wanglab/gogpt-training-data huggingface dataset:
Protein: Ankyrin repeat and KH domain-containing 1 (Ankyrin repeat and KH domain-containing protein 1) (A0A0R4IUB2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQDAVAGTAMLTDGFEDEIDSVTPRSPALGMGVGATPGAGLGGLGIGVGGKKVRLFGEAGGPTTDRLDFKLTAAAVLSSGPGSGSDEDEVSEVESFILDQEDLDNPVLKTASELLLSSAADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAENTLNASQADNRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAASGGYVDIVKLLLVHGADVNAQSSTGNTALTYACAGGFLDVVKVLLKEGANIEDHNENGHTPLMEAASAGHVEVARVLLEYGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQTGADLEHESEGGRTPLMKAARAGHLCTVQFLISKGANVNRATANNDHTVVSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTNVVSYLLDYPNNILSVPAPDLSQLTPPSHDTSQAPRVPFQALAMVVPPQEPDRVPSTIPTPPPVTSKGASKQRLSSLQSNSVASGGLDADLLPPFHPYQPLECIVEETEGKLNELGQRISAIEKAQLQSLELIQGEPLTKDKIEELKKSREEQVQKKKKILKELQKVERQLQLKTQQQFTKEYMETKGLKEELGQAAGGIHEKEDHRPTPTNEEDEDEEEDEDDIDCAKLPQVNTILQPPPPPPPQNQVLQSPPLQTSFVPIQPLTPQLSTDFSSAEYPGSSSPDLQRVLLGQPLTGLGPGLLAQASDGLMVATPAQTLTDTLDDIMAAVNSRVPVVNTTTSPSPQPSAQTPINTASPPSMLPLYPSVDIDAHTESNHDTALTLACAGGHEELVSVLIARGANIEHRDKKGFTPLILAATAGHVGVVEILLDKGGDIEAQSERTKDTPLSLACSGGRQEVVELLLLRGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSKLGISPLMLAAMNGHVPAVKLLLDMGSDINAQIETNRNTALTLACFQGRAEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSSRDTALTIAADKGHYKFCELLISRGAHIDVRNKKGNTPLWLAANGGHFDVVQLLVQAGADVDAADNRKITPLMAAFRKGHVKVVQYLVKEVNQFPSDIECMRYIATIADKELLKKCHQCMETIVKAKDQQAAEANKNASILLKELDLEKSREESKKQALAAKREKRKEKRKKKKEEQKRKLEEEEAKVKEVSFEMLDQKEDSAEEAEVPIEPPSATTTTTIGISATSATFTNSFGKKRANVATTPSTNRKNKKNKTKDTPSEPIILQDPQVALAQQKADKNKIHGEPRGGGATGGTSDSDNLDSTDCNSESSNGSKCQELTDLPSSSSSCSSAPTVFVGSNQPHFANEKRHGLSLPGSREEKVMVSISKPQIKSHEISDLTPSSLPTSFKTISLPVTSPNSKMNPLSPKRTQKREEGWKEVVRRSKKLSVPASVVSRIMGRGGCNITAIQDVTGAHIDVDKQKDKNGERMITIRGGTESTRYAVQLINALIQDPAKELEDLIPRNHIRPPGANTKISSTYTTSTGATSTTAASSKGLPSVVPSANVSFQSTTNFTAQQASKLGKSMASGVRPPFVSLPPLAYAHPQLALLAAQTMNQIRHPRLPMAQFGGTFSPSPNTWGPFPVRPVSPGSANSSPKHSGNSAPRLVSTTPAHIDHPTAPVSSTSTPTASTSSPTSTAPANTPTPSSVRKQLFSSEPKSLAGIAVVTTSSNAPSAQIAPSPISCAPTTPTTPPPSSAATAATPQHPPKPEPASLSTPAKEKPVTEIAAPTAGAPSDGPSASAPLHFTSSPSGPSMLPPQPESRQTLPSHFPPSTESSSSSSSQPGSSHPVTRLPPPTSSNTITNTSSTLPHYGSPTAPGVSPRMQPPTPYYPMAPGALQEQQSVFVPPGATQETLKQQPPPQPTLAPAGMPPPSLPMSSTMGMINGSQMHLHSGKAQLPPNFGPAALFNHFSSIFDNNQVGNNQVWGACHLPARTPPEQPYSGTTNAYIGGMGQMESVMPPPDGSKAPGYRCSTQRMVSSPIGIHPMDGSMSSSTALTSFTTSISASPVFLPGPAPVGTPSFSRQHFSPHPWSASTSCESPVPSVSSGASSPLCTSTVTPALIQAKPSSSNQQDRKVPPPIGTERLARIRQTGSVNHTMLPTSYTPPVGQGGIWSFGVGSASETMSGWSQPLMGGGPVMHQQMQEPSAFSQHQAMERDDTGIVAPSNTFHQPLPTNFMDFPKGLPMSMYGGTMIPPHPQMAEGPGGPVYNGLHTSDPAWNPILKVVPNSAENADPQQVWPGTWAPHVGNVHLNHVN
Protein: D-glycerate 3-kinase, chloroplastic (AtGLYK) (EC 2.7.1.31) (Q944I4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the concluding reaction of the photorespiratory C2 cycle, an indispensable ancillary metabolic pathway to the photosynthetic C3 cycle that enables land plants to grow in an oxygen-containing atmosphere.
