wanglab/gogpt-training-data huggingface dataset:
Protein: formate--tetrahydrofolate ligase (EC 6.3.4.3) (B7ZM99)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGTRLPLVLRQLRRPPQPPGPPRRLRVPCRASSGGGGGGGGGREGLLGQRRPQDGQARSSCSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFKPVLAIIQAGDDNLMQEINQNLAEEAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQISENLFSNKVLNALKPEKDVDGVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSVGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKVGCGSPRIHFGGLIEEDDVILLAAALRIQNMVSSGRRWLREQQHRRWRLHCLKLQPLSPVPSDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGITPTPLGEGKSTVTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEEFNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKALYNRLVPLVNGVREFSEIQLARLKKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYRQAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGMEKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEENIQLVADGCCNLQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVDLARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGFGNLPICMAKTHLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRPCFYDIDLDTETEQVKGLF
Protein: Transaldolase (EC 2.2.1.2) (P9WG33)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Transketolase
- Glucose-6-phosphate isomerase
- Glucose-6-phosphate 1-dehydrogenase 2
- Fructose-bisphosphate aldolase
- Enolase
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase isozyme 2
- Glyceraldehyde-3-phosphate dehydrogenase
- ATP-dependent 6-phosphofructokinase
- Fructose-1,6-bisphosphatase class 2
Sequence:
MTAQNPNLAALSAAGVSVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTVTTDDVRSACDVLVPQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYREVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRIGSRQALELRGQAGVANARLAYATYREVFEDSDRYRSLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIQGDTVTGTASDAQAVFDQLGAIGIDLTDVFAVLEEEGVRKFEASWNELLQETRAHLDTAAQ
Protein: ADP-ribosylation factor GTPase activating protein 3, isoform G (M9PIL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASPAAGPSKQEIESVFSRLRAQPANKSCFDCAAKAPTWSSVTYGIFICIDCSAVHRNLGVHLTFVRSTNLDTNWTWLQLRQMQLGGNANAAQFFRAHNCSTTDAQVKYNSRAAQLYRDKLCAQAQQAMKTHGTKLHLEQTDKSEGNEAAREEDFFAQCDNEVDFNVQNNNDPNPPTVAPVISVETQQGGAPSVNLLNSVVPAAVPSSIGARKVQPKKGGLGARKVGGLGATKVKTNFADIEARANAANEMKTSAAAAPVVKPQTAEDELETVASMRLAYQELSMQKTREEAKLKTMDPAKAKQMERLGMGFNLRGSDMAHSALGDMETIQQSAAPKAKLSLLESENFFTDFSLYGNSSSGGGGGGSSEKRESSVGGTSKLDKFELDALGYETIEPIGGSHSNITSMFSRSNDYDKPKTSAPVKKNSGSSQTHTKGGTSTDPVIAQQKFGNSKGFGSDQYFASEQSSADVSASLNRFQGSRAISSSDYFGDGSPGGTGGNRASSVNFSAPDLDVESVKESVRQGVHKVAGRLSNLANDVMTSWQDKYGY
Protein: Mitogen-activated protein kinase kinase kinase 3 (EC 2.7.11.25) (MAPK/ERK kinase kinase 3) (MEK kinase 3) (MEKK 3) (Q61084)
Organism: Mus musculus (Mouse)
Function: Component of a protein kinase signal transduction cascade. Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 5
- Cerebral cavernous malformations protein 2 homolog
- Dual specificity mitogen-activated protein kinase kinase 3
- TNF receptor-associated factor 6
- NF-kappa-B essential modulator
- Sequestosome-1
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Serine/threonine-protein kinase PAK 2
- Serine/threonine-protein kinase PAK 1
Sequence:
MDEQEALDSIMKDLVALQMSRRTRLSGYETMKNKDTGHPNRQSDVRIKFEHNGERRIIAFSRPVRYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHTSSSPHSGVSRQVRIKPSQSAGDINTIYQAPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSQMSRARSFPDNRKECSDRETQLYDKGVKGGTYPRRYHVSVHHKDYNDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGVAVQYLDPRGRLRSADSENALTVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKILTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLVY
Protein: Terephthalate 1,2-dioxygenase, reductase component 1 (TPADO reductase component) (EC 1.14.12.15) (TER dioxygenase system) (TERDOS) (Q3C1E0)
Organism: Comamonas sp
Function: Component of the terephthalate 1,2-dioxygenase multicomponent enzyme system which catalyzes the dioxygenation of terephthalate (TER/TPA) to 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylic acid (DCD). TphA1 probably reduces TphA2A3. It can also use 2,5-dicarboxypyridine (PDC) and 1,4-napthalenedicarboxylic acid (NDC) as substrates, and preferentially uses NADPH which is the physiological electron donor.
