wanglab/gogpt-training-data huggingface dataset:
Protein: Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Protein asunder homolog) (Spermatogenesis-associated protein 30) (Q8QZV7)
Organism: Mus musculus (Mouse)
Function: Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis. Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing.
Subcellular location: Nucleus {ECO:0000269|PubMed:23904267}. Cytoplasm {ECO:0000269|PubMed:23097494, ECO:0000269|PubMed:23904267}. Note=Nuclear location is required for recruitment of dynein motors to nuclear envelope at G2/M. {ECO:0000250|UniProtKB:Q9NVM9}.
Interaction partners:
- Integrator complex subunit 1
- Integrator complex subunit 5
- Integrator complex subunit 3
- Integrator complex subunit 14
- Integrator complex subunit 6
- Integrator complex subunit 10
- Integrator complex subunit 11
- Integrator complex subunit 4
- Integrator complex subunit 9
- Integrator complex subunit 7
Sequence:
MKIFSESHKTVFVVDHCPYMAESCRQHVEFDMLVKNRTQGIIPLAPISKSLWTCSVESSMEYCRIMYDIFPFKKLVNFIVSDSGAHVLNSWTQEDQNLQELMAALATVGPPNPRADPECCSILHGLVAAVETLCKITEYQHEARTLLMENAERVGNRGRIICITNAKSDSHVRMLEDCVQETIHEHNKLAANSDHLMQIQKCELVLIHTYPVGEDSLVSDRPKKELSPVLTSEVHSVRAGRHLATKLNVLVQQHFDLASTTITNIPMKEEQHANTSANYDVELLHHKDAHVDFLRSGDSHSGSSSREGPFKETVTLKWCTPRTNSIELHYCTGAYRISPVDVNSRPSSCLTNFLLNGRSVLLEQPRKSGSKVISHMLSSHGGEIFLHVLSSSRSILEDPPSISEGCGGRVTDYRITDFGEFMRENRLTPFLDPRYKIDASLEIPLERAKDQLEKHTRYWPMIISQTTIFNMQAVVPLAGVIVKESLTEEDVLNCQKTIYNLVDMERKNDPLPVSTVGTRGKGPKRDEQYRIMWNELETLVRAHISNSEKHQRVLECLMACRSKPPEEEERKKRGRKREDREDKSEQAGKEHGTEKARPDADRLKGILERGKEELAEAEVIKDSPDSPEPPNKKPLVETDETPHMEKSKGPVSLLSLWSNRINTANSRKHQEFAGRLNSVNNRAELYQHLKEENGEEVGLTGGPRTAIPFLKCPRSPVVNRMETTENGKASRQ
Protein: Lysyl oxidase homolog 1 (EC 1.4.3.13) (Lysyl oxidase 2) (Lysyl oxidase-like protein 1) (P97873)
Organism: Mus musculus (Mouse)
Function: Active on elastin and collagen substrates.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:14745449}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:14745449}.
Interaction partners:
- Fibulin-5
- Elastin
- Fibrillin-1
- Microfibrillar-associated protein 2
- Microfibrillar-associated protein 5
- EGF-containing fibulin-like extracellular matrix protein 2
- Latent-transforming growth factor beta-binding protein 3
- Biglycan
- Collagen alpha-1
- Latent-transforming growth factor beta-binding protein 2
Sequence:
MALAGAGSQLRTLVWSACLCVLVHGQQAQPGQGSDPGRWRQLIQWENNGQVYSLLNSGSEYVPAGPQRGETSSRVLLAGAPQTSQRRSQGGPRRRQAPSLPLPGRVGSDTVRGQTRHPFGFGQVPDNWREVAVGDSTGMARARTSVSQQRHGGSASSSVSASAFATTYRQPSPYPQQFPYPQAPFVNQYENYDPASRTYEQGYVYYRGAGGGMGAGAAAVASAGVIYPFQPRARYEDYGGGGGEEQPEYPAQGFYPAPERPYVPQPQPQPQPQPQPQPQPSDGLDRRYSHSLYNEGTPGFEQAYPDPSTDVSQAPAGAGGTYGGAGDPRLGWYPPYAANVPPEAYVPPRAVEPQPPFRVLEPPYLPVRSSDAPSQGGERNGAQQGRLSVGSVYRPNQNGRGLPDLVPDPNYVQASTYVQRAHLYSLRCAAEEKCLASTAYAPEATDYDLRVLLRFPQRVKNQGTADFLPNRPRHTWEWHSCHQHYHSMDEFSHYDLLDASTGKKVAEGHKASFCLEDSTCDFGNLKRYACTSHTQGLSPGCYDTYNADIDCQWIDITDVQPGNYILKVHVNPKYIVLESDFTNNVVRCNIHYTGRYVSTTNCKIVQS
