wanglab/gogpt-training-data huggingface dataset:
Protein: Proline-rich transmembrane protein 2 (Dispanin subfamily B member 3) (DSPB3) (D3ZFB6)
Organism: Rattus norvegicus (Rat)
Function: As a component of the outer core of AMPAR complex, may be involved in synaptic transmission in the central nervous system. In hippocampal neurons, in presynaptic terminals, plays an important role in the final steps of neurotransmitter release, possibly by regulating Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation and down-regulate short-term facilitation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27172900}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Presynaptic cell membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Synapse {ECO:0000250|UniProtKB:E9PUL5}. Cell projection, axon {ECO:0000250|UniProtKB:Q7Z6L0}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:27172900}. Postsynaptic density membrane {ECO:0000269|PubMed:27172900}. Cell projection, dendritic spine {ECO:0000269|PubMed:27172900}.
Interaction partners:
- Multifunctional fusion protein
- Synaptotagmin-1
- Synapse differentiation-inducing gene protein 1
Sequence:
MAASSSEVSEMKGVEDSSNTHSEGPRHSEEGMGPVQVVAENLDQPEALQSGPDTTAAPVDSGPKAELAPETTETPVETPETVQATDLSVNPGEDSKTCPSPKEACQEPASRPEVNREATAEQGAEQQSAAPPEPTSEQALQLNTQSDPQPTSQPPPKPPLQAEPPTQENPTTEVLTESTGEKQENGAVVPLQAGDGEEGPAPQPHSPPSTKTPPANGAPPRVLQKLVEEDRIGRAHGGHPGSPRGSLSRHPSSQLAGPGVEGGEGTQKPRDYIILAILSCFCPMWPVNIVAFAYAVMSRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK
Protein: Putative tyrosinase-like protein tyr-1 (P34269)
Organism: Caenorhabditis elegans
Interaction partners:
- PHAryngeal gland Toxin-related
- Tyrosinase copper-binding domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- N-acyl-aliphatic-L-amino acid amidohydrolase
- Polypeptide N-acetylgalactosaminyltransferase 5
Sequence:
MGRLRAFLLFSGTLAVISTVHADFNCSQAPDSDMVQTCHMLQEWDSAARKAIRKRQAFNAGAPGVQGFSPSNPPRFAPSAQGCMNIACICPYMGGRMANGCILPNGQPYLMAYRKEYRMMSDNERQRWHNALIQLKRSGEYDRLSVMHRQVGSASGAHSGPGFLVWHREYMKRMEIALRMIDPGISMPYWDSVLESYLPDPRDSIMFGPQFMGMTDASGQLVSGPFAGFRTLEGRPNIIRRMATEGKMFTEQNINNLMAQNDLVSVMAFTAPQGGCPFRPYFGALEYTHASIHLWMGGDMKPPSTSANDPVFFLHHTFVDFIWEMWRQNHQNRFARENQYPPDIAACANSQHFSYAQMRPWDKINRDGLSNAYTDNLYHYAPRPTCNRNNANCGSQYLFCDTRGNPHCVAKVKPGGLCRGFEGLDSCYMGTCVAGWCRGGQQFQQPAQTTAVATVQQPQQQPQQQQPQQQRPATTPQSNCYNEDPCCNQWSRQNECRTNTVYMNRYCRKSCGLCQSNDNNRGCHDRHISCAYWRGQNFCTRRRQWMAENCQATCGWCNMNEAQLCASVARQSRRVRRNAKFWLTEPDADDFVDDFMLDYGR
Protein: Sensor histidine kinase GlnK (EC 2.7.13.3) (P40758)
Organism: Bacillus subtilis (strain 168)
Function: Member of the two-component regulatory system GlnK/GlnL that positively regulates the expression of the glsA-glnT operon in response to glutamine. It seems that autophosphorylated GlnK transfers a phosphoryl group to GlnL, which positively regulates the expression of the glsA-glnT operon. Interaction between GlnK-AmtB complex and TnrA protects TnrA from proteolytic degradation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17001076}; Multi-pass membrane protein {ECO:0000305|PubMed:15995196}. Note=ATP concentrations are sensed by GlnK and affect its cellular localization. {ECO:0000269|PubMed:17001076}.
