wanglab/gogpt-training-data huggingface dataset:
Protein: Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13) (P33435)
Organism: Mus musculus (Mouse)
Function: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted.
Interaction partners:
- Metalloproteinase inhibitor 2
- Cathepsin K
- Aggrecan core protein
- Plasminogen
- A disintegrin and metalloproteinase with thrombospondin motifs 5
- Metalloproteinase inhibitor 1
- Collagen alpha-1
- A disintegrin and metalloproteinase with thrombospondin motifs 4
- Metalloproteinase inhibitor 3
- Stromelysin-1
Sequence:
MHSAILATFFLLSWTPCWSLPLPYGDDDDDDLSEEDLVFAEHYLKSYYHPATLAGILKKSTVTSTVDRLREMQSFFGLEVTGKLDDPTLDIMRKPRCGVPDVGEYNVFPRTLKWSQTNLTYRIVNYTPDMSHSEVEKAFRKAFKVWSDVTPLNFTRIYDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQFLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEAELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDILEGYPRKISDLGFPKEVKRLSAAVHFENTGKTLFFSENHVWSYDDVNQTMDKDYPRLIEEEFPGIGNKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSILWC
Protein: Thioredoxin domain-containing protein 8 (Spermatid-specific thioredoxin-3) (Sptrx-3) (Thioredoxin-6) (Q6A555)
Organism: Homo sapiens (Human)
Function: May be required for post-translational modifications of proteins required for acrosomal biogenesis. May act by reducing disulfide bonds within the sperm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15181017}. Golgi apparatus {ECO:0000269|PubMed:15181017}.
Interaction partners:
Sequence:
MVQIIKDTNEFKTFLTAAGHKLAVVQFSSKRCGPCKRMFPVFHAMSVKYQNVFFANVDVNNSPELAETCHIKTIPTFQMFKKSQKVTLFSRIKRIICCYRSGFMSNLIFEFCGADAKKLEAKTQELM
Protein: Transmembrane protein (Q940H5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Preprotein translocase subunit SECE1
- Transmembrane protein
- Transmembrane protein
- Preprotein translocase subunit SCY2, chloroplastic
- GAG1At protein
- Membrane lipoprotein
- TonB-dependent heme receptor A
- AT3g62190/T17J13_150
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Mitochondrial Rho GTPase 3
Sequence:
MVVSPGLLSTVSGVIRLAPSHRILRRDGFGPICFKFSGDLSINGRVSHKHVRGSGTVGSVGSARESWSSHKKLPEEEPLWLSLLRDMVWSTRSLLSFMAEQPSQLKYIEWPTFASTLKTATLSLCLVAVFIVALSSVDAALCYILALILRKAP
Protein: Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein (Cnt-b) (Centaurin-beta) (Q4QQN0)
Organism: Mus musculus (Mouse)
Subcellular location: Endosome membrane {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369028}.
Interaction partners:
Sequence:
MTVEFEECIKDSPRFRATIDEVETDVVEIEAKLDKLVKLCSGMIEAGKAYVTTNRLFVSGVRDLSQQCQGDTVISECLQRFGDSLQEMVNYHTILFDQAQRSVRQQLHNFVKEDVRKFKETKKQFDKVREDMELSLVRNAQAPRHRPHEVEEATGALTVTRKCFRHLALDYVLQINVLQAKKKFEILDSMLSFMHAQYSFFQQGYSLLHQLDPYMKKLAAELDQLVIDSAVEKREMERKHAAIQQRTLLQDFSYDEPKVEFDVDAPSGVVMEGYLFKRASNAFKTWNRRWFSIQNSQLVYQKKLKDALTVVVDDLRLCSVKPCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWVQAVQASIASAYRESPDSCYSERLDRTASPSTSSIDSTTDSRERGVKGESVLQRVQSVAGNSQCGDCGQPDPRWASINLGVLLCIECSGIHRSLGVHCSKVRSLTLDSWEPELLKLMCELGNSTVNQIYEAQCEGPGVRKPTASSSRQDKEAWIKDKYVEKKFLRKLTSAPAREPPRRWRAQKCQRPHSSPHAPTTRRKVRLEPVLPSVAALSSGGRGCQKLHLSSCTWAGLGIGSVQCWKEPPTLNATVGLGRLEAGLHRGTLELSCLSTT
Protein: General negative regulator of transcription subunit 3 (P06102)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT protein subcomplex negatively regulates the basal and activated transcription of many genes. Preferentially affects TC-type TATA element-dependent transcription. Could directly or indirectly inhibit component(s) of the general transcription machinery.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus.
