wanglab/gogpt-training-data huggingface dataset:
Protein: Hexaprenyl pyrophosphate synthase, mitochondrial (HPS) (EC 2.5.1.-) (P18900)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Assembly of polyisoprenoid side chains. The polyprenyl synthase of coenzyme Q biosynthesis catalyzes the formation from isopentenyl diphosphate of all trans-polyprenyl pyrophosphates generally ranging in length of between 6 and 10 isoprene units depending on the species.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Interaction partners:
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein COQ4, mitochondrial
- Atypical kinase COQ8, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Farnesyl pyrophosphate synthase
- Squalene synthase ERG9
- Ubiquinone biosynthesis protein COQ9
Sequence:
MFQRSGAAHHIKLISSRRCRFKSSFAVALNAASKLVTPKILWNNPISLVSKEMNTLAKNIVALIGSGHPVLNKVTSYYFETEGKKVRPLLVLLLSRALSEIPMTERNHLKIDKSDVPEDPIYSKPSQNQLFQRPASSISPLHILHGIKPLNPLTKGPEPLPEETFDKQRGILPKQRRLAEIVEMIHTASLLHDDVIDHSDTRRGRPSGNAAFTNKMAVLAGDFLLGRATVSISRLHNPEVVELMSNSIANLVEGEFMQLKNTSIDADIDTIENGHKLLPVPSKKLEVKEHDFRVPSRQQGLQLSHDQIIETAFEYYIHKTYLKTAALISKSCRCAAILSGASPAVIDECYDFGRNLGICFQLVDDMLDFTVSGKDLGKPSGADLKLGIATAPVLFAWKEDPSLGPLISRNFSERGDVEKTIDSVRLHNGIAKTKILAEEYRDKALQNLRDSLPESDARSALEFLTNSILTRRK
Protein: Proline-rich protein 9-1 (O35328)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
FFFSRCFLLRFRPGPVPYSLPPLSDFSRYSSRSEPNSSSLSSFFRFLGLPGLFSFCFLGPRFRFFTPNAEGSSRISSLSGGGGGGSGGGGGGKRWQLGGLWRSRLRSCPARARVLPLRPPPHRPRRPPPPPPPPRRPLLPPLLPPPTPPSPPPPPPRPSEGKPSCGSGR
Protein: Protein FAM219B (Q5XKK7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATAEPSGRALRLSTPGPRPSGARDRAPGAAGPPSGQIGNRALRLGERTPAAVEKRGPYMVTRAPSIQAKLQKHRDLAKAVLRRKGMLGASPNRPDSSGKRSVKFNKGYTALSQSPDENLVSLDSDSDGELGSRYSSGYSSAEQVNQDVSRQLLQDGYHLDEIPDDEDLDLIPPKPMASSTCSCCWCCLGDSSSCTLQ
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (O15648)
Organism: Trypanosoma brucei brucei
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Glycosome {ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:2940090}.
