wanglab/gogpt-training-data huggingface dataset:
Protein: 26S proteasome non-ATPase regulatory subunit 5 (Q20058)
Organism: Caenorhabditis elegans
Interaction partners:
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 6
- Probable 26S proteasome regulatory subunit 4
- PCI domain-containing protein
- Proteasomal ubiquitin receptor ADRM1 homolog
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 8
Sequence:
MASLEEHEKLIEEWRNDYIAERSSKKGWEILEKLAKMQIEAAQQMETEDDVAAADFDDFSTSKLVKLIIGDISTKDLLVDHQIILLEFIPSAHPNILRHVVRTVREKEGAISLLKSSSVAIGVAFARRVTDAEAGEEVGRLMAHLVDHDLINEELKSQLSVANGRESSSIRSRIYSIATERARISSNTSCIHWLYDKILKSVLDTQDVLAQLDALDTFVDIALSGKQNAEALYELGIVKKIYELMEWSKESPDGGEMYLYGTRFMCYMARSYPQVLKYFPDLARRLMLEIRMFDQLSVVSRLGAFDHFASMCFSVEAKETLEDMFKDSKDLENTLGAAGAACTMGTMELKCRTLQAVTLLFQNTTEKIAETWYERLGGKALTHVAVGNVKKPFPEMKNCIYDFWQQLFTYPSVVHQFITFQGFIDWALDDKSEDNPEYEIRKRQIIHRIIELSENTKSAEVLKADPELIGRLKKYLQPAVAPAPRVEEMAL
Protein: Small nuclear ribonucleoprotein Sm D3 (Sm-D3) (snRNP core protein D3) (Q4Q2F6)
Organism: Leishmania major
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365050}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Sm protein F
- Putative small nuclear ribonucleoprotein
- Small nuclear ribonucleoprotein E
- Sm protein G
- Sm protein B
- Putative U1 small nuclear ribonucleoprotein
- Small nuclear ribonucleoprotein component-like protein
- U5 snRNA-associated splicing factor
- U6 snRNA-associated Sm-like protein LSm4
Sequence:
MAESIPIKVLFDALHLKVSIEVATGEVYHGTVEELQNNMNVLLKDATKTARGGKETKMDSVFVRGSNIVFFQLPDALQTSPALLRAGEVVSKAKDTRGDGKGFGASRKRARNS
Protein: GCS light chain (Gamma-ECS regulatory subunit) (Gamma-glutamylcysteine synthetase regulatory subunit) (Glutamate--cysteine ligase modifier subunit) (Q966L2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTYCHQFLSNLSSLTRFRLHTGNVNGYTQLKVRRFETSAEELAACLDLQLSSNPIADDFKENSCLLLCDNDHIDNYERDEIKITMKVFLSAWDVQQIDQAVTSLKEQLKTKDIEVLILSFPELDLIDGESEEDENNRWFEKVKPLYTYMEKLVETSEIASIGVSDFSARQLKTIIDHFDVKPSINHVRLDGCCQVPPELQALANDNDVQLLVHNDPTPFPTNNIFKTFCEIDSGSQKAVCSPLFETTWLSRYSVWVRKRSIMTSKGYIVQFFRKHD
Protein: Alpha-crystallin B chain (Alpha(B)-crystallin) (Q6DG35)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDIAINPPFRRILFPIFFPRRQFGEHITEADVISSLYSQRSSFLRSPSWMESGVSEVKMEKDQFSLSLDVKHFAPEELSVKIIGDFIEIHAKHEDRQDGHGFVSREFLRKYRVPVGVDPASITSSLSSDGVLTVTGPLKLSDGPERTIAIPVTRDDKTTVAGPQK
Protein: Melanoma-associated antigen D1 (MAGE-D1 antigen) (Neurotrophin receptor-interacting MAGE homolog) (Sertoli cell necdin-related gene protein 1) (SNERG-1) (Q9ES73)
Organism: Rattus norvegicus (Rat)
Function: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as BMAL1 and NFIL3, induced, or NR1D1, repressed.
Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus {ECO:0000250}. Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- UBX domain-containing protein 1
- FAS-associated factor 2
- Neuronal PAS domain-containing protein 4
- Protein BEX3
- E3 ubiquitin-protein ligase XIAP
Sequence:
MAQKPDGGAGLRGFQAEASVEDSALLVQTLMEAIQISEAPPTSQATAAASGPNASPQSSQPPTANEKADTEVSAAAARPKTGFKAQNTTTKGPNDYSQARNAKEMPKNQPKVAFKSQNATSKGPHAASDFSHAASTGKSAAKKSEMAFKGQNTTTKAGPSATYNFTQSPSANEMTNNQPKTAKAWNDTTKIPGADAQTQNVNQAKMADVGTSAGISETDGAAAQTSADGSQAQNVESRTIIRGKRTRKINNLNVEENSNGDQRRASLASGNWRSAPVPVTTQNPPGAPPNVLWQTPLAWQNPSGWQNQTARQTPPARQSPPARQTPSAWQNPVAWQNPVIWPNPVIWQNPVIWPNPIVWPGPIVWPNPMAWQSTPGWQSPPSWQAPPSWQSPQDWQGPPDWQLPPDWSMPPDWSFPSDWPFPPDWIPADWPIPPDWQNLRPSPNLRSSPNSRASQNQGPPQPRDVALLQERANKLVKYLMLKDYTKVPIKRSEMLRDIIREYTDVYPEIIERACFVLEKKFGIQLKEIDKEEHLYILISTPESLAGILGTTKDTPKLGLLLVILGIIFMNGNRATEAVLWEALRKMGLRPGVRHPLLGDLRKLLTYEFVKQKYLDYRRVPNSNPPEYEFLWGLRSYHETSKMKVLRFIAEVQKRDPRDWTAQFMEAADEALDALDAAAAEAEARAEARNRMGIGDEAVSGPWSWDDIEFELLTWDEEGDFGDPWSRIPFTFWARYHQNARSRFPQAFTGPIIGPSGTATANFAANFGAIGFFWVE
Protein: Complexin-2 (Complexin II) (CPX II) (Synaphin-1) (P84087)
Organism: Rattus norvegicus (Rat)
Function: Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Also involved in mast cell exocytosis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:7654227}. Presynapse {ECO:0000269|PubMed:15911881, ECO:0000269|PubMed:7654227}. Nucleus. Perikaryon {ECO:0000269|PubMed:9753100}. Note=Translocated from the perikaryon to the presynaptic terminals during maturation of neuronal cells (PubMed:7654227). In mast cells, cytosol and nucleus. Becomes enriched near plasma membrane following stimulation. {ECO:0000269|PubMed:7654227}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Syntaxin-4
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 3
- Syntaxin-1A
- Alpha-soluble NSF attachment protein
- Syntaxin-8
- Vesicle-associated membrane protein 7
- Syntaxin-7
Sequence:
MDFVMKQALGGATKDMGKMLGGEEEKDPDAQKKEEERQEALRQQEEERKAKHARMEAEREKVRQQIRDKYGLKKKEEKEAEEKAALEQPCEGSLTRPKKAIPAGCGDEEEEEEESILDTVLKYLPGPLQDMFKK
Protein: Nuclear matrix constituent protein 1 (A0A166B1A6)
Organism: Daucus carota subsp. sativus (Carrot)
Function: Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology.
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:9141634}. Nucleus lamina {ECO:0000269|PubMed:9141634}. Note=Localizes at the nuclear periphery. {ECO:0000269|PubMed:9141634}.
Interaction partners:
Sequence:
MGRVEDMGLNAKLMKLETELFDYQYNMGLLLIEKKEWTSKFEELQQVYTETKDALKQEQEAHLIAISDAEKREENLTKALGVEKQCVLDLEKALRDMRSDYAEIKFTSDSKLAEASALITKVEEKSLEVESKLHSADAKLAELSRKGSDIERKSHELEARESALRRERLALNAEREALTDNISRQREDLREWERKLQEDEERLAEVRRLLNQREERANENDRLYQQKQSELDGEQKKIEIIMVSLKNKEDDISSRIAKLNIKEKEADAVKHSLEVKEKDLTEFEQKLNAREQSEIQKLLDEHKAILEVKKQSFEMEMDKRKNDFENDLQNRAVEVEKKEVEVKHLEAKLAKREHALDQKHEKLKEKEQYLASKLQDLNEREKSMKLEENKIEDERNQLLSDKQEMLCLKAEIEKDRASTEEQRLKLSEEIERLKITEEERLELARLQSELKQEIENCRHQRELLLKEEDELKQEKMRFEKEWEDLDERRTALMKDLKDITVQKENFEKLKHSEEDRLNNKKLDTESYVQKELDALRLTKDSFAATMEHEKAVLAERTSSEKKQMLNDFELWKRELETKLFNEREDMENALRLREKQFDEEREKELNNINYIKEVISKEREDIKLERSRIAKEKQEILMHQKHLDEQHVVMQKDIGQLVSLSEKLKDQREQFFKERECFIRFVESQKSCKNCGEMTSEFVVSDLQSLAELENLKALSVPQLAENYLRQDLQGTPDKNLSTVTPGAVGLGSPASGGTKSWLQKCTSKIFIFSASKKNNSPDQNTSRRLHVEASPNKLLNTEVIPELPSGVAGETLEMQNMQVSNSNREMESNLNLSGTEQSNIDSKALDVEDSQQSDVRAGNRKPGKRAKGRVRRKRSAKEVAEEAKTVLADPIELNENEHSNGLASAYTNESRGDSSLVGKRTRNSRKRNPSQPSQSAAGDVGADSEGHSDSVTAGGRQKRRRKVVPAVQAPTGRYNLRRHKTAAPLVANGALSDPNKGKEKEIDDGGGIGEEIPDEVDGNTHLVQVTTLKKRINVVNEFSSAGFHGINATSESQDRDAANQLVSDTMLSEEVNGTPEQSRGYQNQGDTSGAEGEDEDGDEVEHPGEVSMRKKVWKFLTT
Protein: Amine oxidase (EC 1.4.3.-) (A2QTC0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MLPHPLAILSEEETNIARNVILAQHPNTVIDFREIYLSEPPKAQLLEFLALEHSGRLSPTSPRPPRLALCQYDVIGNDRIPSFEESVVDVGTRQRVQHRVVGKEHHASLTLSEFDTLVERCFASPLFQKALADFDLPEGFEVVIEPWPYGGLDYVEEKRRYFQGLCFATDKRKNNPDANFYSYPLPLIPVMDALTQEIIRVDRPATGGKGEGLTEQTFKRDIIGHCKDSDYVPELLPGGTRKDLKPLNVVQPEGPSFRITEESLVEWQKWRFRVAFNPREGATIHDVWYDGRSVLYRLSISEMTVPYADPRPPFHRKQAFDFGDGGGGNMANNLSIGCDCLGVIKYFDAVMTGADGSAKKMPNAICLHEQDNGIGWKHSNWRTGRAVVTRHRELVVQFIITLANYEYIFAYKFDQSGGITVESRATGILNVVNIDAGKVSEYGNVVSGGVLAQNHQHIFCVRIDPAIDGPNNSVQVEESHPVPMNAVTNPNGNFYKVNTETMERAGFFDAAPELNRTVKMVNPHKKNPISQKPVGYKFIPLATQRLLADPNSIQARRAQFAQHHVWVTKYRDGELYAGGRYTLQSQEEIEGVSDAVKRGESVVDTDVVVWSTFGITHNPRVEDWPVMPVEIFQLMIRPADFFTANPSLDVPSDKNVSSRVVGNDCCRNAHI
Protein: Porphobilinogen deaminase, chloroplastic (PBG) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) (Protein RUGOSA1) (Q43316)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Probable delta-aminolevulinic acid dehydratase 2, chloroplastic
- Delta-aminolevulinic acid dehydratase 1, chloroplastic
- S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase, chloroplastic
- Uroporphyrinogen-III synthase, chloroplastic
- Uroporphyrinogen decarboxylase 2, chloroplastic
- Uroporphyrinogen decarboxylase 1, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
- Glutamyl-tRNA reductase 2, chloroplastic
- Probable glutamyl-tRNA reductase 3, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
Sequence:
MDIASSSLSQAHKVVLTRQPSSRVNTCSLGSVSAIGFSLPQISSPALGKCRRKQSSSGFVKACVAVEQKTRTAIIRIGTRGSPLALAQAYETREKLKKKHPELVEDGAIHIEIIKTTGDKILSQPLADIGGKGLFTKEIDEALINGHIDIAVHSMKDVPTYLPEKTILPCNLPREDVRDAFICLTAATLAELPAGSVVGTASLRRKSQILHKYPALHVEENFRGNVQTRLSKLQGGKVQATLLALAGLKRLSMTENVASILSLDEMLPAVAQGAIGIACRTDDDKMATYLASLNHEETRLAISCERAFLETLDGSCRTPIAGYASKDEEGNCIFRGLVASPDGTKVLETSRKGPYVYEDMVKMGKDAGQELLSRAGPGFFGN
Protein: Glycine/sarcosine N-methyltransferase (EC 2.1.1.156) (Betaine synthesis N-methyltransferase A) (Q7U4Z8)
Organism: Parasynechococcus marenigrum (strain WH8102)
Function: Catalyzes the methylation of glycine and sarcosine to sarcosine and dimethylglycine, respectively, with S-adenosylmethionine (AdoMet) acting as the methyl donor. It has strict specificity for glycine and sarcosine as the methyl group acceptors.
Interaction partners:
- Dimethylglycine N-methyltransferase
- Glycine dehydrogenase
- Serine:pyruvate/alanine:glyoxylate aminotransferase
- Serine hydroxymethyltransferase
Sequence:
MTSTQNHPLQTQDDQQRFGQSPESVRETDHYQQEYIEDFTDRWDRLIDWNARAEAEGDFFIRLLKEHGARSVLDVATGTGFHSIRLLEEGFDVVSADGSPNMLARAFRNARNRDQLLRTSQADWRFLNRDIHGEFDAVICLGNSFTHLFKERDRRKALAEYYAVLKHNGILILDHRNYDRLLEGGSAVRQGKGNVYCGKDVEVGPEHVDEGLARFRYSFSDGGVYHLNMFPLRYGYVRRLMSEVGFQQITSFGDYQRDFENPDFYVHVAEKEYRFDVDTTMH
Protein: EngB-type G domain-containing protein (Q57XL1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPLRSRPRYTQQQSDTRKVMDGDALLASSKRRDPNGARLALMDADSGCASDVLCTVPDTTDDDIVLDPSHGRQLQEVSAAGKRMKFGEHHPATRGIGTDVIDLVTDAFKEARERLVEKRRRVLYQVTHPDPSDYTYNGKLVPAPPLSFGRITEEAISLGNKVMLGQHYSLVKQAGMYRDDEEGGSAGHSTATSVEQRRCGRRRTTLYDQHTFFFEINDLYQEIVLVGKACAGKSSLLNALLGQQVAKTSSTPNTTRKLSFYQSVSPEQMQRYLNVKGNGLVKLPGGGLQLTFVDVPGFGLEGMSEQWRDKAIELTDAYLGVRRSVNTLLLCIDCERGLTKVDLRYFTWLENLHGVFFVVLTKCDSVPHSRVCSVMRQIYSVITKNRRKYRKVFPFIIPTSANDGTNIEMLRGLIAETSGLIPGDRLRKILKAKADAEMRLGLEKEEERIREARCLEARMAKAYFESTRSAREVAGKDAKAPGLSLVPSTASPHPPPQPPLHTKPSAKERKFVLSLDCDEEGTVEAVPTPVSDSMADEPLLTFQNDDDAPHIGKSRGDSKLKRRERFLAWRRAHPLQRHASAYGVFRLNTGLERPDTSTLELTYVDGTPDQTDAQLREFDRDSALKGKVIDLEVGGTSYVGGPVDVANHGAQLGVGHGPGNGDGGAAPGRTTELSAVIGAGNTNGGGNRTLPASSKGGVSRFLNLIDQYAQRETQKPRSKREQAKEARWRARLQKGSGTKFFAEESDGRVAEYKAGKKFGPSLISAACDDVAGRRAQWEAHTYMRQAVAARPTAPWAALEVLKRRTERVKQDAAMRGMTKKECEAYLRNCGRVTEKFEEFEGEVTAAKYMNETRHTKTLRSQQQMHLNSTSKISYRSMPVGLWKHYGERETYWPTPRVKGR
Protein: Fatty acid-binding protein, liver (L-FABP) (Liver-type fatty acid-binding protein) (A8MW49)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU369022}.
Interaction partners:
Sequence:
MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNVSWWCSERVAPSA
Protein: Broad substrate specificity ATP-binding cassette transporter ABCG2 (EC 7.6.2.2) (ATP-binding cassette sub-family G member 2) (Breast cancer resistance protein 1 homolog) (Urate exporter) (CD antigen CD338) (Q7TMS5)
Organism: Mus musculus (Mouse)
Function: Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells (By similarity). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (By similarity). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate. Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (By similarity). Mediates the secretion of the riboflavin and biotin vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability. Plays an important role in the exclusion of xenobiotics from the brain. It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux. In placenta, it limits the penetration of drugs from the maternal plasma into the fetus. May play a role in early stem cell self-renewal by blocking differentiation (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9UNQ0}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:12429862}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9UNQ0}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in membrane lipid rafts. {ECO:0000250|UniProtKB:Q9UNQ0}.
Interaction partners:
- ATP-binding cassette sub-family C member 2
- Multidrug resistance-associated protein 1
- Prominin-1
- CD44 antigen
- Epidermal growth factor receptor
- POU domain, class 5, transcription factor 1
- Aldehyde dehydrogenase 1A1
- Polycomb complex protein BMI-1
- Solute carrier family 2, facilitated glucose transporter member 9
- Solute carrier family 22 member 12
Sequence:
MSSSNDHVLVPMSQRNNNGLPRTNSRAVRTLAEGDVLSFHHITYRVKVKSGFLVRKTVEKEILSDINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPKGLSGDVLINGAPQPAHFKCCSGYVVQDDVVMGTLTVRENLQFSAALRLPTTMKNHEKNERINTIIKELGLEKVADSKVGTQFIRGISGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGKLVFHGPAQKALEYFASAGYHCEPYNNPADFFLDVINGDSSAVMLNREEQDNEANKTEEPSKGEKPVIENLSEFYINSAIYGETKAELDQLPGAQEKKGTSAFKEPVYVTSFCHQLRWIARRSFKNLLGNPQASVAQLIVTVILGLIIGAIYFDLKYDAAGMQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFFGKVMSDLLPMRFLPSVIFTCVLYFMLGLKKTVDAFFIMMFTLIMVAYTASSMALAIATGQSVVSVATLLMTIAFVFMMLFSGLLVNLRTIGPWLSWLQYFSIPRYGFTALQYNEFLGQEFCPGFNVTDNSTCVNSYAICTGNEYLINQGIELSPWGLWKNHVALACMIIIFLTIAYLKLLFLKKYS
Protein: 60S ribosome subunit biogenesis protein nip7 (Q1MTQ9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome biogenesis protein ytm1
- Ribosome biogenesis protein brx1
- 25S rRNA
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome assembly factor mrt4
- Probable rRNA-processing protein ebp2
- Ribosome biogenesis protein rlp24
- Probable nucleolar GTP-binding protein 1
- Brix domain-containing protein C4F8.04
- Ribosome biogenesis protein nsa2
Sequence:
MRPLTHEETKTFFEKLAQYIGKNITHLIDRPDDPHCFRLQKDRVYYVSERAMKMATSVARQNLMSLGICFGKFTKTNKFRLHITALDYIAQYARYKIWVKSNGEMPFLYGNHVLKAHVGRITDDTPQHQGVVIYSMNDTPLGFGVTARSTLELRRLEPTAIVAFHQADVGEYLRDEDTLF
Protein: Rubber oxygenase (EC 1.13.-.-) (Latex clearing protein) (b-type cytochrome Lcp) (Q3L8N0)
Organism: Streptomyces sp. (strain K30)
Function: Involved in the initial step of rubber degradation. Catalyzes the oxidative C-C cleavage of poly(cis-1,4-isoprene) in synthetic as well as in natural rubber by the addition of oxygen (O2) to the double bonds, leading to a mixture of oligonucleotide-isoprenoids with terminal keto and aldehyde groups (endo-type cleavage). The cleavage products are of different lengths, ranging from C20 (four isoprene units) to higher oligo-isoprenoids. Is not able to cleave low-molecular-weight substrate analogs with isoprenoid structure such as squalene (1,4-trans-isoprenoid), carotenoids, or alpha-tocopherol.
Subcellular location: Secreted {ECO:0000269|PubMed:18606806}.
Interaction partners:
Sequence:
MDGFSRRRMLMTGGALGAVGALGAATRALARPLWTWSPSASVAGTGVGVDPEYVWDEEADPVLAAVIDRGEVPAVNALLKQWTRNDQALPGGLPGDLREFMEHARRMPSWADKAALDRGAQFSKTKGIYVGALYGLGSGLMSTAIPRESRAVYYSKGGADMKDRIAKTARLGYDIGDLDAYLPHGSMIVTAVKTRMVHAAVRHLLPQSPAWSQTSGGQKIPISQADIMVTWHSLATFVMRKMKQWGVRVNTADAEAYLHVWQVSAHMLGVSDEYIPATWDAANAQSKQVLDPILAHTPEGEALTEVLLGIVAELDAGLTRPLIGAFSRYTLGGEVGDMIGLAKQPVLERLIATAWPLLVAFREGLIPLPAVPAVLWTLEEALRKFVLLFLSEGRRIAIDIPDVNRPS
Protein: NAC097 (A0A178UQH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDISAQRFAMNGRSMRLPPGFRFDPDDEDLVFEYLAKKVLHRPMDFDLPELRSCNVDPWDLLGEKNKEVYYFVKKEERERKGRETLSGYWEECEEEEVMEAGGRDCIHLEGRRKTFAFFIGKKPRGTITPWIMYEFRLLSSRATRWSSSPLPRGEVGKWRAVKVVVKEENDEEMVEDEHESDESDGEEVIQSR
Protein: Proteasome subunit alpha type-5-B (20S proteasome alpha subunit E-2) (Proteasome component Z) (Q42134)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-2-B
- Proteasome subunit beta type-2-A
- Proteasome subunit beta type-1
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-6-A
- Proteasome subunit beta type-7-A
- Proteasome subunit alpha type-2-A
Sequence:
MFLTRTEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGVKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDDHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEGEEESMSRPFGVSLLIAGHDENGPSLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQFNKDITLQEAETIAVSILKQVMEEKVTPNNVDIAKVAPAYHLYTPQEVEAVISRL
Protein: Protein disulfide-isomerase (EC 5.3.4.1) (A0A024R8S5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}. Melanosome {ECO:0000256|ARBA:ARBA00004223}.
Interaction partners:
Sequence:
MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
Protein: Neurexin-related protein bam-2 (Branching abnormal protein 2) (G5ECL4)
Organism: Caenorhabditis elegans
Function: Maintains the normal guidance and termination of axonal branches of VC motorneurons. By associating with cell adhesion protein casy-1, mediates axonal interactions to establish synaptic connections between the male-specific sensory neuron HOA and the AVG interneuron. Plays a role in regulating male mating behavior.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14551437}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:28901288}.
Interaction partners:
- Calsyntenin-1
- Synaptogenesis protein syg-2
- Zwei Ig domain protein zig-1
Sequence:
MSSERRKDNPLRFALILHLLAVLVQGDIQPRFSCYNHYLAGIRTSSVLPISGHSSAPSNVKCIFENDVAFTEIHSALENSYQVMGKKSVNFQVLDLFHLRELVRRSHCTQTLTVTWKNVPEAGKGGLKVVSLLNETTRIEYSGDERQDFLFDETFAGVRHLIPDEDDNESNPTVTTTRLLCKHIPQPECLVRGKFEVDLEANLEWSYAFSFKTDITNQTLFTLRCGDTTSEVRLENDFFIRADGNAPVAVTHLSDATWHTAIVKHNQPDSHFLKIDDFPEIELGKSISDDTDKTITLSISVNGNIQLIDPTDTNDDCMYSFDKPQKRLQETVSTRTMCVGCGCPKLSGTFDGLSKCDEEDENSYNLRRDVDRLSFIHIDNAFDIDSNGAAIPAISTSFKSDSDVGLIFFGYWQNFHGKGRLQVYYHYDTISAVFCKHTDDEECSSCSIRSSEGFGKDQWIQTILWGGGDEIHLAVDSSVCRLQQLSNISLAEVYAIPQISGGAGLFIGGTWHEKKRRGLYKADAEQKYFENTREKAPVLRGCIKDVFVRGSKTDVSEMFEVQKQAMLNEPDDSNAFAVRKYCQSCIPACSEGTRCRSRAPLQDSAMICDCADELQFNTSEGTCNRERDTPVALSTAFLSENQIVLDIQNTKAILSKVWLKFALPKQINQAQRIVEFNSHRETLFNINLETDGTVNVQLHGQDTASRQLNLLDDRVHLLQLQRRTPMGTRHSAKKYDLYIDGFHTVVSDIGKLVLNNVSVTAAETEDEWSSVIVHDLGLSYEYDEHFAISHPSNVIHQVDLHSQLLPYQIRAPDLSKTGILDDSLWEKPAYVTDSEAAPVLESSPHGEVVDFTADIIEPEQLLSGRWILYSLFLTILLCLFILMCIVCYWCVLRPRAMRRTDTGSQRTIIRDSPDYAPVKMRRDSIGGISIDDDGSIGTDDTDLQAYRDIPSHRVKIYRESMVSILVPSIDQPAEAAIVKRSHSTISDQTPSRPHDTSHAPLVAVNDD
Protein: Troponin I, cardiac muscle (Cardiac troponin I) (P19429)
Organism: Homo sapiens (Human)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin T, cardiac muscle
- Tropomyosin alpha-1 chain
- Troponin C, slow skeletal and cardiac muscles
- Troponin T, slow skeletal muscle
- Troponin C, skeletal muscle
- Tropomyosin alpha-3 chain
- Actin, alpha cardiac muscle 1
- Troponin T, fast skeletal muscle
- Serine/threonine-protein kinase TNNI3K
- Myosin-binding protein C, cardiac-type
Sequence:
MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES
Protein: Ceramide kinase, isoform A (EC 2.7.1.138) (Ceramide kinase, isoform B) (LD42647p) (Q9VNA6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neutral ceramidase
- Alkaline ceramidase
- LD18904p
- ceramide glucosyltransferase
- Sphingolipid delta
- Non-lysosomal glucosylceramidase
- Putative neutral sphingomyelinase
- Serine palmitoyltransferase 1
- serine C-palmitoyltransferase
- LD28817p
Sequence:
MTQTKQPAGRSSTSAGDFVAPISSTSASKFTPCSASDHNVLLNNFQLKKKSYRVLLHGQQLVWERLQKIKQSPQGNEAKAPLPPDSPAQPGGICSYGPQSHVLHLDDVVSIRSGDTKASSLKPPSPPGSERSSGCSGDVAQGKPTSQYLTINYAMRLSKSQTDCNRWELRRLTFFNSDPYIVRQWDQELQIRLHSSSPTRMRVRRLLVFINPYGGRKAGAQTYERHVRPIFQLAGVDATCITTQRANQVKDILLSHDLGVYDAVCCVGGDGTVAEVINGLIFRQMRELGLDEQRPPYIPRPALPVGVIPAGSTDTIAYSMHGTADVRTAAIHVILGQHRGLDVCSVSNGQSLLRFCASVLSYGYLGDVAAQSENYRWMGPRRYEYSGVKAFLNNRGYDAELRMLEEPDLLLTTPLEDIPQSPDSVCSLGESVPSVCYANCQRCSFASSIQEQRSSLFIQEESKEAERNQQVETEDSHLAASEAALLRPRPRPGNLRLPTGSISSMRNLGNDQWKVVRGNFFMICGANITCACARSPNGISRYSHLGDGCLDLILVKKTSLLNNVRFLLNTAGRSGDIRNLPFVEVYRTREFRFRTFSASEEDYSLAGSCQPITPPEEMTAHSSSTEFSSWNCDGEVVTDLDITMRSHCQLIEVFMRGPHSYSKPLKGGTTPTTPASSSDNVYCCCKD
Protein: At4g33120 (S-adenosyl-L-methionine-dependent methyltransferases superfamily protein) (Q84TE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEKIIDVAYGASVKAGLTLLEKNLLPDLVIRRLIRLLLASRLRSVYKPTAEMQLSDLLRFVDSLKKMPIAINTETAKTQHYELPTAFFEHALGRNIKYSCCYYSNDSSSLEEAGEAMLALSCERAKVEDGQSVLDIGCGWGSLTLYIARKYSKCKLTGICNSKTQKAFIDEKCRKLGLQNVEIIAADISTFEHEGTYDRIFSIEMFEHMKNYGELLKKIGNWMKEDSLLFVHYLCHKTYAYHFEDVNDDDWITRHFFSGGTMPSADLLLYFQENVSIMDHWLVNGTHYAKTSEEWLKGMDKEIVAVKEIMEVTYGKEEAVKWTVYWRTFFIALAELFAYNNGDEWMIAHFLFKKK