Interaction partners:
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- General negative regulator of transcription subunit 1
- ATP-dependent RNA helicase DHH1
- General negative regulator of transcription subunit 2
- General negative regulator of transcription subunit 4
- Poly
- Protein CAF40
- General negative regulator of transcription subunit 5
- Protein CAF130
- Deadenylation-dependent mRNA-decapping factor PAT1
Sequence:
MAHRKLQQEVDRVFKKINEGLEIFNSYYERHESCTNNPSQKDKLESDLKREVKKLQRLREQIKSWQSSPDIKDKDSLLDYRRSVEIAMEKYKAVEKASKEKAYSNISLKKSETLDPQERERRDISEYLSQMIDELERQYDSLQVEIDKLLLLNKKKKTSSTTNDEKKEQYKRFQARYRWHQQQMELALRLLANEELDPQDVKNVQDDINYFVESNQDPDFVEDETIYDGLNLQSNEAIAHEVAQYFASQNAEDNNTSDANESLQDISKLSKKEQRKLEREAKKAAKLAAKNATGAAIPVAGPSSTPSPVIPVADASKETERSPSSSPIHNATKPEEAVKTSIKSPRSSADNLLPSLQKSPSSATPETPTNVHTHIHQTPNGITGATTLKPATLPAKPAGELKWAVAASQAVEKDRKVTSASSTISNTSTKTPTTAAATTTSSNANSRIGSALNTPKLSTSSLSLQPDNTGASSSAATAAAVLAAGAAAVHQNNQAFYRNMSSSHHPLVSLATNPKSEHEVATTVNQNGPENTTKKVMEQKEEESPEERNKLQVPTFGVFDDDFESDRDSETEPEEEEQPSTPKYLSLEQREAKTNEIKKEFVSDFETLLLPSGVQEFIMSSELYNSQIESKITYKRSRDMCEISRLVEVPQGVNPPSPLDAFRSTQQWDVMRCSLRDIIIGSERLKEDSSSIYAKILENFRTLEMFSLFYNYYFAITPLEREIAYKILNERDWKVSKDGTMWFLRQGEVKFFNEICEVGDYKIFKLDDWTVIDKINFRLDYSFLQPPVDTASEVRDVSVDNNNVNDQSNVTLEQQKQEISHGKQLLKQLKQGKISV
Protein: E3 ubiquitin-protein ligase ZNRF3 (EC 2.3.2.27) (RING finger protein 203) (RING-type E3 ubiquitin transferase ZNRF3) (Zinc/RING finger protein 3) (Q9ULT6)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone. Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22575959}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Leucine-rich repeat-containing G-protein coupled receptor 4
- R-spondin-2
- R-spondin-1
- Leucine-rich repeat-containing G-protein coupled receptor 5
- R-spondin-3
- R-spondin-4
- Polycomb group RING finger protein 3
- Frizzled-7
- Frizzled-4
- Frizzled-6
Sequence:
MRPRSGGRPGATGRRRRRLRRRPRGLRCSRLPPPPPLPLLLGLLLAAAGPGAARAKETAFVEVVLFESSPSGDYTTYTTGLTGRFSRAGATLSAEGEIVQMHPLGLCNNNDEEDLYEYGWVGVVKLEQPELDPKPCLTVLGKAKRAVQRGATAVIFDVSENPEAIDQLNQGSEDPLKRPVVYVKGADAIKLMNIVNKQKVARARIQHRPPRQPTEYFDMGIFLAFFVVVSLVCLILLVKIKLKQRRSQNSMNRLAVQALEKMETRKFNSKSKGRREGSCGALDTLSSSSTSDCAICLEKYIDGEELRVIPCTHRFHRKCVDPWLLQHHTCPHCRHNIIEQKGNPSAVCVETSNLSRGRQQRVTLPVHYPGRVHRTNAIPAYPTRTSMDSHGNPVTLLTMDRHGEQSLYSPQTPAYIRSYPPLHLDHSLAAHRCGLEHRAYSPAHPFRRPKLSGRSFSKAACFSQYETMYQHYYFQGLSYPEQEGQSPPSLAPRGPARAFPPSGSGSLLFPTVVHVAPPSHLESGSTSSFSCYHGHRSVCSGYLADCPGSDSSSSSSSGQCHCSSSDSVVDCTEVSNQGVYGSCSTFRSSLSSDYDPFIYRSRSPCRASEAGGSGSSGRGPALCFEGSPPPEELPAVHSHGAGRGEPWPGPASPSGDQVSTCSLEMNYSSNSSLEHRGPNSSTSEVGLEASPGAAPDLRRTWKGGHELPSCACCCEPQPSPAGPSAGAAGSSTLFLGPHLYEGSGPAGGEPQSGSSQGLYGLHPDHLPRTDGVKYEGLPCCFYEEKQVARGGGGGSGCYTEDYSVSVQYTLTEEPPPGCYPGARDLSQRIPIIPEDVDCDLGLPSDCQGTHSLGSWGGTRGPDTPRPHRGLGATREEERALCCQARALLRPGCPPEEAGAVRANFPSALQDTQESSTTATEAAGPRSHSADSSSPGA
Protein: Nitrate reductase-like protein NarX (P9WJQ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Does not seem to have nitrate reductase activity.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable respiratory nitrate reductase
- Probable nitrate/nitrite transporter NarK2
- Nitrate reductase-like protein NarX
- Nitrate/nitrite transporter
- Probable nitrite extrusion protein 1 NarK1
- Probable integral membrane nitrite extrusion protein NarK3
- assimilatory sulfite reductase
- Nitrite reductase small subunit
- Probable respiratory nitrate reductase
- Nitrate reductase alpha subunit
Sequence:
MTVTPRTGSRIEELLARSGRFFIPGEISADLRTVTRRGGRDGDVFYRDRWSHDKVVRSTHGVNCTGSCSWKIYVKDDIITWETQETDYPSVGPDRPEYEPRGCPRGAAFSWYTYSPTRVRHPYARGVLVEMYREAKARLGDPVAAWADIQADPRRRRRYQRARGKGGLVRVSWAEATEMIAAAHVHTISTYGPDRVAGFSPIPAMSMVSHAAGSRFVELIGGVMTSFYDWYADLPVASPQVFGDQTDVPESGDWWDVVWQCASVLLTYPNSRQLGTAEELLAHIDGPAADLLGRTVSELRRADPLTAATRYVDTFDLRGRATLYLTYWTAGDTRNRGREMLAFAQTYRSTDVAPPRGETPDFLPVVLEFAATVDPEAGRRLLSGYRVPIAALCNALTEAALPYAHTVAAVCRTGDMMGELFWTVVPYVTMTIVAVGSWWRYRYDKFGWTTRSSQLYESRLLRIASPMFHFGILVVIVGHGIGLVIPQSWTQAAGLSEGAYHVQAVVLGSIAGITTLAGVTLLIYRRRTRGPVFMATTVNDKVMYLVLVAAIVAGLGATALGSGVVGEAYNYRETVSVWFRSVWVLQPRGDLMAEAPLYYQIHVLIGLALFALWPFTRLVHAFSAPIGYLFRPYIIYRSREELVLTRPRRRGW
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 (Q9FIJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 10-A
- NADH dehydrogenase subunit 7
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8-A
- NADH dehydrogenase 1 beta subcomplex subunit 9
Sequence:
MAWRGSISKSMKELRILLCQSSPASAPTRTFVEKNYKDLKSLNPKLPILIRECSGVQPQMWARYDMGVERCVNLDGLTEPQILKALENLVKSGATKA
Protein: Diacylglycerol kinase (DAG kinase) (DAGK) (EC 2.7.1.107) (O31502)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. Is more active toward long-chain DAG compared with short-chain DAG. Is not able to phosphorylate substrates other than DAG, such as monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or sphingosine.
Interaction partners:
- Phosphatidate cytidylyltransferase
- Processive diacylglycerol beta-glucosyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Extracellular esterase EstB
- Lipase EstA
- Glycerol-3-phosphate dehydrogenase [NAD
- Aerobic glycerol-3-phosphate dehydrogenase
- Undecaprenol kinase
- Glycerol-1-phosphate dehydrogenase [NAD
- Lipoteichoic acid synthase 2
Sequence:
MKRARIIYNPTSGREIFKKHLAQVLQKFEQAGYETSTHATTCAGDATHAAKEAALREFDLIIAAGGDGTINEVVNGLAPLDNRPTLGVIPVGTTNDFARALGIPREDILKAADTVINGVARPIDIGQVNGQYFINIAGGGRLTELTYDVPSKLKTMLGQLAYYLKGMEMLPSLRPTEVEIEYDGKLFQGEIMLFLVTLTNSVGGFEKLAPDSSLNDGMFDLMILKKANLAEFIRVATMALRGEHINDQHIIYTKANRVKVNVSEKMQLNLDGEYGGMLPGEFVNLYRHIHVVMPKEKAEQLDD
Protein: Large ribosomal subunit protein mL41 (39S ribosomal protein L41, mitochondrial) (L41mt) (MRP-L41) (Bcl-2-interacting mitochondrial ribosomal protein L41) (Cell proliferation-inducing gene 3 protein) (MRP-L27 homolog) (Q8IXM3)
Organism: Homo sapiens (Human)
Function: Component of the mitochondrial ribosome large subunit. Also involved in apoptosis and cell cycle. Enhances p53/TP53 stability, thereby contributing to p53/TP53-induced apoptosis in response to growth-inhibitory condition. Enhances p53/TP53 translocation to the mitochondria. Has the ability to arrest the cell cycle at the G1 phase, possibly by stabilizing the CDKN1A and CDKN1B (p27Kip1) proteins.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16024796, ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL34m
- Large ribosomal subunit protein bL19m
- Mitochondrial ribosomal protein L40
- Large ribosomal subunit protein uL16m
Sequence:
MGVLAAAARCLVRGADRMSKWTSKRGPRSFRGRKGRGAKGIGFLTSGWRFVQIKEMVPEFVVPDLTGFKLKPYVSYLAPESEETPLTAAQLFSEAVAPAIEKDFKDGTFDPDNLEKYGFEPTQEGKLFQLYPRNFLR
Protein: RE16347p (Yuri gagarin, isoform C) (Q9VJP8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASRQAGFVLDAKSMGLNPSRPASSPPPPPSSASQMCRQVQPTGTSASHPHQESTLKASSPDRCTASTEAMSTEHYRCLIQKLRDTNGDAGDMSFELNSIFLKRLDEIDCLDEHEGDDMHTCQLRLVTFQEWVDFLLHVNSVILGNVSDLEKEAYSKIVACCQSVQVRQQHTLEENRRLREDICAIIERVQHSPHCTDFDFNGISLETLTVNQLRGVGKDPAHAECESEKMSESMKSLVGEIAAKHDEIGELKSQINALDEVVHTARQKLLLKDQCIAQLNQQLHEITRCIESRDQAKMEESPNDTLTADAITSDMLENLSIHDTQESEMLRLLNAELNDLLDLHNKQEFQTIEIRRKRVSCFIEKLVSEREDTLKKLESIRSHLTILQSDLDQSCLISVDPESGPCDLDADAQMLEALRRRLLNLSQLNRELHGKYQRLDTESKIKISELEARIESESSVLQRNSDVLREIAELICSLGSKEFSYNEIYDESSKENPFCTTIADMFARKFEQEQNQVEIECDTKTPSQTRKPTKTTKIPGATAKTNKQQPTPKPSNKPTTTKTIPTKNTTTTFRTSK
Protein: Putative pentatricopeptide repeat-containing protein At5g43820 (P0C8R0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM1
- CLAVATA3/ESR
- Protein GOLVEN 2
- Protein RALF-like 22
- Protein SCARECROW
Sequence:
MLRRWNIVIESLRRVHSSDLENLISASLYNRTLCTASESLNHGVVDESYVLAELSSLLPISSNKTSVSKEDSSSKNQVAIDSFLSAEDKLRGVFLQKLKGKSAIQKSLSSLGIGLSIDIVADVLNRGNLSGEAMVTFFDWAVREPGVTKDVGSYSVILRALGRRKLFSFMMDVLKGMVCEGVNPDLECLTIAMDSFVRVHYVRRAIELFEESESFGVKCSTESFNALLRCLCERSHVSAAKSVFNAKKGNIPFDSCSYNIMISGWSKLGEVEEMEKVLKEMVESGFGPDCLSYSHLIEGLGRTGRINDSVEIFDNIKHKGNVPDANVYNAMICNFISARDFDESMRYYRRMLDEECEPNLETYSKLVSGLIKGRKVSDALEIFEEMLSRGVLPTTGLVTSFLKPLCSYGPPHAAMVIYQKSRKAGCRISESAYKLLLKRLSRFGKCGMLLNVWDEMQESGYPSDVEVYEYIVDGLCIIGHLENAVLVMEEAMRKGFCPNRFVYSRLSSKLMASNKTELAYKLFLKIKKARATENARSFWRSNGWHF
Protein: Centrin 3 (E5RH67)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVGVYFNSLCNQQLLGNCLINITF
Protein: 40S ribosomal protein S15a, putative (Q580K6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L27a
- 40S ribosomal protein S13, putative
- 60S ribosomal protein L13a, putative
- Eukaryotic translation initiation factor 1A, putative
- 60S ribosomal protein L28, putative
- 40S ribosomal protein S25
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L17, putative
- Eukaryotic translation initiation factor 5A
- 60S ribosomal protein L37a, putative
Sequence:
MTMMSVLANALRCIAGAERRGKRQVLIRPSSKVVVKFLQVMQKHGYIGEFEIVDDHRAGKIVVNLNGRLNKCGAICPRFDCTARDFEKWVKNILPSRQFGFVVLTTSLGIMDHEEARARNTGGKVLGFFY
Protein: Ecotin (P23827)
Organism: Escherichia coli (strain K12)
Function: General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.
Subcellular location: Periplasm.
Interaction partners:
Sequence:
MKTILPAVLFAAFATTSAWAAESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLENKTLEGWGYDYYVFDKVSSPVSTMMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR
Protein: Rhodanese domain-containing protein (Q382H5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFFVTPRALATITAPQVLAVVRSKLGGSRAAANKIIVDVRSTGEVAATGLIPTAVNIPLNALPAALSDEVDEEEFVKTFGHPKPRKDEAELIFYCERGVRSATATEIAEGLGYRYVKNFVGSFAEWRECYGGAPFDDADGCKG
Protein: UDP-glycosyltransferase 73C1 (EC 2.4.1.-) (Cytokinin-O-glucosyltransferase 1) (Zeatin O-glucosyltransferase 1) (AtZOG1) (Q9ZQ99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the O-glucosylation of trans-zeatin and dihydrozeatin. Also active in vitro on cis-zeatin, dihydrozeatin-9-N-Glc, and olomoucine. Can detoxify the explosive 2,4,6-trinitrotoluene in plant by forming O- or C-glucose conjugates.
Interaction partners:
Sequence:
MASEFRPPLHFVLFPFMAQGHMIPMVDIARLLAQRGVTITIVTTPQNAGRFKNVLSRAIQSGLPINLVQVKFPSQESGSPEGQENLDLLDSLGASLTFFKAFSLLEEPVEKLLKEIQPRPNCIIADMCLPYTNRIAKNLGIPKIIFHGMCCFNLLCTHIMHQNHEFLETIESDKEYFPIPNFPDRVEFTKSQLPMVLVAGDWKDFLDGMTEGDNTSYGVIVNTFEELEPAYVRDYKKVKAGKIWSIGPVSLCNKLGEDQAERGNKADIDQDECIKWLDSKEEGSVLYVCLGSICNLPLSQLKELGLGLEESQRPFIWVIRGWEKYNELLEWISESGYKERIKERGLLITGWSPQMLILTHPAVGGFLTHCGWNSTLEGITSGVPLLTWPLFGDQFCNEKLAVQILKAGVRAGVEESMRWGEEEKIGVLVDKEGVKKAVEELMGDSNDAKERRKRVKELGELAHKAVEEGGSSHSNITFLLQDIMQLEQPKK