Interaction partners:
Sequence:
MAVESRSRVTSKLVKAHRAMLNSVTQEDLKVDRLPGADYPNPSKKYSSRTEFRDKTDYIMYNPRPRDEPSSENPVSVSPLLCELAAARSRIHFNPTETTIGIVTCGGICPGLNDVIRSITLTGINVYNVKRVIGFRFGYWGLSKKGSQTAIELHRGRVTNIHHYGGTILGSSRGPQDPKEMVDTLERLGVNILFTVGGDGTQRGALVISQEAKRRGVDISVFGVPKTIDNDLSFSHRTFGFQTAVEKAVQAIRAAYAEAVSANYGVGVVKLMGRDSGFIAAQAAVASAQANICLVPENPISEQEVMSLLERRFCHSRSCVIIVAEGFGQDWGRGSGGYDASGNKKLIDIGVILTEKVKAFLKANKSRYPDSTVKYIDPSYMIRACPPSANDALFCATLATLAVHEAMAGATGCIIAMRHNNYILVPIKVATSVRRVLDLRGQLWRQVREITVDLGSDVRLARKLEIRRELEAINRNRDRLHEELAKL
Protein: IF rod domain-containing protein (Q382P4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calmodulin, putative
- ODAD1 central coiled coil region domain-containing protein
- BRCT domain-containing protein
- Uncharacterized protein
- Dynein assembly factor 3, axonemal
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
- BTB domain-containing protein
Sequence:
MEVNIPEEGTMAGSDQPSILTIAPLFAVGDDGEFLSGLEEFQWRQDSFPQVAPDDIVAYEYIERSSGMWRCSLGIVCSDVVCRSLYIEPLVPSDQEGGACPLTKALAAVTTEEGRELLLRIPPLQSQLIQHRDEAVRLSQERAKLYRELSMKNLDVATKKREAEMQLRHACHVVRQVDARHWRELVSYRTPPDIVVRVMGLVMVLLGERRRTWSEMQPFLHRAGILQVLMQFDPLTISKECHDELVSQYTNSLNFTYEEALKGSHALGSVQQWVVANMRMICVNWHEHHLRDVQQSGEDATHLQHRVEQVRKRLDVITREIRSLWNNYERLENTDHRGVACSRWKSPSRYGARAPRMDHVHPSERACTPPRAYDEFVSVERFAAKTWVRSLTRQHQRILHSSVLCTIGRSQRSQDTVDLTSDQYARLCNLFTTVLCRNGSPGSGLHRPSPRSSPSARSTIRTSTPYRARYIHQGESSSPVHDSAKRDEGKITRSQWGHLDKSPLQVRHHRLRNEDSPQQSSCADADSKRQRMQPIAQSHKDVNQTRDSSRQLHSITKNCEEKIRQSGNTSTAIFHTAQCDEQMSQNHLQDKKKNEKQEMNREKLEASLKGEMRGLNEQLSEMTGSMTLLEKELKKQLNKVTESRALMEKELKELRKQLSDVTDSKSSLEKELKELRKQPSDVAGSKSSLEKELKELRKQLSDVADSKSSLEKELRKQLSDVAGSKSSLEKELKELRKQPSDVADSKSSLEKELKELRKQPSDVTGSKSSLEKELKELRKQLSDVADSKSSLEKELRKQLSDVAGSKSSLEKEPDELKKQLSDVAGSKSSLEKELRKQLSDVAGSKSSLEKELKELRKQLSDVAGSKSSLEKELRKQLSDVAGSKSSLEKELKELRKQLSDVADSKSSLEKELRKQLSDVAGSKSSLEKELKELRKQLSDVADSKSSLEKELKELRKQLSDVAGSKSSLEKELKELRKQLSDVADSKSSLEKELKELRKQLSDVAGSKSSLEKELKELRKQLSDVADSKSSLEKEPDELRKQLSDVAGSKSSLEKELKELRKQPSDVADSKSSLEKELRKQLSDVTGSKSSLEKELKELRKQLSDVAGSKSSLEKELGKQPSDVAGSKSSLEKELKELKKQLSDVAGSKSSLEKELKELKKQLSDVTGSKSSLEKELKELRKQLSDVAGSKSSLEKELKELKKQLSDVTGSKSSLEKELKELRKQLSDVTGSKSSLEKELKELRKQLSDVAGSKSSLEKELGKQLSDVADSKSSLEKELKELRKQLSDVAGSKSSLERRN
Protein: WAP four-disulfide core domain protein 2 (Epididymal secretory protein E4) (Major epididymis-specific protein E4) (Putative protease inhibitor WAP5) (Q14508)
Organism: Homo sapiens (Human)
Function: Broad range protease inhibitor.
Subcellular location: Secreted {ECO:0000269|PubMed:15781627, ECO:0000269|PubMed:23139753}.
Interaction partners:
Sequence:
MPACRLGPLAAALLLSLLLFGFTLVSGTGAEKTGVCPELQADQNCTQECVSDSECADNLKCCSAGCATFCSLPNDKEGSCPQVNINFPQLGLCRDQCQVDSQCPGQMKCCRNGCGKVSCVTPNF
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-2) (Phospholipase C-beta-2) (PLC-beta-2) (A3KGF7)
Organism: Mus musculus (Mouse)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-15
- Guanine nucleotide-binding protein G
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Guanine nucleotide-binding protein G
Sequence:
MSLLNPVLLPPNVKAYLSQGERFIKWDDETSIASPVILRVDPKGYYLYWTYQNQEMEFLDVTSIRDTRFGKFAKIPKSQKLREVFNMDFPDNHFLLKTLTVVSGPDMVDLTFYNFVSYKENVGKDWAEDVLALAKHPMTVNAPRSTFLDKILVKLKMQLNPEGKIPVKNFFQMFPADRKRVEAALGACHLAKGKNDAINPEDFPESVYKSFLMSLCPRPEIDEIFTSYHSKAKPYMTKEHLTKFINQKQRDPRLNSLLFPPARPEQVQVLIDKYEPSGINVQRGQLSPEGMVWFLCGPENSVLAHDTLLIHQDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDCWKGKPPDEEPIITHGFTMTTDILFKEAIEAIAESAFKTSPYPVILSFENHVDSPRQQAKMAEYCRSMFGETLLTDPLENFPLKPGIPLPSPEDLRGKILIKNKKNQFSGPASPSKKPGGVAEGSLPSSVPVEEDTGWTAEDRTEVEEEEVVEEEEEEESGNLDEEEIKKMQSDEGTAGLEVTAYEEMSSLVNYIQPTKFISFEFSAQKNRSYVVSSFTELKAYELLSKASMQFVDYNKRQMSRVYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMALFEFNGQSGYLLKHEFMRRLDKQFNPFSVDRIDVVVATTLSITIISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSPTANSINPVWKEEPFIFEKILMPELASLRIAVMEEGSKFLGHRIIPINALHSGYHHLCLRSESNMALTMPALFVFLEMKDYIPDTWADLTVALANPIKYFNAQDKKSVKLKGVTGSLPEKLFSGTPVASQSNGAPVSAGNGSTAPGTKATGEEATKEVTEPQTASLEELRELKGVVKLQRRHEKELRELERRGARRWEELLQRGAAQLAELQTQAAGCKLRPGKGSRKKRTLPCEETVVAPSEPHDRADPRVQELKDRLEQELQQQGEEQYRSVLKRKEQHVTEQIAKMMELAREKQAAELKTFKETSETDTKEMKKKLEAKRLERIQAMTKVTTDKVAQERLKREINNSHIQEVVQAVKQMTETLERHQEKLEERQTACLEQIQAMEKQFQEKALAEYEAKMKGLEAEVKESVRAYFKDCFPTEAEDKPERSCEASEESCPQEPLVSKADTQESRL
Protein: DUF4298 domain-containing protein (Q99XU0)
Organism: Streptococcus pyogenes serotype M1
Interaction partners:
Sequence:
MTKQDQLIVEKMEQTYEAFSPKLANLIEALDAFKEHYEEYATLRNFYSSDEWFRLANQPWDDIPCGVLSEDLLFDMIGDHNQLLADILDLAPIMYKHM
Protein: Interleukin-13 (IL-13) (T-cell activation protein P600) (P42203)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that plays important roles in allergic inflammation and immune response to parasite infection. Synergizes with IL2 in regulating interferon-gamma synthesis. Stimulates B-cell proliferation, and activation of eosinophils, basophils, and mast cells (By similarity). Plays an important role in controlling IL33 activity by modulating the production of transmembrane and soluble forms of interleukin-1 receptor-like 1/IL1RL1 (By similarity). Displays the capacity to antagonize Th1-driven proinflammatory immune response and downregulates synthesis of many proinflammatory cytokines including IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially involves suppression of NF-kappa-B. Functions also on nonhematopoietic cells, including endothelial cells where it induces vascular cell adhesion protein 1/VCAM1, which is important in the recruitment of eosinophils. Exerts its biological effects through its receptors which comprises the IL4R chain and the IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of STAT6. Aside from IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for IL13 and mediates internalization and depletion of extracellular IL13 (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Interleukin-13 receptor subunit alpha-2
- Interleukin-4 receptor subunit alpha
- Interleukin-13 receptor subunit alpha-1
- Interleukin-4
- Interleukin-5
- T-cell surface glycoprotein CD4
- Interleukin-33
- Interleukin-2
- Granulocyte-macrophage colony-stimulating factor
- Interleukin 9
Sequence:
