wanglab/gogpt-training-data huggingface dataset:
Protein: D-xylulose reductase (EC 1.1.1.9) (Xylitol dehydrogenase) (A2QM95)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MTSSVVRLGQKCPAFVLHPGGRFDYEERVIPNLQTDRDVIVQVIVTGLCGSDIHYWQHGRIGRYVVEAPIVLGHESAGIVVECGSKSGFAIGDRVALEPGIACNTCHHCRAGRYNLCSAMRFAATPPYDGTLATYYRLPAECCYKLPAHVSLQHGALVEPLSVAVHSCRLAGDMQQKSVVVFGAGPVGLLCASVSRAFGASTVVVVDINSDRLSVAQKYGATHTYKMSNESPEHNAARILEEMELDNGAHIVLDATGAEPCMNCGISVLASGGTFVQVGLGKPNPSLPVGQICDKEAIFRGSFRYGPGDYRTAIGLLSSGRVVLEGLVTHEFPFTQAEEAFKNVGNRQGIKTVIYGPGADENAAKATLT
Protein: DNA replication licensing factor MCM2 (EC 3.6.4.12) (Minichromosome maintenance protein 2) (AtMCM2) (Q9LPD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. May play a crucial role in the control of de-differentiation and cell proliferation processes required for lateral root formation. Is essential for embryo development. Is involved in the geminivirus mungbean yellow mosaic virus (MYMV) DNA replication, presumably in conjunction with other host factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Cell division cycle 45
- Origin of replication complex subunit 2
- Cell division control protein 6 homolog
- Mini-chromosome maintenance complex-binding protein
- Origin of replication complex subunit 5
Sequence:
MAGENSDNEPSSPASPSSAGFNTDQLPISTSQNSENFSDEEEAAVDTQVIRDEPDEAEDEEEEEGEDLFNDTFMNDYRKMDENDQYESNGIDDSVDDERDLGQAMLDRRAADADLDARENRLANRKLPHLLHDNDSDDWNYRPSKRSRTTVPPRGNGGDPDGNPPSSPGVSQPDISMTDQTDDYQDEDDNDDEAEFEMYRIQGTLREWVMRDEVRRFIAKKFKDFLLTYVKPKNENGDIEYVRLINEMVSANKCSLEIDYKEFIHVHPNIAIWLADAPQPVLEVMEEVSEKVIFDLHPNYKNIHTKIYVRVTNLPVNDQIRNIRQIHLNTMIRIGGVVTRRSGVFPQLQQVKYDCNKCGAVLGPFFQNSYSEVKVGSCSECQSKGPFTVNVEQTIYRNYQKLTIQESPGTVPAGRLPRHKEVILLNDLIDCARPGEEIEVTGIYTNNFDLSLNTKNGFPVFATVVEANYVTKKQDLFSAYKLTQEDKTQIEELSKDPRIVERIIKSIAPSIYGHEDIKTALALAMFGGQEKNIKGKHRLRGDINVLLLGDPGTAKSQFLKYVEKTGQRAVYTTGKGASAVGLTAAVHKDPVTREWTLEGGALVLADRGICLIDEFDKMNDQDRVSIHEAMEQQSISISKAGIVTSLQARCSVIAAANPVGGRYDSSKSFAQNVELTDPILSRFDILCVVKDVVDPVTDEMLAEFVVNSHFKSQPKGGKMEDSDPEDGIQGSSGSTDPEVLPQNLLKKYLTYSKLYVFPKLGELDAKKLETVYANLRRESMNGQGVSIATRHLESMIRMSEAHARMHLRQYVTEEDVNMAIRVLLDSFISTQKFGVQRTLRESFKRYITYKKDFNSLLLVLLKELVKNALKFEEIISGSNSGLPTIEVKIEELQTKAKEYDIADLRPFFSSTDFSKAHFELDHGRGMIKCPKRLITW
Protein: Small ribosomal subunit protein uS9 (30S ribosomal protein S9) (P9WH25)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL9
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL18
Sequence:
MTETTPAPQTPAAPAGPAQSFVLERPIQTVGRRKEAVVRVRLVPGTGKFDLNGRSLEDYFPNKVHQQLIKAPLVTVDRVESFDIFAHLGGGGPSGQAGALRLGIARALILVSPEDRPALKKAGFLTRDPRATERKKYGLKKARKAPQYSKR
Protein: Vitamin D-binding protein (DBP) (VDB) (Gc-globulin) (Group-specific component) (P04276)
Organism: Rattus norvegicus (Rat)
Function: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation.