Protein: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (PDPc) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1) (P35816)
Organism: Bos taurus (Bovine)
Function: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:4339797, ECO:0000269|PubMed:6288374}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase protein X component
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
- Acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Protein-serine/threonine kinase
- Protein phosphatase
Sequence:
MPAPTQLFFPLIRNCELSRIYGTACYCHHKHLCCSPPYIPQSRPRYTPHPAYATFYRPKESWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSVLGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESTDIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNEREVERLKLEHPKNEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYYTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRAKMSSVFEDQNAATHLIRHAVGNNEFGAVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQEQ
Protein: Helicase like transcription factor (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 3, isoform CRA_c) (A0A0C4DGA6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSWMFKRDPVWKYLQTVQYGVHGNFPRLSYPTFFPRFEFQDVIPPDDFLTSDEEVDSVLFGSLRGHVVGLRYYTGVVNNNEMVALQRDPNNPYDKNAIKVNNVNGNQVGHLKKELAGALAYIMDNKLAQIEGVVPFGANNAFTMPLHMTFWGKEENRKAVSDQLKKHGFKLGPAPKTLGFNLESGWGSGRAGPSYSMPVHAAVQMTTEQLKTEFDKLFEDLKEDDKTHEMEPAEAIETPLLPHQKQALAWMVSRENSKELPPFWEQRNDLYYNTITNFSEKDRPENVHGGILADDMGLGKTLTAIAVILTNFHDGRPLPIERVKKNLLKKEYNVNDDSMKLGGNNTSEKADGLSKDASRCSEQPSISDIKEKSKFRMSELSSSRPKRRKTAVQYIESSDSEEIETSELPQKMKGKLKNVQSETKGRAKGSSKVIEDVAFACALTSSVPTTKKKMLKKGACAVEGSKKTDVEERPRTTLIICPLSVLSNWIDQFGQHIKSDVHLNFYVYYGPDRIREPALLSKQDIVLTTYNILTHDYGTKGDSPLHSIRWLRVILDEGHAIRNPNAQQTKAVLDLESERRWVLTGTPIQNSLKDLWSLLSFLKLKPFIDREWWHRTIQRPVTMGDEGGLRRLQSLIKNITLRRTKTSKIKGKPVLELPERKVFIQHITLSDEERKIYQSVKNEGRATIGRYFNEGTVLAHYADVLGLLLRLRQICCHTYLLTNAVSSNGPSGNDTPEELRKKLIRKMKLILSSGSDEECAICLDSLTVPVITHCAHVFCKPCICQVIQNEQPHAKCPLCRNDIHEDNLLECPPEELARDSEKKSDMEWTSSSKINALMHALTDLRKKNPNIKSLVVSQFTTFLSLIEIPLKASGFVFTRLDGSMAQKKRVESIQCFQNTEAGSPTIMLLSLKAGGVGLNLSAASRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNKKRELAAGAFGTKKPNADEMKQAKINEIRTLIDL
Protein: FYVE, RhoGEF and PH domain-containing protein 4 (Actin filament-binding protein frabin) (FGD1-related F-actin-binding protein) (O88387)
Organism: Rattus norvegicus (Rat)
Function: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10464238}. Cell projection, filopodium {ECO:0000269|PubMed:10464238}. Note=Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers.