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:29129375}. Note=Expressed in the light. {ECO:0000269|PubMed:29129375}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:29129375}. Note=Expressed in the dark. {ECO:0000269|PubMed:29129375}.
Interaction partners:
- Glycerate dehydrogenase HPR, peroxisomal
- D-3-phosphoglycerate dehydrogenase 2, chloroplastic
- Glyoxylate/hydroxypyruvate reductase A HPR2
- D-3-phosphoglycerate dehydrogenase 1, chloroplastic
- D-3-phosphoglycerate dehydrogenase 3, chloroplastic
- Glyoxylate/hydroxypyruvate reductase HPR3
- Ribulose bisphosphate carboxylase small subunit 3B, chloroplastic
- Ribulose bisphosphate carboxylase small subunit 1A, chloroplastic
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Phosphoglycerate kinase 3, cytosolic
Sequence:
MAVAISGSSLISSTLQHYNNRIYIRDYPIPCHSSNPICNSFNFKRRSFSPSSPKFNDHVVNPSSSYLSSKLSPIRTHSSFAACGCSWIQDNSMVHDYATTTNGTSKRCSALPTTNTVDVSSVSDLFEFICSGPLVNKIGITPQRVGQSIDKWLLYGSQLCRLFQLNELKLTIPQKARLYHYYIPVFIWCEDQIALHNSKFKDGDDVPPLVIGFSAPQGCGKTTLVFALDYLFKTTKKKSATISVDDFYLTAEGQAELRKKNPGNALLEYRGNAGSHDLKLSVETLEALSKLTKEGLKMKVPRYNKSAYSGRGDRADSSTWPEVEGPLSVILFEGWMLGFKPLPADVVKAVDPQLEVVNKNLEAYYDAWDKYIDAWVVIKIQDPSYVYRWRLQAEIAMRQDGQAGMSDEEVNDFVSRYLPAYKAYLPTLYAEGPSGSDPDRVLAIDIDEERNPILAN
Protein: 2-isopropylmalate synthase 1, chloroplastic (EC 2.3.3.13) (Methylthioalkylmalate synthase-like 4) (Q9LPR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). Involved in Leu biosynthesis, but does not participate in the chain elongation of glucosinolates.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- 3-isopropylmalate dehydratase small subunit 2
- 3-isopropylmalate dehydratase small subunit 1
- 3-isopropylmalate dehydratase small subunit 3
- Dihydroxy-acid dehydratase, chloroplastic
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- Branched-chain-amino-acid aminotransferase 3, chloroplastic
- Branched-chain-amino-acid aminotransferase 6
- Acetolactate synthase small subunit 1, chloroplastic
- Branched-chain-amino-acid aminotransferase 5, chloroplastic
- Branched-chain-amino-acid aminotransferase 1, mitochondrial
Sequence:
MASSLLRNPNLYSSTTITTTSFLPTFSSKPTPISSSFRFQPSHHRSISLRSQTLRLSCSISDPSPLPPHTPRRPRPEYIPNRISDPNYVRVFDTTLRDGEQSPGATLTSKEKLDIARQLAKLGVDIIEAGFPAASKDDFEAVKTIAETVGNTVDENGYVPVICGLSRCNKKDIERAWDAVKYAKRPRIHTFIATSDIHLEYKLKKTKAEVIEIARSMVRFARSLGCEDVEFSPEDAGRSEREYLYEILGEVIKAGATTLNIPDTVGITLPSEFGQLITDLKANTPGIENVVISTHCQNDLGLSTANTLSGAHAGARQMEVTINGIGERAGNASLEEVVMAIKCRGDHVLGGLFTGIDTRHIVMTSKMVEEYTGMQTQPHKAIVGANAFAHESGIHQDGMLKHKGTYEIICPEEIGLERSNDAGIVLGKLSGRHALKDRLTELGYQLDDEQLSTIFWRFKTVAEQKKRVTDADIIALVSDEVFQPEAVWKLLDIQITCGTLGLSTATVKLADADGKEHVACSIGTGPVDSAYKAVDLIVKEPATLLEYSMNAVTEGIDAIATTRVLIRGSNKYSSTNAITGEEVQRTFSGTGAGMDIVVSSVKAYVGALNKMMDFKENSATKIPSQKNRVAA
