wanglab/gogpt-training-data huggingface dataset:
Protein: Neurolysin, mitochondrial (EC 3.4.24.16) (Microsomal endopeptidase) (MEP) (Mitochondrial oligopeptidase M) (Neurotensin endopeptidase) (P42676)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:7836437}. Cytoplasm, cytosol {ECO:0000269|PubMed:7836437}.
Interaction partners:
- Neurotensin/neuromedin N
Sequence:
MITLCLSTLRGLHRAGGSRLQLTMTLGKELASPLQAMSSYTAAGRNVLRWDLSPEQIKTRTEQLIAQTKQVYDTVGTIALKEVTYENCLQVLADIEVTYIVERTMLDFPQHVSSDREVRAASTEADKKLSRFDIEMSMREDVFQRIVHLQETCDLEKIKPEARRYLEKSIKMGKRNGLHLSEHIRNEIKSMKKRMSELCIDFNKNLNEDDTSLVFSKAELGALPDDFIDSLEKTDEDKYKVTLKYPHYFPVMKKCCVPETRRKMEMAFHTRCKQENTAILQQLLPLRAQVAKLLGYNTHADFVLELNTAKSTSRVAAFLDDLSQKLKPLGEAEREFILSLKKKECEERGFEYDGKINAWDLHYYMTQTEELKYSVDQESLKEYFPIEVVTEGLLSIYQELLGLSFEQVPDAHVWNKSVSLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMSVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVDSLRKLSKHYKDGHPITDELLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNATLDAASEYAKYCTEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFHSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLQNFLQREPNQKAFLMSRGLNGS
Protein: Protein KRBA1 (A5PL33)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRENYETLVSVGTAELLPLSAFLSPSEPGRAVGGGSHADEGQEPAGCGDPQGGQPRHSLHLTALVQLVKEIPEFLFGEVKGAMDSPESESRGASLDGERASPEAAAAREPCPLRGLLSCLPDGPTSQPHLATTPTDSSCSSGPTGDGVQGSPLPIKTADKPWPTRKEGPGALGGEPSPPTHSPSRRKSHRGQERGTSEAGISPGNSPLQGLINCLKEILVPGPRHPETSPSFLPPLPSLGTSRLTRADLGPGSPPWAVKTEAVSGDCPLQGLLHCLKELPEAQDRHPSPSGVGNRRLQENPGAWKRGSGGPGYLLTPPPHPDLGAGGLLSVKMENSWVQSPPGPASCQPGRQPLSPSATGDTRGVPQPSWGPEAQAASASSSPLEALEACLKGIPPNGSSPSQLPPTSCSQNPQPGDSRSQKPELQPHRSHSEEATREPVLPLGLQSCVRDGPSRPLAPRGTPTSFSSSSSTDWDLDFGSPVGNQGQHPGKGSPPGSSPLQGLENCLKEIPVPVLRPAWPCSSAADRGPRRAEPRNWTADKEGLRAEACESARLGQGRGEAPTRSLHLVSPQVFTSSCVPACHQRGFKDPGATRPGVWRWLPEGSAPKPSPLHCLESALRGILPVRPLRFACVGGPSPSPSPGSSSSFSGSEGEDPRPEPDLWKPLPQERDRLPSCKPPVPLSPCPGGTPAGSSGGSPGEDPRRTEPRYCSGLGAGTAQDPCPVSQLEKRPRVSEASRGLELGHGRPRVAAKTHERLLPQGPPELPSESPPPELPPPEAAPPVLPASSLQPPCHCGKPLQQELHSLGAALAEKLDRLATALAGLAQEVATMRTQVNRLGRRPQGPGPMGQASWMWTLPRGPRWAHGPGHRHLPYWRQKGPTRPKPKILRGQGESCRAGDLQGLSRGTARRARPLPPDAPPAEPPGLHCSSSQQLLSSTPSCHAAPPAHPLLAHTGGHQSPLPPLVPAALPLQGASPPAASADADVPTSGVAPDGIPERPKEPSSLLGGVQRALQEELWGGEHRDPRWGAH
Protein: Disintegrin and metalloproteinase domain-containing protein 23 (ADAM 23) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 3) (MDC-3) (Q9R1V7)
Organism: Mus musculus (Mouse)
Function: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted.
Interaction partners:
- Leucine-rich glioma-inactivated protein 1
- Leucine-rich repeat LGI family member 3
- Leucine-rich repeat LGI family member 2
- Disintegrin and metalloproteinase domain-containing protein 22
- Leucine-rich repeat LGI family member 4
- Disks large homolog 4
Sequence:
MKPPGSISRRPTLTGCSLPGASCGPGRCPAGPVPARAPPCRLLLVLLLLPALATSSRPRARGAAAPSAPHWNETAEKTLGVLADEDNTLQQNSSSRNTSYSSAVQKEITLPSRLVYYINQDSESPYHVLDTKARHQQKHNKAVHLAQASFQIEAFGSKFILDLTLNNGLLSSDYVEIHYEDGKQMYSKGGEHCYYHGSIRGVKDSRVALSTCNGLHGMFEDDTFVYMIEPLELTDDEKSTGRPHIIQKTLAGQYSKQMKNLSTDGSDQWPLLPELQWLRRRKRAVNPSRGVFEEMKYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKDHIDITINPVQMLHDFSKYRQRIKQHADAVHLISRVTFHYKRSSLSYFGGVCSRIRGVGVNEYGLPMAVAQVLSQSLAQNLGIQWEPSSRKPKCECIESWGGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRPTKLFEPTECGNGYVEAGEECDCGFHVECYGVCCKKCSLSNGAHCSDGPCCNNTSCLFQSRGYECRDAVNSCDITEYCTGDSGQCPPNLHKQDGYSCNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIPCSKHDVFCGFLLCTNLTRAPRIGQLQGEIIPTSFYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCLQIQALNMSSCPLDSRGKVCSGHGVCSNEATCICDFTWAGTDCSIRDPVRNPNPPKDEGPKGPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPTQQGPI
Protein: 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) (Zgc:56036) (Q7ZVG1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSLLRGVFIVSAKRTPFGTYGGVLKDHSATDLAEHAAKAALAAGNVAPELVNSVIIGNVMQSSADAPYIARHVGLRCGVPIPVPALTVNRLCGSGFQSIINGAQEICLKESEVVLCGGSESMSQAPYAVRNIRFGTKFGVDLELEDTLWAGLTDLNIKLPMGITAENLAEKYQISREECDQYSHQTQQRWKAAHEAGYFNAEIAPIEVKAKKGKVSMTFDEHPRPQTTLEQMAKLPTVFKKGGTVTAANASGVSDGAAAVIIASEDAVKAHKLTPLARIVSYHTSGCDPSIMGIGPVPAITEALKKAGLSIKDMDLVEVNEAFAPQYLSVAKSLGLDPEKTNVNGGAIAIGHPLGASGTRITAHLVHELRRRGGKYAVGSACIGGGQGIAVILENIK
Protein: Potassium channel subfamily U member 1 (Calcium-activated potassium channel subunit alpha-3) (Calcium-activated potassium channel, subfamily M subunit alpha-3) (Pore-forming subunit of the sperm-specific alkalization activated K(+) current) (KSper) (Slowpoke homolog 3) (mSlo3) (pH-sensitive maxi potassium channel) (O54982)
Organism: Mus musculus (Mouse)
Function: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). Represents the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:22084117}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:31270758}.
Interaction partners:
- Calcium-activated potassium channel subunit beta-4
- Calcium-activated potassium channel subunit beta
- Calcium-activated potassium channel subunit beta-1
- Small conductance calcium-activated potassium channel protein 1
- Leucine-rich repeat-containing protein 52
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Small conductance calcium-activated potassium channel protein 2
- Small conductance calcium-activated potassium channel protein 3
- Intermediate conductance calcium-activated potassium channel protein 4
Sequence:
MSQTLLDSLNQKELTETSCTIEIQAAFILSSLATFFGGLIILFLFRIALKSSRSWKYVKGPRGLLELFSSRRIEANPLRKLYFHGVFRQRIEMLLSAQTVVGQVLVILVFVLSIGSLVIYFINSMDPVRRCSSYEDKIVHVDLSFNAFFSFYFGLRFWAAEDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPKILQILQVIKTSNSVKLSKLLSIVISTWFTAAGFLHLVENSGDPWLNGRNSQTMSYFESIYLVTATMSTVGFGDVVAKTSLGRIFIVFFTLGSLILFANYIPEMVELFSTRKKYTKPYEAVKGKKFIVVCGNITVDSVTAFLRNFLHWKSGEINIEIVFLGETLPCLELETLLKCHTSCTNFVCGTALKFEDLKRVAVENSEACLILANHFCSDLHDEDNSNIMRVLSIKNYYPQTRVIIQILQSQNKVFLSKIPNWDWSAGDNILCFAELKLGFIAQGCLVPGLCTFLTTLFIEQNQKVFPKHPWQKHFLNGLKNKILTQRLSNDFVGMTFPQVSRLCFVKLNLMLIAIQHKPFFHSCCTLILNPSSQVRLNKDTLGFFIADSSKAVKRAFFYCSNCHSDVCNPELIGKCNCKIKSRQQLIAPTIMVMKSSLTDFTTSSHIHASMSTEIHTCFSREQPSLITITTNRPTTNDTVDDTDMLDSSGMFHWCRAMPLDKVVLKRSEKAKHEFQNHIVVCVFGDAQCTLVGLRNFVMPLRASNYTRQELKDIVFIGSLEYFQREWRFLRNFPKIHIMPGSALYMGDLIAVNVEQCSMCVILATPYKALSSQILVDTEAIMATLNIQSLRITSPTPGSSKSEVKPSSAFDSKERKQRYKQIPILTELKNPSNIHFIEQMGGLDGMLKGTSLHLSTSFSTGAVFSDTFLDSLLATSFYNYHVVELLQMLVTGGISSEMEHYLVKEKPYKTTDDYEAIKSGRTRCKLGLLSLDQTVLSGINPRKTFGQLFCGSLDNFGILCVGLYRMIDEEEPSQEHKRFVITRPSNECHLLPSDLVFCAIPFNTTCGKSDSSPSIQAQNNSTNATTPLAQGSNFFDSHHADESHDLYPVDDTGERWSQHHHSRVYPLDTLDASDIVQEK
Protein: Neuronal cell adhesion molecule (Nr-CAM) (Neuronal surface protein Bravo) (mBravo) (NgCAM-related cell adhesion molecule) (Ng-CAM-related) (Q810U4)
Organism: Mus musculus (Mouse)
Function: Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding. Plays a role in mediating cell-cell contacts between Schwann cells and axons. Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20188654}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:14602817}. Secreted {ECO:0000269|PubMed:20188654}. Note=Detected at nodes of Ranvier (PubMed:14602817, PubMed:20188654, PubMed:24719088). {ECO:0000269|PubMed:14602817, ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}.
Interaction partners:
- Ankyrin-3
- Contactin-1
- Neuropilin-2
- Contactin-2
- Receptor-type tyrosine-protein phosphatase zeta
- Gliomedin
- Contactin-5
- Ankyrin-2
- Contactin-associated protein-like 4
- Semaphorin-6D
Sequence:
MQLKIMPKKKHLSAGGVPLILFLCQMISALDVPLDLVQPPTITQQSPKDYIIDPRENIVIQCEAKGKPPPSFSWTRNGTHFDIDKDPLVTMKPGSGTLVINIMSEGKAETYEGVYQCTARNERGAAVSNNIVVRPSRSPLWTKERLEPIVLQNGQSLVLPCRPPIGLPPAIIFWMDNSFQRLPQSERVSQGLNGDLYFSNVLPEDTREDYICYARFNHTQTIQQKQPISLKVISVDELNDTIAANLSDTEFYGAKSSKERPPTFLTPEGNESHKEELRGNVLSLECIAEGLPTPIIYWIKEDGMLPANRTFYRNFKKTLQITHVSEADSGNYQCIAKNALGAVHHTISVTVKAAPYWIVAPQNLVLSPGENGTLICRANGNPKPRISWLTNGVPIEIALDDPSRKIDGDTIIFSNVQESSSAVYQCNASNKYGYLLANAFVNVLAEPPRILTSANTLYQVIANRPALLDCAFFGSPMPTIEWFKGTKGSALHEDIYVLHDNGTLEIPVAQKDSTGTYTCVARNKLGMAKNEVHLEIKDPTRIIKQPEYAVVQRGSKVSFECRVKHDHTLIPTIMWLKDNGELPNDERFSTDKDHLVVSDVKDDDGGTYTCTANTTLDSASASAVLRVVAPTPTPAPIYDVPNPPFDLELTNQLDKSVQLTWTPGDDNNSPITKFIIEYEDAMHDAGLWRHQAEVSGTQTTAQLKLSPYVNYSFRVMAENSIGRSMPSEASEQYLTKAAEPDQNPMAVEGLGTEPDNLVITWKPLNGFQSNGPGLQYKVSWRQKDGDDEWTSVVVANVSKYIVSGTPTFVPYLIKVQALNDVGFAPEPAAVMGHSGEDLPMVAPGNVRVSVVNSTLAEVHWDPVPPKSVRGHLQGYRIYYWKTQSSSKRNRRHIEKKILTFQGTKTHGMLPGLQPYSHYALNVRVVNGKGEGPASTDRGFHTPEGVPSAPSSLKIVNPTLDSLTLEWDPPSHPNGILTEYILQYQPINSTHELGPLVDLKIPANKTRWTLKNLNFSTRYKFYFYAQTSVGPGSQITEEAITTVDEAGIPPPDVGAGKGKEEWRKEIVNGSRSFFGLKGLMPGTAYKVRVGAEGDSGFVSSEDVFETGPAMASRQVDIATQGWFIGLMCAVALLILILLIVCFIRRNKGGKYPVKEKEDAHADPEIQPMKEDDGTFGEYSDAEDHKPLKKGSRTPSDRTVKKEDSDDSLVDYGEGVNGQFNEDGSFIGQYSGKKEKEPAEGNESSEAPSPVNAMNSFV
Protein: Amidohydrolase-related domain-containing protein (Q9HZ64)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- S-methyl-5'-thioinosine phosphorylase
- Polyamine aminopropyltransferase 2
- Polyamine aminopropyltransferase 1
- Adenine deaminase
- Acyl-homoserine-lactone synthase
- Acyl-homoserine-lactone synthase
- Cytosine deaminase
- dCTP deaminase
- Methylthioribose-1-phosphate isomerase
- tRNA
Sequence:
MPNVRNPFDLLLLPTWIVPVEPAGVVLRDHALGIRDGQIALVAPREQAMRHGATEIRELPGMLLAPGLVNAHGHSAMSLFRGLADDLPLMTWLQDHIWPAEGQWVSEDFIRDGTELAIAEQVKGGITCFSDMYFYPQAICGVVHDSGVRAQVAIPVLDFPIPGARDSAEAIRQGMALFDDLKHHPRIRIAFGPHAPYTVSDDKLEQILVLTEELDASIQMHVHETAFEVEQAMERNGERPLARLHRLGLLGPRFQAVHMTQVDNDDLAMLVETNSSVIHCPESNLKLASGFCPVEKLWQAGVNVAIGTDGAASNNDLDLLGETRTAALLAKAVYGQATALDAHRALRMATLNGARALGLERLIGSLEAGKAADLVAFDLSGLAQQPVYDPVSQLIYASGRDCVRHVWVGGRQLLDDGRLLRHDEQRLIARAREWGAKIAASDRS
Protein: Seminal fluid protein 24C1 (E1JHS6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serpin 77Bb
Sequence:
MRSFCILALLITLKFEMGYGNSVCNLQATFIGWCKMTIRGFTFVASKNACRRISGPCAAQDNFFMDKASCETACKKIILP
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (O48500)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: This enzyme decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into viral progeny DNA. This activity is sufficient to exclude uracil from the DNA during phage replication. In the case of dUTPase mutant phages, the host dUTPase activity is not sufficient to exclude uracil from T5 DNA and uracil are incorporated, leading to decreased phage viability.