Interaction partners:
- Transcriptional regulatory protein GlnL
- Glutaminase 1
- Probable sodium/glutamine symporter GlnT
- HTH-type transcriptional regulator TnrA
- Glutamine transport ATP-binding protein GlnQ
Sequence:
MLITVPLAGELKFYPLNEEFRVSFGAPVFFFFLSLLRHVPAVLPGFLTGAAVFIFRVFLELWGGGHNGLTPILYDQASGFFFYMTYACLFSILKANRFRERPIMLGFIGFMIEVVSDCVELTVQFLIFHTVVTPEKITDIAVIAISHTFIVMSFYSVLKLYETQSREKQTRQQHEHMLMIVSNLYEETVHLKKTLKTTEKVTNDSYQLYREMKGKDVQLSGRILRLAGEIHEVKKDNQRIFAGLSKLISNESLRDYMRASDLLQLVIRMNEKYAEALGKQIDFYCSIEGEHDEYHVFIVLSIINNLTANAVEAMDEEGMVSLRLRKPNESMVEFQVEDNGPGISEKIGDIVFDPGFTSKYDEFGTPSTGIGLSYVKEIVTELEGDITFDNQQRGVVFAIRLPVRHLIQKG
Protein: Zinc finger protein 292 (D3ZXZ1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein 644
Sequence:
MADDEAEQERLSGGSCAAELRRLGERLQELERRLCESREPAVEAAAAYCRQLCQTLLEYAEKWKTSEDPLPLLEVYTVAIQSYVKARPYLTSECESVALVLERLALSCVELLLCLPVELSDKQWEQFQTLVQVAHETLMESGSCELHFLATLAQETGVWKNAVLSTILSQEPLDKEKVNEFLAFEGPILLDMRIKHLIKTNQLSQATALAKLCSDHPEIGTKGSFKQTYLVCLCTSSPSEKLIEEISEVDCKDALEMICNLESEGDEKSALVLCTAFLSRQLQQGDMYCAWELTLFWSKLQQRVEPSVQVYLERCRQLSLLTKTVYHIFFLIKVINSETEGAGLATCIELCVKALRLESTENTEVKISICKTISCLLPEDLEVKRACQLSEFLIEPTVDAYYAVEMLYNQPDQKYDEENLPIPNSLRCELLLVLKTQWPFDPEFWDWKTLKRQCLALMGEEASIVSSIDELNDSEVYEKVDYQGERGDTSVNGLSAGLGTDSSLLIDTGDEKQKKKEIKELKDRGFISARFRNWQAYMQYCLLCDKEFLGHRIVRHAQKHYKDGVYSCPICAKNFNSKESFVPHVTLHVKQSSKERLAAMKPLRRLGRPPKITATHENQKTNTNTVAKQEQRPIKKNSLYSTDFIVFNDNDGSDDENDDKDKSYEPEVIPVQKPVPVNEFNCPVTFCKKGFKYFKNLIAHVKGHKDSEDAKRFLEMQSKKVICQYCRRHFVSVTHLNDHLQMHCGSKPYICIQMKCKAGFNSYAELLAHRKEHQVFRAKCLFPKCGRIFSQAYLLYDHEAQHYNTYTCKFTGCGKVYRSQSEMEKHLDDHSAPEKVLPPEDQLTPSGNEVTQNSEGTTGEGRSEHSIEKSEGPDRSGDWEKNKAESAVTTHSQISASELRQADIPLSDGLGNPGDTTVLQTNEVAVSIKVSVNHGIEDDFGKQENLTMEGTGEPLITDVHKPGEGAGVHFRHPGFQEKKDHECLNKAQTAQNSLANSESLKMGDLNPQSLERQVNTLTTFSVQNEGGLEDSSQICKFECGGDVKTSSSLYDLPLKTLESVAFVPSQPDLSSPLGAPSVPPKAPGQKFSCQVEGCTRTYNSSQSIGKHMKTAHPDQYAAFKLQRKTKKGQKSNNLSTPDHGKCVYFLPSQVSSSNHAFFTPQTKASGNPACSAQLQHVSPSIFPAHLASVSTSLLPSVESVLSPNMPSQDKHVQDGMLCSQMENLSNAALPAQMEDLTKTVLPLNIDSGSDPFLPLPTENSSLFSSPAHSENNSVFSQLESSTNHYPSPTEGNLNSSFLKGGSSENGAFPSHVSTADDLSSTSAQQSAPKKVKKDRGRGPNGKERKPKHNKRAKWPAIIRDGKFICSRCYRAFTNPRSLGGHLSKRSYCKPLDGAEIAQELLQTNRQPSLLASMILSTSTVNMQQPQQSNCNPETCFKDPSFLQLLSVENRPNFLPSTFPRCDVSNFNAGVSQEGSEIIKQALETAGIPSTFESAEMLSQVVPIGSVSDAAQVNAEGMPGPTVTPLLQTVCHTNTSPSSQNQTPNSKTSNLKECNSLPIFTTNDLLLKTIENGLCSNSFSSSTEPPQNFTNNSTHVSVISGPQNTRSNHLNKKGNSASKKRKKVTPAVIVSNTSQNVVPTDLTMGLASKNLTVPDTNTRDMIPDCEPQALVENLTQKLNNIDNHLFLTDVKESCKASLEPHTMLTPLTLKTENGDSRMMPLNSCTPVSSDLQISEDNVIQNFEKTLEIIKTAMNSQILEVKSGSQGTGETTQNAQINYSMQLPSVNSIPDNKLPDSSQCSSFLTVMPTKHNIPQSEALHKEDQIQDILEGLQNLKLETDISAPPSQATLINKSVALSPTPTKSTPNIIVQPVSEVIHVQLNDRVNKPFVCQNQGCNYSAMTKDALFKHYGKIHQYTPEMILEIKKNQLKFAPFKCVVPTCTKTFTRNSNLRAHCQLVHHFTIEEMVKLKIKRPYGRKSQGENLSSPQINQVKKQLPMAEEAKTESQPAFEVPAVAGEDALDNVAVIPENQLAEKKSPEKPESSSQPVTASTEQYNANLGNLKTKGRKNKRHRKEKEEKREKNPVSQSFEFPTRYSSYRPYCCVHQGCFAAFTIQQNLILHYQAVHKSNLPTFSAEVEEESEAVKESEETEPKQSMKEFRCQVSDCSRIFQAITGLIQHYMKLHEMTPEEIESMTAAVDVGKFPCDQLECKSSFTTYLSYVVHLEVDHGIGTRTSKTEEDGIYKCDCEGCDRIYATRSNLLRHIFNKHNDKHKAHLIRPRKLTGQENISSKANQEKSKSKHRAIKHNRFGKDGMKGPKTKRKKKSNLESKSAKIVQIEEDKPYSLKRGKHVYSIKARNDALSECTSKFVTQYPCMIKGCTSVVTSESNIIRHYKCHKLSKAFTSQHRNILIVFKRYGNPQEKEVSEQEDEKNDKKDPDSSVLEKNDNSQPASIPQEEGMKGEKDEMDELTELFITKLINEDSTNTETQVSTTLKVNNDFQEHDSCISERQKTGNLKRVYKEKNITQNKKRKIDKTEPEVPLVVNKTHKEEETAVAVQTTEEHPASFDWSSFKPMGFEASFLKFLEESAVKQKKNTDRDHSHSGSKRGSHSNSRKNVDKTAVTGGNHVCSCKESEIFVQFANPSKLQCSENVKIVLDKTLKDCSELVLKQLQEMKPTVSLKKLEVLSNDPDRTVLKELSLGKATGRGQY
Protein: Phosphomevalonate kinase (PMKase) (EC 2.7.4.2) (A0A8I5Y980)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|PIRNR:PIRNR036639}.