Protein: L-tyrosine decarboxylase (TDC) (EC 4.1.1.25) (Levodopa decarboxylase) (L-dopa decarboxylase) (EC 4.1.1.-) (Q838D6)
Organism: Enterococcus faecalis (strain ATCC 700802 / V583)
Function: Catalyzes the decarboxylation of L-tyrosine to produce tyramine. Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecalis.
Interaction partners:
- Amino acid permease family protein
- Na+/H+ antiporter
- Putative agmatine deiminase
- Aminotransferase
- Gelatinase
Sequence:
MKNEKLAKGEMNLNALFIGDKAENGQLYKDLLIDLVDEHLGWRQNYMPQDMPVISSQERTSESYEKTVNHMKDVLNEISSRMRTHSVPWHTAGRYWGHMNSETLMPSLLAYNFAMLWNGNNVAYESSPATSQMEEEVGHEFAHLMSYKNGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVKPELVAGKSDWELLNMPTKEIMDLLESAEDEIDEIKAHSARSGKHLQAIGKWLVPQTKHYSWLKAADIIGIGLDQVIPVPVDHNYRMDINELEKIVRGLAEEQIPVLGVVGVVGSTEEGAVDSIDKIIALRDELMKDGIYYYVHVDAAYGGYGRAIFLDEDNNFIPYEDLQDVHEEYGVFKEKKEHISREVYDAYKAIELAESVTIDPHKMGYIPYSAGGIVIQDIRMRDVISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHVLPLNVAGYGKLIGASIEGSHHFYNFLNDLTFKVGDKEIEVHTLTHPDFNMVDYVFKEKGNDDLVAMNKLNHDVYDYASYVKGNIYNNEFITSHTDFAIPDYGNSPLKFVNSLGFSDEEWNRAGKVTVLRAAVMTPYMNDKEEFDVYAPKIQAALQEKLEQIYDVK
Protein: Plant intracellular Ras-group-related LRR protein 9 (Q8VYG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction. PIRL9 acts redundantly with PIRL1 in the differentiation of microspores into pollen.
Interaction partners:
- N-lysine methyltransferase
- Pyrroline-5-carboxylate reductase
- At5g63130
- F-box protein At3g17710
- Pectinesterase QRT1
- Immune-associated nucleotide-binding protein 4
- Calmodulin-like protein 2
- Eukaryotic translation initiation factor 4B3
- Aspartyl protease family protein At5g10770
- At2g19340
Sequence:
MAAEPNPKNFPVLSYVLARLPSFTAKSPSSSVPPFDIEQPPPSSSSSSIEIVTQMPHLTQPDVLASMTSAISDVAETRSILRTLGPRPDHESVDKARAKLSEIESFLSESFEDIALTDAAAKDEKRRQEMDQEKTWCESILKLDEVHASYEKLLKEAEERLVRIYESAEKNAAEDEENVAAVEVNEEVVGILQHASANPVDRVDLSGRKLRLLPEAFGRIQGLLVLNLSNNKLESIPDSIAGLHSLVELDVSTNSLETLPDSIGLLSKLKILNVSTNKLTSLPDSICRCGSLVILDVSFNRLTYLPTNIGPELVNLEKLLVQYNKIRSFPTSIGEMRSLKHLDAHFNELNGLPDSFVLLTNLEYLNLSSNFSDLKDLPFSFGELISLQELDLSNNQIHALPDTFGTLDSLTKLNVDQNPLVVPPEEVVKEGVEAVKTYMGQRRISMLEEEEKKKMEEEMEQANAGWLTRTTSKLKTYVADVSEYLGSNSPRDPYLERQL
Protein: S-adenosyl-L-methionine-dependent methyltransferase (EC 2.1.1.-) (P95073)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Alcohol dehydrogenase B