MALWVTAVLALACLGGLATPGPVRRSTSPPVALRELIEELSNITQDQKTSLCNSSMVWSVDLTAGGFCAALESLTNISSCNAIHRTQRILNGLCNQKASDVASSPPDTKIEVAQFISKLLNYSKQLFRYGH
Protein: Glutamate NMDA receptor subunit epsilon-1, putative (DUF3598) (F4J2Z0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MMCKKLCVLTKFIHIFIDAHWYCCFLYNVSRSNGFCSALPVFVFVLFRLYIKQPTSATSVSEEEEEEPEWVEYKIKETNMFTVDKYQQIGFFPKERAFSLRYQTAGMLDTTLRQGVLGEDDTGEESPRNLKLPSRRPSLVCENCLYSKEIDRRARAFHIMDPKGVLEMLIVFLEERGLENLAHPVLDNAQNDAERINPFLGTWKGRSVTKRSGVYGATLSEADTVAVLEMNDKGQVVQDISSTSDEKKVTTNVHWEGKMSKDLVTFAEGYQMTLLPGGMYMGCPCDVSKCVADLKSFHLEFCWLESPSSRQRLIRTYDHEGLAVSSTYFTETKM
Protein: E3 ubiquitin-protein ligase RING1 (EC 2.3.2.27) (Polycomb complex protein RING1) (RING finger protein 1) (RING-type E3 ubiquitin transferase RING1) (Transcription repressor Ring1A) (O35730)
Organism: Mus musculus (Mouse)
Function: Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250}.
Interaction partners:
- YY1-associated factor 2
- E3 ubiquitin-protein ligase RING2
- Chromobox protein homolog 8
- Polycomb group RING finger protein 1
- Polycomb group RING finger protein 2
- Polycomb group RING finger protein 6
- Chromobox protein homolog 2
- RING1 and YY1-binding protein
- Polycomb complex protein BMI-1
- Lysine-specific demethylase 2B
Sequence:
MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPMPGSDQTATMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGAGAGASSVGTGGGAAGGACGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQETTEPGGPGGGASDTGGPDGGGGERGVAGGGEGPEEPALPSLEGVSEKQYTIYIAPGGGAFTTLNGSLTLELVNEKFWKVSRPLELCYAPTKDPK
Protein: Ciliary neurotrophic factor (CNTF) (P26441)
Organism: Homo sapiens (Human)
Function: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Subcellular location: Cytoplasm.
Interaction partners:
- Leukemia inhibitory factor receptor
- Ciliary neurotrophic factor receptor subunit alpha
- Interleukin-6 receptor subunit beta
- Interleukin-6 receptor subunit alpha
- Leptin
- Interleukin-27 receptor subunit alpha
- Cardiotrophin-like cytokine factor 1
- Leukemia inhibitory factor
- Erythropoietin
- Granulocyte colony-stimulating factor
Sequence:
MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIPARGSHYIANNKKM
Protein: Three-prime repair exonuclease 1 (EC 3.1.11.2) (3'-5' exonuclease TREX1) (Deoxyribonuclease III) (DNase III) (Q9NSU2)
Organism: Homo sapiens (Human)
Function: Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Plays a key role in degradation of DNA fragments at cytosolic micronuclei arising from genome instability: its association with the endoplasmic reticulum membrane directs TREX1 to ruptured micronuclei, leading to micronuclear DNA degradation. Micronuclear DNA degradation is required to limit CGAS activation and subsequent inflammation. Unless degraded, these DNA fragments accumulate in the cytosol and activate the cGAS-STING innate immune signaling, leading to the production of type I interferon. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:10393201}. Cytoplasm, cytosol {ECO:0000269|PubMed:16818237}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:33476576}; Peripheral membrane protein {ECO:0000269|PubMed:33476576}. Note=Retained in the cytoplasm through the C-terminal region (By similarity). Localization to the endoplasmic reticulum membrane is required to direct TREX1 to ruptured micronuclei (PubMed:33476576). In response to DNA damage, translocates to the nucleus where it is specifically recruited to replication foci (PubMed:16818237). Translocation to the nucleus also occurs during GZMA-mediated cell death (PubMed:16818237). {ECO:0000250|UniProtKB:Q91XB0, ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:33476576}.