Interaction partners:
- GPI ethanolamine phosphate transferase 1
- SH3 domain and tetratricopeptide repeats 2
- LOC691036 protein
- Cell division control protein 42 homolog
Sequence:
MEESNPAPTSCASKGKHSKVSDLISHFEGGSVLSSYTDVQKDSTMNLNIPQTPRQHGLTSTTPQKLPSHKSPQKQEKDSDQNQGQHGCLANGVAAAQSQMECETEKEAALSPETDTQTAAASPDAHVLNGVRNETTTDSASSVTNSHDENACDSSCRTQGTDLGLPSKEGEPVIEAELQERENGLSTEGLNPLDQHHEVKETNEQKLHKIATELLLTERAYVSRLNLLDQVFYCKLLEEANRGSFPAEMVNKIFSNISSINAFHSKFLLPELEKRMQEWETTPRIGDILQKLAPFLKMYGEYVKGFDNAVELVKNMTERVPQFKSVTEEIQKQKICGSLTLQHHMLEPIQRIPRYEMLLKDYLKKLSPDAPDWNDAKKSLEIISTAASHSNSAIRKMENLKKLLEIYEMLGEEEDIVNPSNELIKEGQILKLAARNTSAQERYLFLFNNMLLYCVPRFSLVGSKFTVRTRVGIDGMKIVETHNEEYPHTFQVSGKERTLELQASSEQDKEEWIKALQESIDAFHQRHETFRNAIAKENDIPLEVSTAELGKRAPRWIRDNEVTMCMKCKESFNALTRRRHHCRACGHVVCWKCSDYKAQLEYDGGRLNKVCKDCYQIMSGFAESEEKKRRGILEIESAEVSGNSEVCSFLQYMEKSKPWQKIWCVIPKQDPLVLYMYGAPQDVRAQATIPLLGYIVDDMPKSADLPHSFKLTQSKSVHSFAADSEELKQKWLKIILLAVTGETPDGPSEHLDTLDNLPGPKEKSEC
Protein: Probable transport protein MmpL12 (P9WJT7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable methyltransferase
- Possible methyltransferase
- Probable zinc-binding alcohol dehydrogenase Rv1895
Sequence:
MARHDEAKAGGLFDRIGNFVVRWPLIVIGCWIAVAAALTLLLPTLQAQAAKREQAPLPPGAPSMVLQKEMSAAFQEKIETSALLLVLLTNENGLGPADEAVYRKLIENLRADTQDKISVQDFLAVPEMKELLASKDNKAWNLPITFAGDAASPETQAAFKRVAAIVKQTVAGTSLTVHLSGPIATVADLTELGEKDVRIIEIGTAVSVLIILILVYRNLVTMLVPLATIGASVVTAQGTLSGLAEFGLAVNMQAIVFMSAVMIGAGTDYAVFLISRYHDYVRHGEKSDMAVKKALMSIGKVITASAATVAVTFLAMVFTKLEVFSAVGPAIAVAITVSLLGAVTLLPAILTLTGRRGWIKPRRDLTSRMWRRSGVRIVRRSTIHLVGSLIVLVALAGCTLLIRFNYDDLKTVPQHVESVKGYEAMNRHFPMNAMTPMVLFIKSPRDLRTPGALADIEMMSREIAELPNIVMVRGLTRPNGEPLKETKVSFQAGEVGGKLDEATTLLEEHGGELDQLTGGAHQLADALAQIRNEINGAVASSSGIVNTLQAMMDLMGGDKTIRQLENASQYVGRMRALGDNLSGTVTDAEQIATWASPMVNALNSSPVCNSDPACRTSRAQLAAIVQAQDDGLLRSIRALAVTLQQTQEYQTLARTVSTLDGQLKQVVSTLKAVDGLPTKLAQMQQGANALADGSAALAAGVQELVDQVKKMGSGLNEAADFLLGIKRDADKPSMAGFNIPPQIFSRDEFKKGAQIFLSADGHAARYFVQSALNPATTEAMDQVNDILRVADSARPNTELEDATIGLAGVPTALRDIRDYYNSDMKFIVIATIVIVFLILVILLRALVAPIYLIGSVLISYLSALGIGTLVFQLILGQEMHWSLPGLSFILLVAIGADYNMLLISRIRDESPHGIRIGVIRTVGSTGGVITSAGLIFAASMFGLVGASINTMAQAGFTIGIGIVLDTFLVRTVTVPALTTMIGRANWWPSELGRDPSTPPTKADRWLRRVKGHRRKAPIPAPKPPHTKVVRNTNGHASKAATKSVPNGKPADLAEGNGEYLIDHLRRHSLPLFGYAAMPAYDVVDGVSKPNGDGAHIGKEPVDHLLGHSLPLFGLAGLPSYDRWDDTSIGEPAVGHAGSKPDAKLST
Protein: Euchromatic histone lysine methyltransferase 1 (A0A1B0GV09)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSSAAAADPL
Protein: Neuropilin and tolloid-like protein 1 (Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 1) (Q8R4I7)
Organism: Mus musculus (Mouse)
Function: Involved in the development and/or maintenance of neuronal circuitry. Accessory subunit of the neuronal N-methyl-D-aspartate receptor (NMDAR) critical for maintaining the abundance of GRIN2A-containing NMDARs in the postsynaptic density. Regulates long-term NMDA receptor-dependent synaptic plasticity and cognition, at least in the context of spatial learning and memory.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Postsynaptic density membrane {ECO:0000269|PubMed:19243221}. Note=Component of the postsynaptic density (PSD) of excitatory synapses.