- tRNA
- S-adenosyl-L-methionine-dependent methyltransferase
- D-3-phosphoglycerate dehydrogenase
Sequence:
MPRAHDDNWDLASSVGATATMVAAGRALATKDPRGLINDPFAEPLVRAVGLDFFTKLIDGELDIATTGNLSPGRAQAMIDGIAVRTKYFDDYFRTATDGGVRQVVILAAGLDARAYRLPWPAGTVVYEIDQPQVIDFKTTTLAGIGAKPTAIRRTVYIDLRADWPAALQAAGLDSTAPTAWLAEGMLIYLPPDPRTGCSTTAPNSVLRAARSLPNLSRALWISTQAGYEKWRIRFASTAWTSTWRRWCIPANAATSSTTCAPRAGTLRAQCGPTYSGAMVCPFPPHTTTIRSAKSSSSAVV
Protein: Inner membrane protein YnjF (P76226)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YnbA
- Uncharacterized ABC transporter ATP-binding protein YnjD
- Inner membrane ABC transporter permease protein YnjC
- Protein YnjB
Sequence:
MLDRHLHPRIKPLLHQCVRVLDKPGITPDGLTLVGFAIGVLALPFLALGWYLAALVVILLNRLLDGLDGALARRRELTDAGGFLDISLDFLFYALVPFGFILAAPEQNALAGGWLLFAFIGTGSSFLAFAALAAKHQIDNPGYAHKSFYYLGGLTEGTETILLFVLGCLFPAWFAWFAWIFGALCWMTTFTRVWSGYLTLKSLQRQ
Protein: Methyl-CpG-binding protein 2 (MeCp-2 protein) (MeCp2) (A8WIP2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038006}. Note=Colocalized with methyl-CpG in the genome. {ECO:0000256|PIRNR:PIRNR038006}.
Interaction partners:
Sequence:
MAAAESGEERLGEDKNEDQEGSKDKTQKHKKSKKERHDVEKLETTVSVPPPPSLFTQRDVGQQAEAGKSEPIDPEVGAALSAPESSASAKQRRSVIRDRGPMYEDPSLPQGWTRKLKQRKSGRSAGKFDVYLINPEGKAFRSKVELMAYFQKVGDTITDPNDFDFTVTGRGSPSRREKRPPKKPKMVKPSGRGRGRPKGSGKVRQATEGVAVKRVIEKSPGKLLVKMPFVAPKTEPGAPLGQAPVAKARRGRKRKSEQDPPSTPKKRGRKPATVSQSTVGTGSAAAYAAAAILTAEAKKKALKESSAKPVQERALPIKKRKTRETLEELEASTTSATETFEKRLTASTVTPTGEEAETGQKPHKHPSRKHKEADPGSSSSGTTASGVAPKSHKKRDQRGQHFKHHHHHHHHHHQHQHLQASTPSTYTPQAHQLSLGHSTHGGLENEPQDLSTSRPKAEHVACREEARTGSSSSRDSQNASKMASMTVTGESKELRDIVPPSAVPRPSREETVESRTPVSEPVS
Protein: Uncharacterized protein (Q388K8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRTFLRLGGGGGELFPTSKAAAHLEPQWVMERRPPPPPGPGKCYVTVHKTGTKSGSKWQLLQPHIHTLEVISMDSPPPHKLDVPRPTARAAASFVAGVKSSLEHARKQTTSVSGIAAANIAEKKRCEARMKTRDYAEGKRPVRERPGWEATTDVVELSEWLHKRVNDHRKIVSDNSNGYEREYTPWEKKPVPPEIKKQW
Protein: Listeriolysin O (LLO) (Thiol-activated cytolysin) (P13128)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: A cholesterol-dependent pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome-independent degradation of UBE2I (the SUMO-conjugating enzyme UBC9) and a proteasome-dependent degradation of some sumoylated proteins. Finally, is necessary and sufficient for spacious Listeria-containing phagosomes (SLAPs) formation, suggesting a role for listeriolysin O in promoting L.monocytogenes replication in vacuoles, leading to persistent infection. Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis.
