wanglab/gogpt-training-data huggingface dataset:
Protein: T1N15.19 (Zinc finger (Ran-binding) family protein) (Q9LP67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable LRR receptor-like serine/threonine-protein kinase RFK1
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Peroxidase 59
- Peroxidase 16
Sequence:
MSSSRIFLVGNSIFRPHKPSFPLSFNRFPSVSLRFRCFSSDAAAAVATTVDSDSPSLTPHPWPEWITFVDRLKTKGYFTKDTEDDTVYQEMILVKDACLSFARDRYDVLRSLSSGDVQALVERGCPNLFRKTVNSSKRIRAHVKLNEGDVCGSCDLRSSCDRAYVILKDTEADARTVDVMRLLLFNALDSIVISRGEVPPGKELVHESARRLLLELVEFSEKPLIPALPKPSSKESSLPSKERAFKSRNDEPSQRVAFKSRNDDPSQRVAFKSRNDEPSHRVAFKSRNDESSQRDRPLYSADWACPKCDFVNFARNERCRECNEVADRRPVAAVVKEGDWLCPECSFLNFTRNQSCLKCKAKGPKKTSMVNIVEMKKGDWNCTGCGYMNFASNKQCRECREQRHKTLAEPGDWECPSCDFVNFRRNDACKKCECKRPSQANNDQEDHTWKRPALV
Protein: Patronin (microtubule-binding protein) homolog (U4PAZ9)
Organism: Caenorhabditis elegans
Function: Required for microtubule stability and anchorage by binding to the minus ends of microtubules. Acts redundantly with noca-1 to control circumferential microtubule assembly along the body which is necessary for larval development, viability, morphology and integrity of the epidermis. Promotes microtubule stability and polymerization in neurons. Involved in the maintenance of neurite morphology in ALM and PLM neurons. May play a role in synaptic protein localization in the PLM neuron. May act upstream of dlk-1 in neuronal regeneration. Plays a role in postembryonic epidermal tissue integrity and wound healing.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:25437544}. Cell projection, dendrite {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:24569480, ECO:0000269|PubMed:25437544}. Cell membrane, sarcolemma {ECO:0000269|PubMed:24569477}. Cytoplasm, cytosol {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:27661253}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:27661253}. Perikaryon {ECO:0000269|PubMed:24569480}. Note=Localizes to puncta throughout the dendrites and axon of neurites, within the cytosol of muscle cells and at the sarcolemma (PubMed:24569477). Expressed in puncta along the dendrites of neurons and in the perikaryon (PubMed:24569480, PubMed:25437544). Localizes along microtubules (PubMed:27661253). {ECO:0000269|PubMed:24569477, ECO:0000269|PubMed:24569480, ECO:0000269|PubMed:25437544, ECO:0000269|PubMed:27661253}.
Interaction partners:
- Non-centrosomal microtubule array protein 1
- Kinesin-like protein
- Gamma-tubulin complex component
- Exchange factor for Arf-6
- Serine/threonine-protein kinase zyg-8
- Calponin homology domain-containing protein
- Tubulin gamma chain
- Spastin homolog
- Microtubule-associated protein
Sequence:
MDFPLPALLAIEDYDENEGKLAASIRWLISRVYEEKRDMPDKLRDGVQRDENGHFQIDEAVVGALCNGSLYAQAAAKIFKESALVTKGHGAVLAVLTDYGIDVLHDGNELVEEAQLVASAPFNMSAHLAIIDALMMAHLRDVIPVSRVVEAVSRHTAVEPSEKPIDSVDALLFWINKICLLVRDDVEREDSNTNIPEMEDLYEDISDGQCLCALLHWYRPHEMPVADISFNDSATTRDCQYNLMLLQLFCRHHLAVDPFHFEIEDLLYLRDSLQMNVNAFLADLFVQFEPPVTPEPVETPRIGPSPRRFVPASAIPDLRAANAAARSSMHNRNRPRMYNPPPAVSHSQGPSRSVSRMSQDSLFYSRPASIALQRRSMDQDSVTDFQTIRQGFENQAGTAQLNRYDGSVTASVRLAMEEKRRKHDQQMAQMSFSSANETERLEKSKAAFFALRKNDNDQTSKGKEEWYDHFEAKLRALELRVGLEEGEDGTQSARLNRASSQPSVVQAGQTYPANYMTLPMNAAAQMTQSYIQHPQTPHDYYMQQQMQQQQQQQAQAQSNYASPSQLRNSLSNGMINHAGYIVQSMYPGDYQQQQQQMQMQQGQMPVQPVGAYTPEGYFIPHHMQPIPVQQGYQQMPQPGMGFNGMPATSQPGFNMEGSPAQMGYIQTANKPLDMEMPMQQQPPQQPPQQMLPPNQNAFHLHSKSDDATQVQADPPLEINRNLTNWGMTYKQEMPARSIPSRRTWQNETFIKNELDLVNSKESVPHITDETTTQPEEAARRFPDLMLDNHSENLAPGRGFSRQNDRDDLSTGRKSDDSPTDTPGRTFDDDEGSGENMEKIANERRIAKKAALIAKTMKRKEEIETKVDLAEQRNAERRQVENEKKELALRKKVEKEQQRQKILDEYKRKKLEKELGAELSARSTGRGHSQPPFIRTKSQMSEVTESSRQNTPRMRGQSSVEQRVSVSSLAEPTHKLYAKTVTKSNRGLINNALQFSVFPGAVNNATRQATITQMASSSSKHFLILFRDQKCQYRGLYTWDEISDTAVKISGQGPPKCTEAMMNSMFKYDSGAKNFTNIATKHLSATIDGFAILDQYWQKARIPHSGTPAHKNN
Protein: Ribonuclease 3 (EC 3.1.26.3) (Ribonuclease III) (RNase III) (O67082)
Organism: Aquifex aeolicus (strain VF5)
Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Superoxide dismutase
- GTPase Era
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL19
- Small ribosomal subunit protein bS6
- Large ribosomal subunit protein bL32
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL27
Sequence:
MKMLEQLEKKLGYTFKDKSLLEKALTHVSYSKKEHYETLEFLGDALVNFFIVDLLVQYSPNKREGFLSPLKAYLISEEFFNLLAQKLELHKFIRIKRGKINETIIGDVFEALWAAVYIDSGRDANFTRELFYKLFKEDILSAIKEGRVKKDYKTILQEITQKRWKERPEYRLISVEGPHHKKKFIVEAKIKEYRTLGEGKSKKEAEQRAAEELIKLLEESE
Protein: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (EC 1.17.7.3) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase) (Protein GcpE) (Protein E) (P62620)
Organism: Escherichia coli (strain K12)
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using flavodoxin as the reducing agent.
Interaction partners:
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 1-deoxy-D-xylulose-5-phosphate synthase
- Cytoskeleton protein RodZ
- Farnesyl diphosphate synthase
- Isopentenyl-diphosphate Delta-isomerase
- Histidine--tRNA ligase
Sequence:
MHNQAPIQRRKSTRIYVGNVPIGDGAPIAVQSMTNTRTTDVEATVNQIKALERVGADIVRVSVPTMDAAEAFKLIKQQVNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGNEERIRMVVDCARDKNIPIRIGVNAGSLEKDLQEKYGEPTPQALLESAMRHVDHLDRLNFDQFKVSVKASDVFLAVESYRLLAKQIDQPLHLGITEAGGARSGAVKSAIGLGLLLSEGIGDTLRVSLAADPVEEIKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIGTVNALEQRLEDIITPMDVSIIGCVVNGPGEALVSTLGVTGGNKKSGLYEDGVRKDRLDNNDMIDQLEARIRAKASQLDEARRIDVQQVEK
Protein: PHD finger protein 1 (A0A0G2K557)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAQLPRLSRLGAPSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGSSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSKLLSALNSHKDRFISGREIKKRKCLFGLHARTPPPVELLTGDGSPTRSLVQGGWGKFSRICLEGTCTENGGLGCLGGGWGDKEASYSFPSGQGPGGGVSRPLGKRRKSEPEPLRRRQKGKVEELGPPTAAHSRHGSQEQRALQASESPPPPSPNQSYQGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSEPPDRSPLELHIGFPTDIPKSSPHSVTASSSSVPALTPGLSRHSLPPSPLCRSLSPGTGGGVRGGVSYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF
Protein: Conserved 13E12 repeat family protein (O33266)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1702cMb1728c
- Uncharacterized protein Rv1148c
- Uncharacterized protein Rv1128c
- Uncharacterized protein Rv1945
- Conserved 13E12 repeat family protein
- Uncharacterized protein Rv1588c
- HNH nuclease domain-containing protein
- Uncharacterized protein Rv3466
- HNH nuclease domain-containing protein
- Possible transposase
Sequence:
MPSPEAIAHFDERFECHAPRTTRVSAAFIDRICSATRAENRAAAAQLVALGELFAYRWSRCGGREEWVMDTMAAVAAEVAAALRISQGLAASRLRYARAMRERLPKTAEVFSAGDIGYLMFATIVYRTDLIVDPDVLAAVDAQLAANVARWPSMTKARLAGQVDKIVARADADAVRRRKEYQAQRQFWVGESQDGVCQIGGSLLAVDAHALDARLSALAGTVCEHDPRSREQRRADALGALAGGADRLGCGCGRADCAAGKRPAAPPVVIHLIAEAATINGTGSAPASQMNADGLITAELVAELAKTATLVPLVHPGDAPPEPGYAPSKALADFVRCRDLTCRWPGCDEPATNCDLDHTIPYAAGGPTHASNLKCYCRTHHLVKTFWGWRDQQLPDGTLILTSPSGHTYVSTPGSALLFPSLCHFSGGIPAPEADPPYDHCDQRTAMMPKRRRTRAQDRAYRIATERRQNHAARQRAQVLTQTAAATDTHGPPPDPNDDPPPF
Protein: Glypican-1 (H7C024)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004471}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004471}; Extracellular side {ECO:0000256|ARBA:ARBA00004471}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MEENLANRSHAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKVIQGCGNPKVNPQGPGPEEKRRRGKLAP
Protein: Glycine--tRNA ligase 1, mitochondrial (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Ap4A synthetase) (EC 2.7.7.-) (Glycyl-tRNA synthetase 1) (GlyRS 1) (GlyRS1) (P38088)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (By similarity).
Subcellular location: [Isoform Cytoplasmic]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix.
Interaction partners:
- U3 small nucleolar RNA-associated protein 8
- Alanine--tRNA ligase, mitochondrial
- Valine--tRNA ligase, mitochondrial
- Glycine--tRNA ligase 2
- Lysine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, mitochondrial
- Glutamate--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, cytoplasmic
Sequence:
MSFFNISRRFYSQIVKKSVKIKRMSVEDIKKARAAVPFNREQLESVLRGRFFYAPAFDLYGGVSGLYDYGPPGCAFQNNIIDAWRKHFILEEDMLEVDCTMLTPYEVLKTSGHVDKFSDWMCRDLKTGEIFRADHLVEEVLEARLKGDQEARGLVEDANAAAKDDAEKKKRKKKVKQIKAVKLDDDVVKEYEEILAKIDGYSGPELGELMEKYDIGNPVTGETLESPRAFNLMFETAIGPSGQLKGYLRPETAQGQFLNFNKLLEFNNSKTPFASASIGKSFRNEISPRAGLLRVREFLMAEIEHFVDPLDKSHPKFNEIKDIKLSFLPRDVQEAGSTEPIVKTVGEAVASRMVDNETLGYFIARIYQFLMKIGVDESKLRFRQHMANEMAHYAADCWDGELKTSYGWIECVGCADRSAYDLTVHSKKTKEKLVVRQKLDNPIEVTKWEIDLTKKLFGPKFRKDAPKVESHLLNMSQDDLASKAELLKANGKFTIKVDGVDGEVELDDKLVKIEQRTKVEHVREYVPSVIEPSFGIGRIIYSVFEHSFWNRPEDNARSVLSFPPLVAPTKVLLVPLSNHKDLVPVTTEVAKILRKSQIPFKIDDSGVSIGKRYARNDELGTPFGVTIDFESAKDHSVTLRERDSTKQVRGSVENVIKAIRDITYNGASWEEGTKDLTPFIAQAEAEAETD
Protein: F21F23.12 protein (PLC-like phosphodiesterases superfamily protein) (Q9LMX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Type I inositol polyphosphate 5-phosphatase 10
- Type I inositol polyphosphate 5-phosphatase 4
- Type I inositol polyphosphate 5-phosphatase 8
- Type IV inositol polyphosphate 5-phosphatase 3
- Type II inositol polyphosphate 5-phosphatase 14
- Type I inositol polyphosphate 5-phosphatase 12
- Type IV inositol polyphosphate 5-phosphatase 9
- Large ribosomal subunit protein uL23m
- Type II inositol polyphosphate 5-phosphatase 15
- Type I inositol polyphosphate 5-phosphatase 2
Sequence:
MASFKFFFAAIILVLFHPAAITFVASYGSLQLGDQCSSDEDCNVGLGCFKCGIDVARCVRSNITDQFSIVNNSMPFNKYAFLTTHNSYAIEGKALHVATQEDTIVQQLNSGVRALMLDTYDYEGDVWFCHSFDEQCFEFTKFNRAIDTFKEIFAFLTANPSEIVTLILEDYVKSQNGLTKVFTDSGLKKFWFPVQNMPIGGQDWPLVKDMVANNHRLIVFTSAKSKQETEGIAYQWNYMVENQYGDDGVKPDECSNRADSALLTDKTKALVSVNHFKTVPVKILTCEENSEQLLDMIKTCYVAAGNRWANFVAVNFYKRSNGGGTFQAIDKLNGELLCGRDDVHAC
Protein: aldehyde oxidase (EC 1.2.3.1) (Q9ESH4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMISRYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIRKGHGTQCGFCTPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEGKCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGERTTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNTKQGLTLGAGLSLTQVKNVLSDVVSRLPKEKTQIYCALLKQLKTLAGQQIRNVASLGGHIISRLPTSDLNPILGIGNCILNVASTEGIQQIPLNDHFLAGVPDAILKPEQVLISVFVPRSSKWEFVSAFRQAPRQQNAFATVNAGMKVVFKEDTNTITDLGILYGGIGATVISADKSCRQLIGRCWDEEMLDDAGKMICEEVSLLMAAPGGMEEYRKTLAISFLFMFYLDLLKQLKTRDPHRYPDISQKLLHILEDFPLTMPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFCDDMSVLPGELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGREEESLYAQDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIEPMIVTVQDALQYESFIGPERKLEQGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDIYVSSQDAAFTQEMVARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRPIRFILERRDDMLITGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLRVRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVRELNMYRTIDRTIHNQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGFPKTFYYQAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMSTVTVPNTVTTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFVQSITLSATGYFRGYQADMDWEKGRKVTFFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQIEGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYSSKGLGEAGTFLGCSVFFAIAAAVAAAREERGLSPIWAINSPATAEVIRMACEDQFTNLVPQTDSKCCKPWSIPVA
Protein: Stem-loop (Histone) binding protein (cDNA, FLJ96722, Homo sapiens stem-loop (histone) binding protein (SLBP), mRNA) (Q53XR2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MACRPRSPPRHQSRCDGDASPPSPARWSLGRKRRADGRRWRPEDAEEAEHRGAERRPESFTTPEGPKPRSRCSDWASAVEEDEMRTRVNKEMARYKRKLLINDFGRERKSSSGSSDSKESMSTVPADFETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPKTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIHPVDLESAESSSEPQTSSQDDFDVYSGTPTKVRHMDSQVEDEFDLEACLTEPLRDFSAMS
Protein: Peptide receptor GPCR (Q717R7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVTNMSQPHYCGTGIDDFHTNYKYFHGYFSLIVCILGTIANTLNIIVLTRREMRSPTNAILTGLAVADLAVMLEYIPYTVHDYILSARLPREEQLSYSWACFIKFHSVFPQVLHTISIWLTVTLAVWRYIAVSYPQRNRIWCGMRTTLITIATAYVVCVLVVSPWLYLVTAIAKFLETLDASGKTIASVPLSQYILDYNRQDEVTMQVMSSTTPDVSWPIPSDSANGTAVSLLSLTTVIPLTTLSTGVTTSSSLGERNVTVYKLYHSALALHDRQFRNATFLIYSVLIKLIPCFALTILSVRLIGALLEAKRRRKILACHAANDMQPIVNGKVVTPTQPKSCKLLEKEKQTDRTTRMLLAVLLLFLVTEFPQGIMGLLNVLLGDAFFLQCYLKLSDLMDILALINSSINFILYCSMSRQFRSTFALLFRPRWLDKWLPLSQHDGEGRVGGSGGLGGYGGYGRQRLLHTDAVSKSMAIDLGLTTQVTNV