Interaction partners:
Sequence:
MNHQIHIHDSDIAFPCAPGQSVLDAALQAGIELPYSCRKGSCGNCASALLDGNITSFNGMAVRSELCTSEQVLLCGCTAASDIRIQPSSFRRLDPEARKRFTAKVYSNTLAAPDVSLLRLRLPVGKRAKFEAGQYLLIHLDDGESRSYSMANPPHESDGITLHVRHVPGGRFSTIVQQLKSGDTLEIELPFGSIALKPDDTRPLICVAGGTGFAPIKSVLDDLAKRKVQRDITLIWGARNPSGLYLPSAIDKWRKTWPQFRYIAAITDLGNVPADAHAGRVDDALRTHFGNLHDHVVHCCGSPSLVQSVRTAASDMGLLAQNFHADVFATSPTGSH
Protein: Sulfotransferase (EC 2.8.2.-) (A0MGZ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATLIIAPLDTHKLLIMFSFSITCISILYLLLGCCDSSENSQKLSLGWYDNNNNSRSALRGLEGGVDGNSSGREWMALRRLPHALIIGVKKGGTRALLEFLRLHPDIRALGAEPHFFDRHYSRGLGWYRSMMPKALNGQIVMEKTPRYFVTPETPGRIHAMSKNIKLIVVVRNPITRAISDYTQIISKTPDIPSFESLTFKNRSTGQIDALWSPLYIGLYAKHLERWLAYFPLSQIHFVHGERLISDPAGELGRVQDFLGLERIITDKHFYFNKTKGFPCLKKPEGSSKPHCLGKTKGRTHARIDPDVIQKLREFYQPHNLRFYRMAGMDFGWQ
Protein: Kinesin-like protein KIN-7D, mitochondrial (Mitochondria-targeted kinesin-related protein 2) (Q8W5R5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Kinesin-like protein KIN-10A
- Protein KINESIN LIGHT CHAIN-RELATED 2
- AT4G01090 protein
- SBP family protein
- Kinesin-like protein KIN-12C
- Kinesin-like protein KIN-14E
- Kinesin-like protein KIN-UB
- Kinesin-like protein KIN-14M
- Kinesin-like protein KIN-UA
- Protein CONSERVED ONLY IN THE GREEN LINEAGE 160, chloroplastic
Sequence:
MASSSSRTRSSRPPSPASSTSSSHLSNRLIPRSNSTSASSLITSAAGIASRSMTPSRTFSDSGLIGSGSFGIGSPVPYPSEELLGDPMDDTISSERDSISVTVRFRPLSDREYQRGDEVAWYPDGDTLVRHEYNPLTAYAFDKVFGPQATTIDVYDVAARPVVKAAMEGVNGTVFAYGVTSSGKTHTMHGDQESPGIIPLAIKDVFSIIQDTPGREFLLRVSYLEIYNEVINDLLDPTGQNLRVREDSQGTYVEGIKEEVVLSPGHALSFIAAGEEHRHVGSNNFNLLSSRSHTIFTLMVESSATGDEYDGVIFSQLNLIDLAGSESSKTETTGLRRKEGSYINKSLLTLGTVIGKLSEGKATHIPYRDSKLTRLLQSSLSGHGHVSLICTITPASSSSEETHNTLKFASRAKSIEIYASRNQIIDEKSLIKKYQREISTLKLELDQLRRGMLVGVSHEELMSLKQQLEEGQVKMQSRLEEEEEAKAALMSRIQKLTKLILVSTKNSIPGYSGDIPTHQRSLSAGKDDKFDSLLLESDNLGSPSSTLALLSEGSLGFNHRRSSSKLNDENSPGAEFTQGVMTPDEIDLLVEQVKMLAGEIAFSTSTLKRLVDQSVNDPENSQTQIQNLEREIHEKQRQMRGLEQLIIESGEASIANASLVEMQQKVMSLMTQCNEKSFELEIKSADNCILQEQLQEKCTENKELHEKVNLLEQRLNAVSSEKSSPSCSNKAVSGEYADELKKKIQSQEIENEELKLEHVQIVEENSGLRVQNQKLAEEASYAKELASAAAVELKNLASEVTKLSLQNTKLEKELAAARDLAQTRNPMNGVNRKYNDGARSGRKGRISSSRSSGDEFDAWNLDPEDLKMELQVRKQREVALESALAEKEFIEDEYRKKAEEAKRREEALENDLANMWVLVAKLKKDNGALPEPNGTDPGRELEKSQSHAVLKERQVSSAPRQPEVVVVAKTEETPKEEPLVARLKARMQEMKEKEMKSQANGDANSHICKVCFESPTAAILLPCRHFCLCKSCSLACSECPICRTKISDRLFAFPS