Protein: Lectin (B4EH86)
Organism: Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315))
Interaction partners:
Sequence:
MPLLSASIVSAPVVTSETYVDIPGLYLDVAKAGIRDGKLQVILNVPTPYATGNNFPGIYFAIATNQGVVADGCFTYSSKVPESTGRMPFTLVATIDVGSGVTFVKGQWKSVRGSAMHIDSYASLSAIWGTAAPSSQGSGNQGAETGGTGAGNIGGGGERDGTFNLPPHIKFGVTALTHAANDQTIDIYIDDDPKPAATFKGAGAQDQNLGTKVLDSGNGRVRVIVMANGRPSRLGSRQVDIFKKSYFGIIGSEDGADDDYNDGIVFLNWPLG
Protein: RNA binding motif protein 17 (Q5W012)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGRVGRAGRSQRTKQSTVLAPVIDLKRGGSSDDRQIVDTPPHVAAGLKDPVPSGFSAGEVLIPLADEYDPMFPNDYEKVVKRQREERQRQRELERQKEIEEREKRRKDRHEASGFARRPDPDSDEDEDYERERRKRSMGGAAIAPPTSLVEKDKELPRDFPYEEDSRPRSQSSKAAIPPPVYEEQDRPRSPTGPSNSFLANMGGTVAHKIMQKYGFREGQGLGKHEQGLSTALSVEKTSK
Protein: PhoPQ-activated pathogenicity-related protein (Q86JB6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Ponticulin-like protein C1
- Ponticulin-like protein C2
- CMP/dCMP-type deaminase domain-containing protein
- Ponticulin-like protein C4
- Ponticulin-like protein C5
- Ponticulin-like protein C3
- Probable phosphoglycerate mutase
- Secreted protein A
Sequence:
MKLSIVTFIVTVVVLSVIYIYNSSTLLESRVLKDYVEKYDPNYKWTLNATYNTNVSTIYILELTSQKWDMGNSSSPLWKHWLTVCIPNNATENLETGLLLIDGGSTVNWAVPSVNGWSSFGQQLCKTSNEITATVQQVPNEPLIFDNNGIKRSEDGIVALTWRKYIDTKDSNWVSLLPQTKSAIKAMDAVQEFGKEIGKFSIKNFVVTGASKRGWTTWGTAMSSDKRVVGIAPMVIPILNVAENIGSQMQDLGEWSFELYDYIQNGITNFLYTKYFDNLRKIIDPINYINTLEPIAKYVLNAADDEFFAVDSPKFFYSKLKGETRLNTYPNTNHNGIKKQAVANDIVNFFKLVAFGIERPEIEWSIEYSQDKNFGTIKMKVLKGVPTKISLWFSTTISTTMRDFRMYTCEDASCYQNLDWQSIDIEISPENNYFYTMEKPAAGWTGFFYQVEFETGSYYSTEVSIVPDILPFPKCPMSVCASGIPAYKNKTLEIENN
Protein: Cell division cycle protein 27 homolog (Q24021)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMIQEPVQAAIWHCLNYYDFKDAVFLSERLCSEVESDETIFLLATSYFRSNQVHQAYWLLKEKARRSPQCRFLQAKCAYELKKYAEAESALISTGFADAKNCDELQRDFGDLACFAYQLMAQICMRTERNKLAVSALRRALKLNPFMWHAFADLCLLGQDTDAAAIFQIHSTDVFNTCQGSSVNANAMVLFGAEQQGQQHQERQSLITNLSNVSNYILTTPVDQQQQQINQNQNQHHNSNMVTPINNNNNNNNLNSSISMLRGGLVQNSSMLAMLEDTPMGAPQDPAGQYQQNQQLYDMSSGTPFRKQFKYLSAISPPTPSFGIMPLTSPCTGNDGSFIGNHTPVMNISYSPMPQMLVEVNQEPKMMGKKLKTHVGGLINRKEGSLNKPAVFTQAGNITPRTPNNNNVGNNGNMNVPPNPNAAVRRSSRLFSNSYSVKENNKSPNIANKFVQPRSPPRKAKSRMTKICLNNELIEDKSHHLSEKRKEKVETITSSGANNNSGGRSAAEEAKVLLNNSLNNAQTMAHQLMGLKKQSADGLMALLRGLAEAYQLLSNFQCKAAIKQLETTIPKHHLNSSWVQSLIGLARYEMREYEAAVAIFETIHKTEPCRLDYMEIYSSSLWHLQREVELSALAQDLINQDKTSPVTWCVSGNCFSLQKEHETAIKFFKRAVQVDPDFVYSYTLLGHELVLTEEFDKAMDYFRAAVVRDPRHYNAWYGIGTIYSKQEKYELAEIHYVKALKINPQNSVILVHIGAMQFYMKKKDLSLQTLNTAATLDPKNPLHAIPSRLHLLLAGQVPGGAAATGGAQGSRAQGVGGVLSDRQNPQDARQHGSGADALQLGHRPRSQRCQQSNQRCLRLNGSSQLLSGQHYGPGR