Interaction partners:
Sequence:
IAGIYGIFYARLGGNICAVLRLSGPLKEQYAREHGLDFQKLLDASTYKETYRRDMICWGEEKRQADPGFFCRKIVEGVSQPIWLVSDTRRMSDIQWFQEAYGALTQTVRVVASEQSRQQRGWVFTRGVDDAESECGLDSFGDFDWVIENHGDEQCLEDQLENLLEFIHAKLQR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q86XZ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAKVRLKKLEQLLLDGPWRNESALSVETLLDVLVCLYTECSHSALRRDKYVAEFLEWAKPFTQLVKEMQLHREDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERDVLVNGDCQWITALHYAFQDENHLYLVMDYYVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIDSIHQLHYVHRDIKPDNVLLDVNGHIRLADFGSCLKMNDDGTVQSSVAVGTPDYISPEILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEERFQFPSHVTDVSEEAKDLIQRLICSRERRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFDVDDDVLRNTEILPPGSHTGFSGLHLPFIGFTFTTESCFSDRGSLKSIMQSNTLTKDEDVQRDLEHSLQMEAYERRIRRLEQEKLELSRKLQESTQTVQSLHGSSRALSNSNRDKEIKKKKK
Protein: Ras-related protein Rab-1B (P34140)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Rab1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H0U4}. Membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000250|UniProtKB:Q9H0U4}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0U4}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTINLDGKIIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDHVSFNNVKQWMQEIQRYACDSVTRLLVGNKCDLIEKKIVDTSTAREYADSVGIPFLETSAKSSANVEQAFMIMASEIKKLQGGIQPNNNSTYNAHVVKPTGFTPIGKKKKCSII
Protein: U3 small nucleolar RNA-associated protein NOL7 (U3 snoRNA-associated protein NOL7) (Nucleolar protein 7) (Nucleolar protein of 27 kDa) (Q9UMY1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16205646, ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 4 homolog
- WD repeat-containing protein 43
- WD repeat-containing protein 75
- Nucleolar protein 11
- U3 small nucleolar RNA-associated protein 15 homolog
- rRNA-processing protein FCF1 homolog
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 10
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS7
Sequence:
MVQLRPRASRAPASAEAMVDEGQLASEEEEAEHGLLLGQPSSGAAAEPLEEDEEGDDEFDDEAPEELTFASAQAEAREEERRVRETVRRDKTLLKEKRKRREELFIEQKKRKLLPDTILEKLTTASQTNIKKSPGKVKEVNLQKKNEDCEKGNDSKKVKVQKVQSVSQNKSYLAVRLKDQDLRDSRQQAAQAFIHNSLYGPGTNRTTVNKFLSLANKRLPVKRAAVQFLNNAWGIQKKQNAKRFKRRWMVRKMKTKK
Protein: Addiction module killer protein (Q9A406)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
- HTH cro/C1-type domain-containing protein
Sequence:
MRGLPGDLRPVGGGVSELRVHVGPGYRIYVARRADVVIVLLCGGDKSSQARDIEKARVIARSLEW
Protein: 7SK snRNA methylphosphate capping enzyme bin3 (EC 2.1.1.-) (Bicoid-interacting protein 3) (Q7K480)
Organism: Drosophila melanogaster (Fruit fly)
Function: S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it (By similarity). Required for dorso-ventral patterning in oogenesis and for anterior-posterior pattern formation during embryogenesis, possibly by binding and stabilizing 7SK RNA, thereby promoting formation of a repressive RNA-protein complex.
Interaction partners:
- Uncharacterized protein, isoform A
- IP19903p
- IP10578p
- Cyclin-dependent kinase 9
- Hexamethylene bisacetamide inducible, isoform B
- La-related protein 7
- Nucleolar protein 16
Sequence:
MEKRLSDSPGDCRVTRSTMTPTLRLDQTSRQEPLPQQPDNGPAAAPGKSKSPTPLPGKSQAAQHHQFRAPQQQQGPKNRNKAWSKRQHKAGGKHNPSACVGASSGQAQSTGSSVIAATLLPTAASAHKADLENIQNIHNKNLTAGGGVNHHGNAGTAHHGGGGGAGAHHAAAGGHHHHHNTRLAQNAAAGGASGGGTIQMHKKMLRGHHHHVLCAGNNANHTCCLVTGCNGSSIGGVGVAGSGGATASAGGGGASCKEAQSCKDTSSLSGNSSIAGSAGAGNAVHYCCGRSKFFLPEKRLRKEVIVPPTKFLLGGNISDPLNLNSLQNENTSNASSTNNTPATTPRQSPITTPPKVEVIIPPNIHDPLHLLDPVDSMEYEKQLTSPMKRAGPGGGMLHHRQHHYRTRKNRKRRRFDSNNTSHAGDEGGVGSELTDEPPLPAATSSLAASPVAAPLNVGGSLLLSESAAPAPGETAEMGQQQEQAHVHSPQSASTTTTAAEMPTPTPTSAAAATATAEHKEQSAPAPTATSSPQRQQQHVAAAAEELPTPETSAAAETPAEEMLLSCSATSASLVASTLAERRASRDLRLDLSSTCYGVGGTGLSFGGSISSSVGSSFGGGGRKRKISESSTSQKSKKFHRHDAMDKIVSPVVPQPGAWKRPPRILQPSGARKPSTRRSTSVSESELLSPVEEQPPKQLPLIGVEIPRDDTPDLPDHGLGSPLSTTSGATSHTAGEQDSLAGVDISMGDTLGSGVVGKAPLTSSLMLEPAKIPPIKMLPKFRADGLKYRYGNFDRYVDFRQMNEFRDVRLQVFQRHVELFENKDILDIGCNVGHMTITVARHLAPKTIVGIDIDRELVARARRNLSIFVRIPKEEKLLEVKAEPTVDAKANIAVKDETSGAAHKKTRRGKRRRKVHQGIHHHHHHHHDLEQLQQQQKLNSLLVKPHEFFPISFPLTYGRIPRILSSSKSPNMLGNKNQFPANVFFRHTNYVLKDESLMASDTQQYDLILCLSVTKWIHLNFGDNGLKMAFKRMFNQLRPGGKLILEAQNWASYKKKKNLTPEIYNNYKQIEFFPNKFHEYLLSSEVGFSHSYTLGVPRHMNKGFCRPIQLYAKGDYTPNHVRWSDAYYPQTPYEAYRGIYATLPVHRMGGGGSSAGGSNSGHAQMLHLSSSSRSQNYDTPHYAGSASGSASCRQTPMYQPTYNPLETDSYQPSYDMEYLNHMYVFASPLYQTVWSPPASLRKSSSHTPVFGSVRDAELDGDGSGGGGSGGGSYHRHVYPPNDDTCSPNANACNAFNSIRDADTDDSNQLPGGSRRHVYATNCGESSSSPQVNHHDAVGEFVDGLMDDEQKSSTGGGTGGAAYCDLSDA
Protein: Bridge-like lipid transfer protein family member 3B (Syntaxin-6 Habc-interacting protein of 164 kDa) (UHRF1-binding protein 1-like) (A0JNW5)
Organism: Homo sapiens (Human)
Function: Tube-forming lipid transport protein which mediates the transfer of lipids between membranes at organelle contact sites. Required for retrograde traffic of vesicle clusters in the early endocytic pathway to the Golgi complex.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20163565}. Early endosome {ECO:0000269|PubMed:20163565, ECO:0000269|PubMed:35499567}. Note=Localizes on a subpopulation of vesicle clusters in the early endocytic pathway. {ECO:0000269|PubMed:35499567}.
Interaction partners:
- Syntaxin-6
Sequence:
MAGIIKKQILKHLSRFTKNLSPDKINLSTLKGEGELKNLELDEEVLQNMLDLPTWLAINKVFCNKASIRIPWTKLKTHPICLSLDKVIMEMSTCEEPRSPNGPSPIATASGQSEYGFAEKVVEGISVSVNSIVIRIGAKAFNASFELSQLRIYSVNAHWEHGDLRFTRIQDPQRGEVLTFKEINWQMIRIEADATQSSHLEIMCAPVRLITNQSKIRVTLKRRLKDCNVIATKLVLILDDLLWVLTDSQLKAMVQYAKSLSEAIEKSTEQRKSMAPEPTQSSTVVASAQQVKTTQTSNAPDVNDAIVKLFNDFDVKETSHHLVISHLDLHICDDIHAKEKESNRRITGGAMQLSFTQLTIDYYPYHKAGDSCNHWMYFSDATKTKNGWANELLHEFECNVEMLKQAVKDHNVGSPPKSPTHASPQHTQTEKDYPLKGTCRTPSVLSQQSKAKLMSSSVVVRLADFNIYQVSTAEQCRSSPKSMICCNKKSLYLPQEMSAVYIEFTEYYYPDGKDFPIPSPNLYSQLNALQFTVDERSILWLNQFLLDLKQSLNQFMAVYKLNDNSKSDEHVDVRVDGLMLKFVIPSEVKSECHQDQPRAISIQSSEMIATNTRHCPNCRHSDLEALFQDFKDCDFFSKTYTSFPKSCDNFNLLHPIFQRHAHEQDTKMHEIYKGNITPQLNKNTLKTSAATDVWAVYFSQFWIDYEGMKSGKGRPISFVDSFPLSIWICQPTRYAESQKEPQTCNQVSLNTSQSESSDLAGRLKRKKLLKEYYSTESEPLTNGGQKPSSSDTFFRFSPSSSEADIHLLVHVHKHVSMQINHYQYLLLLFLHESLILLSENLRKDVEAVTGSPASQTSICIGILLRSAELALLLHPVDQANTLKSPVSESVSPVVPDYLPTENGDFLSSKRKQISRDINRIRSVTVNHMSDNRSMSVDLSHIPLKDPLLFKSASDTNLQKGISFMDYLSDKHLGKISEDESSGLVYKSGSGEIGSETSDKKDSFYTDSSSILNYREDSNILSFDSDGNQNILSSTLTSKGNETIESIFKAEDLLPEAASLSENLDISKEETPPVRTLKSQSSLSGKPKERCPPNLAPLCVSYKNMKRSSSQMSLDTISLDSMILEEQLLESDGSDSHMFLEKGNKKNSTTNYRGTAESVNAGANLQNYGETSPDAISTNSEGAQENHDDLMSVVVFKITGVNGEIDIRGEDTEICLQVNQVTPDQLGNISLRHYLCNRPVGSDQKAVIHSKSSPEISLRFESGPGAVIHSLLAEKNGFLQCHIENFSTEFLTSSLMNIQHFLEDETVATVMPMKIQVSNTKINLKDDSPRSSTVSLEPAPVTVHIDHLVVERSDDGSFHIRDSHMLNTGNDLKENVKSDSVLLTSGKYDLKKQRSVTQATQTSPGVPWPSQSANFPEFSFDFTREQLMEENESLKQELAKAKMALAEAHLEKDALLHHIKKMTVE
Protein: START domain-containing protein 10 (StARD10) (PCTP-like protein) (PCTP-L) (Serologically defined colon cancer antigen 28 homolog) (StAR-related lipid transfer protein 10) (Q9JMD3)
Organism: Mus musculus (Mouse)
Function: Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes (By similarity). May play metabolic roles in sperm maturation or fertilization.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:10819773}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Mainly cytosolic (By similarity). In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm. {ECO:0000250}.
Interaction partners:
- Lysophosphatidylcholine acyltransferase 1
- Steroidogenic acute regulatory protein, mitochondrial
- StAR-related lipid transfer protein 3
- StAR-related lipid transfer protein 5
- Ceramide transfer protein
- Phosphoinositide-interacting protein
Sequence:
MEKPAASTEPQGSRPALGRESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQSPLPSLALSELSVQHADSLENIDESAVTESREERAGGAGGEGSDDDTSLT
Protein: Alpha-1-acid glycoprotein 2 (AGP 2) (Orosomucoid-2) (OMD 2) (P19652)
Organism: Homo sapiens (Human)
Function: Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction.
Subcellular location: Secreted.
Interaction partners:
- Alpha-1-acid glycoprotein 1
- Albumin
- Alpha-1-antitrypsin
- Haptoglobin
- Ceruloplasmin
- Alpha-2-HS-glycoprotein
- Alpha-1-antichymotrypsin
- Protein AMBP
- C-reactive protein
- Transthyretin
Sequence:
MALSWVLTVLSLLPLLEAQIPLCANLVPVPITNATLDRITGKWFYIASAFRNEEYNKSVQEIQATFFYFTPNKTEDTIFLREYQTRQNQCFYNSSYLNVQRENGTVSRYEGGREHVAHLLFLRDTKTLMFGSYLDDEKNWGLSFYADKPETTKEQLGEFYEALDCLCIPRSDVMYTDWKKDKCEPLEKQHEKERKQEEGES
Protein: Protein phosphatase (Protein serine/threonine phosphatase PrpC,regulation of stationary phase (EC 3.1.3.16)) (Stp1) (Q8VQA1)
Organism: Streptococcus agalactiae
Interaction partners:
Sequence:
MEISLLTDIGQRRSNNQDFINQFENKAGVPLIILADGMGGHRAGNIASEMTVTDLGSDWAETDFSELSEIRDWMLVSIETENRKIYELGQSDDYKGMGTTIEAVAIVGDNIIFAHVGDSRIGIVRQGEYHLLTSDHSLVNELVKAGQLTEEEAASHPQKNIITQSIGQANPVEPDLGVHLLEEGDYLVVNSDGLTNMLSNADIATVLTQEKTLDDKNQDLITLANHRGGLDNITVALVYVESEAV
Protein: Polycomb group RING finger protein 1 (Q7ZYZ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BSM1}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- RING1 and YY1-binding protein A
- YY1-associated factor 2.
- Chromobox homolog 2
- Polycomb protein eed
- Chromobox homolog 8a
- Polyhomeotic-like protein 2
- Histone-lysine N-methyltransferase EZH2
- Chromobox homolog 4
- Zinc finger protein AEBP2
Sequence:
MAEQGPMAIAMRLRNQLQNVYKLDPLRNEEEVKIKIKDLNEHIVCYLCAGYFIDATTITECLHTFCKSCIVKYLQTSKYCPMCNIKIHETQPLLNLKLDRVMQDIVYKLVPGLQESEDKRIKEFYQSRGLERIIQPSGEESVPDNTGLPYTSFDHSKAHFYRYDEQVSLCLERQSSSFSGKDKNKLTLQQKFVRCSVRAEVRHLRKVLCHRLNVEKHQVQMLFNNESLPDHMTMKRLWLSHWFGKAQPLVLHYTIKDKRTR
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g67720 (EC 2.7.11.1) (C0LGI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein At4g06744
- Vacuolar iron transporter homolog 1
- Cyclase-associated protein 1
Sequence:
MGLCLAQLAVTCLFLVPFVLSQVTEFVSIDCGCSSNYTDPRTGLGWVSDSEIIKQGKPVTLANTNWNSMQYRRRRDFPTDNKKYCYRLSTKERRRYIVRTTFLYGGLGSEEAYPKFQLYLDATKWATVTIQEVSRVYVEELIVRATSSYVDVCVCCAITGSPFMSTLELRPLNLSMYATDYEDNFFLKVAARVNFGAPNMDALRYPDDPYDRIWESDINKRPNYLVGVAPGTTRINTSKTINTLTREYPPMKVMQTAVVGTQGLISYRLNLEDFPANARAYAYFAEIEELGANETRKFKLVQPYFPDYSNAVVNIAENANGSYTLYEPSYMNVTLDFVLTFSFGKTKDSTQGPLLNAIEISKYLPISVKTDRSDVSVLDAIRSMSPDSDWASEGGDPCIPVLWSWVNCSSTSPPRVTKIALSRKNLRGEIPPGINYMEALTELWLDDNELTGTLPDMSKLVNLKIMHLENNQLSGSLPPYLAHLPNLQELSIENNSFKGKIPSALLKGKVLFKYNNNPELQNEAQRKHFWQILGISIAAVAILLLLVGGSLVLLCALRKTKRADKGDSTETKKKGLVAYSAVRGGHLLDEGVAYFISLPVLEEATDNFSKKVGRGSFGSVYYGRMKDGKEVAVKITADPSSHLNRQFVTEVALLSRIHHRNLVPLIGYCEEADRRILVYEYMHNGSLGDHLHGSSDYKPLDWLTRLQIAQDAAKGLEYLHTGCNPSIIHRDVKSSNILLDINMRAKVSDFGLSRQTEEDLTHVSSVAKGTVGYLDPEYYASQQLTEKSDVYSFGVVLFELLSGKKPVSAEDFGPELNIVHWARSLIRKGDVCGIIDPCIASNVKIESVWRVAEVANQCVEQRGHNRPRMQEVIVAIQDAIRIERGNENGLKSSSSSSSKAQSSRKTLLTSFLELESPDISRNSLAPAAR
Protein: Temporin-1Ta (TA) (Temporin-A) (P56917)
Organism: Rana temporaria (European common frog)
Function: Amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-positive bacteria, weak activity against Gram-negative bacteria, and moderate activity against fungi. Mainly acts by causing membrane permeabilization (Probable). Is also able to kill S.aureus (both wild-type and MRSA) that are internalized in human keratinocytes without injuring host cells. Rapidly inactivates both channel catfish herpesvirus (ED(50)=15 uM) and frog virus 3 (ED(50)=58 uM) over a wide temperature range. Also displays anti-leishmania activity by damaging parasite membrane. Acts synergistically with temporin-L which improves temporin-1Ta activity by preventing its self-association in lipopolysaccharides (LPS). Does not show hemolytic activity. In vitro, stimulates insulin release from pancreatic beta-cells in a dose-dependent manner without increasing intracellular calcium, protects beta-cells against cytokine-induced apoptosis and augments beta-cells proliferation. In vivo, intraperitoneal injection together with a glucose load into mice does not have effect on plasma glucose levels. In vivo, when tested on mice with methicillin-resistant S.aureus (MRSA)-infected wounds, this peptide inhibits bacterial growth and shows wound healing effect. In vitro, promotes cell migration and wound healing.
