wanglab/gogpt-training-data huggingface dataset:
Protein: Non-secretory ribonuclease (EC 4.6.1.18) (Eosinophil-derived neurotoxin) (RNase UpI-2) (Ribonuclease 2) (RNase 2) (Ribonuclease US) (P10153)
Organism: Homo sapiens (Human)
Function: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities.
Subcellular location: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule.
Interaction partners:
- Eosinophil peroxidase
- Eosinophil cationic protein
- Ribonuclease inhibitor
- Bone marrow proteoglycan
- Angiogenin
- Ribonuclease T2
- Endothelin-1 receptor
- CMRF35-like molecule 8
- Galectin-10
- Membrane-spanning 4-domains subfamily A member 3
Sequence:
MVPKLFTSQICLLLLLGLLAVEGSLHVKPPQFTWAQWFETQHINMTSQQCTNAMQVINNYQRRCKNQNTFLLTTFANVVNVCGNPNMTCPSNKTRKNCHHSGSQVPLIHCNLTTPSPQNISNCRYAQTPANMFYIVACDNRDQRRDPPQYPVVPVHLDRII
Protein: S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain] (Q9P7E3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Spermidine synthase
- S-adenosylmethionine synthase
- Ornithine decarboxylase
- Arginase
- Uncharacterized protein C57A7.07c
- Uncharacterized MFS-type transporter SPBC409.08
Sequence:
MSPTLVVDQENSEEFNTSSFEGPEKLLELWFSAPIKTNLSAGEKANLGLKAVSRNDWDDMLAQAQCKVLSVVNSEEIDAYLLSESSMFVFAHKIILKTCGTTTLLASLPRLLEIASSVGFDRPLRIFYSRKNFLYPERQLAPHTSWEEEVRYLQLFFPSGCSYVVGPTNKNHWHLFSDLADDYSLLEDSLDPEDETLEVLMTDMSPERSLQFYAPSLDVVRSARGDDYVREKNNLSGGHILGSYVADESGVRDLCSTSDKKAVLDAFQFEPIGFSSNMIYKDRYATIHVTPQEHCSYASFETNVSQFQFGRSISETIEKTVKTFGANKFCLTLFQAKGASQEKHFSAKLKSFSSYKREEFIVYDFPGYDLIFASFTAV
Protein: Immediate early response gene 2 protein (Protein ETR101) (Q9BTL4)
Organism: Homo sapiens (Human)
Function: DNA-binding protein that seems to act as a transcription factor. Involved in the regulation of neuronal differentiation, acts upon JNK-signaling pathway activation and plays a role in neurite outgrowth in hippocampal cells (By similarity). May mediate with FIBP FGF-signaling in the establishment of laterality in the embryo (By similarity). Promotes cell motility, seems to stimulate tumor metastasis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22120713}. Nucleus {ECO:0000269|PubMed:22120713}. Note=Cytoplasmic during quiescence, translocates to the nucleus upon stimulation. {ECO:0000269|PubMed:22120713}.
Interaction partners:
- Early growth response protein 1
- Protein FosB
- Protein c-Fos
- Transcription factor JunB
- Dual specificity protein phosphatase 1
- mRNA decay activator protein ZFP36
- Cyclic AMP-dependent transcription factor ATF-3
Sequence:
MEVQKEAQRIMTLSVWKMYHSRMQRGGLRLHRSLQLSLVMRSARELYLSAKVEALEPEVSLPAALPSDPRLHPPREAESTAETATPDGEHPFPEPMDTQEAPTAEETSACCAPRPAKVSRKRRSSSLSDGGDAGLVPSKKARLEEKEEEEGASSEVADRLQPPPAQAEGAFPNLARVLQRRFSGLLNCSPAAPPTAPPACEAKPACRPADSMLNVLVRAVVAF
Protein: Polypeptide N-acetylgalactosaminyltransferase 8 (pp-GaNTase 8) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 8) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8) (Q9VUT6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels fro Muc5AC-3/13.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- lysozyme
- Tweedlebeta
- Major facilitator superfamily
- IP12247p
- Distal antenna-young, isoform A
- FI08017p
Sequence:
MCLDIWRHKKKVLPLLLLMAIGSIIYYLYTLKLEGERDESATSTTSRLERDIRDLQAVFESEVIPDLGALGRPARGNWTEEQLEAIAKSQRETGYNAWLSKRISPERSLYDMRHRSCKKLKYPMEKLPSVSVVITYHNEEASVLLRTLSSLRSRTPIQLLREVILVDDGSTQADEKLNDFIKIKFLNMVQHRRITTQVGLMHARVVGAELALADVLVFLDSHVEVTKGWLEPLIAPILEDNRTCTTPIIDTIDFDNFAYRRGKPSRGFFNWEFNYIQLPLLKEEAVAMPAPHKNPIMNGGLFAIGREWFSELGGYDKGLKIWGAEQFELSLKLWLCGGQILEVPCSRVGHLFRDGNFQIRYTNKDKNSEKKLISRNYRRVAEIWLDEYKDKLFANMPHLTVIPVGNLAEQRDLKNRLHCKPFKWFLDNLATDFLNLYPILDPAEYASGVLQSISSPKLCLDRKDPSHGQPKLAPCSSDHVFPSPEQYWSLTNHRELRSGFYCLEVRNHGVNVHIYQCHGQSGNQFWSFDSKTHQVISGQQQNFRHCLEAQPELNAVTSSVCDPKNHKQQWKFGYLNSQRLQHFWDNVKTQ
Protein: Polyubiquitin [Cleaved into: Ubiquitin] (P62972)
Organism: Xenopus laevis (African clawed frog)
Function: Ubiquitin Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
QKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
Protein: histidine kinase (EC 2.7.13.3) (O28769)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo4
- Uncharacterized protein AF_1502
- Uncharacterized protein AF_1504
Sequence:
MKLTPQIVLIVVVASLVPLSVLGYLTIAGMTSSAEEAKQGVTTVSQEYLTKAGEEAVRMKAQDLALAVQTYIEAKMKLENKTMLTTFDLIQDPKFRSLGAQRWGAKEYTWVGAGNKVAGRDVAVILTHPAFTGQYEKYLGVDVAMLRWNETMPELYNLLLKITENPEAPKPVCGYYHWDDPETPEKEEIPKYLCHYPTTIKVYDPISKGQLWVVVGTSAYIDGYFQYLTQNPANPAENIASEISKSVEGAIQQVYYALGIAAAIAIVFVIVLAVFTTSTITRPIIELSNTADKIAEGNLEAEVPHQNRADEIGILAKSIERLRRSLKVAMESLEEALK
Protein: WASH complex subunit 4 (Strumpellin and WASH-interacting protein homolog) (WASH complex subunit SWIP homolog) (Q9VXH9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts at least in part as component of the WASH complex which may regulate wash nucleation-promoting factor (NPF) activity and is required for its membrane targeting during endosomal sorting (By similarity). During embryogenesis, not involved in the wash-dependent developmental migration of hemocytes anteriorly from the tail.
Subcellular location: Early endosome {ECO:0000305}.
Interaction partners:
- WASH complex subunit 2
- WASH complex subunit 3
- WASH complex subunit homolog 5
- WASH complex subunit 1
- F-actin-capping protein subunit alpha
- F-actin-capping protein subunit beta
- Vacuolar protein sorting-associated protein 35
Sequence:
MFAEDILRDYGSFISEHDGKLKLLRDKVPNRDVSESAQCVYMSPVVEVNFMGNDSMAPDRSFEESELVANKPLTTLANLCNQCRNLSRKAKRFQLAFLFSDFRLDDTLPPHTHTSEGSAGLEGSLVRMSSSMDFFCQVYFLLNRMIVILQNLWRQIAASVSVPMDINEVHIFAVFDAMSELLEHIVVFNELANQSKISTMWALYKKWLMNLSNSQSANLELNGLSTSLMDIENLITKDFFRILLDNLMELKKQFGLNSVSPITQHSNAYIRRQLLDVDANPSNELKNYEDPKHIIRLTTFVVVVHELGIQMEGKLVKNVIDLVARHKQVPLNRSVFWSPSGFLSLHAKTLMKSSARSQDGQGPKVHSTVLEKFRLSDQRTCRQLGVQLSLWSIQMQRVFDVGVFGHLKTFLQLILNGHSYADQVNLLAVALINRHVALMTPMTRNDWIVVSRLLQYLKVIQKTFESNQINFVRFISSLIQWQKQKVIHLLHTTKKKIVVLKLLQRKINFLATIKLAEKSIMGFPSKQRLTFVNLALGEFLDNRLLPADNQKLIKSILHRVNSISDIMRNIGGQLNTSESSSLVYNHWFLDTSVLKEYTELQRNPYSLQNLVSVSHHLDKIMAMFRGSRCPKQSANDLIIEFLSNHLEFFLRVEALSHLFQSQDQPFQQSALDYRLCINAVAVENDGDYNIIKDHLENYFTATFYNLTTIAPHDWKSYEKMRHLANKVLQLQPIDDHLPNQIIDQGIDVLQIMRNIHTFASSYAYNMNLQVFVETNSRSKHLDIIGTRHVANSVQTHGTGIINTTVNFIYQFLRQKFYTFSTFLHDEQIKSRLLKELRFHTEHKHSKSYQSYPYERADSFLKKIRRLGCSSNGETYMDLFRKVITQVGNAVGYVRLLQAGSKNANFRNRSYKTRFDSNFSCGGSKVHEATEGSIREYEKSLGHMKECYSDSTNYFKLLLQGFQPFLCNPHNHHLRTFYLITPALIMNYIDYRVKQKLKIYKKDQTKISLFEDGFAIGLVYILNMLNQQTEFHELGWSQTITQHLNAERSKVRDILAGQQRTAPEQLDEKLHQTVAITERHVNAYEHEYNLLYATLSSSEIFFQ