Interaction partners:
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- Ribonuclease H2 subunit C
- Ribonuclease H2 subunit A
- Ribonuclease H2 subunit B
- Interferon regulatory factor 3
- Exonuclease 1
- Cyclic GMP-AMP synthase
- Stimulator of interferon genes protein
Sequence:
MGSQALPPGPMQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEITGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALERASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTASARTKPRPSAVTTTAHLATTRNTSPSLGESRGTKDLPPVKDPGALSREGLLAPLGLLAILTLAVATLYGLSLATPGE
Protein: RBPJ-interacting and tubulin-associated protein 1 (RBPJ-interacting and tubulin-associated protein) (Q96K30)
Organism: Homo sapiens (Human)
Function: Tubulin-binding protein that acts as a negative regulator of Notch signaling pathway. Shuttles between the cytoplasm and the nucleus and mediates the nuclear export of RBPJ/RBPSUH, thereby preventing the interaction between RBPJ/RBPSUH and NICD product of Notch proteins (Notch intracellular domain), leading to down-regulate Notch-mediated transcription. May play a role in neurogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21102556}. Nucleus {ECO:0000269|PubMed:21102556}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21102556}. Note=Shuttles rapidly between the cytoplasm and the nucleus. The function of centrosome localization is still unclear.
Interaction partners:
- Recombining binding protein suppressor of hairless
Sequence:
MKTPVELAVSGMQTLGLQHRCRGGYRVKARTSYVDETLFGSPAGTRPTPPDFDPPWVEKANRTRGVGKEASKALGAKGSCETTPSRGSTPTLTPRKKNKYRPISHTPSYCDESLFGSRSEGASFGAPRMAKGDAAKLRALLWTPPPTPRGSHSPRPREAPLRAIHPAGPSKTEPGPAADSQKLSMGGLHSSRPLKRGLSHSLTHLNVPSTGHPATSAPHTNGPQDLRPSTSGVTFRSPLVTSRARSVSISVPSTPRRGGATQKPKPPWK
Protein: G protein pathway suppressor 1 (A0A096LPJ3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPLPVQVFNLQGAVEPMQIDVDPQEDPQNAPDVNYVVENPSLDLEQYAASYSGLMRIERLQFIADHCPTLRVEALKMALSFVQRTFNVDMYEEIHRKLSEATRSSLRELQNAPDAIPESGVEPPALDTAWVEATRKKALLKLEKLDTDLKNYKGNSIKESIRRGHDDLGDHYLDCGDLSNALKCYSRARDYCTSAKHVINMCLNVIKVSVYLQNWSHVLSYVSKAESTPEIAERGERDSQTQAILTKLKCAAGLAELAARKYKQAAKCLLLASFDHCDFPELLSPSNVAIYGGLCALATFDRQELQRNVISSSSFKLFLELEPQVRDIIFKFYESKYASCLKMLDEMKDNLLLDMYLAPHVRTLYTQIRNRALIQYFSPYVSADMHRMAAAFNTTVAALEDELTQLILEGLISARVDSHSKILYARDVDQRSTTFEKSLLMGKEFQRRAKAMMLRAAVLRNQIHVKSPPREGSQGELTPANSQSRMSTNM