Subcellular location: Secreted {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}. Host membrane {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}; Multi-pass membrane protein {ECO:0000269|PubMed:3110067}. Host cell membrane {ECO:0000269|PubMed:3110067}; Multi-pass membrane protein {ECO:0000269|PubMed:3110067}. Note=Secreted as soluble protein that then inserts into the host membrane and forms pores formed by transmembrane beta-strands. {ECO:0000305|PubMed:24751541}.
Interaction partners:
- Zinc metalloproteinase
- 1-phosphatidylinositol phosphodiesterase
- Internalin B
- Phospholipase C
- Actin assembly-inducing protein
- Internalin A
- Listeriolysin regulatory protein
- Uncharacterized protein Lmo0206
- Foldase protein PrsA 2
- Serine/threonine phosphatase stp
Sequence:
MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEVNYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNKVDNPIE
Protein: E3 ubiquitin-protein ligase CCNB1IP1 homolog (EC 2.3.2.27) (RING finger-containing protein HEI10) (OsHEI10) (RING-type E3 ubiquitin transferase HEI10) (I6PL68)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Ubiquitin E3 ligase required for class I crossover (CO) formation during meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:22792078}. Chromosome {ECO:0000269|PubMed:22792078}. Note=Dynamic localization on the meiotic chromosomes. Initially appears as distinct foci. Later observed along the chromosomes and finally restrict to prominent foci that specially localize to chiasma sites. Extends along the chromosome in the wake of synapsis. {ECO:0000269|PubMed:22792078}.
Interaction partners:
- DNA mismatch repair protein MSH5
- Protein SHORTAGE IN CHIASMATA 1 homolog
Sequence:
MKCNACWRELEGQAVSTTCGHLLCTEDAKKILSNDAACPICDQVLSKSHMRPVDTNPNDDWTNMSMAGVSPQILMKSAYRSVMFYIGQKELEMQYKMNRIVGQCRQKCELMQAKFTEKLEEVHTAYQKMAKKCQLMEQEVENLSRDKQELQEKFAEKSRQKRKLDEMYDQLRSEYESAKRSAIQPANNYFPRAQPDLFSGVPNIMDSSDPLRQGLAGLPETPGRRDEGWAPPPRQRRSTSGPFELSAGSPAHNAAPPVDIRPRQPARPVFGTAMNNTSAALRNMIISPVKRPQLSRNRPHMFT
Protein: Fermitin family homolog 3 (Kindlin-3) (MIG2-like protein) (Unc-112-related protein 2) (Q86UX7)
Organism: Homo sapiens (Human)
Function: Plays a central role in cell adhesion in hematopoietic cells. Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for integrin-mediated platelet adhesion and leukocyte adhesion to endothelial cells. Required for activation of integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By similarity).
Subcellular location: Cell projection, podosome {ECO:0000250}. Note=Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells. {ECO:0000250}.
Interaction partners:
- Integrin beta-3
- Integrin alpha-IIb
- Integrin beta-2
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Talin-1
- Filamin-binding LIM protein 1
- RAS guanyl-releasing protein 2
- Pleckstrin
- Talin-2
- Fermitin family homolog 1
Sequence:
MAGMKTASGDYIDSSWELRVFVGEEDPEAESVTLRVTGESHIGGVLLKIVEQINRKQDWSDHAIWWEQKRQWLLQTHWTLDKYGILADARLFFGPQHRPVILRLPNRRALRLRASFSQPLFQAVAAICRLLSIRHPEELSLLRAPEKKEKKKKEKEPEEELYDLSKVVLAGGVAPALFRGMPAHFSDSAQTEACYHMLSRPQPPPDPLLLQRLPRPSSLSDKTQLHSRWLDSSRCLMQQGIKAGDALWLRFKYYSFFDLDPKTDPVRLTQLYEQARWDLLLEEIDCTEEEMMVFAALQYHINKLSQSGEVGEPAGTDPGLDDLDVALSNLEVKLEGSAPTDVLDSLTTIPELKDHLRIFRIPRRPRKLTLKGYRQHWVVFKETTLSYYKSQDEAPGDPIQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYARWMAGCRLASKGRTMADSSYTSEVQAILAFLSLQRTGSGGPGNHPHGPDASAEGLNPYGLVAPRFQRKFKAKQLTPRILEAHQNVAQLSLAEAQLRFIQAWQSLPDFGISYVMVRFKGSRKDEILGIANNRLIRIDLAVGDVVKTWRFSNMRQWNVNWDIRQVAIEFDEHINVAFSCVSASCRIVHEYIGGYIFLSTRERARGEELDEDLFLQLTGGHEAF
Protein: Hybrid signal transduction protein dokA (Q869S5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Part of the osmoregulatory pathway which leads to the increase of intracellular cAMP concentration in response to hyperosmotic stress. Thought to negatively regulate the rdeA-regA pathway by acting as a phosphatase towards the HPt protein rdeA. Has probably no histidine kinase activity.
Interaction partners:
- Phosphorelay intermediate protein rdeA
Sequence:
MSSPHIELHSQRTLSPQPSSNNFELTGNKSCALSASLNGSIDDLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNDGDKNDKKLLIITNAPTPPLTPPQPTKTQQTLLELNQKFQEQQQQQQQQQQLQKQNKQQQSQKQQEEPPSSQQEEPPLSQQQQEQEQEQEQEQEQEEQSKQKIEGKGGGGEEEECEGGGGGEGEGEEQFKEGDEEEHEGIEIDPNLPTTGYTGKRRSSLQINEASPKLIQTPSVDRTLCILDSLPCPIFQIGIIENTENGNITLTGFANERLTTLLSCSSNLLVDSLKSIPSPHYNTVPSLESCNSIPINNLAPGLLPNTDPTKILDPYISLYNKKQLKERYSNNNNNTNTNNNNNNNNNNNNNNNNNNNNNNNDTTTTTTTTTTTTTTTTTTTTTTTTNESDNNNNNNNNNNNNNNNNNNNNNNNEEIKQNTKEGEEILHESTNSTGTGNSISRPNSILQCILDSFHEQKTITEKVLLSNFLIRQQYKSRATIKPFPDGCICIFEYIENINLNYQQPPTSLNDRINSTNKLTNEMELLSLSPDSNHQHVQKLHNHNHNHHNHNHNNTTQRASSTDSPFIHSVSANSLSSMSSNSSVTSACASLSSNSSSNSNNNSNNASSSNCSSNANSNNTNSSSSNCCCCCNNNNNNNTSSTSSTISSASSTKSKSYLHQQHKNSKVYSTLLNSFENLSFLLKSTPIIIWRADHNGEMVFFKKSDEIPIDEKKVVGNNFQDFLQWVPQTYRTNFQEMFQNSLKCGKIFEFLFWFQTPQNYVQLFKIAGYPIFHIDGKDCIASKRYLIGWLGVTYNYLINDGAEISIKGSANLDSMYEKFKIIYEMPNIERTKLTNNGISSGGDITNANNNGGSSESSNKILEKKKHLISEAEKECFLKCKETYNILFKLSLLGVMFSTFKGIILDANDMLLQTIGYTRGDLENGKIDWMLLTPPEHFEISARALQELKAKRWCQPIEKAYIHKSGKRVPVLITSAMIDGSTEQCITFVFDLSRYRQAEMAAIEATRLKTQFITNISHELRTPCHGIVGMSQLLLDSQLTNTQRDNIDSIKRSTDSLISLINDILDFSKLEYGKVTLENESFELLPMIEEVLDSQATAANRKGIDLIFVMGRDYPVPPVIFGDRNSLKKVLLNLVGNAVKFTETGFVLLEISTDYESGDQISLRFTVKDSGIGIPENKIEQIFVPFGQIDGSFSRKYGGSGLGLSFCKELVALMGGYIRVESGDQEGGKGTTFWFAIKVSISSPSYLPNSVPAANQFFYPEYRPSHYNNVIGNGDSPKNVLIIESNQMVIMSIQSILLSMKCECISASKAITALDLLESSKSTENQIDIIVCSDKSTFVQQILDYVTTEKVILYGVDPNSKYNENSKVYSYLVTPITHSKLISSILLSKNLKSKNSFLTTTNNTNNTNNTNNIENKSSIDSPLSITSTSSSIITPILTSNNLDLNNNNNNNNNSILVSNNGGVDGGNNVPSTLTTIQQSQPKKYILVAEDNDINIKVVVRQLEKLGYTAIVGINGLKALEIIGSFPICLILLDCQMPQMDGFTCSTILRQIEPTGQRIPIIAMTANDSKDRCFEVGMDDYLSKPVRVDRLQKTLSDWIKTDENGNPTNSYNFYPLSYSLVYNNFIDTQLKKEKNDD
Protein: SD10773p (Q7KSN0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDTAEIEADQRALQHASVEGTTETPGNAQSSTNDDVIKATVDQIVAQILSESAERKATEEGKTGKAADDVKNTPESGEDANKAAAKEPSGTPVAASSEATVPAPGSASSSNSPLPGTPPKYSNPHNLTIGARLEALSVEGNWLPARIVEVNETEQTLLVRFERNHKLKVSPSTSGSFQEWMAIKSERLRQRLSNRVLPVFELDEKCMARWSGPRKFPGTIRKLLGNDTYEVLFDDGYVKNVRAVHMNKMPKQLPPVQVAEEGASKSPTPVGTPVSSAPVAPKRASTGSLGGSSGSSGSKKSKCAPQRRDWPLLDMASLDIASLGLPEIPHDGEWTCHWVNDQPIGTEGFLIVGEHQKPTVIVQDWRLPPGWIKHMYQRSNVLGKWDVILVSPSGKRFRSKSDLKLFLESQNLVYNPDVYDFSIHRRRAKDINAYVYTHGYNPQPPPKPRPMDVSMNSTLDQSITSQHSLPSTPMPVKESQYMEAPVASLMPPAELMSPQTQPADETKPKIEAEILEASEGGTSQLMLADPHVVENGFAFIGGLKVKIQDNLYVCPREDCAKTYRKEDFLLIHIRHYHKEFAEHVSHCPKMQELAVKRTHPSSIDQVEAVPKNQIPNQQFFAKMHQQDLQQSRSFKRQSVSATATSSTPSDITPTKALLSPKMEPPSVSPTVESGIKQEDVSLDAGPTQSFNPSLSRSCKRARLSPSKRPSGSRKSNRQRSQRRPILSDNPAGHGLTEQDVEETRQSFNTPTPDTRIDSKKRRSGAATTPISSIDSPAMGDSVSTPSSNDQTDINAALAPPPAETLSKAPQYIKENGELIRIVRMRQEEIINCICEYGEEDGLMIQCELCLCWQHGACNGIVKEADVPDKYVCYICRNPQRGRDSMRFKHDQDWLFEGKLPVAAYHTANPQATKQFELLKRSHTLTGNLLDAKRSMHSLLVKINIARNRCHPKLYLWAKKWDEDNLDSTALTPVKRAKLEAPDLPNVPQPEAAIDPEECQYRLIEHIKVQQSLVLDRLNDIEAEMDELEKEDTLDDLKDADISTTKEALATFIKELETMKRLAKLNQVANMKQTLRDSATSK
