFAMYQQSSSSGPYQETYASGPQNFGDAVYPMNGNFTLLPSDFTREPNDSFFYENDGIFDYQRIQQQPTQFQTKQRNDSQQQRFSQEQNFEIDNEVVHNNNRYYEYERSSNEVSPFDDENPNVLSDGMSPTIMATATAVTNANAPLPVNAQANNPLNFTSAPSRTVYLGNVPPNLSVKELLDHVRSGVVEDVKIIPEKMCAFVSFIDESAALLFHSDAILKRLNIGDRDIKIGWGKPTRIDPIVAARISTDGATRNVYIGRMTIEGEESHLSEEQLRVDLEEYGEIDCIKIIKEKGIAFIHFASILNAIKVVTNLPIRNPYYQNKRIFYGKDRCAFITKTQQHNAAQFLGVQPGMEHMIEFSDREFISNALLQQSAAAAAIATSAGGPNNLGNRTVYLGSLPKDVKIEEICNAVRGGLLQSIKLLNDRYVCFVTFIDPTAAAQFYAMSSLYGFTVQKKRCKVGWGKHSGPLPNALALAVSNGASRNVYVGNIDFVGDSLRDERVFTESNLRHIFQQYGEVEQINFLPEKNCCFINYTNISNAILALDKIKSNPYFKDLKINFGKDRCGNVPHQSR
Protein: DNA topoisomerase 2-beta (EC 5.6.2.2) (DNA topoisomerase II, beta isozyme) (Q64511)
Organism: Mus musculus (Mouse)
Function: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q02880}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q02880}. Nucleus {ECO:0000250|UniProtKB:Q02880}.
Interaction partners:
- DNA topoisomerase 1
- DNA topoisomerase 2-alpha
- DNA topoisomerase I, mitochondrial
- Tyrosyl-DNA phosphodiesterase 2
- DNA topoisomerase 3-alpha
- Transcriptional repressor CTCF
- Tyrosyl-DNA phosphodiesterase 1
- DNA topoisomerase 2-binding protein 1
- Structural maintenance of chromosomes protein 6
- DNA topoisomerase 3-beta-1
Sequence:
MAKSSLAGSDGALTWVNNATKKEELETANKNDSTKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCKGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVSKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSSLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLEGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDSQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDTKGREVNDLKRKSPSDLWKEDLAAFVEELDKVEAQEREDILAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIVPEITAMKADASRKLLKKKKGDPDTTVVKVEFDEEFSGTPAEGTGEETLTPSAPVNKGPKPKREKKEPGTRVRKTPTSTGKTNAKKVKKRNPWSDDESKSESDLEEAEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDAAAADDSNDLEELKVKASPITNDGEDEFVPSDGLDKDEYAFSSGKSKATPEKSSNDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDTASVFAPSFGLKQTDKLPSKTVAAKKGKPPSDTAPKAKRAPKQKKIVETINSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKPSKTASKKPKKTSFDQDSDVDIFPSDFTSEPPALPRTGRARKEVKYFAESDEEEDVDFAMFN
Protein: Lymphocyte function-associated antigen 3 (Ag3) (Surface glycoprotein LFA-3) (CD antigen CD58) (P19256)
Organism: Homo sapiens (Human)
Function: Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- T-cell surface antigen CD2
- Intercellular adhesion molecule 1
- T-lymphocyte activation antigen CD80
- T-cell-specific surface glycoprotein CD28
- CD48 antigen
- Integrin alpha-L
- Integrin beta-2
- T-cell surface glycoprotein CD8 alpha chain
- Cytotoxic T-lymphocyte protein 4
- Tumor necrosis factor receptor superfamily member 5
Sequence:
MVAGSDAGRALGVLSVVCLLHCFGFISCFSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTVSGSLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLESLPSPTLTCALTNGSIEVQCMIPEHYNSHRGLIMYSWDCPMEQCKRNSTSIYFKMENDLPQKIQCTLSNPLFNTTSSIILTTCIPSSGHSRHRYALIPIPLAVITTCIVLYMNGILKCDRKPDRTNSN
Protein: Calbindin (Calbindin D28) (D-28K) (Spot 35 protein) (Vitamin D-dependent calcium-binding protein, avian-type) (P07171)
Organism: Rattus norvegicus (Rat)
Function: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase.