Protein: Meiotic coiled-coil protein 1 (O94452)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Meiotic coiled-coil protein 2
- Kinesin-like protein cut7
- Meiotic expression up-regulated protein 23
Sequence:
MELAKIGDRLNNYYNNIYTLSEKLGYSFTKISFNNIILDALSGHQRKLEIKIINIESKCNELSSEISLLRKRLGIIEEIEIPRTLIDQYECLVTYHNGIRAIYNTKKNEAKNMYKEIERLSVILGESVDEVNFVNGDFEDISDIKLEQLSAKLNELHQIYRLRKEKNIEIKEELKKLQDSLSIKLSMPADDLSKNGIKHLIIYKEKLRFSLESRKSRVDEIVNEMKNMCGKNPTSELPTNYSDKTLTLWENELSSMRKVYFVKYKTEYEFLQKRYLSLARIMFVSKKEMLFTSQFKEIPNVNRELIQSMKQEIGNLEVDLHLQGELNNMIRRYLLLESRVYKESQRMKVLSGSASQPFTLKRLQKDFQLLKAKLICALREWEEDNEKKIYVFGKPLSSRLLMIHSPPILQNQENISSNDNSKSSPESSPPARKTTGKIENKKLRNIDVQSKKSIRFPLRLASHEEPLIDRMVNQSPDTRSVSKSKRLVRETSSGCLFKNHSKSNTLSPRRKGSRHGPREPCLSPDASSSSIPVTDIKEILPSQHDTPHNSVKLTGSSTTPASVSLRQMIEPLLSRTPPKGEFTNSLDDTPTQSNVEKVDRFLENHDWETCSESSSASEDQSLCKQLSSFSLSSSDISKKLKNNLNGLHFSSDEGSKLPTFL
Protein: Solute carrier family 37 (Glucose-6-phosphate transporter), member 4 (Q9D1F9)
Organism: Mus musculus (Mouse)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Glucose-6-phosphatase 3
Sequence:
MAAQGYGYYRTVIFAAMFGGYSLYYFNRKTFSFVMPSLVDEIALDKDDLGLITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNVVFSWSSTVSAFAALWFLNGLAQGLGWPPCGKILRKWFEPSQFGTWWAVLSTSMNLAGSLGPILATILAQSYSWRSTLALSGALCVVVSFFCLLLIHNEPADVGLRNLDPAPSKGKKGSSKEESTLQDLLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQERGQSALVGSSYISALEVGGLVGSIAAGYLSDRAMAKAGLSLYGNPRHGLLLLMMAGMAASMFLFRVTVTSDSPKIWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVVCGASTVVFFLLRNIRTKMGRVSKKGE
Protein: Zinc finger protein 34 (A0A0C4DG42)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAALFLSAPPQAEVTFEDVAVYLSREEWGRLGPAQRGLYRDVMLETYGNLVSLGVGPAGPKPGVISQLERGDEPWVLDVQGTSGKEHLRVNSPALGTRTEYKELTSQETFGEEDPQGSEPVEACDHISKSEGSLEKLVEQRGPRAVTLTNGESSRESGGNLRLLSRPVPDQRPHKCDICEQSFEQRSYLNNHKRVHRSKKTNTVRNSGEIFSANLVVKEDQKIPTGKKLHYCSYCGKTFRYSANLVKHQRLHTEEKPYKCDECGKAFSQSCEFINHRRMHSGEIPYRCDECGKTFTRRPNLMKHQRIHTGEKPYKCGECGKHFSAYSSLIYHQRIHTGEKPYKCNDCGKAFSDGSILIRHRRTHTGEKPFECKECGKGFTQSSNLIQHQRIHTGEKPYKCNECEKAFIQKTKLVEHQRSHTGEKPYECNDCGKVFSQSTHLIQHQRIHTGEKPYKCSECGKAFHNSSRLIHHQRLHHGEKPYRCSDCKKAFSQSTYLIQHRRIHTGEKPYKCSECGKAFRHSSNMCQHQRIHLREDFSM
Protein: Uncharacterized protein (Q54IX5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable phosphoglycerate mutase
- Penta-EF hand domain-containing protein 2
- Inositol-3-phosphate synthase
Sequence:
