wanglab/gogpt-training-data huggingface dataset:
Protein: Adenosine 5'-monophosphoramidase HINT2 (EC 3.9.1.-) (HINT-3) (Histidine triad nucleotide-binding protein 2, mitochondrial) (HINT-2) (Q9D0S9)
Organism: Mus musculus (Mouse)
Function: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (By similarity). Hydrolyzes adenosine 5'-O-p-nitrophenylphosphoramidate (AMP-pNA) (By similarity). May be involved in steroid biosynthesis (By similarity). May play a role in apoptosis (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BX68}.
Interaction partners:
Sequence:
MAAAVLLAVGLRAARRTLAAAGARGAQVRGNAGVSDGSEVAKAQKAAPGGASPTIFSRILDRSLPADILYEDQQCLVFRDVAPQAPVHFLVIPRKPIPRISQAEEDDQQLLGHLLLVAKKIAQAQGLKDGYRLVVNDGKMGAQSVYHLHIHVLGGRQLQWPPG
Protein: Sodium/hydrogen exchanger (M9PB53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MLLIVGFALCVLAPGCSATDTDIALDAKATLNHRIQSLDLLVFVFLLALTVLTIWLFKHHRVSWLHETGLAVIYGLIVGAIIRYAGTSATLVHMQVEPQGVPTYSDKLPPDTLWFRYPVNQTNGTKPPEGIKTYAYVFRGQVHDVDENEIDLKATFDPEVFFNIILPPIIFYAGYSLKKKYFFRNLGAILTFAIVGTTLSAFLIGGFMYGCVKLMPKYLSSSFTFLDSLYFGALISPTDPLTILAIFNDLRVDVNLYALVLGESVLNDAVAIVLSGAIQNYGEHYSNTGEFETTAFLRSLSDFFSIFLLSLMIGAAMGCLTALMTKFTRVRDFPLLESALFVLMSYSTFLLAEATELTGVVAVLFCGICQAHYTYNNLSEDSRQRTKQIFELLNFLAENFIFSYIGVSMFTFPKHHFDAGFIITAFICAAIGRAVNVYPLSWLLNIKRKPKISTNFQHMLFFAGLRGAMSFALAIRNTVSDERQTMLTATSLIVIFTVVIQGGAANFLLNWLKIPVGVDDETEQLNNYQVHSSDGYLQDVEGGGVNRNKMRLSGGTDTNLDTPVDGTNGSLGGASGGRRRNSHEKAILARIWGNFDTKYMKPLLTHSRPTLLETLPVCCNPIARLLTTTQQLTQDGSEFRRVDSDSDICIDNDTGNGLSQDGSGAAPGVGRRNSLSRTETQT
Protein: Nucleoside transporter 2 (Q8IB78)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSNSNSKEHYRMDGITENKIINEDDESLLNMKKEEIILNGKFEEEPKLDLTENKIDIEEKNNNMSEFTNIFPNITLCLMGMSSVLMYNCVLNTTPHIHALLNKNIVVSSTFFLYFSILVIVSLLSSLFIEVKTRTYDVCFILSFILQMIYPFIIKYFYDKTVFFYVLVALIGATCSMMKTMIFSISSIVVNDSKVICLSYGLTGIYSLFITSTFFYFVIKINKDIQKLMLSLFITSAINCIFILVSFLCYTVLKRTNNFKEKFKIYTEERKNNKNSRDDSYKYYESITEKKSQNISYPININSIIYESKTENTESKYSLTKNDSNSVGIKSSSNNTNNMTSNEIGDHKILQESHSKNKKFNDILLNENKTLSLTHSKKEDNIDDENKNHKNQFFLFNINKKNLIKQAKIKAFLYKKSFIFLFCSFYNIFLKILLFPVVCPEMWTNNVDERYILIGIVQFADCISRVFPSLAGTFPVFKIFLLTQKKVLIYSLLRTILSVIGLIIPLTQDTFINNFLFKCALIFLNIYLNGWFVIMSFINVPEILKPINSMSNVAIVSSFGSTLLRVGLLTGYGCSTLYKYIISKM
Protein: Protein SNORC (Secondary ossification center-associated regulator of chondrocyte maturation protein) (Q9CXL7)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of chondrocyte maturation and postnatal endochondral ossification. May inhibit cell growth stimulation induced by FGF2.