Protein: Histone-lysine N-methyltransferase set-18 (EC 2.1.1.357) (Q8I4F7)
Organism: Caenorhabditis elegans
Function: Histone methyltransferase. Specifically methylates 'Lys-36' of histone H3, inducing di-methylation. Plays a role in modulating lifespan and oxidative stress resistance, in a manner dependent upon daf-16/Forkhead box protein O and the Insulin/IGF-1-like signaling (IIS) mediated pathway. Represses transcription of daf-16 isoform a, perhaps by methylating histone H3 at the daf-16 promoter, which in turn leads to recruitment of histone deacetylases and thus modulation of expression.
Interaction partners:
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase
- Histone-lysine N-methyltransferase set-2
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- SPK domain-containing protein
- SET domain-containing protein
- protein-histidine N-methyltransferase
Sequence:
MAVKKNKNVPKQEDPLVQKDEISSIHARIKIFETPFATQVLNPKVSEFCANCLRGPAPGEKLLRCGGCNFSMYCSKECQATAWLVHKPECKRLKASFPNLPLTEVLFLSKVIDRIQFLEKNGDKLGIEAERKFSSLVDHKVDIRDDEEKMAHFEKIFEKMGAFRGEEMIEKGEFFDVFCKATINSHSIHTNAGNEVGMALDLGVSKYNHSCRPTCSMVFDGYRVCLRPLVPGVDAENTEEAFISYIDVGRSKYIRRRDLNSRWYFNCECTRCMDPEDDALTAIRCANPACDAPILTSETEEPMNIACEKCKTIVEEDTVKAAQEYMKTLPASFDPKCPAEIEALPGKLKELLAKAEQILHPSNVYVARLRTALFHVTGTLTMDNLSSMHTQIYNNYKMCFPKADRHVGFQLLHIVKALIEKDERDEAMPYAFDAMNIFEVCFGLDHPYYLQTLALWTYLEKKIPKSTEELVQLTNFSDNRPIDIVSLLKRANMLPPPPYAAGTPGVA
Protein: Vacuolar protein-sorting-associated protein 36 (ESCRT-II complex subunit VPS36) (Q91XD6)
Organism: Mus musculus (Mouse)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.
Subcellular location: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Late endosome {ECO:0000269|PubMed:15755741}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with ubiquitinated proteins on late endosomes. Recruited to the endosome membrane to participate in vesicle formation. {ECO:0000269|PubMed:15755741}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein-sorting-associated protein 25
- Vacuolar-sorting protein SNF8
- Charged multivesicular body protein 6
- Tumor susceptibility gene 101 protein
- Charged multivesicular body protein 3
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
Sequence:
MDRFVWTSGLLEINETLVIQQRGVRVYDGEEKIKFDAGTLLLSTHRLIWRDQKNNECCMAIPLSQIVFIEEQAAGIGKSAKIVVHLHPAPSNKEPGPFQSSKNSYIRLSFKEHGQIEFYRRLSEEMTQRRWETVPVSQSLQTNKGPQPGRVRAVGIVGIERKLEEKRKETDKNISEAFEDLSKLMIKAKEMVELSKSIANKIKEKQGDVTEDETIRFKSYLLSMGIANPVTRETYGSGTQYHMQLAKQLAGILQAPLEERGGIMSLTEVYCLVNRARGMELLSPEDLVNACKMLEALKLPIRLRVFDSGVMVIELQTHKEEEMVASALETVSERGSLTSEEFAKLVGMSVLLAKERLLLAEKMGHLCRDDSVEGLRFYPNLFMTQN