Protein: ETS translocation variant 4 (Polyomavirus enhancer activator 3) (Protein PEA3) (P28322)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. May play a role in keratinocyte differentiation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
Interaction partners:
- Nuclear receptor coactivator 3
- Transmembrane protease serine 2
- Solute carrier family 45 member 3
Sequence:
MERRMKGGYLDQRVPYTFCSKSPGNGSLGEALMVPQGKLMDPGSLPPSDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENSFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDSPRQIAIKSPAPGAPGQSPLQPFSRAEQQQSLLRASSSSQSHPGHGYLGEHSSVFQQPVDMCHSFTSPQGGGREPLPAPYQHQLSEPCPPYPQQNFKQEYHDPLYEQAGQPASSQGGVSGHRYPGAGVVIKQERTDFAYDSDVPGCASMYLHPEGFSGPSPGDGVMGYGYEKSLRPFPDDVCIVPEKFEGDIKQEGIGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELTGPAPPFGHRGGYSY
Protein: F5D14.30 protein (NAC domain containing protein 11) (Q9LQK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- HAD superfamily, subfamily IIIB acid phosphatase
- NAC domain protein
Sequence:
MVGSFLPPGFRFYPTDEELVGYYLHRRNEGLEIELEIIPLMDLYKFDPWELPEKSFLPNRDMEWFFFCHRDRKYQNGSRINRATKSGYWKATGKDRKIVCHSSSSSSSSSITGCRKTLVFYMGRAPFGGRTEWVMHEYRLFDNDTSQGSLNFKGDFALCRVIKRNEHTLKKCEIISPEVSDESLSNNVNNFCQASDLEKGSCDASNTRLSSPDFILESSFQGNSHSKTEEDSGFQVFTLPEFEYPLEVFADLNFDLEMEDPFMFDYHPEPHMNNEVMSHHIRG
Protein: Lipoyl synthase, mitochondrial (EC 2.8.1.8) (Lipoate synthase) (LS) (Lip-syn) (Lipoate-protein ligase) (AtLPLA) (Lipoic acid synthase) (Q9ZWT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03128, ECO:0000269|PubMed:24872381, ECO:0000269|PubMed:9808738}.
Interaction partners:
- Octanoyltransferase LIP2p2, chloroplastic
- Octanoyltransferase LIP2, mitochondrial
- Octanoyltransferase LIP2p, chloroplastic
- NifU-like protein 5, mitochondrial
- NifU-like protein 1, chloroplastic
- Biotin synthase, mitochondrial
- Lipoyl synthase, chloroplastic
- Protein BOLA1
- Iron-sulfur cluster assembly protein 1
- Protein BOLA2
Sequence:
MHSRSALLYRFLRPASRCFSSSSAVTPVTVTQSPKSLEALRARLANESPSLTDFIHGDTYSVEVGTKKKPLPKPKWMKESIPGGERYVQIKKKLRDLKLHTVCEEAKCPNLGECWSGGETGTATATIMILGDTCTRGCRFCNVKTSRTPPPPDPNEPNNVAEAIASWGVDYVVITSVDRDDLPDQGSGHFAETVQRLKFLKPEMLIEALVPDFRGDGGCVEKVSKSGLDVLAHNIETVEELQSFVRDHRANFKQSLDVLRMAKEYAPAGTLTKTSVMLGCGETPDQVVKTMEKVRAAGVDVMTFGQYMRPSKRHMPVAEYVTPDAFERYRLLGMEMGFRYVASGPMVRSSYKAGEYYIKSMIEADRVASPSTSP
Protein: Zinc finger CCCH domain-containing protein 14 (H0YJA2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|RuleBase:RU369058}. Note=Colocalizes with poly(A) RNA in nuclear speckles. {ECO:0000256|RuleBase:RU369058}.