Interaction partners:
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, kainate 4
- Lysine--tRNA ligase
- Disks large homolog 4
Sequence:
MIYGRSLFHIIASLIILHSSGATKKGTEKQITPETQKSVQCGTWTKHAEGGVFTSPNYPSKYPPDRECVYIIEAAPRQCIELYFDEKYSIEPSWECKFDHIEVRDGPFGFSPIIGRFCGQQNPPVIKSSGRFLWIKFFADGELESMGFSARYNFTPDPDFKDLGVLKPLPACEFEMGGPEGIVESIQILKEGKASASEAVDCKWYIRAPPRSKIYLRFLDYEMQNSNECKRNFVAVYDGSSSVEDLKAKFCSTVANDVMLRTGLGVIRMWADEGSRNSRFQMLFTSFQEPPCEGNTFFCHSNMCINNTLVCNGLQNCVYPWDENHCKEKRKTSLLDQLTNTSGTVIGVTSCIVIILIIVSVIVQIKQPRKKYVQRKSDFDQTVFQEVFEPPHYELCTLRGTGATADFADVAEDFENYHKLRRSSSKCIHDHHCGSQLSSAKGSRSNLSTRDASILAEIPTQPVKPLIPPVNRRNILVMKHNYSQDAADACDIDEIEEVPTTSHRLSRHEKSVQRFCLIGSLSKHESEYNTTRV
Protein: Lipoprotein binding FH (A0A024A2C9)
Organism: Haemophilus influenzae
Interaction partners:
Sequence:
MNINLKKFSLTILAALTLTACGSGSGASASNAPTAQPSTPATQPSEQAVLEMPKRSPTNTGLVFSIKTESEEDSVGQINTINNEQELSNRTLTSIDVDGKQIPIAFTENWNEAKYIEQPLNGVPHICCNKYTAMRFGAIASNEAGQNDILFYNGIPTEKLPDSGEVTYEGESIMTSKESVIPDDYMKGSSKFIVNFGDKKLSGSLIIDTTKSTSSSQKVKIDIEKAKITGNTFSGTAQSDSFKSQGIAEGKFYGDGAKELGGMVKAKDNSWAGAYGAKAQ
Protein: Prostaglandin F2-alpha receptor (PGF receptor) (PGF2-alpha receptor) (Prostanoid FP receptor) (P43088)
Organism: Homo sapiens (Human)
Function: Receptor for prostaglandin F2-alpha (PGF2-alpha). The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. Initiates luteolysis in the corpus luteum (By similarity). Isoforms 2 to 7 do not bind PGF2-alpha but are proposed to modulate signaling by participating in variant receptor complexes; heterodimers between isoform 1 and isoform 5 are proposed to be a receptor for prostamides including the synthetic analog bimatoprost.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prostaglandin F2 receptor negative regulator
- Type-1 angiotensin II receptor
- Guanine nucleotide-binding protein G
- Aldo-keto reductase family 1 member C3
- Interleukin-8
- Guanine nucleotide-binding protein subunit alpha-12
- Prostaglandin E synthase
- Guanine nucleotide-binding protein G
- Angiotensinogen
- Guanine nucleotide-binding protein subunit alpha-14
Sequence:
MSMNNSKQLVSPAAALLSNTTCQTENRLSVFFSVIFMTVGILSNSLAIAILMKAYQRFRQKSKASFLLLASGLVITDFFGHLINGAIAVFVYASDKEWIRFDQSNVLCSIFGICMVFSGLCPLLLGSVMAIERCIGVTKPIFHSTKITSKHVKMMLSGVCLFAVFIALLPILGHRDYKIQASRTWCFYNTEDIKDWEDRFYLLLFSFLGLLALGVSLLCNAITGITLLRVKFKSQQHRQGRSHHLEMVIQLLAIMCVSCICWSPFLVTMANIGINGNHSLETCETTLFALRMATWNQILDPWVYILLRKAVLKNLYKLASQCCGVHVISLHIWELSSIKNSLKVAAISESPVAEKSAST