MENLKLLKTYKIDRKKINDRSFGIDNKKVIEELIEVTSTENGFIPEVMQFLSKQNKIPIKYLENRMVCETAHAMNAQEKYDDATRYFLKAASQGSAEGCFFLASMKYLGQGCDVNLPMARKLFERGANMEPYIECEDEFLLENKNVLDCCKCLSGFAQEGVGGEIELETAFKYYSKVLKTKENDLDAIHNIGILQCDLKKDLQEGLKLFKRGMQLGSVECTFSYGAYTFDSNPTDAFKYIQRAANDGNEEAIFKLDEYKSKLNLLKK
Protein: Mcf2 proto-oncogene protein (Q99N72)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAVANPPRGKMRFRRNAASFPGSLHLVLVLRPTSFLQRTFTDIGFRFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIEKFAVTVKEMAQMLQSFGTELAETELPQDILSIEEILAGRAERYHLLKNDLTAVTKEGKVLLMNLQVPATEETVSSSLECTQHINGDWQTIKKLLAQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQEAVTQVEFLLSQQRELGDITGNLAQVKQRLKKLEILDDKSQELLTKARIVILRGHKLASNHHYALDLICQRCNELRYLSDILVNEIRTKRVQLSRTFKVHRLLQQARQCCDQGECLLASQGMDKFQTKEDAQKALQDVDNFLQMAMPFINYDIESLQYEFDVLLSPELKAQMQNIQLKLENIRSAFQNQQAGCKSLKEVPEGAFQNLVPASENVMRSRMIFFSPKHVKKSWRQIRAQSNVKVEAVEDSQEKNSDQSPKLDNSLDILKNHVLDELIQTERAYVRELFTVLLGYRSEMDNPQMFDLMPPLLRNKKDVLFGNMAEIYEFHNNIFMSRLEDCSDAPERVGPCFLERKDDFQMYAKYCQNKPRSELIWRKYSECAFFQECQRKLKHRLGLDSYLLKPVQRITKYQLLLKELLKYSKEGEGTTKLKEALDSMLELLKSVNDSMHQTAINAYVGNINELGKMVLQGSFNVWLGHRKGATKMKDFARFKPMQRHLFLYEKAVMFCKRRFESGEGADRYPSYSFKHCLKMEDVGITEHVKGDNRKFEIRYSEKEEIYIVQAPNVDVKMLWLKEIRKILVQQKELMTAKTQQDQALDQDQLFPQQQNAELCKSSPFCVCEETLFNATEAGAEVEQAGALIKVREAAVLAQAEASSAAWNGMLPSAEGAAAIAEHSYNYFSSNNDHGEDRTQMRHMSEVTF
Protein: Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCase subunit beta) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta) (Q5XIT9)
Organism: Rattus norvegicus (Rat)
Function: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Peroxisomal bifunctional enzyme
- Methylglutaconyl-CoA hydratase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Holocarboxylase synthetase
- Pyruvate carboxylase, mitochondrial
Sequence:
MWGALRSVLRPCSRASVPRQRAYHGDAVARLGTQPDSGSSTYQENYEQMKALVNQLHERAQYVRLGGSEKARARHTSRGKLLPRDRIDNLIDPGSPFLEFSQFAGYKLYGEEEVPAGGIITGIGRVSGVECMIVANDATVKGGTYYPVTVKKHVRAQEIALQNRLPCIYLVDSGGANLPRQADTFPDRDHFGRIFYNQAIMSSKNITQIAVVMGSCTAGGAYVPAMADENIIVQRQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRRSGVTDHYALDDHHALHLTRKVVRSLNYQKKLDVTVEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFNEFKALYGDTLVTGFARIFGYPVGIIGNNGVLFSESAKKGAHFVQLCCQRNIPLLFLQNITGFMVGKDYEAEGIAKDGAKMVAAVSCAKVPKITVIIGGSYGAGNYGMCGRAYSPRFLYMWPNARISVMGGEQAATVLATVARDQRAREGKQFSSAEEAALKEPIIKRFEEEGNPYYSSARLWDDGIIDPVDTRLVLGLSISAALNAPIQRTDFGIFRM