Interaction partners:
Sequence:
XSDTNIFDSNVPSNKSNFSRGDERRHEAAVPPLAIPSARPEKRDSRVSTSSQESKTTNVRQTYDDGAATRLMSTVKPLREPAPSEDVIDIKPEPDDLIDEDLNFVQENPLSQKKPTVTLTYGSSRPSIEIYRPPASRNADSGVHLNRLQFQQQQNSIHAAKQLDMQSSWVYETGRLCEPEVLNSLEETYSPFFRNNSEKMSMEDENFRKRKLPVVSSVVKVKKFNHDGEEEEEDDDYGSRTGSISSSVSVPAKPERRPSLPPSKQANKNLILKAISEAQESVTKTTNYSTVPQKQTLPVAPRTRTSQEELLAEVVQGQSRTPRISPPIKEEETKGDSVEKNQGTQQRQLLSRLQIDPVMAETLQMSQDYYDMESMVHADTRSFILKKPKLSEEVVVAPNQESGMKTADSLRVLSGHLMQTRDLVQPDKPASPKFIVTLDGVPSPPGYMSDQEEDMCFEGMKPVNQTAASNKGLRGLLHPQQLHLLSRQLEDPNGSFSNAEMSELSVAQKPEKLLERCKYWPACKNGDECAYHHPISPCKAFPNCKFAEKCLFVHPNCKYDAKCTKPDCPFTHVSRRIPVLSPKPVAPPAPPSSSQLCRYFPACKKMECPFYHPKHCRFNTQCTRPDCTFYHPTINVPPRHALKWIRPQTSE
Protein: Olfactory receptor 10J1 (Olfactory receptor OR1-26) (Olfactory receptor-like protein HGMP07J) (P30954)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MLLCFRFGNQSMKRENFTLITDFVFQGFSSFHEQQITLFGVFLALYILTLAGNIIIVTIIRMDLHLHTPMYFFLSMLSTSETVYTLVILPRMLSSLVGMSQPISLAGCATQMFFFVTFGITNCFLLTAMGYDRYVAICNPLRYMVIMNKRLRIQLVLGACSIGLIVAITQVTSVFRLPFCARKVPHFFCDIRPVMKLSCIDTTVNEILTLIISVLVLVVPMGLVFISYVLIISTILKIASVEGRKKAFATCASHLTVVIVHYSCASIAYLKPKSENTREHDQLISVTYTVITPLLNPVVYTLRNKEVKDALCRAVGGKFS
Protein: Opioid growth factor receptor (OGFr) conserved domain-containing protein (Q38F25)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
- Ubiquitin-like domain-containing protein
Sequence:
MLRGTPVRRASLRYRRPYWMMFLKGVDNWKIYTVIQQPDHQRTEMLYQAWLGGLDRPYTRPKCMANQPLWLSKKRHMLRKERLDGPETPLEKYVLEWHKKFHSFQGTERPTPDDLHTALDLVERPLDLSYALQLLGQCRNLNNIRFAKETFLVFLEACLRVGRRDCAEYALEHAEPLGFWFIDEDHRRYLQGEQTWYKLSPLDNLYYPVEENAKLNEGRKPITRLSPATESPGSGTAISDGEPSTDVEGETTVDDEIAQLEAELAALEREGGGK
Protein: CDC42 effector protein (Rho GTPase binding) 4, isoform CRA_a (cDNA FLJ14479 fis, clone MAMMA1002143, highly similar to Cdc42 effector protein 4 (Binder of Rho GTPases 4)) (cDNA, FLJ92905, Homo sapiens CDC42 effector protein (Rho GTPase binding) 4(CDC42EP4), mRNA) (B2R6D8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MPILKQLVSSSVHSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLNSKAGEPDGESLDEQPSSSSSKRSLLSRKFRGSKRSQSVTRGEREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKGTSKLPKSLSSSPVKKANDGEGGDEEAGTEEAVPRRNGAAGPHSPDPLLDEQAFGDLTDLPVVPKATYGLKHAESIMSFHIDLGPSMLGDVLSIMDKEEWDPEEGEGGYHGDEGAAGTITQAPPYAVAAPPLARQEGKAGPDLPSLPSHALEDEGWAAAAPSPGSARSMGSHTTRDSSSLSSCTSGILEERSPAFRGPDRARAAVSRQPDKEFSFMDEEEEDEIRV
Protein: Tumor necrosis factor receptor superfamily member 13C (B-cell maturation defect) (B-cell-activating factor receptor) (BAFF receptor) (BAFF-R) (BLyS receptor 3) (CD antigen CD268) (Q9D8D0)
Organism: Mus musculus (Mouse)
Function: B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response.