Subcellular location: Membrane {ECO:0000305|PubMed:28323137}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:21624478}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:21624478, ECO:0000269|PubMed:28323137}. Note=Appears as reticular-like structures throughout the cytoplasm and adjacent to the plasma membrane (PubMed:21624478). In proliferation and hypertrophic chondrocytes, detected intracellulary and in the pericellular extracellular matrix. In primary spongiosa, detected only in the extracellular matrix (PubMed:28323137). {ECO:0000269|PubMed:21624478, ECO:0000269|PubMed:28323137}.
Interaction partners:
Sequence:
MASCLALRVALLLISGVLAPAVLTAEGPQEPDPTLWNEPIELPSGEGPLESTSHNQEFAVSGPPFPTSAPAPEDSTPPARVDQDGGSLGPGAIAAIVIAALLATCVVLALVVVALRKFSAS
Protein: S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase) (P0A817)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. Is essential for growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Methionine synthase
- S-adenosylmethionine decarboxylase proenzyme
- 5,10-methylenetetrahydrofolate reductase
- Homocysteine S-methyltransferase
- Met repressor
- DNA-cytosine methyltransferase
- Aromatic-amino-acid aminotransferase
- Free methionine-R-sulfoxide reductase
- Cystathionine gamma-synthase
Sequence:
MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHFGREHFPWEKTDKAQLLRDAAGLK
Protein: methionine--tRNA ligase (EC 6.1.1.10) (Q8I716)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Methionyl-tRNA formyltransferase, putative
- methionine--tRNA ligase
- leucine--tRNA ligase
- leucine--tRNA ligase
- glutamine--tRNA ligase
- glutamate--tRNA ligase
- glutamate--tRNA ligase
- isoleucine--tRNA ligase
- Isoleucine--tRNA ligase, putative
- arginine--tRNA ligase
Sequence:
MKIYFIFILFLYLNFFILIIEILSKDIIKTRRSFPSYIKDGEKRKSNKIKRKRIKNDAYINVYRKNILDSINIKGDQNKIKEKWLQNLKKKKAFDKISVRLSNYNDDKKEIFDITFVNNKEDRNDDNYDNKSCIKKVCNAEEYLLISTPVYYSNDRPHIGHAYCNILCDVLYKYEKLKGVEKKKKGIIFFSGMDEHGLKIEKKCNKNKMKIIEYIDDISNYYKDMNKKLSVDVNLFYRTSYSFHKMFVQNVWKYLVHNNYIYKDTYKGYYNINEERYISEQELREGKYKIDNENIIYVEEENSYFFNILKFKDYLIDFYEKNENFIYPPYLRKQVIYTLKNELRNICISRYNTKWAIQIPNEAEGTIYVWFDALLSYVSSMLYLHKIKKNNNNNNNNNNKNNNNNNNKNNNNKNNKNNNNVINCTNGTKDVNISSTCDTDSPICSYDDILNIVNLNANNNNTQSNILPHISSNICDEKKNEKREKNIPFNKVIGKKFWNPFIQVIGKDILNFHAILYICLLKSLNLELPQKILCHGLIKNENIKMSKSLNNVVNPFDLLKKYNPDVLRLYFMGCGSIYEDKNYKEQNIESFELFLRNNVGNLLYRVVSLCIENNYNMVPVIKTNDYDSNIILNEWKDNIKNKLIPYLDNMEYIQFLELIMTLIKNVNKFFVHNTPWNYKKDTQHFHTTIYVTLECMKYFSILMFPFIPNISLAILRNIGFDDIDEENISLDMLETRTTKFMLNGLIKIV
Protein: Guanyl-specific ribonuclease pgl-1 (EC 4.6.1.24) (P granule abnormality protein 1) (E3M3V1)
Organism: Caenorhabditis remanei (Caenorhabditis vulgaris)
Function: Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate. Essential role in male and female postembryonic germline development; maternally provided protein maintains a population of proliferating germ cells and zygotic expression is required for correct oogenesis (By similarity). Together with the P-granule component pgl-3, is involved in the formation of P-granules (By similarity). Together with pgl-3, probably recruits other granule components such as pos-1, mex-3 and glh-1 to P-granules (By similarity). In addition, may act redundantly with pgl-3 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (By similarity). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (By similarity). May protect somatic cells from excessive apoptosis during normal development (By similarity).
Subcellular location: Cytoplasmic granule {ECO:0000250|UniProtKB:Q9TZQ3}. Note=Localizes to P granules in germline precursor cells. Localizes to P granules in germ cells at all stages of development except in spermatogenesis. Co-localizes with pgl-3 in P-granules, but localization in P-granules is not dependent on an association with pgl-3. {ECO:0000250|UniProtKB:Q9TZQ3}.
Interaction partners:
- CRE-NPP-11 protein
- CRE-UNC-10 protein
- Uncoordinated protein 79
- CRE-UNC-79 protein
- Uncharacterized protein
- CRE-UTX-1 protein
- Uncharacterized protein
- CRE-ASH-2 protein
- Nuclear pore complex protein
- CRE-NPP-15 protein
Sequence:
MENNKRGVVEAKGIKSHYFQTLANYVSNNLELLHNNPKQANSFAASVFGSTAPIDEKDLLDLLVPSDANADALAAGMDCCLLLGEKYRPHFDAAVQQLARLGRTHDVATVIDDEKKFTALSKKTKLKKTDEAKILQAFFKIHSTEDEEKFEAISELCQLDLDFDAYVFIKALTLENEENQELVETIKDNLVEAWNKSNPLLVKLLLEGVKEQDPVDKFTYLLLQPLTEATLSDAVNFIVEKYSAELPDEGDASLVVRSQLGCQFFFLVTRTLAHDQRELAKLVQTLIPRPVRLEVFPGLQRSVFKSSVFLGHHIIQIFMGCEFCSIQSIKNTMFSAKKPFQDWSFVGLAQDFECPWRRLAIAELLKKFSVSVVEKVFDNPVALIPQHESDNEALIELVTNALRFALWIVEFYETETNEKSIKELAFLDHSSKTLLIESFTKFLQGKDVKDQDHLKRIIDALEKSRTQETKSNLEYSREEIKTKMPSSSSAKAQVLHGLNTSAAAGLIVPSLSLLEIPVDEVDSTSHLTTSKDIGQGVFVKAQDTVTEKQKEAPLVAQQTAFHHEPQTATLVPPSPNEESMAAESISTDGWDSPTKSVVLPLDDMILEEEERDALKPDSVNSHRSEETTPVPEQLPQETSERVTSPPPGERSRTAWGDGDATPMILATPTNDYKVSGFGGAKLAKGFGTMGSTGGGFGGGGGGGSYGGRGGYGGGDRGGRGGGFGGGDRGGRGGYGGGDRGGRGGGYGGGDRGGYGQRGGYVAGGDRGGRGGYRGGGGNF
Protein: Intracellular phospholipase A2 (IPLA-2) (PLA(2)) (EC 3.1.1.4) (Calcium-independent phospholipase A2) (Q20500)
Organism: Caenorhabditis elegans
Function: Phospholipase that plays a critical role during oogenesis, ovulation, and/or embryogenesis.
Interaction partners:
- phospholipase A2
- Phospholipase A2
- Phospholipase A2
- PhosphoLipase A2 Group
- Patatin-like phospholipase domain-containing protein ZK370.4
- 1-alkyl-2-acetylglycerophosphocholine esterase
- Platelet-activating factor acetylhydrolase homolog 2
- Phospholipase
- Phosphatidylserine synthase
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MTTTNKDGPFRQQYLPGVHKEPNLAISESTHSSDWYSATSSEDCFQAASQSFSSQKSNGNVITQQPGKLHCEISDPKSCSFVPAISTDNAQMGTSGIIKYRSYSNPDLLVAMSPLAYRDEAPQSQKSVANSRQDLTQTSCEVVTVSETVVNADSITTTTVTSSTTTTATASQEDFIMVEAEQDETAGLCDATMPLVDKKNITTSSTTSSPSRQITPRIENGLSFENVVSLVKIFPAFVNKLLKKPWYASRCDEVCQFPKAELAYYDIVSTDVDDEHFVIVAGKVTTDEHLMDNQFHLVFAPVGFSEDVSLDERPFSLFRATDKKDLMDLLHLCDEKSFLFTSLDMSTMRADILRSKIEELVIQIRLKPHYHMIHVAIATDRLDFFSDGMIKTMNETLEPFESQLRCLCHTENCYPVHLALTMDRQKIVERLLELDPTLFCETDKAGNNVWHHVNSSFCAQIIWDRCPASQHFIDERNMDGQSPLNEAVSTAKPLVATFLIGKGAKFTRGDRNELFVAMTSKNAQSVVEVVLTDKPEIANERDALGNSAIHVALYKESLNALLNRKVELGLDIDVKNNAGETALLLFITTRKPDLLPLLVTLYAHGANMNATDPHGNTALHKSAALVDAKKISLECVKFLISAGSNPNKINLRGESPRHLAASLQNQEMLAILKAAGATRCPKGYKGCRSNCRHDCSSAEDEYEETLQKIRIGNESDYEKTEFTASEKLNIQDTLDGSRRGKKAKVNLISMDGGGIRGLVIIQTLIAIEERLGDDIFKYFDWSAGTSTGSLIMAGLATGKSLREMQQTYLLLKDRVFDGIMPPYDTVQLEKFIQDQFGTGTVWEIPYPRLMISAVNSEKLPVRLEMARNYKPAKDVAPETPKEMPLWMALRRSTAAPVLFKPSEDRYIDGGIISNNPALDLMSEVHAYNRELQLSGRKSDAVQMNVLVSFGTGQIPSTVIETLSIDSNSPLQSIKTIKNLAAMFIDQATASEGAPVARSRQWADSLEIPFFRFSAPLSKNIFLSSTSDLDVCTMMWDSFIYCRKHRDYIDELVKVLKHDTDHPHVKTPFTDL
Protein: Transposon Ty1-BL Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12490)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPIFHGSACASVTSKEVQTTQDPLDISASKTEECEKVSTQANSQQPTTPPSSAVPENHHHASPQAAQVPLPQNGPYPQQRMMNTQQANISGWPVYGHPSLMPYPPYQMSPMYAPPGAQSQFTQYPQYVGTHLNTPSPESGNSFPDSSSAKSNMTSTNQHVRPPPILTSPNDFLNWVKIYIKFLQNSNLGDIIPTATRKAVRQMTDDELTFLCHTFQLFAPSQFLPPWVKDILSVDYTDIMKILSKSINKMQSDTQEVNDITTLATLHYNGSTPADAFEAEVTNILDRLNNNGIPINNKVACQFIMRGLSGEYKFLPYARHRCIHMTVADLFSDIHSMYEEQQESKRNKSTYRRSPSDEKKDSRTYTNTTKPKSITRNSQKPNNSQSRTARAHNVSTFNNSPGPDNDLIRGSTTEPIQLKNTHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSNDLNIESDHDFQSDIELYPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTDSGGMHRLDVPLLAPMSQSNTHESSYASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRSPSIDTSSSESNSLHHVVPIKTSDTCPKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYHITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Eukaryotic translation initiation factor 3 subunit M (eIF3m) (Q8W4A0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03012}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit F
Sequence:
MTTIVPTSEENPFLAVVRFTSQLAWADAGPEAAEPEITRLCREAEESMVAEKWLELSSLMVTSAELVSSKISEKDLECTYTIICSIVKNAKSPEQVLEMVKAIASKVAQQPSDKASLRLKILFNLYNLVDHPYARFQVYMKALTLAVDGKVTEYIVSSFKKIDNFLKEWNIDIKDQRELFLAIANVLKENKSLVNESLKFLTKYLATFSNEDAQVLDEAKEEAVRAVIEFVKASSIFQCDLLDLPAVAQLEKDAKYAPVYQLLKIFLTQRLNAYTEFQNANSGFLQSYGLSNEDCVTKMRLLSLVDLASDESGKIPYTSIKDTLQVNEQDVELWIVKAITAKLIECKMDQMNQVLIVSRSSEREFGTKQWQSLRTKLATWKDNISSIITTIESNKVTEEGSQASSSSAAAIQGLSVR
Protein: Anaphase-promoting complex subunit 15 (APC15) (P60006)
Organism: Homo sapiens (Human)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. In the complex, plays a role in the release of the mitotic checkpoint complex (MCC) from the APC/C: not required for APC/C activity itself, but promotes the turnover of CDC20 and MCC on the APC/C, thereby participating in the responsiveness of the spindle assembly checkpoint. Also required for degradation of CDC20.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit CDC26
- Anaphase-promoting complex subunit 16
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 13
- Cell division cycle protein 16 homolog
- Anaphase-promoting complex subunit 2
- Cell division cycle protein 27 homolog
Sequence:
MSTLFPSLFPRVTETLWFNLDRPCVEETELQQQEQQHQAWLQSIAEKDNNLVPIGKPASEHYDDEEEEDDEDDEDSEEDSEDDEDMQDMDEMNDYNESPDDGEVNEVDMEGNEQDQDQWMI
Protein: C-type lectin domain family 9 member A (Dendritic cell natural killer lectin group receptor 1) (CD antigen CD370) (Q8BRU4)
Organism: Mus musculus (Mouse)
Function: Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner.
Subcellular location: Membrane {ECO:0000269|PubMed:18408006}; Single-pass type II membrane protein {ECO:0000269|PubMed:18408006}.
Interaction partners:
- Chemokine XC receptor 1
- Lymphocyte antigen 75
- C-type lectin domain family 4 member E
- Thrombomodulin
- Interferon regulatory factor 8
- C-type lectin domain family 4 member K
- Basic leucine zipper transcriptional factor ATF-like 3
- C-type lectin domain family 4 member D
- Integrin alpha-E
- Tyrosine-protein kinase SYK
Sequence:
MHAEEIYTSLQWDIPTSEASQKCQSPSKCSGAWCVVTMISCVVCMGLLATSIFLGIKFFQVSSLVLEQQERLIQQDTALVNLTQWQRKYTLEYCQALLQRSLHSGSDCSPCPHNWIQNGKSCYYVFERWEMWNISKKSCLKEGASLFQIDSKEEMEFISSIGKLKGGNKYWVGVFQDGISGSWFWEDGSSPLSDLLPAERQRSAGQICGYLKDSTLISDKCDSWKYFICEKKAFGSCI
Protein: Enolase 3 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 3) (2-phosphoglycerate dehydratase 3) (Q74IV0)
Organism: Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
Interaction partners:
Sequence:
MLKSVIENVHALEIFDSRGNPTVEVFVTLSNGVVGKAEVPSGASTGENEAVELRDGGSRLGGKGVMNAVNNVNTEINDALKGLDPHDQPNIDATMIALDGTPNKGRLGANAILGVSMATAAAAAKDNHQPLYRYLGGTDLEMPQTFHNVINGGEHADNGIDIQEFMITPVAKTSFRDGFEKIVNVYHTLKKVLEDMGYETGLGDEGGFAPNMKNSEEALKALHESIIKAGYKPGEDIAIACDCAASYFYNKEDGKYHLEGKVLTDEELADYYDKLLDEFPELISMEDPYDENDVEGMVKFTQSHKDRIQIVLDDFICTNPKLLNKAIHEGAGNASLIKLNQIGTVTETLETIRLSRKNGYNTMISHRSGETGDTFIADFAVAVNGGQLKTGAPARSERVEKYNRLLEIEEELGKGERLAFFPDNVDLD
Protein: At3g20340 (Protein expression protein) (Q9LTR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g00080
- Putative methylesterase 13, chloroplastic
- Protein PHLOEM PROTEIN 2-LIKE A6
- Glutamine-dependent NAD
- Probable isoaspartyl peptidase/L-asparaginase 2
- RPW8-like protein 2
- HVA22-like protein b
- Light-regulated protein 1, chloroplastic
- Homeobox-leucine zipper protein HAT22
- CLAVATA3/ESR
Sequence:
MGNCLRHESEMHWAGEDWDEFITEDEEDHHYSSKTTRDGKPVIVTRDSKSSVPSHEIKIRLTKKQLHDLLSKVNVHDLTFQQQTFSCPILNNRGYEEANQQRLWRPVLQSIPEVN
Protein: Peptidase M15A (R4JMG7)
Organism: Burkholderia phage ST79
Interaction partners:
Sequence:
MQLTDHFTLEELTASDVARTRQIDNTPSAATVENLRRLAQTLEQARVLLGGKPMQITSGYRCPALNRAVGGVASSAHLAGLAADFVCPKFGAPLDVVRKLAASNLAFDQLIHEGGRWVHIGLAAAGVKPRRQVLTAHFSGETASYTVGA
Protein: Zinc finger protein 950 (A0A0U1RP12)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAVTYDEVHVNFTQEEWALLDHSQKSLYRDVMLETYKNLTAIGYNWDDHNIEEHCQSSRRHGRRMFSLPRSVTP
Protein: Glutarate 2-hydroxylase (G-2-H) (EC 1.14.11.64) (Carbon starvation induced protein D) (P76621)
Organism: Escherichia coli (strain K12)
Function: Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG) in the stationary phase of E.coli. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Other dicarboxylic acids (oxalate, malonate, succinate, adipate, and pimelate) are not substrates for this enzyme.
Interaction partners:
- L-2-hydroxyglutarate dehydrogenase
- Succinate-semialdehyde dehydrogenase [NADP
- 4-aminobutyrate aminotransferase GabT
- Gamma-aminobutyric acid permease
- HTH-type transcriptional repressor GlaR
Sequence:
MNALTAVQNNAVDSGQDYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRFRVAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLATAVAHLIGRSNFDAMSGQYYARFVVKNVDNSDSYLRQPHRVMELHNDGTYVEEITDYVLMMKIDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAPPSKNVSKDVFHPVFDVDQQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSVPVPVGKFLLINNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTHQ
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (P37040)
Organism: Mus musculus (Mouse)
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:
- Heme oxygenase 1
- Cytochrome P450 3A11
- Cytochrome b5
- Cytochrome b5 type B
- Cytochrome P450 3A13
- Cytochrome P450, family 4, subfamily f, polypeptide 37
- Cytochrome P450 3A16
- Cholesterol 24-hydroxylase
- Fanconi anemia group C protein homolog
- Cytochrome P450 4V2
Sequence:
MGDSHEDTSATVPEAVAEEVSLFSTTDIVLFSLIVGVLTYWFIFKKKKEEIPEFSKIQTTAPPVKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEGDPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEHFNAMGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEFFGVEATGEESSIRQYELVVHEDMDTAKVYTGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSTLVNQIGEILGADLDVIMSLNNLDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELAQYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAILQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVAVEYEAKSGRVNKGVATSWLRTKEPAGENGRRALVPMFVRKSQFRLPFKPTTPVIMVGPGTGVAPFMGFIQERAWLREQGKEVGETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSREQAHKVYVQHLLKRDKEHLWKLIHEGGAHIYVCGDARNMAKDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVWS
Protein: Menaquinone reductase (MK reductase) (EC 1.3.99.38) (P9WNY9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reduction of a single double bond in the isoprenoid tail of menaquinone (MK-9) in M.tuberculosis, likely the beta-isoprene unit, forming the predominant form of menaquinone found in mycobacteria, MK-9(II-H2). Is required for M.tuberculosis survival in host macrophages.
Interaction partners:
- 2-heptyl-1-hydroxyquinolin-4
- Uncharacterized protein Rv0559c
- Electron transfer flavoprotein subunit beta
- Nonaprenyl diphosphate synthase
- Protease HtpX homolog
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
Sequence:
MSVDDSADVVVVGAGPAGSAAAAWAARAGRDVLVIDTATFPRDKPCGDGLTPRAVAELHQLGLGKWLADHIRHRGLRMSGFGGEVEVDWPGPSFPSYGSAVARLELDDRIRKVAEDTGARMLLGAKAVAVHHDSSRRVVSLTLADGTEVGCRQLIVADGARSPLGRKLGRRWHRETVYGVAVRGYLSTAYSDDPWLTSHLELRSPDGAVLPGYGWIFPLGNGEVNIGVGALSTSRRPADLALRPLISYYTDLRRDEWGFTGQPRAVSSALLPMGGAVSGVAGSNWMLIGDAAACVNPLNGEGIDYGLETGRLAAELLDSRDLARLWPSLLADRYGRGFSVARRLALLLTFPRFLPTTGPITMRSTALMNIAVRVMSNLVTDDDRDWVARVWRGGGQLSRLVDRRPPFS
Protein: Tryptophan-rich antigen 3 (Q8IK14)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
- Merozoite-associated tryptophan-rich antigen
Sequence:
MQINPMEKSSFVQTRIFPPKPTIFSLEKNDDFLNTHNEGFLILSYCFAISLFMYIVLKNLYYLYIFKRTRIKIIESLNNDNNVENEIEEMKRVKNLIMEQVIHELMRKSIISKRRTRKDIETDLSQNVRNEDMNLKENEIEMTQVETLKHLIHNNLLTEFHDTKEKNLESFIKFLQQLMTLEKNEKEFSNNILVKDLMDYIINIGKKEIQKSNTQLSQNSSQNYIPSNENDIYIFQIQVIKELLKNNIIITHSNDGKQLDDEIITKILEESLMSQANVVEYFYIEMIKNILGNDYNELNNISYTHDDLYLQKYEKELIKKKLSQYAYKNMNTKQNNKYVQDKTVNKHIHKNQIEQNENTTNLIEKENTFEKTNKFDNNGMIQNNIPIQNETNDESMKNIIQHKELLKNHDKENKNEEIENMNQHKKEECNYNDKKNVTEHSKKSRKNFKRKCMKKRDIRHLYQIDKLQDKILKNLMGQDSIESDSKNNDIQQLEEQKSDIQNEKLNTSNEQEETRNTNNEHKENEVNMDQNNMKLNIYNLNNQDIQNHYDKNVKEKLEEENILSDNIIKPEGSMASEGSYSSYESIYPYGSMAAEGSYSSYDSIYPEGSMDTEGSYSSYESIYPDGSMAAEGSYTSYDSINPEESVTPEGNNSTSETIKEEDNMTSQNNYSSNGSYNSEEDKDNMDKIKMYDEIIQNGLIDRINKPRTFEKKIEKCRRYSILTNRENRTYLSNWNNEKIDIKEYENKSEEELEQWKNKQWEDWKVYLEKQWSVWLEISENDKIEWLEDKEREFRSYIKYIYNIWFKWLKKRKGELTGEQKPWMTWNEQEWETFFETRYKKQFLDEWYDMLKYMDKILNIRKYTLWNKWKGKKLTQWLMQDWKLIEDDEWEKYEEDKSWSKRFDMKKKNEWKKWRNRIFKEYIEWKEWIYYKGQSANVSDVSYWEEWKEKKTNELKEWLDALTKQWMLQGKWKELIRNQE