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2) (Q9BZQ4)
Organism: Homo sapiens (Human)
Function: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16118205}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8BNJ3}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BNJ3}. Cytoplasm {ECO:0000269|PubMed:16118205}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BNJ3}. Note=Delivered to axons with Golgi-derived cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q8BNJ3}.
Interaction partners:
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinate phosphoribosyltransferase
- Glutamine-dependent NAD
- NAD-dependent protein deacetylase sirtuin-3, mitochondrial
- Nicotinamide phosphoribosyltransferase
- Nicotinamide riboside kinase 1
- 5'-nucleotidase
- NAD-dependent protein deacetylase sirtuin-1
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- Nicotinamide riboside kinase 2
Sequence:
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG
Protein: Copper-transporting ATPase (EC 7.2.2.8) (Cu(2+)-ATPase) (P38995)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone ATX1 and incorporates it into trans-Golgi vesicles.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:9325307, ECO:0000269|PubMed:9520490}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Copper chaperone ATX1
- Iron transport multicopper oxidase FET3
- Superoxide dismutase 1 copper chaperone
- Plasma membrane iron permease
- Mannosyl phosphorylinositol ceramide synthase SUR1
- Iron-regulated transcriptional activator AFT1
- Copper transport protein CTR2
- Copper transport protein CTR3
- Cytochrome c oxidase copper chaperone
- Ferric/cupric reductase transmembrane component 1
Sequence:
MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIEDCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEECHVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSSVSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTTQLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLFYRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMFHPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVERNETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIAGSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVLTFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTGVGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLACIKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIGNEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNGYETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGINDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKLNLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIESHGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL