wanglab/gogpt-training-data huggingface dataset:
Protein: Flotillin-1 (O75955)
Organism: Homo sapiens (Human)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular location: Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:20682791}. Endosome {ECO:0000269|PubMed:20682791}. Membrane, caveola {ECO:0000250|UniProtKB:O08917}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08917}. Melanosome {ECO:0000269|PubMed:17081065}. Membrane raft {ECO:0000269|PubMed:25893292}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Membrane-associated protein of caveola (By similarity). {ECO:0000250|UniProtKB:O08917, ECO:0000269|PubMed:17081065}.
Interaction partners:
- Flotillin-2
- Sorbin and SH3 domain-containing protein 1
- Caveolin-1
- CD63 antigen
- Sodium-dependent dopamine transporter
- Cadherin-1
- Prostate tumor-overexpressed gene 1 protein
- Stomatin
- CD81 antigen
- Myocilin
Sequence:
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA
Protein: Pentatricopeptide repeat-containing protein At3g49170, chloroplastic (Protein EMBRYO DEFECTIVE 2261) (Q5G1T1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in embryogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol 4-kinase gamma 6
- Pentatricopeptide repeat-containing protein At1g30610, chloroplastic
- Brefeldin A-inhibited guanine nucleotide-exchange protein 2
- Ankyrin repeat domain-containing protein EMB506, chloroplastic
- Cytosolic sulfotransferase 5
Sequence:
MAMISFSFPSPAKLPIKSQPSVSNRINVADRLILRHLNAGDLRGAVSALDLMARDGIRPMDSVTFSSLLKSCIRARDFRLGKLVHARLIEFDIEPDSVLYNSLISLYSKSGDSAKAEDVFETMRRFGKRDVVSWSAMMACYGNNGRELDAIKVFVEFLELGLVPNDYCYTAVIRACSNSDFVGVGRVTLGFLMKTGHFESDVCVGCSLIDMFVKGENSFENAYKVFDKMSELNVVTWTLMITRCMQMGFPREAIRFFLDMVLSGFESDKFTLSSVFSACAELENLSLGKQLHSWAIRSGLVDDVECSLVDMYAKCSADGSVDDCRKVFDRMEDHSVMSWTALITGYMKNCNLATEAINLFSEMITQGHVEPNHFTFSSAFKACGNLSDPRVGKQVLGQAFKRGLASNSSVANSVISMFVKSDRMEDAQRAFESLSEKNLVSYNTFLDGTCRNLNFEQAFKLLSEITERELGVSAFTFASLLSGVANVGSIRKGEQIHSQVVKLGLSCNQPVCNALISMYSKCGSIDTASRVFNFMENRNVISWTSMITGFAKHGFAIRVLETFNQMIEEGVKPNEVTYVAILSACSHVGLVSEGWRHFNSMYEDHKIKPKMEHYACMVDLLCRAGLLTDAFEFINTMPFQADVLVWRTFLGACRVHSNTELGKLAARKILELDPNEPAAYIQLSNIYACAGKWEESTEMRRKMKERNLVKEGGCSWIEVGDKIHKFYVGDTAHPNAHQIYDELDRLITEIKRCGYVPDTDLVLHKLEEENDEAEKERLLYQHSEKIAVAFGLISTSKSRPVRVFKNLRVCGDCHNAMKYISTVSGREIVLRDLNRFHHFKDGKCSCNDYW
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A8I6GKS9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LCLPPERQESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKVGRPVNPSNHRLLFEVFDENRLTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSEQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRSTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEASEGGGEGPEPWETISEEVNMAGDSLSLALPPPPASPVSRTSPQELSEELSRRLQITPDSNGEQFSALIQREPSSRLRSCSVTDTVAEQAHLPPPSTPTRRARSSTVTGGEESTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLVEPQIRRPRSLSSPTVTLSAPLEGAKDSPIRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKASLNPNDLGPLPVSILQRHEMVQKCVLILPKFMGSLCTCPSAPCPSAPCPSAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD
Protein: ATP-binding cassette sub-family B member 6 (EC 7.6.2.5) (ABC-type heme transporter ABCB6) (Q9VF20)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}. Endosome, multivesicular body membrane {ECO:0000256|ARBA:ARBA00004333}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}. Late endosome membrane {ECO:0000256|ARBA:ARBA00004414}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}. Melanosome membrane {ECO:0000256|ARBA:ARBA00024320}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
- Protoporphyrinogen oxidase
- ATP-binding cassette sub-family D member 1
- Iron-sulfur cluster assembly enzyme IscU
- Uroporphyrinogen decarboxylase
- Ferrochelatase, mitochondrial
Sequence:
MLYCPPNVTLSEVWTQHGISHCFMDTVGPAVYGGFLLLFGSIQLLMYRKYATRITDPTQISKSRLFAMQLFLLLLLPVLALLRFLMNARIYPDSAVYGYMIFSTCVVCFSYPFSICLILKERYYQLPSMPTRGHGLVLLLFWTLAFINESLAFINLRHEDWWFHLKTNKDQIEMGLFVTRFLCSLLIFVLGLKAPGIMAPYNPHQRLDNDTANESQGNVQTGSAFRNGWRKLRTVFPYLWPKKNIALQIAVIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWDFVLIYVALSFLQGGGTGSMGLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLREDGIYADMWQQQLKNLDAEQSGGSDNGDASAESGSEKRRAGGAGGPSGTGTGGAHFRAGHAHGGAR
Protein: Dermaseptin-B2 (DRS-B2) (Adenoregulin) (Dermaseptin BII) (P31107)
Organism: Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor)
Function: Cationic amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-negative and Gram-positive bacteria, fungi and protozoa. Acts in a synergistic effect in combination with Plasticin-B1 at doses that are not active alone. Acts by disturbing membrane functions. On model mebranes, induces a strong perturbation of anionic lipid bilayers, resides at the hydrocarbon core-water interface, parallel to the plane of the membrane, and interacts preferentially with the polar head groups and glycerol backbone region of the anionic phospholipids, as well as the region of the lipid acyl chain near the bilayer surface. It induces a positive curvature of the bilayer and clustering of anionic lipids, consistent with a carpet mechanism, that may lead to the formation of mixed peptide-phospholipid toroidal, transient pores and membrane permeation/disruption once a threshold peptide accumulation is reached. Also enhances binding of agonists to adenosine A1 receptors (ADORA1), adenosine A2a receptors (ADORA2A), alpha-2 adrenergic receptors (ADRA2A) and 5-hydroxytryptamine 1A receptors (HTR1A). In addition, it enhances guanyl nucleotide exchange which may result in the conversion of receptors to a high affinity state complexed with guanyl nucleotide free G-protein. It affects human behavior eliciting profound malaise, followed by listlessness and then euphoria. It does not show cytotoxic activity on CHO cells. It does not act as a chemoattractant. It does not show hemolytic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:1438301}. Target cell membrane {ECO:0000269|PubMed:19113844}. Note=Firstly parallelly oriented to the membrane surface, the peptide may mix to phospholipids, forming toroidal and transient pores in the membrane. {ECO:0000269|PubMed:19113844}.
Interaction partners:
Sequence:
MAFLKKSLFLVLFLGLVSLSICEEEKRENEDEEEQEDDEQSEMKRGLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAVGEQ
Protein: Uncharacterized protein (Q38AS3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEPLEKLQSEIDRLKREIAVLSCAEDEEALRDIYDEFRMDIKEHYSNSIGVYVLKCFTVPIIVGICVFLFWLSYENIRSWWMRKSVTKGLNNISIVADEISERKLTQAAWRSTRRRVCFFVVIKCFIAVTCIFFFVGMRFLMEASVRVWLRNVLVPSMEENVTAYDSPVGTSNDFNPMSGIRYEVHNFLASLLGLDWVRDLQSVYLFYLFGPGLLAFGLGVMRSAAIDMMALGEKFSLPLDTLKMYRTKKKEVYDLQMQKRVEEVMTKLYALADPSIPLLEEDKRVDDEEEMPGE
Protein: Partitioning defective 6 homolog gamma (PAR-6 gamma) (PAR6D) (Q9BYG4)
Organism: Homo sapiens (Human)
Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (By similarity).
Subcellular location: Cytoplasm. Cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
Interaction partners:
- Protein kinase C zeta type
- Cell division control protein 42 homolog
- Partitioning defective 3 homolog
- Protein kinase C iota type
- Partitioning defective 6 homolog beta
- Protein PALS1
- LLGL scribble cell polarity complex component 2
- Ras-related C3 botulinum toxin substrate 3
- Ras-related C3 botulinum toxin substrate 2
- Protein crumbs homolog 3
Sequence:
MNRSFHKSQTLRFYDCSAVEVKSKFGAEFRRFSLDRHKPGKFEDFYKLVVHTHHISNSDVTIGYADVHGDLLPINNDDNFCKAVSSANPLLRVFIQKREEAERGSLGAGSLCRRRRALGALRDEGPRRRAHLDIGLPRDFRPVSSIIDVDLVPETHRRVRLHRHGCEKPLGFYIRDGASVRVTPHGLEKVPGIFISRMVPGGLAESTGLLAVNDEVLEVNGIEVAGKTLDQVTDMMIANSHNLIVTVKPANQRNNVVRGGRALGSSGPPSDGTAGFVGPPAPRVLQNFHPDEAESDEDNDVVIEGTLEPARPPQTPGAPAGSLSRVNGAGLAQRLQRDLALDGGLQRLLSSLRADPRHSLALPPGGVEEHGPAVTL
Protein: Activating transcription factor 1 (F8VYN3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDSHKSTTSETAPQPGSAVQGAHISHIAQQVSSLSESEESQDSSDSIGSSQKAHGILARRPSYRKILKDLSSEDTRGRKGDGENSGVSAAVTSMSVPTPIYQTSSGQYIAIAPNGALQLASPGTDGVQGLQTLTMTNSGSTQQGTTILQYAQTSDGQQILVPSNQVVVQTASGDMQTYQIRTTPSATSLPQTVVMTSPV
Protein: Alpha-pyrone synthesis polyketide synthase-like Pks18 (EC 2.3.1.-) (Alpha-pyrone synthesis polyketide synthase type III Pks18) (Chalcone synthase-like protein) (CHS-like) (P9WPF1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of tri- and tetraketide alpha-pyrones. Pks18 catalyzes the extension of medium- and long-chain aliphatic acyl-CoA substrates by using malonyl-CoA as an extender molecule to synthesize polyketide products.
Interaction partners:
- Probable conserved membrane protein
- Conserved hypothetical membrane protein
- Glycolipid sulfotransferase Rv1373
- Probable integral membrane nitrite extrusion protein NarK3
- Mutator family transposase
- Uncharacterized protein Rv1518
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit omega
- ATP synthase subunit c
- DNA-directed RNA polymerase subunit alpha
Sequence:
MNVSAESGAPRRAGQRHEVGLAQLPPAPPTTVAVIEGLATGTPRRVVNQSDAADRVAELFLDPGQRERIPRVYQKSRITTRRMAVDPLDAKFDVFRREPATIRDRMHLFYEHAVPLAVDVSKRALAGLPYRAAEIGLLVLATSTGFIAPGVDVAIVKELGLSPSISRVVVNFMGCAAAMNALGTATNYVRAHPAMKALVVCIELCSVNAVFADDINDVVIHSLFGDGCAALVIGASQVQEKLEPGKVVVRSSFSQLLDNTEDGIVLGVNHNGITCELSENLPGYIFSGVAPVVTEMLWDNGLQISDIDLWAIHPGGPKIIEQSVRSLGISAELAAQSWDVLARFGNMLSVSLIFVLETMVQQAESAKAISTGVAFAFGPGVTVEGMLFDIIRR
Protein: Nuclear factor 1 B-type (CCAAT-box-binding transcription factor) (Nuclear factor I/B) (TGGCA-binding protein) (A0A0S2Z4H3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDLFWNHMPASPPSNAL
Protein: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC 5.3.1.16) (Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase) (P10371)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Imidazole glycerol phosphate synthase subunit HisF
- Histidine biosynthesis bifunctional protein HisB
- Histidine biosynthesis bifunctional protein HisIE
- ATP phosphoribosyltransferase
- Imidazole glycerol phosphate synthase subunit HisH
- Histidinol-phosphate aminotransferase
- Histidinol dehydrogenase
- Tryptophan biosynthesis protein TrpCF
- GMP synthase
- Bifunctional protein TrpGD
Sequence:
MIIPALDLIDGTVVRLHQGDYGKQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLIKTLVAGVNVPVQVGGGVRSEEDVAALLEAGVARVVVGSTAVKSQDMVKGWFERFGADALVLALDVRIDEQGNKQVAVSGWQENSGVSLEQLVETYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPQVAFQSSGGIGDIDDVAALRGTGVRGVIVGRALLEGKFTVKEAIACWQNA
Protein: Epididymis secretory sperm binding protein (A0A384MTY2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATKIDKEACRAAYNLVRDDGSAVIWVTFKYDGSTIVPGEQGAEYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGENVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIKSELKKAGGANYDAQTE
Protein: Protein sof1 (U3 small nucleolar RNA-associated protein sof1) (U3 snoRNA-associated protein sof1) (O74340)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for ribosomal RNA processing.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C57A7.06
- Probable U3 small nucleolar RNA-associated protein 7
- U3 small nucleolar RNA-associated protein 21 homolog
- Probable U3 small nucleolar RNA-associated protein 13
- U3 small nucleolar ribonucleoprotein protein mpp10
- U3 small nucleolar RNA-associated protein 4
- KRR1 small subunit processome component homolog
- Uncharacterized protein C1604.06c
- U3 small nucleolar RNA-associated protein 6
- U3 small nucleolar RNA-associated protein 10
Sequence:
MKVKTITRGTSLTRLNDQDPVKRNLDPSLHPFERAREYTRALNATKMDRMFAAPFLGQLGRGHQDGVYSLARDTKTLIDCASGSGDGAVKLWDASERCERWTSKAHEGIVRGLVFSNQGDVLSCASDRYVYMLNKQDGKVKRSYLGDSSLLDIDTSKGGDLFATSGENVSIWDYSRDTPVTKFEWGADTLPVVKFNYTETSVLASAGMDRSIVIYDLRTSSPLTKLITKLRTNSISWNPMEAFNFVAGSEDHNLYMYDMRNLKRALHVYKDHVSAVMSVDFSPTGQEFVSGSYDKTIRIYNVREGHSRDVYHTKRMQRVTAVKFSMDAQYIFSGSDDSNVRLWRARASSRASIRSTREENRLKYLDSLRERYKHIPEIRRIARHRHLPTNVKKAAEIKREEINSLKRREENIRRHSKKGAVPYEKERERHVVGIQK
Protein: Ribonuclease inhibitor (Ribonuclease/angiogenin inhibitor 1) (E9PIK5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLHCPLQGTAAPGPDGGNRCLAVSQVPLTASVCVGD
Protein: Uncharacterized protein (Q9VXU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRQGVHCCCLVAIALAMAIRQVSMGISASDRRFQCLQTRLIGQANCSPCADLYVFNRQSAYRRCEHVNGNCYPHRTVFASARMCELTCQPYIRRPTLHEVTTLPPPPPIVEPFGDSDEEFE
Protein: Kinase (EC 2.7.-.-) (Q9VYE7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALYPSSSRPRTLMEQLLARKIEAAAAAGGAPSAATATPTASGSATPTPSPTSPNPPAVGGMGLPMPLTLGLGLGLGMGMGVVSRLRRTDSLDSTSSLGSLAFGEDVCRCDDCLLGIVDLYVISAAEAAKKKSSGWRKIRNIVQWTPFFQTYKKQRYPWVQLAGHQGNFKAGPEPGTVLKKLCPKEEECFQILMHDLLRPYVPVYKGQVTSEDGELYLQLQDLLSDYVQPCVMDCKVGVRTYLEEELSKAKEKPKLRKDMYDKMIQIDSHAPTAEEHAAKAVTKPRYMVWRETISSTATLGFRIEGIKKSDGTSSKDFKTTKSREQIKLAFLEFLSGHPHILPRYIQRLRAIRATLAVSEFFQTHEVIGSSLLFVHDQTHASIWLIDFAKTVELPPQLRIDHYSAWKVGNHEDGYLIGINNLIDIFVELQASMEAEAHAQAQAEAIQSPVSGSGGDQAEQTGEESKP
Protein: Spondin-1 (F-spondin) (Vascular smooth muscle cell growth-promoting factor) (Q9HCB6)
Organism: Homo sapiens (Human)
Function: Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). Major factor for vascular smooth muscle cell.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Amyloid-beta precursor protein
- Low-density lipoprotein receptor-related protein 8
- Beta-1,3-glucosyltransferase
- Amyloid beta precursor protein binding family B member 1
- GDP-fucose protein O-fucosyltransferase 2
- Amyloid beta precursor like protein 1
- Amyloid beta precursor like protein 2
Sequence:
MRLSPAPLKLSRTPALLALALPLAAALAFSDETLDKVPKSEGYCSRILRAQGTRREGYTEFSLRVEGDPDFYKPGTSYRVTLSAAPPSYFRGFTLIALRENREGDKEEDHAGTFQIIDEEETQFMSNCPVAVTESTPRRRTRIQVFWIAPPAGTGCVILKASIVQKRIIYFQDEGSLTKKLCEQDSTFDGVTDKPILDCCACGTAKYRLTFYGNWSEKTHPKDYPRRANHWSAIIGGSHSKNYVLWEYGGYASEGVKQVAELGSPVKMEEEIRQQSDEVLTVIKAKAQWPAWQPLNVRAAPSAEFSVDRTRHLMSFLTMMGPSPDWNVGLSAEDLCTKECGWVQKVVQDLIPWDAGTDSGVTYESPNKPTIPQEKIRPLTSLDHPQSPFYDPEGGSITQVARVVIERIARKGEQCNIVPDNVDDIVADLAPEEKDEDDTPETCIYSNWSPWSACSSSTCDKGKRMRQRMLKAQLDLSVPCPDTQDFQPCMGPGCSDEDGSTCTMSEWITWSPCSISCGMGMRSRERYVKQFPEDGSVCTLPTEETEKCTVNEECSPSSCLMTEWGEWDECSATCGMGMKKRHRMIKMNPADGSMCKAETSQAEKCMMPECHTIPCLLSPWSEWSDCSVTCGKGMRTRQRMLKSLAELGDCNEDLEQVEKCMLPECPIDCELTEWSQWSECNKSCGKGHVIRTRMIQMEPQFGGAPCPETVQRKKCRIRKCLRNPSIQKLRWREARESRRSEQLKEESEGEQFPGCRMRPWTAWSECTKLCGGGIQERYMTVKKRFKSSQFTSCKDKKEIRACNVHPC
Protein: Izumo sperm-egg fusion protein 1 (Oocyte binding/fusion factor) (OBF) (Sperm-specific protein izumo) (Q6AY06)
Organism: Rattus norvegicus (Rat)
Function: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interaction probably does not act as a membrane 'fusogen'.
Subcellular location: Cell membrane {ECO:0000269|PubMed:37951137}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:Q9D9J7}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes initially to the acrosome membrane of the sperm head (both outer and inner acrosomal membranes). During the acrosome reaction, translocates to the plasma membrane. {ECO:0000250|UniProtKB:Q9D9J7}.
Interaction partners:
- Sperm-egg fusion protein Juno
- CD9 antigen
- Sperm acrosome associated 1
- Zona pellucida sperm-binding protein 3 receptor
- Transmembrane protein 95
- Zona pellucida sperm-binding protein 2
- IZUMO family member 4
- Folate receptor alpha
- Zona pellucida sperm-binding protein 1
- Folate receptor beta
Sequence:
MGLHFTLLLAALANCLCPARLCIICDPFVVAAIKTLEQNYLPTHLAPEHHEDVMKRVEQEVRNFADLPLNQNTFLGVVDEDTLEQASWSFLKDLKRITDSDVKGELFVKELFWMLRLQKDIFATLVARFQKEVYCPNQCGTMSQTLIWCNKCEKQMHFCRKSMDCGERQIEVHRLEDMVLDCQLSWHHASEGLTDYSFYRVWGNSSETLMSKGKEPYLTKTMVGPEDAGNYRCELDTVNAGPATIIYYHVTVLPPRSVEEKPPPNIVTQEEEETPVQVIVPTLEPEPEPEPIPTVTHRPEKKLKSRLLILLILGFVVLVASVIASVLHFRKTRVKSKNSNVENKTSAAEFKSEAESPQKMGSRKLSQAEFHTDSSDKVEEADN
Protein: Pyruvate dehydrogenase E1 component (PDH E1 component) (EC 1.2.4.1) (P9WIS9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). AceE has reductase activity with pyruvate but does not react with 2-oxoglutarate.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
- Multifunctional 2-oxoglutarate metabolism enzyme
- 3-methyl-2-oxobutanoate dehydrogenase subunit alpha
- Pyruvate kinase
- 2-oxoglutarate oxidoreductase subunit KorA
- Putative malate oxidoreductase
- Pyruvate carboxylase
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
Sequence:
MTTDFARHDLAQNSNSASEPDRVRVIREGVASYLPDIDPEETSEWLESFDTLLQRCGPSRARYLMLRLLERAGEQRVAIPALTSTDYVNTIPTELEPWFPGDEDVERRYRAWIRWNAAIMVHRAQRPGVGVGGHISTYASSAALYEVGFNHFFRGKSHPGGGDQVFIQGHASPGIYARAFLEGRLTAEQLDGFRQEHSHVGGGLPSYPHPRLMPDFWEFPTVSMGLGPLNAIYQARFNHYLHDRGIKDTSDQHVWCFLGDGEMDEPESRGLAHVGALEGLDNLTFVINCNLQRLDGPVRGNGKIIQELESFFRGAGWNVIKVVWGREWDALLHADRDGALVNLMNTTPDGDYQTYKANDGGYVRDHFFGRDPRTKALVENMSDQDIWNLKRGGHDYRKVYAAYRAAVDHKGQPTVILAKTIKGYALGKHFEGRNATHQMKKLTLEDLKEFRDTQRIPVSDAQLEENPYLPPYYHPGLNAPEIRYMLDRRRALGGFVPERRTKSKALTLPGRDIYAPLKKGSGHQEVATTMATVRTFKEVLRDKQIGPRIVPIIPDEARTFGMDSWFPSLKIYNRNGQLYTAVDADLMLAYKESEVGQILHEGINEAGSVGSFIAAGTSYATHNEPMIPIYIFYSMFGFQRTGDSFWAAADQMARGFVLGATAGRTTLTGEGLQHADGHSLLLAATNPAVVAYDPAFAYEIAYIVESGLARMCGENPENIFFYITVYNEPYVQPPEPENFDPEGVLRGIYRYHAATEQRTNKAQILASGVAMPAALRAAQMLAAEWDVAADVWSVTSWGELNRDGVAIETEKLRHPDRPAGVPYVTRALENARGPVIAVSDWMRAVPEQIRPWVPGTYLTLGTDGFGFSDTRPAARRYFNTDAESQVVAVLEALAGDGEIDPSVPVAAARQYRIDDVAAAPEQTTDPGPGA
Protein: Vitamin K epoxide reductase complex subunit 1-like protein 1 (VKORC1-like protein 1) (EC 1.17.4.4) (Q6TEK3)
Organism: Rattus norvegicus (Rat)
Function: Involved in vitamin K metabolism. Can reduce inactive vitamin K 2,3-epoxide to active vitamin K, and may contribute to vitamin K-mediated protection against oxidative stress. Plays a role in vitamin K-dependent gamma-carboxylation of Glu residues in target proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:23928358}; Multi-pass membrane protein {ECO:0000305|PubMed:23928358}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
- NAD
- Vitamin K epoxide reductase complex subunit 1
Sequence:
MAAPVLLRVSVPRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALVLMTSSIVSVVGSLYLAYILYFVLKEFCIICVTTYVLNFLLLIINYKRLVYLNEAWKRQLQPKED
Protein: NAD(+)--arginine ADP-ribosyltransferase (EC 2.4.2.31) (Alt protein) [Cleaved into: Mature NAD(+)--arginine ADP-ribosyltransferase] (P12726)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: ADP-ribosyltransferase that efficiently ADP-ribosylates one of the two alpha subunits of host RNA polymerase RPOA on an arginine located in the C-terminal region. ADP-ribosylation of RPOA alpha subunit enhances the transcription of viral early genes. Also ribosylates RPOA subunits beta, beta' and sigma 70 and performs an autoribosylation reaction. Additional in-vitro identified targets include proteins involved in either translation or cellular metabolism such as elongation factor-Tu or GroeL. Mono-ADP-ribosylates host MAZF which may inactivate the latter.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04139, ECO:0000269|PubMed:376872, ECO:0000269|PubMed:4615179}. Note=About 25-50 copies per virion. This protein is injected into the bacterial cell along with the viral DNA. {ECO:0000255|HAMAP-Rule:MF_04139, ECO:0000269|PubMed:376872, ECO:0000269|PubMed:4615179}.
Interaction partners:
Sequence:
MELITELFDEDTTLPITNLYPKKKIPQIFSVHVDDAIEQPGFRLCTYTSGGDTNRDLKMGDKMMHIVPFTLTAKGSIAKLKGLGPSPINYINSVFTVAMQTMRQYKIDACMLRILKSKTAGQARQIQVIADRLIRSRSGGRYVLLKELWDYDKKYAYILIHRKNVSLEDIPGVPEISTELFTKVESKVGDVYINKDTGAQVTKNEAIAASIAQENDKRSDQAVIVKVKISRRAIAQSQSLESSRFETPMFQKFEASAAELNKPADAPLISDSNELTVISTSGFALENALSSVTAGMAFREASIIPEDKESIINAEIKNKALERLRKESITSIKTLETIASIVDDTLEKYKGAWFERNINKHSHLNQDAANELVQNSWNAIKTKIIRRELRGYALTAGWSLHPIVENKDSSKYTPAQKRGIREYVGSGYVDINNALLGLYNPDERTSILTASDIEKAIDNLDSAFKNGERLPKGITLYRSQRMLPSIYEAMVKNRVFYFRNFVSTSLYPNIFGTWMTDSSIGVLPDEKRLSVSIDKTDEGLVNSSDNLVGIGWVITGADKVNVVLPGGSLAPSNEMEVILPRGLMVKVNKITDASYNDGTVKTNNKLIQAEVMTTEELTESVIYDGDHLMETGELVTMTGDIEDRVDFASFVSSNVKQKVESSLGIIASCIDIANMPYKFVQG