Protein: Asparagine--tRNA ligase, cytoplasmic 1 (EC 6.1.1.22) (Asparaginyl-tRNA synthetase 1) (AsnRS 1) (Protein EMBRYO DEFECTIVE 2755) (Q9SW96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Glutamyl-tRNA
- Proline--tRNA ligase, cytoplasmic
- proline--tRNA ligase
- Proline--tRNA ligase, chloroplastic/mitochondrial
- At1g07030
- Cysteine--tRNA ligase 2, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase 1, cytoplasmic
Sequence:
MADEIVPPATQLAAVSLENDGSTVQRAQFSNRVLIRTILDRPDGGAGLAGQTVRIGGWVKSGRDQGKRTFSFLAVNDGSCPANLQVMVDPSLYDVSNLVATGTCVTVDGVLKVPPKGKGTQQQIELNVVKVIDVGTVDASKYPLPKTKLTLETLRDVLHLRSRTNSISAVARIRNALAFATHSFFQEHSFLYIHTPIITTSDCEGAGEMFQATTLINYTERLEQDLIDNPPPTEADVEAARLIVIERGNVVAELKAAKASKEAITAAVAELKIAKETFAHIDERSRLRPGLPKKDGNIDYSKDFFGRQAFLTVSGQLQVETYACALSNVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFADLEDDMNCAEAYVKYMCNWLLEKCYADMELMAKNFDSGCIDRLKLVASTPFGRITYTKAIELLEEAVAKGKEFDNNVEWGIDLASEHERYLTEVLFQKPLIVYNYPKGIKAFYMRLNDDEKTVAAMDVLVPKVGELIGGSQREERYDVIKKRIEEMGLPIEPYEWYLDLRRYGTVKHCGFGLGFERMILFATGLDNIRDVIPFPRYPGKADL
Protein: Mitochondrial fission regulator 2 (DUF729 domain-containing protein 1) (Q6P444)
Organism: Homo sapiens (Human)
Function: May play a role in mitochondrial aerobic respiration essentially in the testis. Can also promote mitochondrial fission (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}. Note=Associated with membranes. {ECO:0000250}.
Interaction partners:
- Meiotic nuclear division protein 1 homolog
Sequence:
MSLILNILREMLEYFGVPVEQVLLIWENKDYGSTRSIVRIIGKMLPLEPCRRPNFELIPLLNSVDSDNCGSMVPSFADILYVANDEEASYLRFRNSIWKNEEEKVEIFHPLRLVRDPLSPAVRQKETVKNDLPVNEAAIRKIAALENELTFLRSQIAAIVEMQELKNSTNSSSFGLSDERISLGQLSSSRAAHLSVDPDQLPGSVLSPPPPPPLPPQFSSLQPPCFPPVQPGSNNICDSDNPATEMSKQNPAANKTNYSHHSKSQRNKDIPNMLDVLKDMNKVKLRAIERSPGGRPIHKRKRQNSHWDPVSLISHALKQKFAFQEDDSFEKENRSWESSPFSSPETSRFGHHISQSEGQRTKEEMVNTKAVDQGISNTSLLNSRI
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (EC 3.1.11.-) (Gene product 5) (Gp5) (P00581)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Replicates viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'-5' direction (By similarity). Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.