Interaction partners:
- Parvalbumin alpha
- Protein S100-G
- 45 kDa calcium-binding protein
- Glutamate decarboxylase 1
- Somatostatin
- RNA binding protein fox-1 homolog 3
- Pro-neuropeptide Y
- Glial fibrillary acidic protein
- Tyrosine 3-monooxygenase
- Glutamate decarboxylase 2
Sequence:
MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALILSAGDN
Protein: Protein REGULATOR OF FATTY ACID COMPOSITION 3, chloroplastic (Q948R9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds together with S18 to 16S ribosomal RNA (By similarity). Prevents non-specific action of the splicing factor CFM3b during plastid rRNA biogenesis to improve the accuracy of plastid rRNA processing. Required for plastid functions such as photosynthesis, intracellular distribution, plastid rRNAs biosynthesis and plastid gene expression in roots. Involved in a sucrose-conditional process important for the organization of root lateral and apical meristems (e.g. establishment of RAM from pericycle and symplasmic connectivity), and subsequent primary and lateral roots development. Modulates C18 unsaturated fatty acid metabolism (Ref.6).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12581310, ECO:0000269|PubMed:29367414}. Plastid {ECO:0000269|PubMed:29367414, ECO:0000269|PubMed:32143506}. Note=Present in root plastids and chloroplasts in leaves. {ECO:0000269|PubMed:29367414, ECO:0000269|PubMed:32143506}.
Interaction partners:
- Small ribosomal subunit protein bS6c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- CRM-domain containing factor CFM3B, chloroplastic
- CRM-domain containing factor CFM3A, chloroplastic/mitochondrial
- At1g31410
- Endoribonuclease YBEY, chloroplastic
- At4g39040
- 18S rRNA
- snRNA-activating protein complex subunit
- Replication factor C subunit 5
Sequence:
MESLLHASSSLVSLRPRIDGRDSFINPSRVCLNPSLGRRGSKPLPLVAAAKKKKSKKDDNHNFSARPDEATGPFPESILLKEKKIDEEGDLLPEFADAEEKELYQFLDLQLQSDLNEERMRHYEVVYLIHEKHAEEVESINQKVQDYLKEKKGKVWRFSDWGMRRLAYKIQKAENAHYILMNFEIEAKYLNEFKGLLDSDERVIRHLVMKRDEAITEDCPPPPEFHSVRAGDEYYDDDEEEEIEEDEDEGEGEDEEDADNIEYEVDDDGNVVMVLYGDEEEGEEEEDGASEQEEGQDKSTNGRRETRRTVNVGG
Protein: Guanine nucleotide-binding protein G(i) subunit alpha-1 (EC 3.6.5.-) (Adenylate cyclase-inhibiting G alpha protein) (P10824)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis. Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity).