Subcellular location: Secreted {ECO:0000269|PubMed:34235566, ECO:0000269|PubMed:9022710}. Target cell membrane {ECO:0000269|PubMed:24039798}. Target cell, target cell cytoplasm {ECO:0000269|PubMed:24514087}.
Interaction partners:
Sequence:
FLPLIGRVLSGIL
Protein: CALX (O18367)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MQLLLKSIFTCALFVIFVYATAQSLLKVQETEARQAYLNVTSSSSSNLSQDDGHFLSRRLRQVSHGEEGDEGAPSQMDDELEQMTKVHGEAPDAEDVRECSEGLVLPLWMPQRNISVGDRLVRGFVYFVLLIYLFVGVSIIADRFMAAIEAITSIERAVVVKGPNNTKQVMHVRIWNETVANLTLMALGSSAPEILLSVIEIYAKDFESGDLGPGTIVGSAAYNLFMIIAVCMIWIPAGEVRRIRHLRVFFVTALFSVFAYVWLWLILSVFTPGVILVWEAIVTLLFFPLTVLWAYIAERRLLVYKYMDKNYRVNKRGTVVAGEHDQVEMDAEKGPKQPMVTSARGNDAEAFDEARREYITLLTELRQKYPDADLEQLEMMAQEQVLARSGRSRAFYRIQATRKMVGSGNLMRKIQERAHSDLTGVKAQLHAGDDEEADDPIRMYFEPGHYTVMENCGEFEVRVVRRGDISTYASVEYETQDGTASAGTDFVGRKGLLSFPPGVDEQRFRIEVIDDDVFEEDECFYIRLFNPSEGVKLAVPMIATVMILDDDHAGIFAFTDSVFEITESVGRFELKVMRYSGARGTVIVPYWTENDTATESKDYEGARGELVFENNESEKFIDLFILEESSYEKDVSFKVHIGEPRLAPDDELAAKIKEVEKKPVQDLTELDRILLLSKPRNGELTTAYVRIRESQEFKATVDKLVAKANVSAVLGTSSWKEQFKDALTVIPADESEFDNDDEEEEVPSCFSYVSHFVCLFWKVLFAFVPPTDICGGYVTFVVSIFVIGVITAIIGDAASYFGCALNIKDSVTAILFVALGTSIPDTFASMIAAKHDEGADNCIGNVTGSNAVNVFLGIGLAWTIAAVYHSSHGMTFNVEPGTIGFAVALFCGEALIAIMLIMFRRWHKGIGAELGGPKVSKYISAAILVFLWVFYVVICILEAYDVIRV
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (P16435)
Organism: Homo sapiens (Human)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- Cytochrome b5
- Cytochrome b5 type B
- Cytochrome P450 3A4)
- Heme oxygenase 1
- Lanosterol 14-alpha demethylase
- Cytochrome P450 3A5
- Cytochrome P450 4F3
- Cytochrome P450 3A7
- Peptidyl-prolyl cis-trans isomerase G
- Cytochrome P450 4F2
Sequence:
MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTLTSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEHFNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPFIGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQSHKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVDYIKKLMTKGRYSLDVWS