wanglab/gogpt-training-data huggingface dataset:
Protein: Meiotically up-regulated gene 143 protein (P87133)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C306.11
Sequence:
MIRYSLNGIRLFGSLNLFNATRILPISLGRASYAHARLFTSKVEKSGTAEESALPSVDEEEDKLNSLLGNIKVRTAQEDGVSVEEVLMHHPELLRNAPHALQQSVKEILASKEVGDAFKKN
Protein: Forkhead box protein S1 (Forkhead-like 18 protein) (Forkhead-related transcription factor 10) (FREAC-10) (O43638)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that suppresses transcription from the FASLG, FOXO3 and FOXO4 promoters. May have a role in the organization of the testicular vasculature (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MQQQPLPGPGAPTTEPTKPPYSYIALIAMAIQSSPGQRATLSGIYRYIMGRFAFYRHNRPGWQNSIRHNLSLNECFVKVPRDDRKPGKGSYWTLDPDCHDMFEHGSFLRRRRRFTRQTGAEGTRGPAKARRGPLRATSQDPGVPNATTGRQCSFPPELPDPKGLSFGGLVGAMPASMCPATTDGRPRPPMEPKEISTPKPACPGELPVATSSSSCPAFGFPAGFSEAESFNKAPTPVLSPESGIGSSYQCRLQALNFCMGADPGLEHLLASAAPSPAPPTPPGSLRAPLPLPTDHKEPWVAGGFPVQGGSGYPLGLTPCLYRTPGMFFFE
Protein: Actin-like protein 8 (Cancer/testis antigen 57) (CT57) (Q9H568)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Dynactin subunit 2
- Actin-related protein 10
Sequence:
MAARTVIIDHGSGFLKAGTAGWNEPQMVFPNIVNYLPCKENPGPSYARRRVSLGIDICHPDTFSYPIERGRILNWEGVQYLWSFVLENHRREQEVPPVIITETPLREPADRKKMLEILFELLHVPSVLLADQLQMSLYASGLLTGVVVDSGYGLTRVQPFHQGRPLPASGKTLEFAGQDLSAYLLKSLFKEDCDRRCLFQLETVAVTQMNKCYVPQNLGEALDFRERQQSALDESNTYQLPDGSRVELTPMQRVAPEMFFSPQVFEQPGPSIPRAIVESVESCEISLRPLLVSHVMACGGNTLYPGFTKRLFRELMGDHVSSTKATVWEGSNRNFSVWLGASVVAHLSTYQSEWMSREEYGEHMRM
Protein: Ethanolamine kinase (EK) (EC 2.7.1.82) (Protein easily shocked) (P54352)
Organism: Drosophila melanogaster (Fruit fly)
Function: Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- RE24176p
- FI05338p
- Alanine--glyoxylate aminotransferase 2-like
- GH11618p
- LD22655p
- ethanolamine-phosphate cytidylyltransferase
- diacylglycerol cholinephosphotransferase
- Kazachoc, isoform G
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MGTETKSNSYTGQISTSGGNPKVMKDSLSLVRQTVNQQTLSLSQSNQVQNQLNSHSNSNSYPNPSGSENKNENEQNSRDIRAKPEDKSRKEAIVPFVPIFVEEADVIQGAKELLKVIRPTWDLSHVEFKIRVVPQIEDRYPAQNAMVMMTLYSFTDGITNKLVGCFHKEISKLNDENGGSYLPIKTQGLSPVQSEDPVIIEKEDDDEFTDDRAADDGSPVQYSDNVVLVRIYGNKTDLLIDRKAETQNFLLLHTYGLAPSLYATFKNGLVYEYVPGTTLNTDSVLCPEIWPLVARRMAEMHRKVRKHGDSSATKPMPMIWKKTQSFLDLVPERFSDAEKHKRVKETFLPIGRLREEFNKLYEYLEALDSPIVFSHNDLLLGNVIYTQSLNTVNFIDYEYADYNFQAFDIGNHFAEMCGVDEVDYSRYPKREFQLQWLRVYLEEYLQRSNIQNDEVELLYVQVNQFALASHIFWTVWSLLQAEHSTIDFDYVGYAFLRYNEYLARKVEFLSLTAAKNNK
Protein: Photoactivated adenylate cyclase subunit beta-like protein FB (P84741)
Organism: Euglena gracilis
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:16121285}. Note=Paraxonemal body. And paraxonemal bodies (PABs).