Subcellular location: Nucleus. Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:21158412}; Peripheral membrane protein {ECO:0000305|PubMed:24596087, ECO:0000305|PubMed:25037222}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P63096}. Membrane {ECO:0000269|PubMed:26253820}; Lipid-anchor {ECO:0000269|PubMed:26253820}. Note=Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane. {ECO:0000269|PubMed:21158412}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 4
- Lysophosphatidic acid receptor 1
- D
- Adhesion G protein-coupled receptor L3
- Guanine nucleotide-binding protein G
- Chaperone Ric-8A
- Gamma-aminobutyric acid type B receptor subunit 2
- Guanine nucleotide-binding protein subunit gamma
- Mu-type opioid receptor
Sequence:
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Protein: Zcf32p (Q5ANG4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEKKKIRRSRNGCHTCKRSKIKCDENKPTCSYCSKTKAICDYSLKLTWGGRPFKDANKRKQLPSVKKEVQPMLNDFPVMTSTSLSTSITNNSNTKGDTGLTFILHEFNTESIKSPSSPSESVSSHIDPPAPHRNGKRKIIEIDSIADSEIKKRDTHMTLTDITPELNNGIENLTNALIDFGGQQFQLQNSDIFSTYIQNPQRYMGVTQYGSDSDSSATSFLNNYSEDISRIDKYLPNDQSNLIGDTFPMRSLYSSINESPTSVDIWDSIPPSLTPLPTLLLNVPFYRNLMHFWVTVASQNLVPAPSSIYKDNPYKILLTQMAMEYPAILNTLLAFSAKLRSSLIGTDDTPDIVIDQLLSRSCTELLQLLKDESKATSDEALATALLLSCYEVFNSKDFSRHRAHNIGARQIIKARSNTPHKRGPEAGTESDMTFFLMRWFVYTDVIGALSSTTDSHDYLLTSNDLSTYEPLESLTMLHEIDKMEDETQYPKKTIDYLMGFNIKFLPHFTKITILVRETNAHLGKTKASAANLPLEIVYKALEVKEALIETQRKDEESILQSHEKIIELKSGNGQQLYADDLPQETVTLIRENDILRFTNKIFCDAGLIHLYRRVLLIPRESNLVQDLANGIGELAKLHIESRSPADICCIFCLFTAGCEVLCPEMQQFFEQRFQNLGQMGNINARKGLQIMKRCWKTNEDWITAAEKIGVDLTLL
Protein: Lysine--tRNA ligase (EC 2.7.7.-) (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) (Q5XIM7)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages (By similarity). Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19524539, ECO:0000269|PubMed:23159739}. Cytoplasm {ECO:0000250|UniProtKB:Q15046}. Nucleus {ECO:0000269|PubMed:19524539, ECO:0000269|PubMed:23159739}. Cell membrane {ECO:0000250|UniProtKB:Q15046}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15046}. Secreted {ECO:0000250|UniProtKB:Q15046}. Note=Secretion is induced by TNF-alpha (By similarity). Cytosolic in quiescent mast cells. Translocates into the nucleus in response to mast cell activation by immunoglobulin E (PubMed:19524539, PubMed:23159739). {ECO:0000250|UniProtKB:Q15046, ECO:0000269|PubMed:19524539, ECO:0000269|PubMed:23159739}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Glutamine--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
Sequence:
MLMQAAVRLVRGSLRQTSWAEWGQRELRLGQLAPFTTLRKDKPLSDRRSELKRRLKAEKKLAEKEAKQKELSEKQLNQTTAAAATNHTADNGVGAEEETLDPNQYYKIRSQAVQQLKVSGEDPYPHKFHVDISLTQFIQEYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFVHINNKLRRGDIIGVEGNPGKTKKGELSIVPREMTLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMLSGMVRSITGSYKITYHPDGPEGQAYEIDFTPPFRRISMVEELEKVLGVKLPETSLFETEETRKILDDICVARAVECPPPRTTARLLDKLVGEFLEVTCISPTFICDHPQIMSPLAKWHRCKEGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVTMFLTDSNNIKEVLLFPAMKPEDKKETATATETPESTEASPSV