Subcellular location: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 13B
- TNF receptor-associated factor 3
- Tumor necrosis factor receptor superfamily member 5
- Tumor necrosis factor receptor superfamily member 13B
- TNF receptor-associated factor 2
- CD40 ligand
- Tumor necrosis factor receptor superfamily member 3
- B-lymphocyte antigen CD19
- Tumor necrosis factor receptor superfamily member 17
- Tumor necrosis factor ligand superfamily member 13
Sequence:
MGARRLRVRSQRSRDSSVPTQCNQTECFDPLVRNCVSCELFHTPDTGHTSSLEPGTALQPQEGSALRPDVALLVGAPALLGLILALTLVGLVSLVSWRWRQQLRTASPDTSEGVQQESLENVFVPSSETPHASAPTWPPLKEDADSALPRHSVPVPATELGSTELVTTKTAGPEQ
Protein: Exocyst complex component 2 (Exocyst complex component Sec5) (Q96KP1)
Organism: Homo sapiens (Human)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Midbody, Midbody ring {ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18756269}. Note=Recruitment to the midbody does not require RALA, nor RALB (PubMed:18756269). Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214). {ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18756269}.
Interaction partners:
- Exocyst complex component 7
- Exocyst complex component 6
- Exocyst complex component 4
- Exocyst complex component 1
- Ras-related protein Ral-B
- Exocyst complex component 3
- Ras-related protein Ral-A
- Exocyst complex component 8
- Exocyst complex component 5
- Serine/threonine-protein kinase TBK1
Sequence:
MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGRGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKSKFSQKDLEMLFHGMSADFTSENFSAAWYLIENHSNTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIERNIQKGDYDVVINDYEKAKSLFGKTEVQVFKKYYAEVETRIEALRELLLDKLLETPSTLHDQKRYIRYLSDLHASGDPAWQCIGAQHKWILQLMHSCKEGYVKDLKGNPGLHSPMLDLDNDTRPSVLGHLSQTASLKRGSSFQSGRDDTWRYKTPHRVAFVEKLTKLVLSQLPNFWKLWISYVNGSLFSETAEKSGQIERSKNVRQRQNDFKKMIQEVMHSLVKLTRGALLPLSIRDGEAKQYGGWEVKCELSGQWLAHAIQTVRLTHESLTALEIPNDLLQTIQDLILDLRVRCVMATLQHTAEEIKRLAEKEDWIVDNEGLTSLPCQFEQCIVCSLQSLKGVLECKPGEASVFQQPKTQEEVCQLSINIMQVFIYCLEQLSTKPDADIDTTHLSVDVSSPDLFGSIHEDFSLTSEQRLLIVLSNCCYLERHTFLNIAEHFEKHNFQGIEKITQVSMASLKELDQRLFENYIELKADPIVGSLEPGIYAGYFDWKDCLPPTGVRNYLKEALVNIIAVHAEVFTISKELVPRVLSKVIEAVSEELSRLMQCVSSFSKNGALQARLEICALRDTVAVYLTPESKSSFKQALEALPQLSSGADKKLLEELLNKFKSSMHLQLTCFQAASSTMMKT
Protein: Condensin complex subunit capg-1 (G5EFJ4)
Organism: Caenorhabditis elegans
Function: Member of two distinct condensin I complexes, the condensin I complex and the condensin I-like dosage compensation complex. The condensin I complex is required for conversion of interphase chromatin into mitotic-like condensed chromosomes and for chromosome segregation in meiosis and mitosis. As a member of the condensin I complex, further controls crossover number and distribution in meiosis by restricting double strand break formation, probably by influencing higher-order chromosome structure. Regulatory subunit of the condensin I-like dosage compensation complex that associates specifically with hermaphrodite X chromosomes to reduce their gene transcription during interphase, possibly through chromatin reorganization.
Subcellular location: Chromosome {ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23684975}. Note=During meiosis and mitosis, localizes to condensed chromosomes in both sexes (PubMed:19119011). Localizes to the spindle midzone in between separating chromosomes during anaphase and to the midbody during cytokinesis (PubMed:23684975). During interphase, localizes specifically to X chromosomes in hermaphrodites after the onset of dosage compensation (PubMed:19119011). {ECO:0000269|PubMed:19119011, ECO:0000269|PubMed:23684975}.
Interaction partners:
- Chromosome condensation protein dpy-27
- Condensin complex subunit dpy-26
- Condensin complex subunit 1
- Mitotic chromosome and X-chromosome-associated protein mix-1
- Structural maintenance of chromosomes protein 4
- CAP-G condensin subunit
- Condensin-2 complex subunit kle-2
- Condensin-2 complex subunit hcp-6
- Kinetochore protein ndc-80
- Zinc finger protein sdc-3
Sequence:
MPPKKRIRGPKLPALREEKSTGTDVASDESFNESADFLNNEELNNDQNDAENTVLSEGVSTLRINENMTKEDRACISAALFIKKRVVESIRTVFQSRDDINDEIHTSSRKLIAAFKKADQNRKKKVDLMKVFLDEIDVRLSMIIEEVTVPEHRARVFKLIAVTITEIQAFKLPSDLLDFIINFINTWGHSDNVAARINTTCFISYIFETGKRYLTTEGEYSGFEVKIAAKMFLQLKRALLDKEQTARVPAIRGLGFLQEIPIPSNWPVDAMKHSPRELLLRSCRDTAWECRLVAVQSMVPLETDVRLLSDIVYYDKCLNVRVAALEQFSNLRPNKHVREKIEMLDLCLKDHEVNIRDAAKEVLKNWVRNLSTRWSESQKSKDSNDVVILNSNSESTTGEENKMKGYILAAQALTLLWLTGALETLEGHSNLRRLITHTLDVIRQMYVCQADPINTFAEVLISDLREKMKSSAVPIITKSTVGSILDDSELADTQDPSTNRAMIFFWRCLVDYISDRKRNDADKINAMSRFVSPLRTMVEHVEKILVRVKNLDVYPNISQRADYEDHTFVLQMSIVENIICVMRHAPTDQPGVDAYKQMLISMLMNVFYQKKVIDLIVQELAQFYKEDPNALFTLFNDRIEEMRSKYKSGQFPVIENSVPVGETKVRKDLEEETRKTGRRTISDKDGIAVIDLYELKVLNALLKTGILLGWSTTYQNRYNNKLREGISSKDLSTRVLCTECIGIGAIYDYDQAENTLREMMKSFNTQDEPVQCSLIAALTDIQIEHGDQVDALFSWNSKQPNFAVFLSDIVVNAHVSGECETMLRAVEAISRLFLNTKIDPNQQKWQRTMVTLMTRASYAITNRFSAKVRSTIIVMLKFFCSINKNNQLLLIKSFHNFFDMWANSTTPERLTENRHEMVTKLKRCAATFVALTRHSTLPLEEQKKCKPTHVDLVDDIFHEMAGAPDSTSVDYYICALNFVEYQSLSRSALTKIHGDLESYIFLHELDGDKHRYNELRKAHRKIAKILGLNEDEIEEVPSKTDLRKEAAPSKTNKRNANLISTDIAVDNDVNMEEDDKPGPSRPATVRKPRAPRATPASATKKKPLVEEDALEILKSPPRNTKKPPSRPTTATRPTAVAARTAPPRSARKLRSEK
Protein: PUM-HD domain-containing protein (Q9U2G4)
Organism: Caenorhabditis elegans
Interaction partners:
- Chondroitin proteoglycan 1
- Embryonic mRna
- C-type lectin domain-containing protein 87
- C-type lectin domain-containing protein 91
- E3 ubiquitin-protein ligase marc-3
- G2/mitotic-specific cyclin-B
- CCCH-type zinc finger protein oma-2
- Uncharacterized protein
- Pumilio domain-containing protein 5
- RING-type domain-containing protein
Sequence:
MSQNTGSSNLGRYYESPPTATEARGTFGGCFNANSSTNIWTPNRKVDSSMGFRSSSPTPQSAWAPNRQGFGGQFSKWRTSTPMTTPARYPQQAVRLIDLENNASFSKSLNSTTRSHKCTLPIWAGDGEGNVSDSVTLQDVLANDALVEFATDKNGCRFLQEHYPTENDNDVHQKLFRKLVEDRAIFLSLCSNMFGNFFVQRVLECSNTEEQEILTEHLATDLYNLCLDKSACRVIQLAIQKLDVHLATRLSLELRDTHLVRLSIDQNGNHVIQKIVKTLPVSSWTFLVDFFADDDNLIHVCQDKYGCRVIQSTVETLSTDQYAQCYQHRVILLRSLMAGVTRNCTQLASNEFANYVVQHVIKCGDALAVYRDIIIEQCLLQNLLSMSQEKYASHVVEVAFECAPYRLVAEMMNEIFEGYIPHPDTNRDALDILLFHQYGNYVVQQMIQTCVLGQNARDQKQSEMYGMWLEKIHGRVMRNAHRLERFSSGKKIIEALQSMSLY
Protein: Single-strand-selective monofunctional uracil-DNA glycosylase 1 (D6RA78)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEVSGARFWGFFRNLCGQPEVFFHHCFVHNLCPLLFLAP
Protein: Multifunctional non-homologous end joining DNA repair protein LigD (NHEJ DNA repair protein D) (Mt-Lig) (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase/primase); 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase) (PE); DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP])] (P9WNV3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: With Ku forms a non-homologous end joining (NHEJ) repair enzyme which repairs DNA double-strand breaks (DSB) with reduced fidelity. Recognizes, processes and reseals DSBs, including repairs on incompatible DSB which require 3'-resection, gap filling and ligation. Anneals the 3' overhanging strands from opposing breaks to form a gapped intermediate, which then can be extended in trans by using the termini as primers for extension of the annealed break. Binds to the recessed 5'-phosphate moiety of the downstream DNA strand forming a stable synaptic complex even when the 3'-protruding ends of the template DNA strands are not complementary. Has numerous activities; gap filling copies the template strand, and prefers a 5'-phosphate in the gap and rNTPS, DNA-directed DNA or RNA polymerase on 5'-overhangs, terminal transferase (extending ssDNA or blunt dsDNA in a non-templated fashion, preferentially with rNTPs), DNA-dependent RNA primase (synthesizes short RNAs on unprimed closed ssDNA) and 3'- to 5'-exonuclease on ssDNA. Isolated Pol domain (and presumably the holoenzyme) is able to form complexes between 2 noncompatible protruding 3'-ends DNA ends via microhomologous DNA strands, in a end-bridging function to which it adds a templated nucleotide. Minimal primer length is 2 nucleotides.
Interaction partners:
- Non-homologous end joining protein Ku
- Possible bifunctional enzyme: 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase
- DNA polymerase I
- DNA ligase A
- Putative lipoprotein LppK
- Beta sliding clamp
- Protein RecA
- 5'-3' exonuclease
- D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Probable exodeoxyribonuclease III protein XthA
Sequence:
MGSASEQRVTLTNADKVLYPATGTTKSDIFDYYAGVAEVMLGHIAGRPATRKRWPNGVDQPAFFEKQLALSAPPWLSRATVAHRSGTTTYPIIDSATGLAWIAQQAALEVHVPQWRFVAEPGSGELNPGPATRLVFDLDPGEGVMMAQLAEVARAVRDLLADIGLVTFPVTSGSKGLHLYTPLDEPVSSRGATVLAKRVAQRLEQAMPALVTSTMTKSLRAGKVFVDWSQNSGSKTTIAPYSLRGRTHPTVAAPRTWAELDDPALRQLSYDEVLTRIARDGDLLERLDADAPVADRLTRYRRMRDASKTPEPIPTAKPVTGDGNTFVIQEHHARRPHYDFRLECDGVLVSWAVPKNLPDNTSVNHLAIHTEDHPLEYATFEGAIPSGEYGAGKVIIWDSGTYDTEKFHDDPHTGEVIVNLHGGRISGRYALIRTNGDRWLAHRLKNQKDQKVFEFDNLAPMLATHGTVAGLKASQWAFEGKWDGYRLLVEADHGAVRLRSRSGRDVTAEYPQLRALAEDLADHHVVLDGEAVVLDSSGVPSFSQMQNRGRDTRVEFWAFDLLYLDGRALLGTRYQDRRKLLETLANATSLTVPELLPGDGAQAFACSRKHGWEGVIAKRRDSRYQPGRRCASWVKDKHWNTQEVVIGGWRAGEGGRSSGVGSLLMGIPGPGGLQFAGRVGTGLSERELANLKEMLAPLHTDESPFDVPLPARDAKGITYVKPALVAEVRYSEWTPEGRLRQSSWRGLRPDKKPSEVVRE