Interaction partners:
Sequence:
MYILVWKKGQQIKTFHTLDEAAQFKAASNIDEAQMFSVTVAPAISASGGSNEATNLRRLMYLSKSTNPEECNPQFLAEMARVATIRNREIGVSGFLMYSSPFSFQVIEGTDEDLDFLFAKISADPRHERCIVLANGPCTGRMYGDWHMKDSHMDSITTHPAMKTILYQIARSFSSMWSYLPKSAGNMLLLGKDPAAQPPEPMSVVVTFIYLVEFGSILSNPNLTDQAAEVLSTFVDVCVKNVEGSGGNIAKFITGICMAYWPINRTEEALTAIQQISEDLAQLRSQQAPGSAVSLMYSQAGVHYGRPMLCNAGRRKSDFTLLGDCINTTSRIATLAKKFKTPLLFSQEVRCLLRDEMREEIVGAGMHQVKGRDKPVVVYQFPGPELDVEMVRQKIEQFTPGRFRCQMPVVEYEGLPNSQRPPIFDDTPKANRRPRTPGYGGRQRSDSQVDRPIMIAKLAGPSVSATGDTTLTTLTYISQATRPMSRQDLSAIMRTATRRNAQQSITGTLLHVNGLFVQTLEGPKDAVANLYLRVRQDPRQTDVTTVHMAPLQERVYPSEWTLTSATAEMLATFPPLQDVLAQLAKSFTSLETYVPSTVVRHLTAGNNPRNLMPVSCGVVMLATDICSFTSLTEKSSLTEVWMICNTFIDACTSAICQDGREVIKLIGDCVTAYSPGNNADSAVAAAQELFTFCRQLREAFVDVLDVRGCVSCGVGLEYGQVVMAQCGSMGLTEYVVAGAVSARVMEVEAITREVGYAIVVTEPVADRLSPQLRDHGIVPTPQAIEGLPCYGIAGEEFELDVDSIKRGIKALHAARSGEKPLTEPEAAKPDFRVSPGRVRHGDSGRRSNSAQGKRSIQVR
Protein: poly(A)-specific ribonuclease (EC 3.1.13.4) (Q8I0I5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPSAISGAPHAHIPSNEECGIRDVWKQNLEEEFRTIRKVVQKYHYVAMDTEFPGVVARPVGEFRSTADYHYQLLRCNVDLLRIIQLGLTFMDDDGKTPPGYSTWQFNFKFNLSEDMYAQDSIDLLQNSGIQFKKHEEDGIDPIDFAELLMSSGIVLVENIKWLCFHSGYDFGYLLKLLTDQNLPPDESEFFDLLHIYFPNIFDIKYLMKSCKNLKGGLQEVADQLELRRVGPQHQAGSDALLTGMAFFKMREMFFEDNIDHAKYSGHLYGLGTSFIVNGTNFHDSNGETNSAS
Protein: Iodotyrosine deiodinase (EC 1.21.1.1) (Halotyrosine dehalogenase) (T2MBC4)
Organism: Hydra vulgaris (Hydra) (Hydra attenuata)
Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine. Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MFDNLSGVSYGLLAGILAMLIHLVYQKITELKRRKDELKERESHPTDDLFPKEDFIPYHPSRYSEEEMIKRSNDFYLSMNARRSVRFFSNEDVPDEVIDNIIRTAGTSPSGAHTEPWTFVVIKNKLLKAKVREIIEEEEELNYKQRMGQKWVDDLKPLKTNWIKEYLTEAPYLILVFKQTYGITEDGQKKTHYYNEISASISCGFLLAAIQNAGLVALTSTPLNAGSKLRNLVGRGPNEKIVILLPVGYPSKNCQVPNLKRKPLNEIMIKFD
Protein: Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (A0A8I6G8H1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365053}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365053}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000256|RuleBase:RU365053}.
Interaction partners:
Sequence:
MAYRGQGQKVQKVMVQPINLIFRYLQNGFDEYMNLVLDDAEEIHSKTKSRKQLGRIMLKGDNITLLQSVSN
Protein: Securin (Pituitary tumor-transforming gene 1 protein) (P97613)
Organism: Rattus norvegicus (Rat)
Function: Regulatory protein, which plays a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESPL1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESPL1. Its function is however not limited to a blocking activity, since it is required to activate ESPL1. Negatively regulates the transcriptional activity and related apoptosis activity of p53/TP53. The negative regulation of p53/TP53 may explain the strong transforming capability of the protein when it is overexpressed. May also play a role in DNA repair via its interaction with Ku, possibly by connecting DNA damage-response pathways with sister chromatid separation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 20 homolog
- separase
- Cell division cycle protein 27 homolog
- Ubiquitin-conjugating enzyme E2 C
- G2/mitotic-specific cyclin-B1
- Anaphase-promoting complex subunit 11
- Fizzy-related protein homolog
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK1
- Aurora kinase A
Sequence:
MATLIFVDKDNEEPGSRLASKDGLKLGSGVKALDGKLQVSTPRVGKVFGAPGLPKASRKALGTVNRVTEKPVKSSKPLQSKQPTLSVKKITEKSTKTQGSAPAPDDAYPEIEKFFPFDPLDFESFDLPEEHQISLLPLNGVPLMILNEERGLEKLLHLDPPSPLQKPFLPWESDPLPSPPSALSALDVELPPVCYDADI
Protein: WAT1-related protein At2g39510 (O80638)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein GLUTAMINE DUMPER 1
- Lysine histidine transporter 1
- Amino acid permease 3
- Amino acid permease 8
- Amino acid permease 5
- Peptide transporter family protein
- Amino acid permease 1
- Uncharacterized protein At5g19190
- Cationic amino acid transporter 6
- At5g43870)
Sequence:
MALKTWKPFITVVSLQFGYAGLSIIAKFALNQGMSPHVLASYRHIVATIFIAPFAYFLDRKIRPKMTLSIFFKILLLGLLEPTIDQNLYYTGMKYTSATFTAAMTNVLPAFAFIMAWIFRLEKVNVKKIHSQAKILGTIVTVGGAMLMTVVKGPLIPLPWANPHDIHQDSSNTGVKQDLTKGASLIAIGCICWAGFINLQAITLKSYPVELSLTAYICFLGSIESTIVALFIERGNPSAWAIHLDSKLLAAVYGGVICSGIGYYVQGVIMKTRGPVFVTAFNPLSMVIVAILGSIILAEVMFLGRILGAIVIVLGLYSVLWGKSKDEPSSSFSDMDKELPLSTPQIVLPSKANAKMDTNDASVVISRPNTNESV
Protein: Guanine nucleotide-binding protein G(i) subunit alpha-1 (EC 3.6.5.-) (Adenylate cyclase-inhibiting G alpha protein) (P63096)
Organism: Homo sapiens (Human)
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 (By similarity). 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.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:26766442}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm, cell cortex {ECO:0000269|PubMed:22327364}. Membrane {ECO:0000250|UniProtKB:P10824}; Lipid-anchor {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805}. Note=Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody (PubMed:17635935). Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane. {ECO:0000250|UniProtKB:P10824, ECO:0000269|PubMed:17635935}.
Interaction partners:
- Guanine nucleotide-binding protein G
- D
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 1
- Regulator of G-protein signaling 14
- Cannabinoid receptor 1
- Prostaglandin E2 receptor EP3 subtype
- Sphingosine 1-phosphate receptor 1
- Mu-type opioid receptor
- Gamma-aminobutyric acid type B receptor subunit 2
Sequence:
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Protein: Haptoglobin-related protein (P00739)
Organism: Homo sapiens (Human)
Function: Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron.
Subcellular location: Secreted {ECO:0000269|PubMed:16778136}. Note=Secreted into blood plasma and associated with subtypes of high density lipoproteins (HDL). {ECO:0000269|PubMed:16778136}.
Interaction partners:
- Apolipoprotein L1
- Apolipoprotein A-I
- Haptoglobin
- Serum paraoxonase/arylesterase 1
- Hemoglobin subunit alpha
- Hemoglobin subunit beta
- Apolipoprotein A-II
- Beta-2-glycoprotein 1
- Scavenger receptor cysteine-rich type 1 protein M130
- Apolipoprotein C-I
Sequence:
MSDLGAVISLLLWGRQLFALYSGNDVTDISDDRFPKPPEIANGYVEHLFRYQCKNYYRLRTEGDGVYTLNDKKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQVDIGLIKLKQKVLVNERVMPICLPSKNYAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEGSTCPKWKAPKSPVGVQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDLEEDTWYAAGILSFDKSCAVAEYGVYVKVTSIQHWVQKTIAEN
Protein: Arogenate dehydratase 2 (PhADT2) (EC 4.2.1.91) (Prephenate dehydratase ADT3) (EC 4.2.1.51) (D3U716)
Organism: Petunia hybrida (Petunia)
Function: Converts the prephenate and L-arogenate produced from the shikimate-chorismate pathway into 3-phenylpyruvate and phenylalanine (Phe), respectively. Involved in floral volatile benzenoids and phenylpropanoids (FVBP) production (By similarity).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:20215586}.
Interaction partners:
Sequence:
MAATTTLRSPKIPHPPPESTPSNLSYLSQISLTPVPKRRRFISIYACSNAESNSQFGSEIKKSQAIELNKVSDEHPYEFNSKDSPNPLPRPLTSADLSNMATEGSRLRVAYQGVRGAYSESAAEKAYPNCEAVPCEQFDTAFEAVERWLVDRAVLPIENSLGGSIHRNYDLLLRHRLHIVGEVKLAIRHCLLANNGVKIEDLKRVLSHPQALAQCENNLTKLGLVREAVDDTAGAAKYIAFQQLKDAGAVASLAAARIYGLNVLAQDIQDDSDNVTRFLMLAREPIIPGTDKPFKTSVVFSLDEGPGVLFKALAVFAMRNINLTKIESRPLQKQALRVLDDSADGFPKYFPYLFYVDFEASMADQRAQNALGHLKEFATFLRVLGSYPSDSGIA
Protein: Adenine deaminase (ADE) (EC 3.5.4.2) (Adenine aminohydrolase) (AAH) (P53909)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. Also exhibits a low activity towards N(6)-substituted adenines that are commonly known as the plant hormones cytokinins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03145, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03145, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Adenosine kinase
- Adenine phosphoribosyltransferase 1
- Purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase 2
- SCF-associated factor 1
- IMP-specific 5'-nucleotidase 1
- AMP deaminase
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenylosuccinate lyase
- Adenylosuccinate synthetase
Sequence:
MVSVEFLQELPKCEHHLHLEGTLEPDLLFPLAKRNDIILPEGFPKSVEELNEKYKKFRDLQDFLDYYYIGTNVLISEQDFFDLAWAYFKKVHKQGLVHAEVFYDPQSHTSRGISIETVTKGFQRACDKAFSEFGITSKLIMCLLRHIEPEECLKTIEEATPFIKDGTISALGLDSAEKPFPPHLFVECYGKAASLNKDLKLTAHAGEEGPAQFVSDALDLLQVTRIDHGINSQYDEELLDRLSRDQTMLTICPLSNVKLQVVQSVSELPLQKFLDRDVPFSLNSDDPAYFGGYILDVYTQVSKDFPHWDHETWGRIAKNAIKGSWCDDKRKNGLLSRVDEVVTKYSH
Protein: Probable integral membrane protein (O06540)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MPRDYTAPRWAHAWAGEPRPARWHPANQPAHPDHSNRESPACMSQSTTPYRSSVLAEFRRAITNVAVPHHEPPGIVRRRRVVVGVTLVIGAVMLGFSLRRTPGESSFYWLTLALAAVWIAGALMSGPLHLGGICWRGRNQRPVITGTTVGLLLAGIFGVGAMIVRAIPGAAEPIARVLQFAHQGTLLPILLITLINGIAEEMFFRGALYTALGRRYPVTISTVLYVGATMASANLMLGFAAIFVGTVCALERRASGGVLAPILTHFVWGLIMVFALPPLFAV
Protein: Endolysin PlyC, large catalytic subunit (PlyCA) (EC 3.2.1.-) (EC 3.5.1.28) (Q7Y3F1)
Organism: Streptococcus phage C1
Interaction partners:
Sequence:
MSKKYTQQQYEKYLAQPANNTFGLSPQQVADWFMGQAGARPVINSYGVNASNLVSTYIPKMQEYGVSYTLFLMYTVFEGGGAGNWINHYMYDTGSNGLECLEHDLQYIHGVWETYFPPALSAPECYPATEDNAGALDRFYQSLPGRTWGDVMIPSTMAGNAWVWAYNYCVNNQGAAPLVYFGNPYDSQIDSLLAMGADPFTGGSITGDGKNPSVGTGNATVSASSEANREKLKKALTDLFNNNLEHLSGEFYGNQVLNAMKYGTILKCDLTDDGLNAILQLIADVNLQTNPNPDKPTVQSPGQNDLGSGSDRVAANLANAQAQVGKYIGDGQCYAWVGWWSARVCGYSISYSTGDPMLPLIGDGMNAHSIHLGWDWSIANTGIVNYPVGTVGRKEDLRVGAIWCATAFSGAPFYTGQYGHTGIIESWSDTTVTVLEQNILGSPVIRSTYDLNTFLSTLTGLITFK
Protein: Mitochondrial RNA binding complex 1 subunit (Q57ZC9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- p22 protein
- RNA-editing ligase 1, mitochondrial
Sequence:
MRTQGSFGREGGNFRRGDGRSGGRGFGGGGGGGSGKPPTDAPQRRALINQTFDGELSEGTRVVMRDDTKVLMSVIKHIPQNGAITIKSLNAQLSPDVQEAVSEKHSGLKSFLEQRKQLFVVKANPSDGVLYVAATPLAYQKLTARERQRETMQEMLGLTRRGGRGRGGRPMNGGGGGFRGRNGAGGGRGGGGRGRGGGGGGEDRGRNDRGGGGGGGFRGGRGNGGRDSGRMGRGEERGFGGQYRR
Protein: Anaphase-promoting complex subunit 2 (Q12440)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit CDC23
- Anaphase-promoting complex subunit CDC26
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit DOC1
Sequence:
MSFQITPTRDLKVITDELQTLSSYIFHTNIVDDLNSLLTWMSPNDAKSNHQLRPPSLRIKNIIKVLFPNNATTSPYSMINTSQANNSIVNEGNTNKELQLQLFSTLKEFYIFQVRYHFFLHFNNINYLKDIQRWENYYEFPLRYVPIFDVNVNDWALELNSLRHYLLNRNIKFKNNLRTRLDKLIMDDDFDLADNLIQWLKSANGSLSSTELIVNALYSKINKFCEDNMSRVWNKRFMIMETFNKFINQYWSQFSKLVGCPEDDHELTTTVFNCFESNFLRIRTNEIFDICVLAYPDSKVTLLELRKIMKDFKDYTNIVTTFLSDFKKYILNPSVTTVDALLRYVKTIKAFLVLDPTGRCLHSITTFVKPYFQERKHLVNVLLYAMLDLPEEELKEKINFNVDMKALLSLVDTLHDSDINQDTNITKRDKNKKSPFLWNLKVKGKRELNKDLPIRHAMLYEHILNYYIAWVPEPNDMIPGNIKSSYIKTNLFEVLLDLFESREFFISEFRNLLTDRLFTLKFYTLDEKWTRCLKLIREKIVKFTETSHSNYITNGILGLLETTAPAADADQSNLNSIDVMLWDIKCSEELCRKMHEVAGLDPIIFPKFISLLYWKYNCDTQGSNDLAFHLPIDLERELQKYSDIYSQLKPGRKLQLCKDKGKVEIQLAFKDGRKLVLDVSLEQCSVINQFDSPNDEPICLSLEQLSESLNIAPPRLTHLLDFWIQKGVLLKENGTYSVIEHSEMDFDQAQKTAPMEIENSNYELHNDSEIERKYELTLQRSLPFIEGMLTNLGAMKLHKIHSFLKITVPKDWGYNRITLQQLEGYLNTLADEGRLKYIANGSYEIVKNGHKNS
Protein: LEM3 (Ligand-effect modulator 3) family / CDC50 family (Q38DJ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSFGRLLKQQRLPAWQLNLTPRIVCVILWTIAFICIPLGIFVEFCNRNAKEASFRYDNEPTKCTEETFSLIGGQGTGKRTVCETHFEFVLAETLRQPVYFYYGLTKMYQNHRRYTNSRSGKQLMGADVRSETDANPFVIPGDTMDNTNKPIEFGGRNHTYKDFVYVPVGLVAWSMFNDTFTLFRKEKNGSNPGEVLICNGTDFSRHTNKPLHRSVSHNHCDKNGIAWESDIKKKFLEPKWDGSGPVWTAPRSEYGKPSIESNDTYFNNGWYAGEEGHMIPVVTDEDFMVWMRASPLPNVRKLYRIIRTDLRAGKYVMKIRQNYNTKPYGGEKSFIFLQPSMLGGKLTSLSITYFAVGGLALIFTVLVLFASHVWGHHSFAVVERLLTK
Protein: SH2 domain containing 4A (H0YAT1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LLAELSEEQKQILFFKMREEQIRRWKEREAAMERKESLPVKPRPKKENGKSVHWKLGADKEVWVWVMGEHHLDKPYDVLCNEIIAERARLKAEQEAEEPRKTHSEEFTNSLKTKSQYHDLQAPDNQQTKDIWKKVAEKEELEQGSRPAPTLEEEKIRKKESMKKKQDEEINQIEEERTKQICKSWKEDS
Protein: Acyl-CoA thioester hydrolase YciA (EC 3.1.2.-) (Protein P14) (P0A8Z0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of the thioester bond in palmitoyl-CoA and malonyl-CoA.
Interaction partners:
- UPF0259 membrane protein YciC
- Acyl-CoA thioesterase 2
- Long-chain acyl-CoA thioesterase FadM
- 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
- Acyl-CoA thioester hydrolase YbgC
- Inner membrane-spanning protein YciB
- Thioesterase 1/protease 1/lysophospholipase L1
- Acyl-coenzyme A thioesterase PaaI
Sequence:
MSTTHNVPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTTSVSINIEVWVKKVASEPIGQRYKATEALFKYVAVDPEGKPRALPVE
Protein: Calpain 5 (F1MQD1)
Organism: Bos taurus (Bovine)
Interaction partners:
- Calpain small subunit 1
- Calpastatin
Sequence:
MFSCVKPYENQNYSALKRACLRRKVLFEDPNFPATDDSLYYKGSPGPTVRWKRPKDICEDPRLFVDGISSHDLHQGQVGNCWFVAACSSLASRESLWQKVIPDWKEQEWDPEKPNAYAGIFHFHFWRFGEWVDVVIDDRLPTVNNQLIYCHSSSRNEFWCALVEKAYAKLAGCYQALDGGNTADALVDFTGGVSEPIDLTEGDFANDEAKRNQLFERVLKVHSRGGLISASIKAVTAADMEARLACGLVKGHAYAITDVRKVRLGHGLLAFFKSEKLDMIRLRNPWGEREWNGPWSDTSEEWQKVSKSEREKLGVTVQDDGEFWMTFEDLCRYFTDIIKCRLINTSYLSIHKTWEEARLRGAWTRHEDPLQNRSGGCINHKDSFFQNPQYIFDVKKPEDEVLISIQQRPKQSTRRDGKGENLAIGFDIYKVEENRQYRMHSLQHRAASSIYINSRSVFLRTEQPEGRYVIIPTTFEPGHTGEFLLRVFTDVPSNCRELRLDEPPRTCWSSLCGYPQQVTQVHVLGAAGLKDSPTGANSYVIIKCEGDKVRSAVQKGTSTPEYDVKGVFYRKKPSQPITVQIWNHRVLKDEFLGQVHLKANADDLQALHTLHLRDRNSRQPSDLPGTVAVRVLSSASLTAV
Protein: Iron transport multicopper oxidase FET3 (G8B5Q0)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Iron transporter FTH1
- FTR1
- Iron transporter FTH1
- Plasma membrane iron permease
- P-type Cu
Sequence:
MKSFISLIFLTILALVTAETHTWYYTANWVDGLNPDGVKERRMIGWNDTWPLPTLRVKKGDRVNLYLTNGFDDRNTSLHFHGMFQRGTNQMDGPEMVTQCPIPPGETMLYNFTVDEQVGSYWYHSHTSGQYGDGMRGVFIIEEPSKDDYPYDYDEEVVLTLNEHYHEESEDLMPKFLSRFNPTGAELIPQNILFNETRNETWKVEPNKTYLLRIINMGRFLSHYVWMEDHDMTIVEVDGVYVEKNTTNLIYITVAQRYTVLVTTKNSTDKNYAFMHRLDPDMLDTQPSDLELNGTNTIMYNEKLGKAEPYDLTQDELDDYFDDFFLVPLNKEKLYDDADYTITIQVQMDNLGDGINYAFFNNITYTKPRVPTLLTVLSAGDEATNELIYGTNTNTFVLQKDDVVDIVLNNLDTGKHPFHLHGHIFQLIERHEAIDDDDDPVAYNASDHAEWPEYPMMRDTVFLQPQSYMVLRFKADNPGVWFFHCHIEWHLDQGLAIQLIEDPMGIQNNSTQQITDNHKQICEKVGVPWEGNAAGNKENVLDLKGENLQHKRLPTGFTARGIVALVFSCVAGVLGLAAIAFYGMQDINNVEERVARDLDVDLDEEDESGAEIVRQTSSTEGSSTHKH
Protein: cyclin-dependent kinase (EC 2.7.11.22) (C8V2V9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MSTSKSRWADEDPETEALIAQRKREKEEKRRAKAEKQRLEEQAKAQAAAERQAGDSRLNGDPSEAPPKKRRRLSNEQQPGSSGEQAAKQGKPTTLLQFPALEWGPCRHVDNFERLNHIEEGSYGWVSRAKELTTGEVVALKKLKLDNSPDGFPVTGLREIQTLLEARHQNVVYLREVVMGNKMDEVYLVMDFLEHDLKTLLDDMREPFLPSETKTLLLQFISGLDFLHSQWIMHRDLKTSNLLLNNRGELKIADFGMARYYGDPPPKLTQLVVTLWYRSPELLLGAESYGPEVDMWSVGCIFGELLTKEPLLQGKNEVDQVSKIFALTGPPTPQNWPGFRSLPNAKSLRIPPTQTSSTLLPRSKFPFLTNAGLQLLSSLLALNPTSRPTAAKCLSHPYFREDPRPKPKEMFPTFPSKAGMERRRRRETPEAPKRGQEAPKLDFASVFGGQSAGDYGESGAGFTLRLG