Protein: V-type proton ATPase subunit a (B4DQF7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTFGVILGIFNHLHFRKKFNIYLVSIPELLFMLCIFGYLIFMIFYKWLVFSAETSRVAPSILIEFINMFLFPASKTSGLYTGQEYVQRVLLVVTALSVPVLFLGKPLFLLWLHNGRSCFGVNRSGYTLIRKDSEEEVSLLGSQDIEEGNHQVEDGCREMACEEFNFGEILMTQVIHSIEYCLGCISNTASYLRLWALSLAHAQLSDVLWAMLMRVGLRVDTTYGVLLLLPVIALFAVLTIFILLIMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFSLLSSKFNNDDSVA
Protein: Serine/threonine-protein kinase spe-6 (EC 2.7.11.1) (Defective spermatogenesis protein 6) (Q95PZ9)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which is involved in spermatogenesis. In spermatocytes, regulates meiosis and the localization and assembly of major sperm protein (MSP) into fibrous bodies. In addition, may suppress the initiation of spermiogenesis downstream of spe-8, spe-12, spe-27 and spe-29.
Interaction partners:
- Spermatocyte protein spe-8
- Spermatocyte protein spe-27
- Spermiogenesis protein SPE-29
- Serine protease inhibitor swm-1
- Integral membrane protein
- CX domain-containing protein
- SPE-12
- Transporter
- Trypsin-like protease try-5
- Major sperm protein
Sequence:
MSEQRDSRGMPQAGFIIEHQSSDHKWKVLRNIYSGPFSDVYVVADTVTNEKYAMKCERQEGNSRPVLKLDVMVLMATKGLRGFPNFVAAGRTDVYRYCIMQLVGPDLGRLRRTRPERKFSLPTALQILGQTLRRLEDLHNCGWLCRDVKAPNFCIGVGENESTVYILDFGFARKFVDKEGKIIPPRTAAALMGTFQYCAVSAHSHKDQCARDDLESWFYMGIELLKGPLPWANIDGHKNHKQIGEAKVAIRSEPLRSEFFEGVPKQFNEILTILDQTSYFDRPNYKKLGDLLSQAATEHQVTLKEPLDWQNNERMQQKAIFVGELGESHQASAKLDAKDNANESMDIEFDDMPPKEGISKSLSAEKSCTKNVETARTEK
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q965R3)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Serpentine receptor class r-10
- Innexin-19
- Clc-like protein
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Serpentine Receptor, class AB
- Homeobox-containing protein 1
- Seven TM Receptor
Sequence:
MSSTVAMINQICISTEIVVFNVLGLFGNINFLCLTYIKPALRSKSYYIQCALSVSHIFCLLFELPNAVLLFTGIQLRRNICFPAISLYIFFICAQAVIMLMLVVDLFIIVFFTTFYRRIENTTYTAMMLFIPFVYSAFTVAWGFVKMDDELVIFCNPPISLHPVVSRWWSMSNVALNSITLCLFLFLIITFHFRGKKQKSDTRKLMKRLKVSVVVFVFSWYMCTLGVDLFVAIGMTGSVLVFFQSNMVFFALLCYTQPFYVMLWRSSEYRIAFVEMWSFLGCVKSMKSKGWLEKTSKVTTAVSVMDSSKQ
Protein: Bifunctional protein Aas [Includes: 2-acylglycerophosphoethanolamine acyltransferase (EC 2.3.1.40) (2-acyl-GPE acyltransferase) (Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase); Acyl-[acyl-carrier-protein] synthetase (EC 6.2.1.20) (Acyl-ACP synthetase) (Long-chain-fatty-acid--[acyl-carrier-protein] ligase)] (P31119)
Organism: Escherichia coli (strain K12)
Function: Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Lysophospholipid transporter LplT
- Lysophospholipase L2
- Phosphatidylserine decarboxylase proenzyme
- Acyl carrier protein
- Phospholipase A1
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase
- Probable glycerol-3-phosphate acyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
Sequence:
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE
Protein: Peroxynitrite isomerase THAP4 (EC 5.99.-.-) (Ferric Homo sapiens nitrobindin) (Hs-Nb(III)) (THAP domain-containing protein 4) (Q8WY91)
Organism: Homo sapiens (Human)
Function: Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo, possibly modulating the transcriptional activity residing in the N-terminal region.
Subcellular location: Cytoplasm. Nucleus. Note=Localizes mainly in the cytoplasm and partially in the nucleus. {ECO:0000269|PubMed:32295384}.
Interaction partners:
- THAP domain-containing protein 11
- 52 kDa repressor of the inhibitor of the protein kinase
Sequence:
MVICCAAVNCSNRQGKGEKRAVSFHRFPLKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRLEDQHRLLKPTAVPSIFHLTEKKRGAGGHGRTRRKDASKATGGVRGHSSAATSRGAAGWSPSSSGNPMAKPESRRLKQAALQGEATPRAAQEAASQEQAQQALERTPGDGLATMVAGSQGKAEASATDAGDESATSSIEGGVTDKSGISMDDFTPPGSGACKFIGSLHSYSFSSKHTRERPSVPREPIDRKRLKKDVEPSCSGSSLGPDKGLAQSPPSSSLTATPQKPSQSPSAPPADVTPKPATEAVQSEHSDASPMSINEVILSASGACKLIDSLHSYCFSSRQNKSQVCCLREQVEKKNGELKSLRQRVSRSDSQVRKLQEKLDELRRVSVPYPSSLLSPSREPPKMNPVVEPLSWMLGTWLSDPPGAGTYPTLQPFQYLEEVHISHVGQPMLNFSFNSFHPDTRKPMHRECGFIRLKPDTNKVAFVSAQNTGVVEVEEGEVNGQELCIASHSIARISFAKEPHVEQITRKFRLNSEGKLEQTVSMATTTQPMTQHLHVTYKKVTP
Protein: Protein FAM153B (P0C7A2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGCAYSCCLEVCCGEDEIVYPRMPGESTVCHREREKPITYHWYHWHPGHIYPRVASMEDYDEDLVQEASSEDVLGVHMVDKDTERDIEMKRQLRRLRELHLYSTWKKYQEAMKTSLGVPQCERDEGSLGKPLCPPEILSETLPGSVKKRVCFPSEDHLEEFIAEHLPEASNQSLLTVAHADTGIQTNGDLEDLEEHGPGQTVSEEATEVHMMEGDPDTLAELLIRDVLQELSSYNGEEEDPEEVKTSLGVPQRGDLEDLEEHVPGQTVSEEATGVHMMQVDPATPAKSDLEDLEEHVPGQTVSEEATGVHMMQVDPATLAKQLEDSTITGSHQQMSASPSSAPAEEATEKTKVEEEVKTRKPKKKTRKPSKKSRWNVLKCWDIFNIF
Protein: Serpin A12 (OL-64) (Visceral adipose tissue-derived serine protease inhibitor) (Vaspin) (Visceral adipose-specific serpin) (Q8IW75)
Organism: Homo sapiens (Human)
Function: Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues.
Subcellular location: Secreted {ECO:0000305|PubMed:28668641}.
Interaction partners:
- Intelectin-1
- Filaggrin-2
- Retinoic acid receptor responder protein 2
- Endoplasmic reticulum chaperone BiP
- Nicotinamide phosphoribosyltransferase
- Resistin-like beta
- Resistin
- Adiponectin
- Apelin
- Leptin
Sequence:
MNPTLGLAIFLAVLLTVKGLLKPSFSPRNYKALSEVQGWKQRMAAKELARQNMDLGFKLLKKLAFYNPGRNIFLSPLSISTAFSMLCLGAQDSTLDEIKQGFNFRKMPEKDLHEGFHYIIHELTQKTQDLKLSIGNTLFIDQRLQPQRKFLEDAKNFYSAETILTNFQNLEMAQKQINDFISQKTHGKINNLIENIDPGTVMLLANYIFFRARWKHEFDPNVTKEEDFFLEKNSSVKVPMMFRSGIYQVGYDDKLSCTILEIPYQKNITAIFILPDEGKLKHLEKGLQVDTFSRWKTLLSRRVVDVSVPRLHMTGTFDLKKTLSYIGVSKIFEEHGDLTKIAPHRSLKVGEAVHKAELKMDERGTEGAAGTGAQTLPMETPLVVKIDKPYLLLIYSEKIPSVLFLGKIVNPIGK
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (Q7KTG6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
- Cell division cycle 50, isoform A
Sequence:
MPSANTEDLRRKFLVVQQQRSAPPNLTGDTLSSGIPNASASSATTSLMMTTSTGLGGVAMGAGEPERTYVFPGGNPVVGSAPGGGGQGIPGVAMAAPSRGHARSISHGGGAIVGANGRPIKSAMKGHQRAFSQGQITDSPPGSAAPAGRGHSRVGSKTDFILPPGHKEEPAREPSAPTSATGGRGHSRQASRSESIYTLRRTEAPPWWKRLTLCNYNTGDKFEERSYRTVVPNHTVPPKTPKRDHPNGQFVGNKIRTTKYTLLSFIPKNLLEQFHRVANLYFIFIVLLNWVPEISAFGKEVAMIPVLFVLGVTAVKDLFEDRRRRASDKRINNTTCRVYDGETERYKKVKWQELRVGDIVHLSNNETVPADILLLRTSDPQGVCYIDTCDLDGETNLKRREVVRGFEEMQSIFVPSKFVSRVEADAPTTKLYRFHGALIHPTGERVPISTECLLLRESRLKNTDYIEGIVVYAGHETKSMLNNSGPRYKRSQVEQQMNIDVIWCVIILLILCVVGAIGCRMWLSSFTHFPVPYLPPNKLTANMESMWIFWTYIVILQVMIPLSLYVTIELCKILQVFHIHNNVDLFDAETNKQTECRAMNITEELGQIQHIFTDKTGTLTENKMIFRRCVVNGSDYNHPPSELEKIYSKPGAPAPPLIPNDNLNSDMAQLTQGTYLTPHAQRIQEFLVVLAICNTVIVGAAPHRDMMNASGIIEVQQIGNSPANLKHGKQRQKLLASSTSTTTTTTIINGPTTQPQVVSIPADRYIRLAESRSVTPSPPPNLLFALPAQSHQPTLSPISSSAESSPNSESESPSPPMKNKSLSNSISPTGRAKAVINSKITSIATFLNAKTQGKRMKLPSSKTGTIYRTADGRPLYEAESPDELALVNAAYSYDCCLLNRSPNQILVSMPMAGATREYEILKVLPFDSSRKCMSIVVRQIGSQEIVLYTKGADSSIMPVLVPCSHNSPEGILREQTQQLLDRYAREGLRILVMAKRTLNSADYTDWWARHQEIEMSLENRERRLRDSFAKLESNLTLLGATGIEDRLQDGVPETIASLLSAGISVWVLTGDKPETAINIAYSAKLFTQQMELIRLTARSRDAAETAINFYLTDMENDKTTSTLGYGQSLRKKQRALVVDGKTLTFILDPKSKLILPFLRLSKRCASVLCCRSTPLQKAYLVKVVKEELNLRTLAIGDGANDVSMIQMADVGVGISGQEGMQAVMAADFTLPRFRYLERLLLAHGYWCYDRLSRMILYFFYKNAAFVFLIFWYQLYCGFSGQVMMDQMYLMLYNLIFTSLPPLAIGVYDKRVAEDLLLKNPYLYKNGRLGVAYRPHDFWLILLDALYQSLVIFFVALCAYAESDVGIWEFGTTITASCLFANLVHCAIEIRSWTVLHVLSIVLSLGSFYLFAIVYDSVCMNCFGVRSSYWVIFVCFASAVHWLVIMLSTVVAVLPRLLLTTVRISLCPDDSTKVILQSKRERSRGEALLVTWSRSTSASSIYRITDYGSKNQIITTIT