Interaction partners:
Sequence:
MIVSDIEANALLESVTKFHCGVIYDYSTAEYVSYRPSDFGAYLDALEAEVARGGLIVFHNGHKYDVPALTKLAKLQLNREFHLPRENCIDTLVLSRLIHSNLKDTDMGLLRSGKLPGKRFGSHALEAWGYRLGEMKGEYKDDFKRMLEEQGEEYVDGMEWWNFNEEMMDYNVQDVVVTKALLEKLLSDKHYFPPEIDFTDVGYTTFWSESLEAVDIEHRAAWLLAKQERNGFPFDTKAIEELYVELAARRSELLRKLTETFGSWYQPKGGTEMFCHPRTGKPLPKYPRIKTPKVGGIFKKPKNKAQREGREPCELDTREYVAGAPYTPVEHVVFNPSSRDHIQKKLQEAGWVPTKYTDKGAPVVDDEVLEGVRVDDPEKQAAIDLIKEYLMIQKRIGQSAEGDKAWLRYVAEDGKIHGSVNPNGAVTGRATHAFPNLAQIPGVRSPYGEQCRAAFGAEHHLDGITGKPWVQAGIDASGLELRCLAHFMARFDNGEYAHEILNGDIHTKNQIAAELPTRDNAKTFIYGFLYGAGDEKIGQIVGAGKERGKELKKKFLENTPAIAALRESIQQTLVESSQWVAGEQQVKWKRRWIKGLDGRKVHVRSPHAALNTLLQSAGALICKLWIIKTEEMLVEKGLKHGWDGDFAYMAWVHDEIQVGCRTEEIAQVVIETAQEAMRWVGDHWNFRCLLDTEGKMGPNWAICH
Protein: LD47348p (Q960K4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFGFEEPSPHAHLEHLCINLCAETMQHFYNTHIFKSSVESCRDEGIVCDTEVDYVDNVPCIDLISSLRTGLLSMLDAECSVRGTAESYVTKLKVQHRSSTRLETKPTAEPHDPRMFLIRHFAGRVEYDTTDFLDTNRDVVPDDLVGVFYKHTCNFGFATHLFGSELKALYAQQQAPRGLSFRISPTSHSDLLNGDEPVSTLTQDFHTRLDNLLRTLVHARPHFVRCIRSNGTEAARSFDRATVVRQIRSLQVLETVNLMASGFPHRMRFKQFNARYRMLAPFRLLRRSEDKALEDCQLILKYAMEQPPVLDGSVTLAWAPGKRHVFLSEGIRQHLEHLRTEIRHKSATLMQATWRGWWWRKKMGNGGAKRSKIPGLQQAPLPNNKTTPNSAAQNKAASSTMAALAAVAAAAPISVPRLSAKTTSLGIGGTVARPRPQPIAGTPPPDPQEKCDQKIIQQTCNLFGLDLERPPPVPPSRSYTITGNSKISYPQNRVMKMNFPEEGQSEAPQLKKGEAVTVRGHLMVEHKGQSFHVPFQFMTLSK
Protein: Cell division control protein 73 C-terminal domain-containing protein (Q383Q6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- FACT complex subunit
- RNA polymerase-associated protein CTR9
- Histone chaperone RTT106/FACT complex subunit SPT16-like middle domain-containing protein
- Transcription initiation protein, putative
- Spt4/RpoE2 zinc finger domain-containing protein
- Uncharacterized protein
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- Plastid-encoded RNA polymerase subunit alpha
- Telomerase-associated protein, putative
Sequence:
MFTRPLFNFSPRHLCLFLSAHSSPPSLREPMSLREDWGRLVDEVCNMDSTEPLPEEFVPSEFLPGGCELPADLLHYLRSGANAFEAETADLFQPQTSTEEGFHAAPIVSRYGTAGTLRNLVGDRGENPRLPRHEGPNFYEAYRAHAALNGEGGGRNNLTSSASAAAAAGSAGANNILRSIGNGIRINPGFMVPEYHSQRNRKLNFVPLILISPSVSSVLQVINIKDFLEDGVYVEPSSRFLNPVTGDMNVEDAPKHITVKPGSFLDADKYRVAYREFRVVNGPKQVKNWNHVCACIVDGNEWQFNRWFPDEVPSLCVSRLFQRVCGFLPYFEEDKPPKALQEWHVTPLKLTRRVVKSHTHIRQASAFWEHLYLFLDTHPLFKLFTVPPDQP
Protein: Leucine-rich repeat transmembrane protein FLRT2 (Fibronectin leucine rich transmembrane protein 2) (Q8BLU0)
Organism: Mus musculus (Mouse)
Function: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells. May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D. Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members. Plays a role in fibroblast growth factor-mediated signaling cascades. Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24585683, ECO:0000269|PubMed:25374360}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16872596, ECO:0000305|PubMed:24585683}. Cell junction, focal adhesion {ECO:0000269|PubMed:16872596}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24585683}. Synapse, synaptosome {ECO:0000250|UniProtKB:D3ZTV3}. Microsome membrane {ECO:0000269|PubMed:24585683}. Secreted {ECO:0000269|PubMed:21673655}. Note=Proteolytic cleavage gives rise to a shedded ectodomain. {ECO:0000269|PubMed:21673655}.
Interaction partners:
- Netrin receptor UNC5D
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L1
- Netrin receptor UNC5B
- Adhesion G protein-coupled receptor L2
- Netrin receptor UNC5A
Sequence:
MGLQTTKWPGRGAFILKFWLIISLGLYLQVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANLRKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKWVTEWLKYIPSSLNVRGFMCQGPEQVRGMAVRELNMNLLSCPTTTPGLPVFTPAPSTVSPTTQSPTLSVPSPSRGSVPPAPTPSKLPTIPDWDGRERVTPPISERIQLSIHFVNDTSIQVSWLSLFTVMAYKLTWVKMGHSLVGGIVQERIVSGEKQHLSLVNLEPRSTYRICLVPLDAFNYRTVEDTICSEATTHASYLNNGSNTASSHEQTTSHSMGSPFLLAGLIGGAVIFVLVVLLSVFCWHMHKKGRYTSQKWKYNRGRRKDDYCEAGTKKDNSILEMTETSFQIVSLNNDQLLKGDFRLQPIYTPNGGINYTDCHIPNNMRYCNSSVPDLEHCHT
Protein: BTB/POZ domain-containing protein (Q54RA9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MATINIINNNNNQNNNNQNNNNNINHTEYFNNGFKSLLGEFKKYTDIKIKCGGQIFPTHRIILANSSEFFGRLLLSDFKESSQSVIELKQPDPFNVFPMVLEFMYDGIIYLSPENVIPLLAMSDHYLIRDLQHLCLLFLDQNLHRENVLTILKYSIDFHFEPITERCITIISKNFTFVCENLYKQTKINQNNNNNCINIENNKKHLNTSSASSSLNSSTSSASSSSSSSNNNYYTTTTTTTTTTTASSSNFNKNLTNCKVTGQQQQQQQQQQQQQQQQQQQQQQQQPIYDFSFLPASIFYQILDHDYLVVNSEYTLYRIVLNFIEKFFGENFTEITYNTNITDQLKVSDLMSQIRYILMPYDQLTLITKDPLIPKEILFETLLERLKRFEGKTSSPSSSSTSSSPSNTSNSPTKQTSPSKYQQQQQQQQQQQQQQQQQQPQTIHQMIQQSQLTIHQIVQQNIQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPQQQPQQQPQQPQPQIIQQQPQQPQIIQQQPQQLQQLQQPQQPQTIQQMVQQQQNIQQQQQQQQQQQNIQQQQTQNMQQQLQQQLLQQIQQQQQQQQQPQIIKQFTPSSSPLSSSFISLNASQSKLSINNATNTTNNNNNNSNNVTNTNNNNIINNNNNNNNKQTQSNNNDNKILKRYQPRPPQSILFEYSFDFDFKGIIFWISTDGGNEKWSNPHSTSKIKITSSSIDKGNLYDIVELTPNAFWTKDVPASWVMIDLGPNRTVVPMYYTIRHGLSYKSDSLRTWDFQGSTNGEQWTVLKRHTNDPSLNYKYATHSWPVTGCETAFRYFRILQTGKNSNNRNFLVIGGLEIYGELCETNPNPN
Protein: Peroxiredoxin bcp1 (Prx) (EC 1.11.1.24) (Bacterioferritin comigratory protein 1) (BCP) (Nuclear thiol peroxidase) (nTPx) (Thioredoxin peroxidase) (Thioredoxin-dependent peroxiredoxin bcp1) (O94561)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (By similarity). Acts as a scavenger of H(2)O(2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
- Tryptophan synthase
- Glutathione peroxidase-like peroxiredoxin gpx1
Sequence:
MDAPRRSSRLAAKIANVLDSKGTIIPEAAPVMLKKPAKDESVDSTIQVGDVIPDITLPDEDGTSIRLRDITANKGLVIFAYPKASTPGCTKQGCGFRDNYPKIQASDYEVLGLSFDTSKAQKAFKDKQNFPYHLLSDPKGELIKKLGAEKPGGGKLFRSHWIFEKGTGKCIVKEIDISPLVSVDKAFAVITDSEP