Interaction partners:
Sequence:
MIKIKLTHPDCMPKIGSEDAAGMDLRAFFGTNPAADLRAIAPGKSLMIDTGVAVEIPRGWFGLVVPRSSLGKRHLMIANTAGVIDSDYRGTIKMNLYNYGSEMQTLENFERLCQLVVLPHYSTHNFKIVDELEETIRGEGGFGSSGSK
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSW9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL32
- L21
- 60S acidic ribosomal protein P0
- Small ribosomal subunit protein eS6
- L23
- 60S ribosomal protein L36
- Candida glabrata strain CBS138 chromosome M complete sequence
- Large ribosomal subunit protein uL23
- RP41
Sequence:
MSSLVVAEQGSFQHILRLLNTNVDGNIKIVYALTTIKGVGRRYANLVCKKADVDLNKRAGELTQEELERVVQIMQNPTQYKIPAWFLNRQRDIADGKDYHTLANQVESKLRDDLERLKKIRAHRGIRHFWGLRVRGQHTKTTGRRRA
Protein: Golgin subfamily A member 8O (A6NCC3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEETQHNKLAAAKKKLKEYWQKNRPRVPAGVNRNRKTNGSIPETATSGGCQPPGDSATGFHREGPTSSATLKDLESPCQERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELNNENKSTLQLEQQVKELQEKLGEEHLEAASQQNQQLTAQLSLMALPGEGHGGEHLDSEGEEAPRPMPSVPEDPESREAMSSFMDHLKEKADLSELVKKQELRFIQYWQERCHQKIHHLLSEPGGRAKDAALGGGHHQAGAQGGDEGEAAGAAADGIAAYSNYNNGHRKFLAAAHNSADEPGPGAPAPQELGAADKHGDLREVTLTSSAQGEAREDPLLDKPTAQPIVQDHQEHPGLGSNCCVPLFCWAWLPRRRR
Protein: Membrane-associated progesterone receptor component 1 (mPR) (O55022)
Organism: Mus musculus (Mouse)
Function: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:27599036}; Single-pass membrane protein {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:27599036}. Secreted {ECO:0000250|UniProtKB:O00264}.
Interaction partners:
- Sigma intracellular receptor 2
- Ferrochelatase, mitochondrial
- Membrane progestin receptor alpha
- Progesterone receptor
- Cytochrome b5
- SERPINE1 mRNA-binding protein 1
- Membrane progestin receptor beta
- Insulin-induced gene 1 protein
- Lanosterol 14-alpha demethylase
- Cytochrome b5 type B
Sequence:
MAAEDVVATGADPSELEGGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPGASGDNDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKEGEEPTVYSDDEEPKDETARKNE
Protein: Arginine decarboxylase 2 (ADC 2) (ARGDC 2) (AtADC2) (EC 4.1.1.19) (ADC-N) (O23141)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the biosynthesis of putrescine. Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine. Is a major contributor to basal arginine decarboxylase (ADC) activity and putrescine biosynthesis. Accumulation of putrescine plays a positive role in salt stress tolerance. Accumulation of putrescine plays a positive role in freezing tolerance. Production of PA is essential for normal seed development. Controls PA homeostasis which is crucial for normal plant growth and development.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:28109885, ECO:0000269|PubMed:28716421}. Cytoplasm, cytosol {ECO:0000269|PubMed:28109885}. Note=Localizes mainly in the chloroplast. {ECO:0000269|PubMed:28109885}.
Interaction partners:
- Agmatine deiminase
- Arginase 1, mitochondrial
- Arginase 2, chloroplastic/mitochondrial
- Spermine synthase
- Spermidine synthase 1
- Spermidine synthase 2
- Argininosuccinate lyase, chloroplastic
- Thermospermine synthase ACAULIS5
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 2
Sequence:
MPALACVDTSFVPPAYAFSDTAGDVFIPASSPTSAAVVVDRWSPSLSSSLYRIDGWGAPYFIANSSGNISVRPHGSETLPHQDIDLLKIVKKVTGPKSSGGLGLQLPLIVRFPDVLKNRLECLQSAFDYAIKSQGYDSHYQGVYPVKCNQDRFVVEDIVKFGSSFRFGLEAGSKPEILLAMSCLCKGSPDAFLVCNGFKDAEYISLALLGRKLALNTVIVLEQEEELDLVIELSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVRKLRQSGMLDCLQLLHFHIGSQIPSTSLLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSGESDLSVAYSLEEYAEAVVASVRVVCDRSSVKHPVICSESGRAIVSHHSVLIFEAVSADKPMVHQATPGDIQFLLEGNEEARANYEDLYAAVMRGDHESCLLYVDQLKQRCVEGFKEGVLSIEQLASVDGLCEWVLKAIGASDPVHTYNINLSVFTSIPDLWGIDQLFPIVPIHKLDQRPGARGILSDLTCDSDGKINKFIGGESSLPLHELDKNGSGGRYFLGMFLGGAYEEALGGVHNLFGGPSVVRVSQSDGPHSFAVTRAVPGQSSADVLRAMQHEPELMFQTLKHRAEEMMHTKGGSEGENEEEEEDDEFNNVAASLDRSFHNMPYLATEQASPSNSLSAAISNLGFYYCDEDVYDYISA
Protein: Profilin (P07274)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Protein BNI1
- Actin
- Cofilin
- BNI1-related protein 1
- Actin-related protein 2
- Actin-related protein 3
- Adenylyl cyclase-associated protein
- Bud site selection protein 6
- Twinfilin-1
- Actin-binding protein
Sequence:
MSWQAYTDNLIGTGKVDKAVIYSRAGDAVWATSGGLSLQPNEIGEIVQGFDNPAGLQSNGLHIQGQKFMLLRADDRSIYGRHDAEGVVCVRTKQTVIIAHYPPTVQAGEATKIVEQLADYLIGVQY
Protein: Meiosis protein mei2 (P08965)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Crucial for commitment to meiosis but it is not sufficient itself for the commitment. May be a splicing regulator.
Interaction partners:
- Transcription factor ste11
- RNA binding exosome specificity factor Mmi1
- Serine/threonine-protein kinase tor2
- Negative regulator of sexual conjugation and meiosis
- Polyadenylate-binding protein 2
- NURS complex subunit red1
- Poly
- UPF0400 protein C337.03
- Meiosis inducing protein mei3
- Rpb7-binding protein seb1
Sequence:
MIMETESPLSITSPSPSDSTFQVDMEKTMHALPSSLLDSPLLSTNEHYPPKSTLLLSGPSPIRNIQLSATKSSESNSIDYLTDTQNIFPNFVNNENNYQFSTAPLNPIDACRVGERKVFTTGNVLLSADRQPLSTWQQNISVLSESPPQNGIQSYISSSEQAAQALTRKPSVTGFRSSSLNSNSDDIDIFSHASRYLFVTNLPRIVPYATLLELFSKLGDVKGIDTSSLSTDGICIVAFFDIRQAIQAAKSLRSQRFFNDRLLYFQFCQRSSIQKMINQGATIQFLDDNEGQLLLNMQGGSVLSILQLQSILQTFGPLLIMKPLRSQNVSQIICEFYDTRDASFALDELDGRIIHNCCLQVAYYDAMADSVSTSSASSLSVPRGFSGMLNNNSEWNNSMTMSSNQETPTAASCAVSRIGSSYGMSNNFGSVPLGRTESSPAWGTSGYYDVSSTSPVAPSDRNPSRQYNSIRYGLDVNPIAPPNSSRLKQRNSDLLNGINPQWSPFSSNTGKVFDSPTGSLGMRRSLTVGANASCSNPTNLSFASLTLHDSKADSTLSASSLNPDLNLQRYTPTVEKHASDRNSVDYAQIASGIDTRTTVMIKNIPNKFTQQMLRDYIDVTNKGTYDFLYLRIDFVNKCNVGYAFINFIEPQSIITFGKARVGTQWNVFHSEKICDISYANIQGKDRLIEKFRNSCVMDENPAYRPKIFVSHGPNRGMEEPFPAPNNARRKLRSIASAQQIGLFPPTASKC
Protein: Kinesin-related protein 2 (Kinesin family member 2) (Kinesin-14) (Q9BPU3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-dependent motor that is probably involved in microtubule organization in the mitotic spindle.
Subcellular location: Nucleus {ECO:0000269|PubMed:10854856}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10854856}. Note=Localizes in the nucleus at the interphase and on the mitotic spindle during mitosis.
Interaction partners:
- Kinesin-related protein 13
- Microtubule-associated protein RP/EB family member 1
- Dynein heavy chain, cytoplasmic
- Kinesin-related protein 10
- Kinesin-related protein 11
- Kinesin-related protein 12
- Mitotic spindle assembly checkpoint protein MAD2A
- Kinesin-related protein 8
- Kinesin-related protein 3
- Kinesin-related protein 7
Sequence:
MEKRQLYSSQSQSQPLNIITNTINSRPSLLRKPASSSSQSNDRISYPPSTDSKFIQQQYHQPLLTNTDIKLEDIESSSSNNNPLKNSINNVSMQISQLNSSHHSRALLMQKRNNPTTNIRPTVKKKLDDTHKPLTSNFKKPITPISKLNTNMNNNNINNKNNNININSNNSSNSNNNILSPVQNNTISPNSNLLNSSIKFEKSNFFSTMYSSPTTITTTSTTLNNDNNNNISISSSCSNNSSFDLQQQHALHERMNKIDQFTQTVRGNLQSQFDNISEQLKPPRLSLSIQDIKTRLDFEEKNKEVEKIKLELKNVLQSLKEKEKELMEAHYKVSQVSVLKDNMERDLQQSNQMILDLQHEIRSSSLKAIQVDEKFNNMKDVTKDLDDEILRLNQLVRERDTEIESLRKENRELLEKSRSDEKVRRKLHNTIQELKGNIRVFCRIRPDFSSGQGANGSVFNIPAGTDNLVEVKSPTIDSFNGEASIKKSTFTFDRVFGPSSTQELVFEDISQLVQSSLDGYNTCIFTYGQTGSGKTHSILGDLKVPSQRGMIPRTVEKIFSSIQDLTEKGWTYQIECFFLEIYNETINDLLNTTTTTTGGNSKSNEIKYEIKHNPDTNVTTVTNMTVVPVTHPSQVYELLNLANKNRSVAKTLCNERSSRSHTVFQLKLIGYNQQSSERTQGLLNLIDLAGSERVSRSGVEGKQLKETQAINKSLSSLGDVISALANKEQHIPYRNSKLTFLLQNSIGGNSKTLMFVNISPELKDLQESTSSLRFAAKVNSCELGAARKQKII
Protein: Vitellogenin (Q9PSX4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MRAVVLALTLALVASQSVNFAPDFAASKTYVYKYEALLLGGLPEEGLARAGVKVISKVLISAVAENTYLLKLVNPEIFEYSGVWPKDPFVPAAKLTSALAAQFSIPIKFEYAKGVVGKVFAPTAVFETVLNVHRGILNILQLNIKKTQNVYELQEAGAQGVCKTHYVIREDAKAERIHLTKSKDLNNCQQRIMKDFGLAYTEKCVECRQRGEALMGAATYNYLMKPAANGALILEATVTELHQFTPFNEMSGAAQMEAKQMLTFVEIKKDPIVVPDNNYVHRGSIRYEFATEILQMPIQLLKISNARAQ
Protein: DNA replication ATP-dependent helicase/nuclease DNA2 (EC 3.6.4.12) (DNA replication ATP-dependent helicase-like homolog) (F8VR31)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEQLNELELLMEKSFWEEAELPAELFQKKVVASFPRTVLSTGMDNRYLVLAVNTVQNKEGNCEKRLVITASQSLENKELCILRNDWCSVPVEPGDIIHLEGDCTSDTWIIDKDFGYLILYPDMLISGTSIASSIRCMRRAVLSETFRSSDPATRQMLIGTVLHEVFQKAINNSFAPEKLQELAFQTIQEIRHLKEMYRLNLSQDEIKQEVEDYLPSFCKWAGDFMHKNTSTDFPQMQLSLPSDNSKDNSTCNIEVVKPMDIEESIWSPRFGLKGKIDVTVGVKIHRGYKTKYKIMPLELKTGKESNSIEHRSQVVLYTLLSQERRADPEAGLLLYLKTGQMYPVPANHLDKRELLKLRNQMAFSLFHRISKSATRQKTQLASLPQIIEEEKTCKYCSQIGNCALYSRAVEQQMDCSSVPIVMLPKIEEETQHLKQTHLEYFSLWCLMLTLESQSKDNKKNHQNIWLMPASEMEKSGSCIGNLIRMEHVKIVCDGQYLHNFQCKHGAIPVTNLMAGDRVIVSGEERSLFALSRGYVKEINMTTVTCLLDRNLSVLPESTLFRLDQEEKNCDIDTPLGNLSKLMENTFVSKKLRDLIIDFREPQFISYLSSVLPHDAKDTVACILKGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICTLVPAPEQVEKGGVSNVTEAKLIVFLTSIFVKAGCSPSDIGIIAPYRQQLKIINDLLARSIGMVEVNTVDKYQGRDKSIVLVSFVRSNKDGTVGELLKDWRRLNVAITRAKHKLILLGCVPSLNCYPPLEKLLNHLNSEKLISLIFHQENMKVFATYWVTFKENKTLFPLPFHTRAVSPLASAHTENSITIQNLMQYLCFKAQVYRKL