Subcellular location: Secreted {ECO:0000269|PubMed:3713442}.
Interaction partners:
- Cubilin
- Low-density lipoprotein receptor-related protein 2
- Alpha-2-HS-glycoprotein
- Albumin
- Protein AMBP
- Transthyretin
- Vitamin D 25-hydroxylase
- Fibrinogen beta chain
- 1,25-dihydroxyvitamin D
- Alpha-1-macroglobulin
Sequence:
MKRVLVLLLALAFGHALERGRDYEKDKVCQELSTLGKDDFRSLSLILYSRKFPSSTFEQVSQLVKEVVSLTEECCAEGADPNCYDTRTSELSIKSCESDAPFPVHPGTSECCTKEGLERKLCMAALSHQPQEFPAYVEPTNDEICEAFRKDPKGFADQFLFEYSSNYGQAPLPLLVGYTKSYLSMVGSCCTSAKPTVCFLKERLQMKQLLLLTTMSNRVCSQYAAYGKEKSRMSHLIKLAQKVPTANLEDVLPLAEDLTEILSRCCKSTSEDCMARELPEHTLKICGNLSKKNSKFEECCYETTPMGIFMCSYFMPTAEPLQLPAIKLPTSKDLCGQSATQAMDQYTFELSRRTQVPEVFLSKVLDTTLKTLRECCDTQDSVSCFSTQSPLMKRQLTSFIEKGQEMCADYSENTFTEYKKKLAERLRTKMPNASPEELADMVAKHSDFASKCCSINSPPRYCSSQIDAEMRDILQS
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (Q4KSH6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAPSPSGGGGSGGGGGTPGPIGPPASGHPAVSSMQGKRKALKLNFANPPVKSTARFTLNPNTTGVQNPHIERLRTHSIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERTVEVACYVCKILDQMPATPSSPMYVD
Protein: Glutamate receptor-interacting protein 1 (GRIP-1) (Q925T6)
Organism: Mus musculus (Mouse)
Function: May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons (By similarity). Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity).
Subcellular location: [Isoform 2]: Membrane; Lipid-anchor.; SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9Y3R0}. Perikaryon {ECO:0000250|UniProtKB:P97879}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97879}. Cytoplasm {ECO:0000250|UniProtKB:P97879}. Endomembrane system {ECO:0000250|UniProtKB:P97879}; Peripheral membrane protein {ECO:0000250|UniProtKB:P97879}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P97879}. Postsynaptic density {ECO:0000250|UniProtKB:P97879}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y3R0}; Peripheral membrane protein {ECO:0000250|UniProtKB:P97879}. Note=Membrane-associated with vesicles, peri-Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic plasma membrane and postsynaptic densities. {ECO:0000250|UniProtKB:P97879}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 3
- PRKCA-binding protein
- GRIP1-associated protein 1
- Glutamate receptor 1
- Chondroitin sulfate proteoglycan 4
- Glutamate receptor 4
- Ephrin-B2
- Kinesin heavy chain isoform 5A
- Ppfia1 protein,-interacting protein
Sequence:
MIAVSFKCRCQILRRLTKDESPYTKSASQTKPPDGALAVRRQSIPEEFKGSTVVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEVEYELPPVSVQGSSVMFRTVEVTLHKEGNTFGFVIRGGAHDDRNKSRPVVITCVRPGGPADREGTIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEATLLIEYDVSVMDSVATASGPLLVEVAKTPGASLGVALTTSVCCNKQVIVIDKIKSASIADRCGALHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVKLEILPHHQTRLALKGPDHVKIQRSDRQHPWDAWASNQCGVHTNHHHNTYHPDHCRVPALTFPKALPPNSPPAMVPSSSPTSMSAYSLSSLNMGTLPRSLYSTSPRGTMMRRRLKKKDFKSSLSLASSTVGLAGQVVHTETTEVVLTADPVTGFGIQLQGSVFATETLSSPPLISYIEADSPAERCGVLQIGDRVMAINGIPTEDSTFEEANQLLRDSSITSKVTLEIEFDVAESVIPSSGTFHVKLPKKHSVELGITISSPSSRKPGDPLVISDIKKGSVAHRTGTLELGDKLLAIDNIRLDNCSMEDAVQILQQCEDLVKLKIRKDEDNSDEQESSGAIIYTVELKRYGGPLGITISGTEEPFDPIIISSLTKGGLAERTGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTLKIKKQTDAQSASSPKKFPIPGHSGDLGDGEEDPSPIQKPGKLSDAYPSTVPSVDSAVDSWDGSGIDASYGSQGSTFQTSGYNYNTYDWRSPKQRTSLSPVPKPRSQTYPDVGLSNEDWDRSTASGFVGASDSADAEQEENFWSQALEDLETCGQSGILRELEEKADRRVSLRNMTLLATIMSGSTMSLNHEAPMARSQLGRQASFQERSSSRPHYSQTTRSNTLPSDVGRKSVTLRKMKQEIKEIMSPTPVELHKVTLYKDSGMEDFGFSVADGLLEKGVYVKNIRPAGPGDVGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDLVISRNPLASQKSIEQPALPSDWSEQNSAFFQQPSHGGNLETREPTNTL
Protein: Collagen type VI alpha 5 chain (A0A287BK35)
Organism: Sus scrofa (Pig)
Interaction partners:
- Collagen type V alpha 1 chain
- Collagen alpha-2
Sequence:
MKSLTIIFVLIFWTETLTDQSPGPGPEYADVVFLVDSSDHLGTKSFPYMKTFINKMINSLPIETDKYHVGLAQYSDKLHTEFQLNTFKSKGPMLNHLKKNFGFLGGSLRIGNALREVHRTYFSNGRDRKQFPPILVVLASADSEDAVEEAAEALRKDGVRIISVGMQRVSEETLKAMATGQFHYNLRTVRDLSAFSQNMTQVLKEAIQYKEGAPSPWVCSNLHTFSLSKGPFLRACEKDSLADVIFLVDESVGTSQNLRNLQNFLKNITSYMDVKDNCLRLGLMSYSDRAETLSVLKSSTSQAEFQKQIQKLSLRAGKSNVGAAVEKMRREGFSASSGSRRALGVPQIAVLVTNRPSDDEVREATLNLRLDDVTVFAMGIHGANKTQLEEIASYPPRQTISMLESYADLGNYTNNFLKKLQNEIWSQISTKAEQKELDKTGCVDTKEVDIYFLIDGSGSIRSDHFEQIKKFMLEVIENFDIGPDKVRVGAVQYSDTREKEFDITDYTTDETLRKAISNIRQLGGGTYTGEALDFILQIIKKGREQRINKVPCYLIVLTDGMSMDDVLEPAEKLRAENIAVHAIGIGEANRTQLQQIAGKEERVSFGQNFDSLKNIKNEVLHSICTEKGCEDMKADIMFLVDSSGSIGPENFRTMKSFMKNLLAKIQIGLDKTRIGVVQFSDVTKEEFKLDTYFTQKEISDAIERMSPIEQNTLTGKALTSIEPYFTESKGARSMVRKFLILITDGEAQDDVRNPAKVLRDKGVVIFAVGVFRANRTQLEEISGDSSLVFQVESFSDLQEIENKLIFRVCALHDCKRIKELDVVFVLDHSSSIQPRDQESMINLTMHLVKKSDVGPNRVQFGALRYSNEPDIIFYLNSNRSAIMEYLRSLSAKGGDTYTAKALERANILFTEEHGSRIKQNVKQMLIIITDGKSHDHIHLSDKASKLRAKGIIIYAVGVGEANQEELETMAGNKHYTIHVSNFDSLKDVYQPLQESMCTNAQESCSISEADVIFFCDGSDMVSDSDFVTMTTFLSDLIDNFDIESQRIKIGMAQFGSRYQEIIELQNSLNKTQWKSQIQTTTKSKGLPRMDLALKKVKFMFEQSVGGRRNAGVPQTLMVITSADPRHDVAEAVKTLRESGICIMVLGLGNVHKERLLPITGNSEKIITFQDFDKLKNVDVKKRMVREICQSCSKTNCFLDIVVGFDISTHRQGQLLFHGHPRLESYLPGILEDITSIRGVSCGAGAEVQVSVAFKVNSDQNFTTKFHIYKKTVFDRLLELTVNGATHLNAQFLQSMWATFNDTSASRGQVLLIFSDGLGGESKAMLEDQSDRLRKAGLDALLVVSLNAPIHNEFSSFEFGKGFDYRTPLTIGTRELGKMLSQYLGNIAERTCCCTFCKCSGTPGPPGIRGPQALKGEPGIPGDPGPVGPTGQRGKQGDYGIPGYGRVGKKGVKGPRGFPGDIGQKGDVGDPGIPGGPGPKGFRGLTVKKCPVYPTELVFALDQSYDITEQRFNETRDIITSIVNDLHIWENNCPVGARVVVVSYNSGTSYLIRGSDYRNKKQLLQLLSQIKYQNSGEVRDMGNAMRFVARNIFKRTFSGPNVRRVAVFFSNGQATSSSSIITATMEFSALDISPAVFAYNERVFLDEAFGFDNTGTFQVLPVPLNGEYEPLEKLRRCTLCYDKCFPDACSKKIFLPEDTYMDVAFLLDNSRNIASDEFKNVKALVSSMLDNFDIASYPLISDSGDRIALLSYSPWDRRKKDAIKTEFEFTTYDNQVLMKNHIQNYLQQLNGEATIGHALLWTMENLFPGTPNLRKHRVIFVVSAGENHERKEFLRKMALRAKCQGYVIFVISLGSTQEGDMEELASYPLDHHLIQLGRTHKPNLDYIVKFLKPFVYSVRRGFNQYPPPTLANACRLIDSEEDNPNTGLLFASEAHEISSGEDSFLGQELSAAKDSPFVMEDSGNDHLIYTPSQKIVPQKLMTKYEKYQDSEVIASLTSEHETGGRREEPGLTSELRDASLQEYYMDVAFLIDASRKVGNDEFKEVKAFISSVLDYFHLAPDPLTSTLGDRVAVLTYSPPGYMPNTEECPVYLEFDLVTYNSMHQMKHHLQDSLQQLNGDVFIGHALQWTIDNVFIGTPNLRKNKVIFVISAGETNPLDKEVLRNVSLRAKCQGYSIFVFSFGPLHNDKELEQLASQPLDHHLVQLGRTHKPDMNYIIKFVKPFVHSVRRAINKYPPADLRPKCVDITSPNPENDDTENTVFLLPEVYEIETENSEPWGGFGSQQQHLFELGDSHDNGSGIIDDLIQKLSMFFLTEELMMKDEEEAHSEEITAAENDRQ
Protein: Prohibitin-7, mitochondrial (Atphb7) (Q9FFH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:18189341}; Single-pass type II membrane protein {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:18189341}.
Interaction partners:
- Prohibitin-4, mitochondrial
- Prohibitin-3, mitochondrial
- Prohibitin-5, mitochondrial
- At5g40700
- At5g54100
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Hypersensitive-induced response protein 4
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase 1 alpha subcomplex subunit 8-A
Sequence:
MNVKKVPNVPGSPALSALLKLGVIGGLGLYCIGSSMYNVDGGHRAIVFNRFTGIKDRVYPEGTHFKIPLFERAIIYDVRSRPYVENSQTGSNDLQTVTIGLRVLTRPMGDRLPEIYRTLGQNYGERVLPSIINETLKAVVAQYNASHLITQREAVSREIRKIVTERAAKFNIALDDVSITNLKFGKEFTEAIEKKQVAAQEAERAKFIVEKAEQDKKSAIIRAQGEAKSAQLIGQAIANNEAFITLRKIEAAREIAQTIAKSANKVYLNSSDLLISKQ
Protein: N-acetylgalactosamine-6-sulfatase (EC 3.1.6.4) (Chondroitinsulfatase) (Chondroitinase) (Galactose-6-sulfate sulfatase) (N-acetylgalactosamine-6-sulfate sulfatase) (GalNAc6S sulfatase) (Q571E4)
Organism: Mus musculus (Mouse)
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
- Beta-galactosidase
- Formylglycine-generating enzyme
- Lysosomal protective protein
Sequence:
MAACTAAQQLLLVLSALGLLAAGAPQPPNIVLLLMDDMGWGDLGVNGEPSRETPNLDRMAAEGMLFPSFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIMGGIPNSEHLLPELLKKAGYTNKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKAKPNIPVYRDWEMVGRFYEEFPINRKTGEANLTQLYTQEALDFIQTQHARQSPFFLYWAIDATHAPVYASRQFLGTSLRGRYGDAVREIDDSVGKILSLLQNLGISKNTFVFFTSDNGAALISAPNEGGSNGPFLCGKQTTFEGGMREPAIAWWPGHIAAGQVSHQLGSIMDLFTTSLSLAGLKPPSDRVIDGLDLLPTMLKGQMMDRPIFYYRGNTLMAVTLGQYKAHLWTWTNSWEEFTQGTDFCPGQNVSGVTTHTQEEHTELPLIFHLGRDPGERFPLSFHSDEYQDALSRTTQVVQEHQKSLVPGQPQLNVCNQAVMNWAPPGCEKLGKCLTPPESVPEKCFWAH
Protein: Ubiquitin-associated and SH3 domain-containing protein A (Suppressor of T-cell receptor signaling 2) (STS-2) (T-cell ubiquitin ligand 1) (TULA-1) (Q3V3E1)
Organism: Mus musculus (Mouse)
Function: Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. May inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain (By similarity). Exhibits negligigle protein tyrosine phosphatase activity at neutral pH. May act as a dominant-negative regulator of UBASH3B-dependent dephosphorylation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase ZAP-70
- E3 ubiquitin-protein ligase CBL
- Lymphocyte cytosolic protein 2
Sequence:
MAAGETQLYAKVSNKLKGRSTPSLLDPLLAMGFPTHTALKALAATGRKTAEAAADWLHGHCNDPSLDDPIPQEYALFLCPTGPLLEKLQEFWRESRRQCAKNRAHEVFPHVTLCDFFTCEDQKVECLYEALRRAGDRILGSFPTLVPLVLHSSISYLGFFINDSPADAIREFAMAFATEAAVLADCTIKPCTKQLHLTLAHKFYPHHQRTLEQLAKAIQPSHSCQWTAALYSRDMRFVHYQTLKALFQYKPQNADELMLSAGDYIFVDPTQQEEASEGWAIGISHRTGCRGFLPENYTERANEADTWVKHRTYTFNLAMDLNSRKDFEASCRGNGEPHTPSMSKSVSSIQALQATISRRGILVVRHGERVDQVFGKSWLQQCTTADGKYYRPDLNFPRSLPRRSNGIKDFENDPPLSSCGIFQARLAGEALLDSGVRVTAVFASPALRCVQTAKHILEELKLEKKLKIRVEPGIFEWMKWEASKATLTFLTLEELKEANFNVDLDYRPALPRCSLMPAESYDQYVERCAVSMGQIINTCPQDMGITLIVSHSSALDSCTRPLLGLPPRECGDFAQLVRKIPSLGMCFCEENREDGKWDLVNPPVKTLTHGANSVFNWRNWISSN
Protein: ABC transporter G family member 25 (ABC transporter ABCG.25) (AtABCG25) (White-brown complex homolog protein 26) (AtWBC26) (Q84TH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity abscisic acid (ABA) transporter that mediates the export of ABA, with a preference for (+)-ABA, through the plasma membrane, especially in vascular tissues (e.g. phloem companion cells), and is involved in the intercellular ABA signaling pathway. Together with ABCG31, export ABA from the endosperm to deliver it to the embryo via ABCG30 and ABCG40-mediated import to suppress radicle extension and subsequent embryonic growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20133881}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DETOXIFICATION 50
- Protein NRT1/ PTR FAMILY 4.6
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- Protein NRT1/ PTR FAMILY 6.3
Sequence:
MSAFDGVENQMNGPDSSPRLSQDPREPRSLLSSSCFPITLKFVDVCYRVKIHGMSNDSCNIKKLLGLKQKPSDETRSTEERTILSGVTGMISPGEFMAVLGPSGSGKSTLLNAVAGRLHGSNLTGKILINDGKITKQTLKRTGFVAQDDLLYPHLTVRETLVFVALLRLPRSLTRDVKLRAAESVISELGLTKCENTVVGNTFIRGISGGERKRVSIAHELLINPSLLVLDEPTSGLDATAALRLVQTLAGLAHGKGKTVVTSIHQPSSRVFQMFDTVLLLSEGKCLFVGKGRDAMAYFESVGFSPAFPMNPADFLLDLANGVCQTDGVTEREKPNVRQTLVTAYDTLLAPQVKTCIEVSHFPQDNARFVKTRVNGGGITTCIATWFSQLCILLHRLLKERRHESFDLLRIFQVVAASILCGLMWWHSDYRDVHDRLGLLFFISIFWGVLPSFNAVFTFPQERAIFTRERASGMYTLSSYFMAHVLGSLSMELVLPASFLTFTYWMVYLRPGIVPFLLTLSVLLLYVLASQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGYYVNKVPSGMVWMKYVSTTFYCYRLLVAIQYGSGEEILRMLGCDSKGKQGASAATSAGCRFVEEEVIGDVGMWTSVGVLFLMFFGYRVLAYLALRRIKH
Protein: Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) (Tripeptide aminopeptidase LTA4H) (EC 3.4.11.4) (P30349)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities (By similarity). Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides. In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P09960}.
Interaction partners:
- Leukotriene C4 synthase
- Polyunsaturated fatty acid 5-lipoxygenase
- Cytochrome P450 4F3
- Cytochrome P450 4F1
- Cytochrome P450 4F6
- Arachidonate 5-lipoxygenase-activating protein
- Leukotriene B4 receptor 1
Sequence:
MPEVADTCSLASPASVCRTQHLHLRCSVDFARRALTGTAALTVQSQEDNLRSLTLDTKDLTIEKVVINGQEVKYTLGESQGYKGSPMEISLPIALSKNQEVVIEISFETSPKSSALQWLTPEQTSGKQHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGEAPDPEDPSRKIYRFNQRVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFHALGGWGELQNTIKTFGESHPFTKLVVDLKDVDPDVAYSSIPYEKGFALLFYLEQLLGGPEVFLGFLKAYVEKFSYQSVTTDDWKSFLYAHFKDKVDLLNQVDWNAWLYAPGLPPVKPNYDVTLTNACIALSQRWVTAKEEDLNSFSIEDLKDLSSHQLNEFLAQVLQKAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEEAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKACMHPVTAMLVGKDLKVD
Protein: Snake venom metalloproteinase-disintegrin-like mocarhagin (MOC) (Mocarhagin-1) (SVMP) (EC 3.4.24.-) (Zinc metalloproteinase mocarhagin) (Q10749)
Organism: Naja mossambica (Mozambique spitting cobra)
Function: Snake venom zinc metalloproteinase that inhibits platelet aggregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu-298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to GPIBA. Cleaves P-selectin glycoprotein ligand-1 (PSGL-1/SELPLG) at Tyr-51/Asp-52, and completely abolishes the binding of PSGL-1 to P-selectin. Anionic amino acid sequences containing sulfated tyrosines are needed for cleavages. Inhibits the thrombin-induced platelet aggregation, and the thrombin-induced release of ATP and ADP. Has lectin activity (inhibited by heparin).
Subcellular location: Secreted {ECO:0000269|PubMed:8664285}.
Interaction partners:
Sequence:
MIQALLVAICLAVFPYQGSSIILESGNVNDYEVVYPQKVPALSKGGVQNPQPETKYEDTMQYEFHVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSSPVQDHCYYHGYIQNEADSSAVISACDGLKGHFKHQGETYFIEPLELSDSEAHAIYKDENVEEEEEIPKICGVTQTTWESDEPIEKSSQLTNTPEQDRYLQAKKYIEFYVVVDNVMYRKYTGKLHVITRRVYEMVNALNTMYRRLNFHIALIGLEIWSNGNEINVQSDVQATLDLFGEWRENKLLPRKRNDNAQLLTSTEFNGTTTGLGYIGSLCSPKKSVAVVQDHSKSTSMVAITMAHQMGHNLGMNDDRASCTCGSNKCIMSTKYYESLSEFSSCSVQEHREYLLRDRPQCILNKPSRKAIVTPPVCGNYFVERGEECDCGSPEDCQNTCCDAATCKLQHEAQCDSGECCEKCKFKGAGAECRAAKNDCDFPELCTGRSAKCPKDSFQRNGHPCQNNQGYCYNGTCPTLTNQCATLWGPGAKMSPGLCFMLNWNARSCGLCRKENGRKILCAAKDVKCGRLFCKKKNSMICHCPPPSKDPNYGMVAPGTKCGVKKVCRNRQCVKV
Protein: SD04054p (Q960F4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKSCLSVSEESNMIVAVRVRPLNALECTRGQVTNVVQVHGNSNELTVQAGSSADASAGVTHFFSYDQVYYSCDPERKNFACQAKVFEGTARPLIDTAFEGYNACLFAYGQTGSGKSYSMMGIEALDDAALDGGPPHYEAGIIPRFCHELFRRIEAVKSQQQLQVEVEVSYFEIYNEKIHDLLSVQHAAATTGESTPIQQQQQQQRPALKVREHPIFGPYVVDLSAHSVDSYSALRNWLAVGNSQRATASTAMNDKSSRSHSIFNIVLNLTDLSSDDGLSSDTDSSTASSLRQTRRSKISLVDLAGSERISVSGSNGERIREGVSINKSLLTLGKVIAALADSRKASANGPLVSGTPSTFVPYRESVLTWLLRENLGGNSKTVMLATISPASIHADETLATLRYACKARSIVNRVKVNESPHDKIIRDLRAEVDRLKSLRNEYERQRRLSGNSNNPVPRKIIIETSVDETEVEALRQQLAERERELSRAQKSWMEKLKEAEDQRKSELRVLKRRGLALELTAEQKQACLVNLTADPILSGTLFYLLPQGLVRIGRGRLPGGSSSSQPDIVLDGPLVALQHCSIEHERGGKLYVIPGSEDFETYVNGELLKDRRQLYHGDRLVIGGSHYFRISNPFCSQRGKADHPVDFQLAHQEVLQKQEQQLRSELEAEKRAALTKIEQERAQHARDFEERLQCLELEQFKYKCNSEMLETERQALALAQQQEHTPLRHEDGVSTPAQKSTILEDIQRIMLNPSEESLHKTQLMVKEATQRCRQLDLPLEFRQTQTPDEFGLLRTVILILDKQRGMKAEWPTARLGVWLDLVRDNAEQQEKLNATTIFQSVEVNWEPLDADLNETLSDTHNSSRIALNLSAMKDVLLNKPLKRLLNASSSKSNTPRQTSTPSPGSQLVHFTKRLLTYDPEEIPESQSSFTTLVQQELQIMQRSAQRLRRHCEAALLERENHQDNGVLAVSLQEALARMDTVLNGMHTSLARAEATACVTSPTKTQKAVRFLID
Protein: Mitogen-activated protein kinase kinase kinase 10 (EC 2.7.11.25) (D3ZG83)
Organism: Rattus norvegicus (Rat)
Function: Activates the JUN N-terminal pathway.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- Huntingtin
- Kinesin light chain
- Protein phosphatase 1 regulatory subunit 37
- Kinesin-like protein
Sequence:
MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPTDLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKQLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMSQLSQEKPRVRKRKGNFKRSRLLKLREGSSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGSSGGSGTWSRSGPPKKEELVGGKKKGRTWGPSSTLQKERAGGEERLKALGEGSKQWSSSAPNLGKSPKHTPMAPGFASLNEMEEFAEADEGNNVPPSPYSTPSYLKVPLPAEASPCAQPPWEPPAATPSRPGHGARRRCDLALLGCATLLSAVGLGADVAEARAGDGEEQRGWLDGLFFPRPGRFPRGLSPTGRPGGRREETAPGFGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPTAPSPPPSLLPPSPSTNPLVDVELESFKKDPRQSLTPTHVTAAHAVSRGHRRTPSDGALRQREPPELTNHGPRDPLDFPRLPDPQALFPTRRRPLEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLSISPPSRPDTPESPGPLSVQPTLLDMDMEGQSQDNTVPLCGAYGSH
Protein: Mannose-1-phosphate guanylyltransferase catalytic subunit beta (EC 2.7.7.13) (GDP-mannose pyrophosphorylase B) (GTP-mannose-1-phosphate guanylyltransferase beta) (Q9Y5P6)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23768512}.
Interaction partners:
- Mannose-1-phosphate guanylyltransferase regulatory subunit alpha
- Phosphomannomutase 2
- Phosphomannomutase 1
- GDP-mannose 4,6 dehydratase
- Protein O-mannosyl-transferase 2
- dTDP-D-glucose 4,6-dehydratase
- Protein O-mannosyl-transferase 1
- Ribitol 5-phosphate transferase FKRP
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Ribitol-5-phosphate xylosyltransferase 1
Sequence:
MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQVLEKEMKAQEQRLGIRISMSHEEEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFVEKPQVFVSNKINAGMYILSPAVLQRIQLQPTSIEKEVFPIMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQSLRQKQPERLCSGPGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDARIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGASVLPHKSIGESVPEPRIIM
Protein: Transcriptional regulator (Q9CHA6)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Interaction partners:
Sequence:
MNEVEFNVSNAELIVMRVIWSLGEARVDEIYAQIPQELEWSLATVKTLLGRLVKKEMLSTEKEGRKFVYRPLMEECTAINLMADGLIQKVCETKHVNVLQEMIEKSTLTAKDIELLQESLNAKEVVGQKHCNCLETSGLCACKHEHEQISA
Protein: Methyl-CpG-binding domain protein 3-like 2 (MBD3-like protein 2) (Q8NHZ7)
Organism: Homo sapiens (Human)
Function: May displace the NuRD complex from chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15701600}.
Interaction partners:
- Methyl-CpG-binding domain protein 3-like 3
- Tripartite motif-containing protein 43
- Paired-like homeodomain transcription factor LEUTX
- Acrosomal protein SP-10
- Zinc finger and SCAN domain-containing protein 4
- Dolichol-phosphate mannosyltransferase subunit 1
- demerged
- Metastasis-associated protein MTA1
- Double homeobox protein 4-like protein 2
Sequence:
MGEPAFTSFPSLPVLGKLKRNMMPWALQKKREIHMAKAHRRRAARSALPMRLTSCIFRRPVTRIRSHPDNQVRRRKGDEHLEKPQQLCAYRRLQALQPCSSQGEGSSPLHLESVLSILAPGTAGESLDRAGAERVRSPLEPTPGRFPAVAGGPTPGMGCQLPPPLSGQLVTPADIRRQARRVKKARERLAKALQADRLARRAEMLTGG