Protein: Ankyrin 1 (A0A8I6A0H1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGFCKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTSMVKLLLENDASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVQLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKPMKYEDAQHILCHLNVTMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPDRRHGDREYSLSPSQVNGYSSLQDELLSPASLHYALPSPLCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSSGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKSQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTVDWYKQGSAASYPQEAAQSSWQEEVTQGPQSFQRRITTIQGPEPGTLQEYEQVVVSTREHVQRGPPESDSPKAGKDPSLWASESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVIVEGPLADPGDLEADIESFMKLTKVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: Homeobox protein (Q13028)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
FDLKRYLSTAERAGLAASLQLTETQVKIWFQNRR
Protein: Spectrin repeat containing nuclear envelope protein 1 (A0A5F9ZHE1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
XDNLQKRVTSILRRLKHFIGQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDEHDLSDRELELEDSAALSDLHWHDRSADSLLSPQPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRGAVGLSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEESLPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIELQIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQIFTGQVGRPFLNIKGFHEMSHGLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGNRLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTVHKRWLRFLPF
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (K7EIL8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELA
Protein: IMP-specific 5'-nucleotidase 1 (PfISN1) (EC 3.1.3.99) (A0A144A134)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine. By dephosphorylating IMP, plays a role in the purine salvage pathway. Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32591529}.
Interaction partners:
- AMP deaminase
- Adenosine deaminase
- Inosine-5'-monophosphate dehydrogenase
- nicotinate phosphoribosyltransferase
- Adenylosuccinate synthetase
- Hypoxanthine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
Sequence:
MKNLDINTFDNIEDIPLGSSEQDPYDFFTLSDRNVMNSDMKKNIVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEMFIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPPTFNEVRHILNLAQILSLEEGLDLLTFDADETLYPDGHDFNDEVLASYISCLLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMGGESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVIKDFGLCAQIQRKEKSIGLVPNKIPSLNIKNEQKNYMIKYEVLEEAVIRIKKEIIKNKITAPYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDFPTRFCSLTLWVSNPQETKACLKSIMHLNIKSFIPEVLYENQ
Protein: Frizzled-2 (Fz-2) (rFz2) (Q08464)
Organism: Rattus norvegicus (Rat)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism.
Subcellular location: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein Wnt-5a
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- Protein Wnt
- LDL receptor related protein 5
- Low-density lipoprotein receptor-related protein
- Protein Wnt
Sequence:
MRARSALPRSALPRLLLPLLLLPAAGPAQFHGEKGISIPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSICERARQGCEALMNKFGFQWPERLRCEHFPRHGAEQICVGQNHSEDGTPALLTTAPPSGLQPGAGGTPGGPGGGGAPPRYATLEHPFHCPRVLKVPSYLSYKFLGERDCAAPCEPARPDGSMFFSHHHTRFARLWILTWSVLCCASTFFTVTTSLVAMQRFRYPERPIIFLSGCYTMVSVAYIAGFVLQERVVCNERFSEDGYRTVGQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHAAIEANSQYFHLAAWAVPAVKTITILAMGQIDGDLLSGVCFVGLNRLDPLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEPLERLMVRIGVFSVLYTVPATIVIACYFYEQAFREHWERSWVSQHCKSLAIPCPAHYTPRTSPDFTVYMIKYLMTLIVGITSGFWIWSGKTLHSWRKFYTRLTNSRHGETTV
Protein: Uncharacterized ABC transporter ATP-binding protein Rv1273c (P9WQJ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Fatty acid ABC transporter ATP-binding/permease protein
- Possible lipoprotein LprC
- Putative lipoprotein LprB
- Multidrug efflux system ATP-binding protein Rv1218c
- Probable conserved ATP-binding protein ABC transporter
- Probable second part of macrolide-transport ATP-binding protein ABC transporter
Sequence:
MLLALLRQHIRPYRRLVAMLMMLQLVSTLASLYLPTVNAAIVDDGVAKGDTATIVRLGAVMLGVTGLQVLCAIGAVYLGSRTGAGFGRDLRSAMFEHIITFSERETARFGAPTLLTRSTNDVRQILFLVQMTATVLVTAPIMCVGGIIMAIHQEAALTWLLLVSVPILAVANYWIISHMLPLFRRMQSLIDGINRVMRDQLSGVRVVRAFTREGYERDKFAQANTALSNAALSAGNWQALMLPVTTLTINASSVALIWFGGLRIDSGQMQVGSLIAFLSYFAQILMAVLMATMTLAVLPRASVCAERITEVLSTPAALGNPDNPKFPTDGVTGVVRLAGATFTYPGADCPVLQDISLTARPGTTTAIVGSTGSGKSTLVSLICRLYDVTAGAVLVDGIDVREYHTERLWSAIGLVPQRSYLFSGTVADNLRYGGGPDQVVTEQEMWEALRVAAADGFVQTDGLQTRVAQGGVNFSGGQRQRLAIARAVIRRPAIYVFDDAFSALDVHTDAKVHASLRQVSGDATIIVVTQRISNAAQADQVIVVDNGKIVGTGTHETLLADCPTYAEFAASQSLSATVGGVG
Protein: SD07644p (Uncharacterized protein, isoform A) (Q9VXU4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEALVNYSSEDDQEDAGFQIRAPQQQQQLRHLPHAKSPKTTTDSLLKQKNNNNYGSGNSPRGKEREREREREREKTKPMSQQQSHRSSSRGRIDEVKTCRCTKSIFTSHNIYQIPYAIVLHTYVCVCVSGLERKRIFHVPFPSAAAKGDAIADCAASSSTYRGRQNNSTESALNQTSNV
Protein: Matrix metalloproteinase-20 (MMP-20) (EC 3.4.24.-) (Enamel metalloproteinase) (Enamelysin) (P57748)
Organism: Mus musculus (Mouse)
Function: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Amelogenin, X isoform
- Kallikrein-4
- Enamelin
- Ameloblastin
- WD repeat-containing protein 72
- Amelotin
- Kallikrein 1-related peptidase-like b4
Sequence:
MKVLPASGLAVLVTALKFATADPNLLAATPRTFRSNYHLAQAYLDKYYTKKGGPQAGEMVARESNPMIRRIKELQIFFGLKVTGKLDQNTMNVIKKPRCGVPDVANYRLFPGEPKWKKNILTYRISKYTPSMSPTEVDKAIQMALHAWSTAVPLNFVRINSGEADIMISFETGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGTNGFNLFTVAAHEFGHALGLGHSTDPSALMYPTYKYQNPYRFHLPKDDVKGIQALYGPRKIFPGKPTMPHIPPHKPSIPDLCDSSSSFDAVTMLGKELLFFKDRIFWRRQVHLPTGIRPSTITSSFPQLMSNVDAAYEVAERGIAFFFKGPHYWVTRGFHMQGPPRTIYDFGFPRHVQRIDAAVYLKEPQKTLFFVGEEYYSYDERKKKMEKDYPKNTEEEFSGVSGHIDAAVELNGYIYFFSGRKTFKYDTEKEDVVSVVKSSSWIGC
Protein: Equilibrative nucleotide transporter 7 (AtENT7) (Nucleoside transporter ENT7) (Q944P0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleoside transporter that can mediate uptake of adenosine, uridine, guanosine or cytidine when expressed in a heterologous system (yeast).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}. Note=Plasma membrane.
Interaction partners:
- SWI-SNF-related chromatin binding protein
- F-box/LRR-repeat protein 16
- F-box protein At1g47056
- Transcription factor bHLH118
- Uridine nucleosidase 1
- Adenine/guanine permease AZG1
Sequence:
MTNPEDIPSRIEGKNVARLVCCFLGVGSLVAWNAMLTITDYYYQLFPKYHPSRVLTIVYQLVANVFIITLATKEAKLNTRLRNIFGYSLYTAGTFCLIILDLASHGSGSVVAYVLLCLIVALFGLADAFVQGAMVGDLSFMSPDFIQAFMAGLGIAGALTSVLRLITKAIFDNSPDGLRKGALLFIGIATLIELACVFLYTLVFAKLPIVKYYRAKAGKEGAKTVSADLAAAGLQEQAEQVHQMDESKIQKLTKKQLLRENIDLGINLSLIYVVTLSIFPGFLYENTGEHRLGDWYAPVLVAMYNGWDAISRFIPSIKPLAMESRKWITVCVVARLLLVPAFYFTAKYADQGWMLFLTSFLGLSNGYLTVCIFSTAPKGYNGPEANALGNLMCVFLLGGIFAGVCLGWLWLIGNDSF
Protein: Mitochondrial RNA binding protein (Q389F5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRHTSRNNALHAFVRSPHYRTIPSAGPNGIVVNRDMLVHQFRDFYKTLQHCSLVDKVHLMSERPSVEALRVADQMVSIGATFLEMPLTGMEHRATEFMESMRYVRGAGGPSTLASYLQDTENCRCNSGDVVCLPNGIAVGHGPRTNAVAHTTLKQLFEVKDDQFSFDVFTLEQEGDAPPLGDYFGFAGSNVLLTWKDEHGLLAVDQYQQKQPHTEMNVVYLEPGCHFLSFYGVDHTIDVLVQKGYERSMDSIAAAGLNPIPVQWSEMDKLGISMRAAVLPLKFFKANVGGMLSRNKSRGARWQTHQLQK
Protein: Vacuolar calcium ion transporter (Vacuolar calcium exchanger) (J9VDQ4)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Has a role in promoting intracellular calcium ion sequestration via the exchange of calcium ions for hydrogen ions across the vacuolar membrane.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:20889719}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSPPRRVSFPPDTLQEDPPLADSPLSSPKLPEYDRQSSSTPIVSSNLPTDTTNSASAGPRRRQQPSRQVTLDASPPSATRRETTESARTQRSRAGSRRTSNSLDPNPGLMRRVTTVLFTPPKKIGKAPTYWGSMKAAITSTWLNVLLVFIPIGWALYLAKHNGGKDSISDTAVFCCTFIAIIPLAGLLGFATEEAALRLGQTLGGLLNATLGNAVELIVAILALIKCELQVVQSSLVGSILSNILLVLGMCFFAGGVRFAEQAIKSTAAQLNASLLLIAVIAVLIPSAFHFSISSSTSNTDASELANGEGADLLSMSHAVSILLLILYLGYLLFQMWTHATYYVDDAVTGSTQYPEAITNVSEKLKFRNFHRRKHDEEESYSTATTVSDAAVPPSARAEGGEVPATHGPGTAAAETGNRVEHEDAEEEEEEETPQMNVVCTIALMVIDTVLVGVTAEFLVDSINGMVESNPSLSAEWVGLILLPIVGNAAEHFTAVSVSVKDKLDLSISVAVGSSIQIALFVIPVIELLAWTIGKPMTLLFDPYESIVLFLSVLIVNQTLADGRSNWMEGMVLMMLYIIIAVSFWYYPGSTTATLLGCQDSSSVTG
Protein: Bub1 kinase, isoform A (Bub1 kinase, isoform B) (Bub1 kinase, isoform C) (LD22858p) (Q9VMS5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}.
Interaction partners:
- Mitotic checkpoint protein BUB3
- Mitotic spindle assembly checkpoint protein MAD2A
- Cell division cycle protein 20 homolog
- Kinetochore protein NDC80
- Cell division cycle protein 27 homolog
- separase
- Cell division cycle 16
- Anaphase-promoting complex subunit 10
- FI09619p
- Bub1-related kinase
Sequence:
MAMHSYMRQGSGSGGGAGAVAAGAPPLASPDEMHGFLNDKQAWEHAISLYQGPDPLDHWYNYICWYENHAQSDPELKYRETLERCLTVYEHNDYYRQDVRLVRLWLKYIAMQTDPLHFYQVLFQRGTGRQVAAFYIGWAAYYESREEYKDAEAVFNLAFQEKAQSTSELQHAHTKFAYARSLFYQRQQQQQQQQQQHQQHPPQDALQQLTNYAQQQMPQSYNQHRPQPYQQNVYQQYHPQAQAHQAPQPHQPAPQQQLPPEQQVPYQTHYQERPRYEPHPATQSPTAIPPSQVQQQSHYAPVAESHYAPAQQSQLPPQQTTVPQLHAQQPQQQQNGNGNPPPQQSPPVTNEVAGLRLPRNFHAYGRNNHETWKPALTLEEPDDPSRVCHYAKQLVYPPGAGVEYSPEEILARKFKQLMDQKAKPSEPPEQEQQTLYDSYETEKSYYMTAVDGALYGQNTSSGQENTGEEDEDNDAEEGEEEEDGGEENEEDDSDEEEEDDEEEEEHSGPYTNGVQFSAQTTFEQENRSIKIKFRKEPSSTYSAYTIENVYQQQQQQQQEQHQIIHQPPQAVHHPSPDPAPASPIPIQRQRNGSHHHFHPYMLGQTSTPKSEANGYRRARTKVKRSKFQPDLCSNSNSASSVADVASSSVLAGAPGTFNDNANFSFSSATALDNSNSSLALAVDRLNFRDTSQQQILHPVNKTLQIHNNNNNTSNNNNGTSTMADFSTFQENSYFATQHDTEAQERRLSKAVETIARHMDKEAIDPFNSELCRAFLAKLDFPGNHDAHASYKIVQTPLPKISNTRTLNVLEGVTFSIDKEVGRGSYGSVYKATDSRTGNVVALKYQKPPNTWEIYICDQVLKRIKEPEVLPGVMDISTAIIAPNASLIATEFSPFGSLLDINNKIRQATTKVMHESLVMHFSAQICNIVDHLHRQHIIHADIKPDNFLLMRVPNVDSPLPSLRLIDFGCAIDMTLFPDGEKTKFRKVVQTDGFTCIEMQEGRSWSYETDLFCIAATVHVMLFGDYMQPQKKGSSWEIRQKLPRYLKKHVWTKFFGDLLNMQADKLPALHEMRLIFEEEAYRMDSELQKQIRTLSNILHRR
Protein: Protein lin-61 (Abnormal cell lineage protein 61) (B2D6M2)
Organism: Caenorhabditis elegans
Function: Synthetic multivulva class B (synMuvB) protein required to repress the induction of vulval development by Ras signaling. Unlike other synMuv proteins it does not associate with the multiprotein DRM complex and the NuRD-like complex. Interaction with methylated histone H3 is essential for vulva development. It has a role in maintaining genome stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:17409073}. Chromosome {ECO:0000269|PubMed:17409073}.
Interaction partners:
- Chromo domain-containing protein.
- Zinc finger protein lin-13
- Chromobox protein homolog hpl-1
- Chromo domain-containing protein cec-4
- Transcription factor dpl-1
- Retinoblastoma-like protein homolog lin-35
- Histone-lysine N-methyltransferase set-25
- Chromo domain-containing protein cec-3
- Protein let-418
- E2F/DP family winged-helix DNA-binding domain-containing protein
Sequence:
MLKLVILCFALFYNTVSSTRFLFGVEVKCDFDEVFQLTVSHWEDDGNTFWDRDEDITGRMTMFARKKIFFYQDGHHGFEFGKLEPYGWFLHNCTKNGNFREYRHGLSSTSGSNGLEYIEYTMSEFLKIVRANKKSDRKLDKTYLWESYLHQFEKGKTSFIPVEAFNRNLTVNFNECVKEGVIFETVVHDYDKNCDSIQVRWFARIEKVCGYRVLAQFIGADTKFWLNILSDDMFGLANAAMSDPNMDKIVYAPPLAINEEYQNDMVNYVNNCIDGEIVGQTSLSPKFDEGKALLSKHRFKVGQRLELLNYSNSTEIRVARIQEICGRRMNVSITKKDFPESLPDADDDRQVFSSGSQYWIDEGSFFIFPVGFAAVNGYQLNAKKEYIEHTNKIAQAIKNGENPRYDSDDVTFDQLAKDPIDPMIWRKVKVGQKFELIDPLAQQFNNLHVASILKFCKTEGYLIVGMDGPDALEDSFPIHINNTFMFPVGYAEKYNLELVPPDEFKGTFRWDEYLEKESAETLPLDLFKPMPSQERLDKFKVGLRLEAADMCENQFICPATVKSVHGRLINVNFDGWDEEFDELYDVDSHDILPIGWCEAHSYVLQPPKKYNY