Protein: Serpin family H member 1 (E9PIG2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSLLLLSAFCLLEAALAAEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENILVSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRD
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 3 (A0A090N8Z9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPGLQHPPTVVQRPGMPSGARMPHQGAPMGPPGSPYMGSPAVRPGLAPAGMEPARKRAAPPPGQSQAQSQGQPVPTAPARSRSAKRRKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRVDIQEALKRPMKQKRKLRLYISNTFNPAKPDAEDSDGSIASWELRVEGKLLDDPSKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTPTTQETDGFQVKRPGDLSVRCTLLLMLDYQPPQFKLDPRLARLLGLHTQSRSAIVQALWQYVKTNRLQDSHDKEYINGDKYFQQIFDCPRLKFSEIPQRLTALLLPPDPIVINHVISVDPSDQKKTACYDIDVEVEEPLKGQMSSFLLSTANQQEISALDSKIHETIESINQLKIQRDFMLSFSRDPKGYVQDLLRSQSRDLKVMTDVAGNPEEERRAEFYHQPWSQEAVSRYFYCKIQQRRQELEQSLVVRNT
Protein: Chitin synthase 3 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 3) (Class-IV chitin synthase 3) (J9VXM5)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. Activated by CSR2, it produces chitin that is deacetyled to chitosan, which is required to maintain cell wall integrity. Conversion of chitin to chitosan offers an advantage during infection, as chitosan is less readily detected by host immunosurveillance mechanisms.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25970403}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSRPHLQQNVSFQDTKPPSRRAGRDDIPPRPPTKSDPSKASLTTTTTVQSVGGYNNHQLDFDDNAYVDAGSSNPQGFSDYNGVRRKKSMVRPERERIDPNHRLWHYREHAAEDQVDIQPSSTGNQPYNQYNNQRPGANLRRGKSLLARETDDVDDSSGLNIFKRGATIRRKASRATPRQAPTGAQSNRVSAGQKEDEECCCLGNFAPGPKNCWMIYCYLLTICIPGFVIAKVFGKKTPDAQRAWREKIGIVSIVLYLMGAVGFITFGFTQTVCGDTQLRLPGGSANTGSLVINGYDYDFSTWRHPVAGDTFNGTTSPLYMDQYMAGGMDASFLFQNVNQNCLGLITPASGTGIDHDGDQMGWYFPCNLHDQNGTSAANLTGITDRTNCHVSSYARSNFSAVVPTAEIYYTWDRVKDESRNLAVYKSAVIDMNLLQWLDDTQVSYPEFFNTIKNRNDSYAGKDITALIERAGLSQYARCLTDVIQIGFVDTITIGCIMSELVLYVSLVFILGAVFIKFGMAVVFGWFLSWRMGNFKGESYQERMKRAAEIENWTDDIYRPAPGYLRPNATGTARTGVKKNFLPTTSRFSRAEPMLVSSSRPSTSYGMVGETRRQGSSIYGNKLGPPAHTTPPGSPLLRNSRSSTSLPFRDDSRHSISDRSVNNNVPCPFPLGNVVPQPAPDFEPFGYPLIHSICLVTAYSESIEGLRTTLDSLATTDYPNSHKLILVICDGMVRGSGSKQYTPEIVLGMMKELVTPAEEVEAHSYVAIADGHKRHNMAKVYAGFYAYDSETVEASKQQRVPMVLVSKVGNPLEVNDAKPGNRGKRDSQIVLMSFLQKVMFDERMTTLEYEFFNAVWRCTGIPPDRYETVLCVDADTKVFPDSLTRMNACMVNDHEIMGLCGETKIANKSETWVTMIQVFEYYISHHNTKAFESVFGGVTCLPGCFSMYRIKAPKGERGFWVPILANPDICEHYAENVVDTLHKKNLLLLGEDRYLSTLMLKTFPKRKMVFCPQAVCKTIVPDTFRVLLSQRRRWINSTVHNLCELILVRDLCGTFCFSMQFVVFMDLVGTLVLPAAISFTLYIIMISIIPQSVTGMPRPYVSLVLLAFILGLPGVLIVITSRKIAYVGWMLVYLISLPVWNLILPAYSYWHMDDFTWGETRKIAGEVKEEAHGGKEGTFDSSHIVMKKWAEFERERRWRTGTASRDSQYFDVVQRANSPRSGIPSNRYSIVSTSETFNSGLGTAESNHLFRQSQSFASMSQVAPSPETNYGNVPQLALPPPRGASIGREHSPSSTESGTSNNYAYGSTEEPTASNVDPYYQPFTNEVYQDEAEQPILPSEYTTTSPEPVYQTAPARVRQPSQRGVSLVDTGPVRSAQAAPHDAVRRVSRHQRRSSSKNQLVSPISSGGHTGSLPPGAAPPQY
Protein: Kunitz-type protein bli-5 (Blistered cuticle protein 5) (Kunitz-type protease inhibitor bli-5) (O62247)
Organism: Caenorhabditis elegans
Function: Appears to lack serine protease inhibitor activity in vitro when tested with bovine pancreatic alpha-chymotrypsin and elastase. Involved in cuticle biosynthesis.
Interaction partners:
- Endoprotease bli-4
- peroxidase
Sequence:
MVSIHNSFILLMLMISICFCEKCLTNEECDLKWPDAICVRGRCRCSENTIRKKSASREWVCLATNDATGNSGPPLTCPTPEGAGYQVMYRKDGEPVKCSSKKKPDTCPEGFECIQGLSILGALDGVCCPDRAKTCVHPIFDHPDDGYLSRWGFDGEQCIEFKWNPERPSSANNFKTRAHCEDYCIGSINGITNYHQSNFHLF
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (6PF-2-K/Fru-2,6-P2ase) (PFK/FBPase) (6PF-2-K/Fru-2,6-P2ase liver isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (Q91348)
Organism: Gallus gallus (Chicken)
Function: Synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- 6-phosphofructokinase
- ATP-dependent 6-phosphofructokinase
- Uncharacterized protein.
- Fructose-bisphosphatase 2
- FBPase domain-containing protein
- Uncharacterized protein.
- Uncharacterized protein.
- Hexokinase domain containing 1.
- Mannose-6-phosphate isomerase
- 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2.
Sequence:
MAAVASGQLTQNPLQKVWVPLSLHRLRRRGSTVPQFTNCPTMVILVGLRRPGKTYISRKLTRYLNWIGMPTRVFNVGQYRREAVQSYKNYEFFRHDNEEAMQIRRQCALAALQDVRTYLSSEEGQVAVFDATNTTRERRALIMQFARENGYKVLFVESICDDPAIIEENIKQVKLSSPDYKGCTPEEAVADFLQRIECYKATYEPLDEQLDSGLSYIKIFDVGVRYLANRVQGHVQSRTVYYLMNTHVTPRAIYLSRHGESQLNLKGRIGGDAGLSTRGRQYAQALAEFIRSQSIRELKVWTSHMKRTIETAEALGVPYEQWKALNEIDAGVCEEMTYEEIQERYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSEELPYLRCPLHTVLKLTPVAYGCEVESIFLNVEAVNTHRERPQNVDISRPPAEALVTVPEHY
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial (Complex I-39kD) (CI-39kD) (NADH-ubiquinone oxidoreductase 39 kDa subunit) (Q9DC69)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase 1 beta subcomplex subunit 9
Sequence:
MAAAVRFRVVRALPMSRPAITAAATSVFCGSSHRQLHHAVIPHGKGGRSSVSGVVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDVYDIMHLRLMGDLGQLTFLEWDARDKDSIRKAVQHSNVVINLIGREWETRNFDFEDVFVNIPRAIAQASKEAGVERFIHVSHLNASMKSSSKSLRSKAVGEKEVRSVFPEAIIIRPSDIFGREDRFLNHFANYRWFLAVPLVSLGFKTVKQPVYVADVSKGIVNATKDPDAVGKTFAFTGPNRYLLFHLVKYIFGMTHRTFIPYPLPLFVYSWIGKLFGLSPFEPWTTKDKVERIHISDVMPTDLPGLEDLGVQPTPLELKSIEVLRRHRTYRWLSSEIEETKPAKTVNY
Protein: Sodium/potassium/calcium exchanger 3 (Na(+)/K(+)/Ca(2+)-exchange protein 3) (Solute carrier family 24 member 3) (Q9EPQ0)
Organism: Rattus norvegicus (Rat)
Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9HC58}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
RDLLLSQLCFLASVALLLWSLSSLREQKELDLMDLIGEDRKWMVGRKLMQVNDTLTSEDAGLRSSKNCTEPALHEFPRDIFSNEDRRQGAVVLHVLCAMYMFYALAIVCDDFFVPSLEKICERLHLSEDVAGATFMAAGSSAPELFTSVIGVFITKGDVGVGTIVGSAVFNILCIIGVCGLFAGQVVALSSWCLLRDSIYYTLSVVALIVFIYDEKVSWWESLVLVLMYLIYIIIMKYNACIHQCFERRTKGAGNMVNGLANNAEIDDSSNCDATVVLLKKANFHRKASVIMVDELLSAYPHQLSFSEAGLRIMITSHFPPKTRLSMASRMLINERQRLINSRAYTNGESEVAIKIPIKHTVENGTGPSSAPDRGVNGTRRDDIVAEADNETENENEDENNENDEEEDEDDDEGPYTPFDPPSGKLETVKWAFTWPLSFVLYFTVPNCNKPHWEKWFMVTFASSTLWIAAFSYMMVWMVTIIGYTLGIPDVIMGITFLAAGTSVPDCMASLIVARQGMGDMAVSNSIGSNVFDILIGLGLPWALQTLAVDYGSYIRLNSRGLIYSVGLLLASVFVTVFGVHLNKWQLDKKLGCGCLFLYGVFLCFSIMTEFNVFTFVNLPMCGD
Protein: Aldehyde dehydrogenase [NAD(P)+] 2 (EC 1.2.1.3) (P54114)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Involved in pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
- Catalase T
- Glutamate decarboxylase
- Acyl-coenzyme A oxidase
- NADP-dependent alcohol dehydrogenase 6
- Acetyl-CoA hydrolase
- 4-aminobutyrate aminotransferase
- Polyamine oxidase FMS1
- NADP-dependent alcohol dehydrogenase 7
Sequence:
MPTLYTDIEIPQLKISLKQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPFHSNAKQDLAQIIELTRYYAGAVDKFNMGETIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACRKMQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNVIPGYGSVVGKALGTHMDIDKISFTGSTKVGGSVLEASGQSNLKDITLECGGKSPALVFEDADLDKAIEWVANGIFFNSGQICTANSRVYVQSSIYDKFVEKFKETAKKEWDVAGKFDPFDEKCIVGPVISSTQYDRIKSYIERGKKEEKLDMFQTSEFPIGGAKGYFIPPTIFTDVPETSKLLRDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINQTNQEEAKVPFGGFKMSGIGRESGDTGVDNYLQIKSVHVDLSLDK
Protein: Methyl-CpG binding domain protein 1 (Q66HB8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEAWQDCPALGPGWKRREAFRKSGASCGRSDIYYRSPTGEKIRSKIELTRYLGPACDLTLFDFRQGILCHPVPKTHPLAVPSKKKKKTSKPAKAKKQQVGPQRSEVRKETPREGNKVAPATALLPVTASAPAPVPVPVSAPAPAPAPLCCENCGIHLSWDGIKRERRRTLCKDCRAQRIAFNREQRMFKRVGCGECTACLVKEDCGVCSICCLQLPNDVASGLFCKCEQRRCLRIVEKGKYDHSKRGPRVASRRHSRAPPLPPHAASQHPEPTELHISDQTPTAPAEFVYDCVEEDELKRLLPSIGPGSEEEARLLPHHTHQKRSASTRQLQLSSPLKAPLAVVTTPPGPVQDSGKRQAGSGFVLPQPDTDLVYLQEGTSSLMQVPGPAAASTENPAQETQGSAPGWVVALPQVKQEKADAPEEWTAVTTFLTSSTVQPGFLSKASGLDPPPVKREPPGPEEDGEENKEDDVSESAPAEEIGGIGTPVITEIFSLGGTRLRDAEAWLPRLHKLLAVNENEYFTELQLKEEIL