wanglab/gogpt-training-data huggingface dataset:
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (H0Y4R1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03156}.
Interaction partners:
Sequence:
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVAPKIPPDIKSHSPKCPSTVTGCYMLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Protein: RNA-splicing ligase RtcB homolog (EC 6.5.1.8) (3'-phosphate/5'-hydroxy nucleic acid ligase) (P90838)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs. Required for the ligation of mRNAs and specifically, regulates xbp-1 mRNA splicing during the endoplasmic reticulum stress-induced unfolded protein response. Has a neuroprotective role in the age-dependent degeneration of dopamine neurons, which is mediated by xbp-1.
Subcellular location: Nucleus {ECO:0000269|PubMed:25366321}. Cytoplasm {ECO:0000269|PubMed:25366321}.
Interaction partners:
- Probable RNA 3'-terminal phosphate cyclase-like protein
- Uncharacterized protein E02H1.5
- Protein archease-like
- ATP-dependent RNA helicase DDX1
- Schlafen-like protein 2
- BZIP domain-containing protein.
- ZP domain-containing protein
- Large ribosomal subunit protein mL62
- Eukaryotic translation initiation factor 2 subunit 1
- Spectrin beta chain
Sequence:
MPRTFEEECDFIDRLTDTKFRIKKGFVPNMNVEGRFYVNNSLEQLMFDELKFSCDGQGIGGFLPAVRQIANVASLPGIVGHSIGLPDIHSGYGFSIGNIAAFDVGNPESVISPGGVGFDINCGVRLLRTNLFEENVKPLKEQLTQSLFDHIPVGVGSRGAIPMLASDLVECLEMGMDWTLREGYSWAEDKEHCEEYGRMLQADASKVSLRAKKRGLPQLGTLGAGNHYAEVQVVDEIYDKHAASTMGIDEEGQVVVMLHCGSRGLGHQVATDSLVEMEKAMARDGIVVNDKQLACARINSVEGKNYFSGMAAAANFAWVNRSCITFCVRNAFQKTFGMSADDMDMQVIYDVSHNVAKMEEHMVDGRPRQLCVHRKGATRAFPAHHPLIPVDYQLIGQPVLIGGSMGTCSYVLTGTEQGLVETFGTTCHGAGRALSRAKSRRTITWDSVIDDLKKKEISIRIASPKLIMEEAPESYKNVTDVVDTCDAAGISKKAVKLRPIAVIKG
Protein: 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase) (G3XCW9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Beta-hexosaminidase
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
- AmpG
- Beta-lactamase
- HTH-type transcriptional activator AmpR
- Anhydro-N-acetylmuramic acid kinase
- AmpE protein
- Porin D
- Multidrug resistance operon repressor
- Peptidoglycan D,D-transpeptidase FtsI
Sequence:
MHFDSVTGWVRGVRHCPSPNFNLRPQGDAVSLLVIHNISLPPGQFGTGKVQAFFQNRLDPNEHPYFEEIRHLTVSAHFLIERDGAITQFVSCHDRAWHAGVSCFDGREACNDFSLGIELEGTDTEPYTDAQYTALAGLTRLLRAAFPGITPERIQGHCDIAPERKTDPGEAFDWSRYRAGLTDSKEET
Protein: Apoptosis regulator BHRF1 (Early antigen protein R) (EA-R) (Nuclear antigen) (P03182)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Prevents premature death of the host cell during virus production, which would otherwise reduce the amount of progeny virus. Acts as a host B-cell leukemia/lymphoma 2 (Bcl-2) homolog, and interacts with pro-apoptotic proteins to prevent mitochondria permeabilization, release of cytochrome c and subsequent apoptosis of the host cell.
Subcellular location: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host mitochondrion {ECO:0000269|PubMed:11836425, ECO:0000269|PubMed:9367386}. Note=also observed in the perinuclear region of the cell.
Interaction partners:
Sequence:
MAYSTREILLALCIRDSRVHGNGTLHPVLELAARETPLRLSPEDTVVLRYHVLLEEIIERNSETFTETWNRFITHTEHVDLDFNSVFLEIFHRGDPSLGRALAWMAWCMHACRTLCCNQSTPYYVVDLSVRGMLEASEGLDGWIHQQGGWSTLIEDNIPGSRRFSWTLFLAGLTLSLLVICSYLFISRGRH
Protein: Homeobox protein Nkx-2.6 (Homeobox protein NK-2 homolog F) (A6NCS4)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator. In conjunction with NKX2-5, may play a role in both pharyngeal and cardiac embryonic development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cryptic protein
Sequence:
MLLSPVTSTPFSVKDILRLERERSCPAASPHPRVRKSPENFQYLRMDAEPRGSEVHNAGGGGGDRKLDGSEPPGGPCEAVLEMDAERMGEPQPGLNAASPLGGGTRVPERGVGNSGDSVRGGRSEQPKARQRRKPRVLFSQAQVLALERRFKQQRYLSAPEREHLASALQLTSTQVKIWFQNRRYKCKRQRQDKSLELAGHPLTPRRVAVPVLVRDGKPCLGPGPGAPAFPSPYSAAVSPYSCYGGYSGAPYGAGYGTCYAGAPSGPAPHTPLASAGFGHGGQNATPQGHLAATLQGVRAW
Protein: Ribosome-recycling factor (RRF) (Ribosome-releasing factor) (P0A805)
Organism: Escherichia coli (strain K12)
Function: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein uS2
- Elongation factor G
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL20
- Elongation factor Ts
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL19
- Uridylate kinase
Sequence:
MISDIRKDAEVRMDKCVEAFKTQISKIRTGRASPSLLDGIVVEYYGTPTPLRQLASVTVEDSRTLKINVFDRSMSPAVEKAIMASDLGLNPNSAGSDIRVPLPPLTEERRKDLTKIVRGEAEQARVAVRNVRRDANDKVKALLKDKEISEDDDRRSQDDVQKLTDAAIKKIEAALADKEAELMQF
Protein: Transcription factor SOX-30 (O94993)
Organism: Homo sapiens (Human)
Function: Acts as both a transcriptional activator and repressor. Binds to the DNA sequence 5'-ACAAT-3' and shows a preference for guanine residues surrounding this core motif. Binds to its own promoter and activates its own transcription (By similarity). Required to activate the expression of postmeiotic genes involved in spermiogenesis (By similarity). Binds to the promoter region of CTNNB1 and represses its transcription which leads to inhibition of Wnt signaling. Also inhibits Wnt signaling by binding to the CTNNB1 protein, preventing interaction of CTNNB1 with TCF7L2/TCF4.
Subcellular location: Nucleus {ECO:0000269|PubMed:10359848, ECO:0000269|PubMed:29739711}. Cytoplasm {ECO:0000269|PubMed:29739711}. Note=Enriched at the chromocenter. {ECO:0000250|UniProtKB:Q8CGW4}.
Interaction partners:
Sequence:
MERARPEPPPQPRPLRPAPPPLPVEGTSFWAAAMEPPPSSPTLSAAASATLASSCGEAVASGLQPAVRRLLQVKPEQVLLLPQPQAQNEEAAASSAQARLLQFRPDLRLLQPPTASDGATSRPELHPVQPLALHVKAKKQKLGPSLDQSVGPRGAVETGPRASRVVKLEGPGPALGYFRGDEKGKLEAEEVMRDSMQGGAGKSPAAIREGVIKTEEPERLLEDCRLGAEPASNGLVHGSAEVILAPTSGAFGPHQQDLRIPLTLHTVPPGARIQFQGAPPSELIRLTKVPLTPVPTKMQSLLEPSVKIETKDVPLTVLPSDAGIPDTPFSKDRNGHVKRPMNAFMVWARIHRPALAKANPAANNAEISVQLGLEWNKLSEEQKKPYYDEAQKIKEKHREEFPGWVYQPRPGKRKRFPLSVSNVFSGTTQNIISTNPTTVYPYRSPTYSVVIPSLQNPITHPVGETSPAIQLPTPAVQSPSPVTLFQPSVSSAAQVAVQDPSLPVYPALPPQRFTGPSQTDTHQLHSEATHTVKQPTPVSLESANRISSSASTAHARFATSTIQPPREYSSVSPCPRSAPIPQASPIPHPHVYQPPPLGHPATLFGTPPRFSFHHPYFLPGPHYFPSSTCPYSRPPFGYGNFPSSMPECLSYYEDRYPKHEGIFSTLNRDYSFRDYSSECTHSENSRSCENMNGTSYYNSHSHSGEENLNPVPQLDIGTLENVFTAPTSTPSSIQQVNVTDSDEEEEEKVLRDL
Protein: Essential MCU regulator, mitochondrial (Q7JX57)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential regulatory subunit of the mitochondrial calcium uniporter MCU channel, a protein that mediates calcium uptake into mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9H4I9}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H4I9}.
Interaction partners:
- Calcium uptake protein 1 homolog, mitochondrial
- Calcium uniporter protein, mitochondrial
- Mitochondrial calcium uptake 3, isoform D
- Uncharacterized protein, isoform A
- AFG3 like matrix AAA peptidase subunit 2, isoform A
- Mitochondrial proton/calcium exchanger protein
- Paraplegin, isoform A
Sequence:
MIVPRLALPISLALQRVSRRVAEHPHNLRILQRHMSSVYFRSGAIKPKPEEMPFGLLAIFCAVIPGLFVGATISKNVANFLEENDLFVPADDDDDED
Protein: Myosin-4 (Myosin heavy chain B) (MHC B) (Uncoordinated protein 54) (P02566)
Organism: Caenorhabditis elegans
Function: Required for muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin regulatory light chain 1
- Myosin, essential light chain
- Myosin regulatory light chain 2
- Myosin-3
- Tropomyosin isoforms a/b/d/f
- Troponin I 2
- UNC-45
- Protein unc-119
- Troponin T
- Cuticle collagen rol-6
Sequence:
MEHEKDPGWQYLRRTREQVLEDQSKPYDSKKNVWIPDPEEGYLAGEITATKGDQVTIVTARGNEVTLKKELVQEMNPPKFEKTEDMSNLSFLNDASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGNDLLVEIWQDYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGSLSEEMFRIGLTKVFFKAGVLAHLEDIRDEKLATILTGFQSQIRWHLGLKDRKRRMEQRAGLLIVQRNVRSWCTLRTWEWFKLYGKVKPMLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRASASVAPGLQSSASAAVIRSPSRARASDF
Protein: Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase (EC 2.4.1.256) (Alpha-1,2-glucosyltransferase ALG10-A) (Alpha-2-glucosyltransferase ALG10-B) (Asparagine-linked glycosylation protein 10 homolog B) (Potassium channel regulator 1) (O88788)
Organism: Rattus norvegicus (Rat)
Function: Putative alpha-1,2-glucosyltransferase, which adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity). When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2. Has a role in maintenance of cochlear outer hair cell function (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9722534}; Multi-pass membrane protein {ECO:0000255}. Note=Also detected at the plasma membrane. {ECO:0000269|PubMed:14525949}.
Interaction partners:
- Alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Serine/threonine-protein kinase Chk1.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Tumor suppressor candidate 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Mannosyltransferase
- Mannosyltransferase
Sequence:
MAQLEGYYFSAALSCTFLVSCLLFSAFSRALREPYMDEIFHLPQAQRYCEGRFSLSQWDPMITTLPGLYLVSVGVVKPASWILGWSEHVVCSIGMLRFVNLLFSVGNFYLLYLLFRKIQPRNKASSSIQRILSTLTLAVFPTLYFFNFLYYTEAGSVFFTLFAYLMCLYGNHRTSALLGFCGFMFRQTNIIWAAFCAGHIIAQKCSEAWKTELQKKKEERLPPAKGPLSELRRVLQFLLMYSMSLKNLSMLFLLTWPYMLLLLAFFVFVVVNGGIVVGDRSSHEACLHFPQLFYFFSFTAFFSFPHLLSPTKVKTFLSLVWKRRVQFSVITLVSVFLVWKFTYVHKYLLADNRHYTFYVWKRVFQRHEIVKYLLVPAYMFAGWAVADSLKSKSIFWNLMFFVCLVASTVPQKLLEFRYFILPYIIYRLNMPLPPISRLVCELGCYAVVNFLTFYIFLNKTFQWSDSHDIQRFMW
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (F8VVE9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATSVCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSL
Protein: Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (Pp4) (EC 3.1.3.16) (Protein phosphatase X) (PP-X) (P97470)
Organism: Mus musculus (Mouse)
Function: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on Ser-140 (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair (By similarity). Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin (By similarity).
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 3A
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Serine/threonine-protein phosphatase 4 regulatory subunit 3B
- Serine/threonine-protein phosphatase 4 regulatory subunit 4
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Immunoglobulin-binding protein 1
Sequence:
MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL
Protein: E3 ubiquitin-protein ligase TRIM48 (EC 2.3.2.27) (RING finger protein 101) (Tripartite motif-containing protein 48) (Q8IWZ4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which promotes K48-linked polyubiquitination of protein methyltransferase PRMT1, leading to PRMT1 degradation. This suppresses methylation of the PRMT1 substrate MAP3K5/ASK1, promoting its activation and increasing MAP3K5-dependent cell death induced by oxidative stress. TRIM48-mediated ubiquitination of PRMT1 also suppresses methylation of FOXO1 by PRMT1, leading to inhibition of FOXO1 transcriptional activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29186683}.
Interaction partners:
Sequence:
MSRRIIVGTLQRTQRNMNSGISQVFQRELTCPICMNYFIDPVTIDCGHSFCRPCFYLNWQDIPILTQCFECIKTIQQRNLKTNIRLKKMASLARKASLWLFLSSEEQMCGIHRETKKMFCEVDRSLLCLLCSSSQEHRYHRHCPAEWAAEEHWEKLLKKMQSLWEKACENQRNLNVETTRISHWKAFGDILYRSESVLLHMPQPLNLALRAGPITGLRDRLNQF
Protein: Lipid storage droplets surface-binding protein 2 (Lsd2) (Q9VXY7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for embryogenesis. Required for normal deposition of neutral lipids in the oocyte.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12077142, ECO:0000269|PubMed:12676093, ECO:0000269|PubMed:14550535}. Lipid droplet {ECO:0000269|PubMed:12077142, ECO:0000269|PubMed:12676093, ECO:0000269|PubMed:14550535}. Note=Cytoplasm and on surface of neutral lipid storage droplets in oocytes. Colocalizes with Lsd-1 to the droplet surface in cells of fat bodies. {ECO:0000269|PubMed:14550535}.
Interaction partners:
- triacylglycerol lipase
- Hormone-sensitive lipase, isoform A
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
Sequence:
MASAEQKHATGNGTTGNGTAMNDVDQPKDAKDLLPHLESLERIIKLPVVNAAWDKSQDVYGKVKGKNRVFEWALTAAEDCVTRAVTTAAPFVTKLDRPIAYVDQTLVKGIDKLEVKAPIIKDTPQEIYNQAKSKVIDVVQPHLERVVKFKAAGQQKAASLKDLAWQKANEVLATQYGSLAVNGVDTTTALAERLLEYYFPKCESDVEEDNDDKQNAVVQNGKSSENDMPVPASEDPVLHTVQTVGRLSNKISRRVYRNVSRQIKQVQKGNINDYLSSLIAALKLHQYINFINSSMGTNVEQSGGSSSDACSPFGTTTSTTTTTTTSSTSNNKPVVALPHVAKSKRAPAVSSQ
Protein: Rho-GAP domain-containing protein (Q58AA5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MCIDELENALSVARLNLPSPIRDHDKSFSTQSNRPETPPAQPLPTQQFGVPLEFILSHCGGNIPPIVDQLIEYLEAHALTMEGVFRKSANIGSIKRLQDRINKGEKIDFENDPEYKDNEYVASLHASVLLKTFFRSLGEPLTTNRLYPKLAALSEVSKTEKSAAVKEFVKLLPRENYILLKTVIKFLTRVAENSKVNLMTANNLSVVFGPNLTWPTDQEVPISQLNNLNNFCYKLIVDYDSVFDH
Protein: Prospore formation at selected spindle poles protein 1 (Accumulates dyads protein 1) (P38872)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required to localize MPC54 to all four spindle pole bodies, and localize DON1 and SPO14 to four prospore membranes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11553705}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:11553705}. Note=Nuclear in mononucleate meiotic cells. May not be localized to the spindle pole body or prospore membrane.
Interaction partners:
- Casein kinase I homolog HRR25
- Probable 26S proteasome regulatory subunit p27
- Sporulation-specific protein 74
- Meiotic plaque component protein 54
- Sporulation-specific protein 21
- Meiosis-specific protein SPO13
Sequence:
MNQGYTQLSAPELKETKTSKLNKMNNFRSSPIAEIINKIPPDCGKIQNTTFPEFNPALRRRQHEQWPAYEKPIRVTDSMSPQLSSINCLPNLYPHGTLPLPNPYLSYLNHIEKVNCQDVKFSNWSVLHNSNNGFEIPTYFSPRTTQNMPCSEKVESWLERLPIFVGFDGYLFTNCFDYEYMLDWEETEFTFEKTSCMETDYSKALTDTDIIYIQEKKIEALIRNQYLKEYEFSQKDF
Protein: Interleukin-32 (IL-32) (Natural killer cells protein 4) (Tumor necrosis factor alpha-inducing factor) (P24001)
Organism: Homo sapiens (Human)
Function: Cytokine that may play a role in innate and adaptive immune responses. It induces various cytokines such as TNFA/TNF-alpha and IL8. It activates typical cytokine signal pathways of NF-kappa-B and p38 MAPK.
Subcellular location: Secreted {ECO:0000269|PubMed:15664165}.
Interaction partners:
- Myeloblastin
- Integrin beta-3
- Hepatocyte growth factor receptor
- Protein kinase C delta type
- Interleukin-18 receptor accessory protein
- C-C motif chemokine 5
- Interleukin-8
- Tumor necrosis factor
- Interleukin-18
- Hepatocyte growth factor
Sequence:
MCFPKVLSDDMKKLKARMVMLLPTSAQGLGAWVSACDTEDTVGHLGPWRDKDPALWCQLCLSSQHQAIERFYDKMQNAESGRGQVMSSLAELEDDFKEGYLETVAAYYEEQHPELTPLLEKERDGLRCRGNRSPVPDVEDPATEEPGESFCDKVMRWFQAMLQRLQTWWHGVLAWVKEKVVALVHAVQALWKQFQSFCCSLSELFMSSFQSYGAPRGDKEELTPQKCSEPQSSK
Protein: PTS system lactose-specific EIIA component (EIIA-Lac) (EIII-Lac) (Lactose-specific phosphotransferase enzyme IIA component) (A0A0H2UNP1)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKSKEEINMLGFTIVAYAGDARSDLMDALAFARDGYFEQARELVESANDSIVSAHREQTNLLAEEAYGDNFEVSFIMIHGQDTLMTTMLLYDQVKFFIDEYERIRKIEEHIGLQ
Protein: Carbamoyl phosphate synthase large chain (EC 6.3.4.16) (EC 6.3.5.5) (Carbamoyl phosphate synthetase ammonia chain) (Q72FQ1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase small chain
- Amidophosphoribosyltransferase
- Dihydroorotase
- Argininosuccinate synthase
- Phosphoribosylformylglycinamidine synthase I
- Ornithine carbamoyltransferase
- GMP synthase
- Uracil permease
- Dihydroorotate dehydrogenase
Sequence:
MPKRTDLKRIMVIGSGPIIIGQACEFDYSGTQAVKALKEEGYEVVLVNSNPATIMTDPGLADRTYIEPIEPETVAAIIRKERPDALLPTLGGQTGLNTALALAASGVLDECGVELIGANRAVIEKAESRELFRLAMANIGLKVPASGIARSMDDVRRLGTEMPFPLIIRPAFTMGGTGGGIAYNMEDLEEIASRGLTASITSEVMIEQSVLGWKEYEMEVMRDKADNCVIICSIENFDPMGVHTGDSITVAPAQTLTDVEYQMMRDASIAIMREIGVETGGSNVQFGINPDNGDMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDITRETMASFEPTIDYVVTKIPRFTFEKFPGARDELTTAMKSVGEAMSIGRTFKESLQKGLRSLEVGAPGLGSRFRDKLPEHEEIVAKLRTPNSRRIFYVRLAMLSGMTIDDIHEITNIDPWFLRQMRELVDMEGDLRDFALANSMTPDNGELVTLLRRAKEYGFSDRQLAEMWKRPESDVRALRDATGIRPTYYLVDTCASEFEAYTPYYYSTYETGHEIEAESRRKVIILGGGPNRIGQGIEFDYCCCHASFALKEMGVQAIMVNSNPETVSTDYDTSDRLYFEPLTFEDVMHIIEAEKPDGVIVQFGGQTPLNLAVPLQRAGVPILGTSPDAIDRAEDRERFQALIHKLDLRQPANATVMNLRQAIAGANSIGYPVVVRPSYVLGGRAMEIVYDEEQLTSYFQNSVGEAPEHPILLDKFLENATEVDVDALSDGTDVYVAGIMEHIEEAGIHSGDSACSIPPYSLPSSITDEISRQTVALAKELRVVGLMNIQFAVKDGVIFILEVNPRASRTAPFVSKATAVPLPRLATQVMLGKTLKELDPWSMRRSGYVSVKESVFPFNRFPGVDILLGPEMRSTGEVMGIAPTFEEAYLKGQLAGGQRLPQQGKVFISVNDRDKTLVPDVARIFADLGFEIVATAGTAKLLKEHGVPTTHVNKVYEGRPNIVDMIKNGDIALVVNTASGKRTVQDSKSIRQATLMYGVPYSTTVSGARAIAKSIAASRTCGVNVKSLQEYYGL
Protein: Cytochrome c biogenesis B (Q8HCM3)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cytochrome c biogenesis Fc
- Putative cytochrome c biosynthesis ccmC-like mitochondrial protein
- Cytochrome c biogenesis Fn
- Maturase-related protein
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase chain 3
- ATP synthase subunit a
- NADH-ubiquinone oxidoreductase chain 6
- NADH-ubiquinone oxidoreductase chain 4L
Sequence:
MRRLFLEQFYKQIFSSTPITSFFLFLLYIVVTPLMIGFEKDFLCYFHLGLIWIPLLFSFLSEPFFRNDKEFGTLELYYLSAYCLPKILLLQLVGHWVIQISCVFCAFPMLQLLYQFDRSGMDWLNILLGSLVLTLLCGIHSGLALGITSSSGWNSLQNLTTLPTLLPLTVFCTSIETEGFHVLLLIGYFFLFVSLYPILVSISLQD
Protein: Uncharacterized protein C409.16c (Q9UUA8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C1322.02
- Mating-type switching protein swi10
Sequence:
MCSVEKIVRLRHNLLCHVRIHFKTKEDLDIRAFLFSLQRELHAVAFLNQGSIRTLYEKRVVDITSESVQSHAIIETARNFALPNTAEEEENMDRKPELQLSFKGSMTSKIIHIYVQPFDS
Protein: Uncharacterized protein (Q57ZN8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MESYKDVILSQPPAMYQRLPQPSNVAVENYKGILLCACPVNIPNGASMELRGNNATAPTGPVFVPAGGSNTPLGLGPSAEERATMERNHRQRVENLKSQRANVCAVVSQHKRWLRSFAKQMRQMKEEEVVREVERARRVDQMRRKWAQKASEATAQEQQERGAALDADRGGQGGQQQQQQQQRLSEGAMGNVPSAPEAKEKKKVGKKKKKPKWALTEDEALEDEIAEADDLLEFAKNLDYDKFISDYEVAGALAIMRDRVEELTRENNWTKESVERAAKENADDEDEHECDYEGEAEKKGAYDAEARGQRRKELQQQLSSTAVARKAAPAQVAAHDKEWSNSTSIAGALRRAIMRDALQLAERILASSESMQRIHTKFSLARILQYCAVCGEDPREAMQKPSIGGKKGLEKEPQIVKLHPDATGLETETSDGQGGQRRVLLDLQRSKERTQGLPYLYRCPAI