wanglab/gogpt-training-data huggingface dataset:
Protein: PHD finger protein 14 (O94880)
Organism: Homo sapiens (Human)
Function: Histone-binding protein. Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity). Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (By similarity). Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (By similarity).
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23688586}. Chromosome {ECO:0000269|PubMed:23688586}. Note=Mainly localized in the nucleus of interphase cells. In mitotic cells, colocalizes with condensed chromatin during metaphase and anaphase. {ECO:0000269|PubMed:23688586}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:23688586}.
Interaction partners:
- High mobility group protein 20A
Sequence:
MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDASKDSGEGSCSDSEENILEEELNEDIKVKEEQLKNSAEEEVLSSEKQLIKMEKKEEEENGERPRKKKEKEKEKEKEKEKEKEREKEKEKATVSENVAASAAATTPATSPPAVNTSPSVPTTTTATEEQVSEPKKWNLRRNRPLLDFVSMEELNDMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDEDEGSGSDEDENDEGNDEDHSSPASEGGCKKKKSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCGVSPSCELCPNQDGIFKETDAGRWVHIVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHADRLDRKWKRKNYLALQSYCKMSLQEREKQLSPEAQARINARLQQYRAKAELARSTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDNSDTSSSVDGRRKHKQPALTADFVNYYFERNMRMIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSEGQGIWALLGRITGQKLNIPAILRAPKERKPSKKEGGTQKTSTLPAVLYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQAGSSDMEADMAMETLPDGTKRSRRQIKEPVKFVPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKPKAEDLRTECATCKGTGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDSSSSKEDENEAERKNISQELNMEQKNPKK
Protein: Histone deacetylase (EC 3.5.1.98) (A0A1D8PJ17)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037913}.
Interaction partners:
- Snt1p
- NAD-dependent protein deacetylase HST1
- SIR4-interacting protein SIF2
- Histone-binding protein
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone deacetylase
- Transcriptional regulatory protein SDS3
- Ume1p
- NAD-dependent protein deacetylase HST2
- Histone acetyltransferase type B subunit 2
Sequence:
MTISISETDTFTTDIKTRENTPIYDPNHPGTNNKYNVSYHYNPEVSRFHYGALHPMKPFRLMLTDHLVISYKLYEKMDLYTPRRATKDELLEFHSEDYIDFLQSITPEKCKTISNDTLAQFNIGDDCPIFDGMYDYSAIYAGASLDATRKLISGMSDIAINWSGGLHHAKKFEPSGFCYVNDIVLSIINLLRVHPRVMYIDIDLHHGDGVQEAFYNTDRVMTVSFHKYNGEFFPGTGSVDEVGIGSGKNYAINVPLRDGIDDESYIRLFKSIMEPLITKFQPTCIVQQCGADSLGYDRLGCFNLNIRAHGECVKFIKSFGIPMLVVGGGGYTPRNVSRLWCYETSVLNDVNLDHKIPNYLPTYDWFGPDYSLHPQLDGRIDNKNSKKYLQSVQTTIMEQIRYLNHAPSVQMYEIPPDLTGLTEDEDKAIQELNEDMERDEKIMKDETKLGELMT
Protein: Centrosomal protein of 104 kDa (Cep104) (Q80V31)
Organism: Mus musculus (Mouse)
Function: Required for ciliogenesis and for structural integrity at the ciliary tip.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60308}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O60308}. Note=In interphase non-ciliated cells, localizes to the distal ends of both the mother and daughter centrioles. In ciliated cells, present at the distal end of the daughter centriole, but not on the mother centriole, and at the tip of primary cilium. Localization at the ciliary tip is also observed in motile cilia. Throughout S phase, associated with both mother and daughter centrioles in each centrosome. During metaphase and telophase, present at both spindle poles. {ECO:0000250|UniProtKB:O60308}.
Interaction partners:
- Centriolar coiled-coil protein of 110 kDa
- Centrosomal protein of 97 kDa
- Centrosomal protein of 89 kDa
- Katanin-interacting protein
- Leucine-rich repeat-containing protein 47
Sequence:
MPHKIGFVVVSSSGHEDGFSARELMIHAPTVSGWRSPKFCQFPQEIVLQMVERCRVRKLQLLAHQYMISSKVEFYISESLPEYLVPYQAERFRRLGYVSLCDNEKTGCKARELKSVYVDAVGQFLKLIFHQNHANKYNIYNQVALVAINIIGDPADLGDESNITSREKLIDHYLGHSPHNPEDPALDGTFSGRSDYISPLDDLAFDMYQDPEVAQIIRRLDERKREAVKKERYDHAKKLKQAIADLQKVGERLGRYEVEKRCAVEKEDYDLAKEKKQQMARYRAQVYEQLELHGLLQGEPEMQRPFALPLQPLASPSSPQHWKAVSSLPRTEKLVAEDSFAGPVLQEKPSASSPQHSAVDPSPPAAGHAPRSHTEVLPYDERPLPVTRKQLGEASAEAEVKEADSDVRRRGVAGEPEPLTEKALREASAAIDTLGEALVAGAYSKMWSCREDALLALYKKLMEMPVGTQKEDLKNMLRASVFLIRRAIKDIVASVFQASLKLLKMIITQYIPKHKLGKLDTTHCVERAFPLLLARAGDSSARLRVMALNFIQEMALFKEVKSLQLIPSYLVQPLKANASVHLAMSQVDLLARLLRDLGTESSGFTVDNVMKFAVSALEHRVYEVRETAVRIILDMYRQHPALTLEHLPPDDSATRRNLLYKAIFEGFAKIDGSVLPTEAEVRAQKRVATKEAEKQKKEEMKALQGQSGELRETQAGVQEKESEAVKLRNQDPQGRKAVLPDTPEIPANHFLDNLCIFCGERNESFTEEGLDLHYWKHCLMLTRCDHCRQVVEISSLTEHLLTECDRRDGFGKCPRCSEAIPKEELPGHIKTKECSPAKPEKVANHCPLCHENFAPGEEAWKVHLMGPAGCTMNLRKTHVLYKATAPQQGKGPAAAKSSTSAPKVGSKIPTPKGGLSKSSSRTYMRR
Protein: Galactoside 2-alpha-L-fucosyltransferase (EC 2.4.1.-) (Alpha-(1,2)-fucosyltransferase fut-2) (Fucosyltransferase fut-2) (P91200)
Organism: Caenorhabditis elegans
Function: Selectively catalyzes the addition of fucose in alpha 1-2 linkage to Gal-beta-(1->4)-Xyl-beta-R, Gal-beta-(1->6)-GlcNAc-R, Gal-beta-(1->3)-Gal-beta-(1->4)-Glc and Gal-beta-(1->3)-Gal-beta-(1->4)-Xyl-R acceptors but not Gal-beta-(1->3)-GlcNAc-beta-(1->3)-Gal-beta-(1->4)-Glc. Unlike in mammals, unable to fucosylate Gal-beta-(1->4)-Glc-beta-R.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305|PubMed:12163507}; Single-pass type II membrane protein {ECO:0000305|PubMed:12163507}.
Interaction partners:
- Fucosyltransferase
- Alpha-
- Alpha-
- Alpha-
- UAA transporter
- FTH domain-containing protein
- Beta-1,4-galactosyltransferase galt-1
- Alpha-
- BAAT/acyl-CoA thioester hydrolase protein
Sequence:
MRNVKGLFSYMTKTKSFYISIIVIIFIIFIVNRMGPRNYNYKQIGTEINCVKHKVDEQRYLLFPMITILYKYGLGNQLFEVFSLLGSAQTLNRTAIFNADDDILQSKLDLLQKQVPQVAARIISIPIEIAESTRYLFLPACCHYQFPSLFSCERSKFLVIDGQYFQSFKYFSAIDSLIRKLLKPPIDEEIILKKMIGRKDELRFKNCVHIRRGDYVNDFDHAETSSYFTIRAIDYVHTLHPGLVYLISDDPKWVRKQIAEHLDYHDDVKIMETPINAAIRDLYFSQAHCDSVLITAPSSTFGWWIGYMSKNQSNVYYRDIQETDDMVKYKMVEEDFFPPTWKKLGMSRNGSIISK
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 (Q384D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298, ECO:0000256|RuleBase:RU368034}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298, ECO:0000256|RuleBase:RU368034}; Matrix side {ECO:0000256|ARBA:ARBA00004298, ECO:0000256|RuleBase:RU368034}.
Interaction partners:
- NADH-ubiquinone oxidoreductase complex I subunit
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Uncharacterized protein
- SET domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Flavoprotein monooxygenase, putative
- Uncharacterized protein
Sequence:
MIRKTPPRLVRDPVPTDTKAFYSWFSGQAYRQERVIPGGYPAVRVYPVYGKRWFTGRTVMAMIAGFSLFGAWHRPEKERYNMEMMIEWSERQAAHLPYQKAEVNLRCLITSYKRHRYEQENLIDKGFVGLTSEFRKFFYHDDVWRPPLHDVLMHPYAKYGGPLFSYNWTIGYF
Protein: Glycine oxidase (GO) (EC 1.4.3.19) (O31616)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Thiazole synthase
- Sulfur carrier protein ThiS adenylyltransferase
- Thiazole tautomerase
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
- Aminomethyltransferase
- Sulfur carrier protein ThiS
- Aminopyrimidine aminohydrolase
- Thiamine-phosphate synthase
- Thiamine-monophosphate kinase
- Putative HMP/thiamine permease protein YkoE
Sequence:
MKRHYEAVVIGGGIIGSAIAYYLAKENKNTALFESGTMGGRTTSAAAGMLGAHAECEERDAFFDFAMHSQRLYKGLGEELYALSGVDIRQHNGGMFKLAFSEEDVLQLRQMDDLDSVSWYSKEEVLEKEPYASGDIFGASFIQDDVHVEPYFVCKAYVKAAKMLGAEIFEHTPVLHVERDGEALFIKTPSGDVWANHVVVASGVWSGMFFKQLGLNNAFLPVKGECLSVWNDDIPLTKTLYHDHCYIVPRKSGRLVVGATMKPGDWSETPDLGGLESVMKKAKTMLPAIQNMKVDRFWAGLRPGTKDGKPYIGRHPEDSRILFAAGHFRNGILLAPATGALISDLIMNKEVNQDWLHAFRIDRKEAVQI
Protein: Inactive angiotensin-converting enzyme-related protein (ACE-like non-metallopeptidase protein 1) (Q18581)
Organism: Caenorhabditis elegans
Function: Inactive as a metallopeptidase, due to a lack of active site residues. Required for larval molting, male tail development, and formation of adult alae. Acts in the heterochronic pathway and plays a role in the developmental timing of postembryonic hypodermal seam cell division and adult alae production. Acts synergistically with apl-1 in let-7 regulated postembryonic cell division events. Might act downstream of the heterochronic protein lin-41. Negative regulator of lifespan, heat and oxidative stress response and age-related degenerative changes like reduced pharyngeal pumping and decreased body movements. Lifespan restriction is dependent on the forkhead-type transcription factor daf-16.
Interaction partners:
- Uncharacterized protein
- SSD domain-containing protein
- Papilin
- NOmpA Homolog
- PAN domain protein
- MAM domain-containing protein
- P-granule-associated novel protein 1
Sequence:
MKFHILLLLLVGACLPVFTQEIKPKPELLPADEAPKDPEAVFSEGEPFELTDALDTPKNGSVPVPEPEPKPEPEPEPEPKPEPEPSPTPEPEPAIKFDNIESEDYGDVAETAASTQPDELNTEVIEQLVDTFLNTGSIASNKTNKGPVFANPVAQALVNSSNYWKTDNLQAPGSIKDEEKLRSWLAGYEAEAIKVLREVALSGWRYFNDASPSLKLALDEAENVLTMFVRSTSMQAKQFDMASVTDEKVMRQLGYVSFEGMSALAPSRFADYSQAQAALNRDSKDSTICDKDVPPPCALQKIDMDSIFRNEKDASRLQHLWVSYVTAIAKSKPSYNNIITISNEGAKLNGFANGGAMWRSAFDMSSKVHKAEFDLNKQIDKIYSTIQPFYQLLHAYMRRQLAGIYSNPVGLSKDGPIPAHLFGSLDGGDWSAHYEQTKPFEEESETPEAMLSAFNTQNYTTKKMFVTAYRYFKSAGFPHLPKSYWTSSIFARVWSKDMICHPAAALDMRAPNDFRVKACAQLGEPDFEQAHSLLVQTYYQYLYKDQSLLFREQASPVITDAIANAFAHLSTNPHYLYSQKLVPSEHLDIKDSVIINKLYKESLESFTKLPFTIAADNWRYELFDGTVPKNKLNDRWWEIRNKYEGVRSPQPYNTSNLDALIHNSVSQVHSPATRTLISYVLKFQILKALCPEGTILSEGCILSEDTTEKLRETMKLGSSITWLKALEMISGKGELDAQPLLEYYEPLINWLRNTNEIDQVVVGWDGEGTPFTVEEIPKTRQPGDGGNGLPSEDRVAFPGGECVNGQECLLDSHCNGTICVCNDGLYTLEIGNTFNCVPGNPADSGFGDGKGGLVIGLFNNEVTTPEPSAEPEPTAKTTTKMPPRVRAATSPFSLYLTVLLIIYFAL
Protein: Glutaredoxin-3 (PKC-interacting cousin of thioredoxin) (PICOT) (PKC-theta-interacting protein) (PKCq-interacting protein) (Thioredoxin-like protein 2) (Q9JLZ1)
Organism: Rattus norvegicus (Rat)
Function: Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (By similarity). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator. Required for hemoglobin maturation (By similarity). Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O76003}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O76003}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9CQM9}. Note=Under the plasma membrane (By similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In the Z line, found associated with CSRP3 (By similarity). {ECO:0000250|UniProtKB:Q9CQM9}.
Interaction partners:
- BolA-like protein 2
- BolA-like protein 1
- Anamorsin
- T-complex protein 1 subunit delta
- COP9 signalosome complex subunit 5
- Glutaredoxin-related protein 5, mitochondrial
- T-complex protein 1 subunit theta
- BolA-like protein 3
- Calcyclin-binding protein
- Cysteine and glycine-rich protein 3
Sequence:
MAAGAAEAAEAAVAVVEVGSARQFEELLRLKTKSLLVVHFWAPWAPQCVQMNDVMAELAKEHPHVSFVKLEAEAVPEVSEKYEISSVPTFLFFKNSQKVDRLDGAHAPELTKKVQRHVSSGSFPPSTNEHVKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKTYSNWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKTFSNWPTYPQLYVRGDLVGGLDIVKELKDNGELLPILKGEN
Protein: Lysosomal phospholipase A and acyltransferase (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (1-O-acylceramide synthase) (ACS) (LCAT-like lysophospholipase) (LLPL) (EC 3.1.1.5) (Lysophospholipase 3) (Lysosomal phospholipase A2) (LPLA2) (Phospholipase A2 group XV) (PLA2G15) (Q8NCC3)
Organism: Homo sapiens (Human)
Function: Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments. Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines. Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines (By similarity). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide. Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress. Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance (By similarity). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines.
Subcellular location: Lysosome {ECO:0000269|PubMed:23958596}. Secreted {ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:20410020}. Membrane {ECO:0000269|PubMed:25727495}; Peripheral membrane protein {ECO:0000269|PubMed:25727495}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 6
- Acyl-protein thioesterase 1
- Phospholipase B1, membrane-associated
- Patatin-like phospholipase domain-containing protein 7
- Phosphatidylcholine-sterol acyltransferase
- Glycerophosphocholine phosphodiesterase GPCPD1
- Phospholipase A and acyltransferase 3
- 85/88 kDa calcium-independent phospholipase A2
- Phospholipase A2, membrane associated
- Cytosolic phospholipase A2
Sequence:
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Protein: Ras-dva-2 small GTPase (Rasd family member 4) (Zgc:153845) (Q5XWT8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}.
Interaction partners:
Sequence:
MSLEVKEKTEVRLVFMGAAGVGKTALIKRFLQDSFEPKHRRTVEELHSKEYEVAGVKVTINIMDTSGSYSFPAMRKLSIQNGDAFALVYSVDDPESLEVVNRLREEILEVKEDKFTPIVVVGNKKDRLIERRVSADDVLAKVEMDWNNCFMEASAKENENVMEVFKELLQQANLPSRLSPALRRRRETFPKDLSLRPPMNKTNSCSVS
Protein: Inositol-3-phosphate synthase (MIP synthase) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (IPS) (MI-1-P synthase) (J9VYL3)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11986}.
Interaction partners:
Sequence:
MSPTALDACDHHDSFSLPAQDQSKVHPSARRTPEGGLIKVESDSTVYEADGIKAKFTDRGASVIKGSDGKLSVKKTEKNFEFFTKSTVGRVGLMLVGLGGNNGTTVLATNLANKYNISWHTKNGIQQPNYIGSVVRASTVRLGTDPETGKDVFVPISDMLPMVHPNDFVIGGWDISSLSMDKAMLRAKVLEWDLQRQLIPLMENVKPLPSIYYPDFIAANQADRADNLIPGDDKKVHLEHIRADIRRFKADNHLDSVVVLWTANTERYADIIPGVNDTADNLLKAVETSHEEVSPSTIFAMASILEGVPFINGSPQNTFVPGCIELAEKHKAFIGGDDFKSGQTKVKSVLAEFLVNAGIKPLSISSYNHLGNNDGKNLSSQRQFRSKEISKSSVVDDMVAANPILYKTAEDLSKATGEIVKKGEHPDHIVVIKHVPAVGDSKRAIDEYYSELLMGGRNVMNIFNECEDSLLATPLIFDLAILAELLTRVTYRENATGEWQPLYSVLSLLSYMLKAPLVKPGEDVVNSLNRQRNALEQFLKACLGLEHSNDLLLNTRVW
Protein: Cytochrome c, testis-specific (P00015)
Organism: Mus musculus (Mouse)
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular location: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
Interaction partners:
- Apoptotic protease-activating factor 1
- Caspase-9
- Caspase-3
- Apoptosis regulator Bcl-2
- Non-selective voltage-gated ion channel VDAC2
- Apoptosis-inducing factor 1, mitochondrial
- Bcl-2-like protein 1
- Heat shock protein beta-2
- Heat shock protein beta-1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
Sequence:
MGDAEAGKKIFVQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIWSEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIKYLKQATSS
Protein: Acylhomoserine lactonase (I7HB71)
Organism: Chryseobacterium sp. StRB126
Interaction partners:
Sequence:
MNRRELLKSGLLAGTLSFMPFSNVFAETKLFSEKTEDDLSGFKKIKLGELELFILTDGYIHEENLISFAPRGNVAELKTILKDNFRADHYIDMAINILLVKTKEKLILMDTGMGIFADERTGFLLKSLQKAGFSAHDITDIFLSHAHPDHIGGVVDKQNKLVFPNASIFISKIEHDFWINASIKDFNNSALKAHPERLNQIIPALQNILKAIQPKLKFYDLNKTLYSHFNFQLAPGHTPGLTVTTISSGNEKLMYVADLIHSDVILFPHPDWGFSGDTDLDIATASRKKFLKQLADTKARAFTSHLPWPGLGFTKVKAPGFEWIPESFMN
Protein: Kunitz trypsin inhibitor 2 (AtKTI2) (Cysteine protease inhibitor WSCP) (Kunitz-type cysteine protease inhibitor WSCP) (Water-soluble chlorophyll protein) (AtWSCP) (Q9C7S6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Water-soluble and chlorophyll-binding protein that probably does not function as a chloroplast chlorophyll carrier and is not involved in photosynthesis. Involved in the control of cell death in the transmitting tract and septum epidermis during flower development. Binds and inhibits the activity of the cysteine protease RD21A as a pro-death protein. May play a role in herbivore resistance activation during seedling greening.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:26016527, ECO:0000269|PubMed:26160583}. Endoplasmic reticulum {ECO:0000269|PubMed:26289422}. Note=Targeted to ER bodies. {ECO:0000269|PubMed:26289422}.
Interaction partners:
- Cysteine proteinase RD21A
- Glycoprotein membrane GPI-anchored
- Serpin-ZX
- AT2G24420 protein
- Dem-like protein
- Defensin-like protein 192
- Uveal autoantigen with coiled-coil/ankyrin
- Nuclear protein
- Protease inhibitor
- Subtilisin-like protease SBT5.4
Sequence:
MKNPSVISFLIILLFAATICTHGNEPVKDTAGNPLNTREQYFIQPVKTESKNGGGLVPAAITVLPFCPLGITQTLLPYQPGLPVSFVLALGVGSTVMTSSAVNIEFKSNIWPFCKEFSKFWEVDDSSSAPKEPSILIGGKMGDRNSSFKIEKAGEGARANVYKLTTFYGTVGAIPGVWLSAPQLIITKDTAKTLLVKFKKVDDATTATSNLYFPG
Protein: Glutamate synthase [NADPH] large chain (EC 1.4.1.13) (Glutamate synthase subunit alpha) (GLTS alpha chain) (P96218)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Glutamate synthase small chain
- NADPH-ferredoxin reductase FprA
- Probable NADPH dependent 2,4-dienoyl-CoA reductase FadH
- Probable ferredoxin/ferredoxin--NADP reductase
- Carbamoyl phosphate synthase large chain
- Glutamine synthetase
- Probable glutamine synthetase GlnA4
- Probable glutamine synthetase GlnA3
- Glutamine synthetase
- Glutamine--fructose-6-phosphate aminotransferase
Sequence:
MTPKRVGLYNPAFEHDSCGVAMVVDMHGRRSRDIVDKAITALLNLEHRGAQGAEPRSGDGAGILIQVPDEFLREAVDFELPAPGSYATGIAFLPQSSKDAAAACAAVQKIAEAEGLQVLGWRSVPTDDSSLGALSRDAMPTFRQVFLAGASGMALERRCYVVRKRAEHELGTKGPGQDGPGRETVYFPSLSGQTLVYKGMLTTPQLKAFYLDLQDERLTSALGIVHSRFSTNTFPSWPLAHPFRRIAHNGEINTVTGNENWMRAREALIKTDIFGSAADVEKLFPICTPGASDTARFDEVLELLHLGGRSLAHAVLMMIPEAWERHESMDPARRAFYQYHASLMEPWDGPASMTFTDGTVVGAVLDRNGLRPSRIWVTDDGLVVMASEAGVLDLHPSTVVRRMRLQPGRMFLVDTAQGRIVSDEEIKADLAAEHPYQEWLDNGLVPLDELPEGKDVRMPHHRIVMRQLAFGYTYEELNLLVAPMARLGAEPIGSMGTDTPVAVLSQRPRMLYDYFHQLFAQVTNPPLDAIREEVVTSLQGTTGGERDLLNPDQNSCHQIVLPQPILRNHELAKLVSLDPNDKVNGRPHGLRSKVIRCLYRVSEGGAGLAAALEEVRGAAAAAIADGARIIILSDRESDEEMAPIPSLLAVAGVHHHLVRERTRTQVGLVVESGDAREVHHMAALVGFGAAAINPYLVFESIEDMLDRGVIEGIDRTAALNNYIKAAGKGVLKVMSKMGISTLASYTGAQLFQAVGISEQVLDEYFTGLTCPTGGITLDDIAADVAARHRLAYLDRPDERAHRELEVGGEYQWRREGEYHLFNPETVFKLQHSTRTGQYKIFKEYTRLVDDQSERMASLRGLLKFRTGVRPPVPLDEVEPASEIVKRFSTGAMSYGSISAEAHETLAIAMNRLGARSNCGEGGEDVKRFDRDPNGDWRRSAIKQVASARFGVTSHYLTNCTDLQIKMAQGAKPGEGGQLPGHKVYPWVAEVRHSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANPSARVHVKLVSENGVGTVAAGVSKAHADVVLISGHDGGTGATPLTSMKHAGAPWELGLAETQQTLLLNGLRDRIVVQVDGQLKTGRDVMIATLLGAEEFGFATAPLVVAGCIMMRVCHLDTCPVGVATQNPLLRERFTGKPEFVENFFMFIAEEVREYLAQLGFRTVNEAVGQAGALDTTLARAHWKAHKLDLAPVLHEPESAFMNQDLYCSSRQDHGLDKALDQQLIVMSREALDSGKPVRFSTTIGNVNRTVGTMLGHELTKAYGGQGLPDGTIDITFDGSAGNSFGAFVPKGITLRVYGDANDYVGKGLSGGRIVVRPSDDAPQDYVAEDNIIGGNVILFGATSGEVYLRGVVGERFAVRNSGAHAVVEGVGDHGCEYMTGGRVVILGRTGRNFAAGMSGGVAYVYDPDGELPANLNSEMVELETLDEDDADWLHGTIQVHVDATDSAVGQRILSDWSGQQRHFVKVMPRDYKRVLQAIALAERDGVDVDKAIMAAAHG
Protein: Outer dynein arm-docking complex subunit 2 (Armadillo repeat-containing protein 4) (E1B8W3)
Organism: Bos taurus (Bovine)
Function: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:34715025}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5T2S8}.
Interaction partners:
- Outer dynein arm-docking complex subunit 4
- Outer dynein arm-docking complex subunit 3
- Outer dynein arm-docking complex subunit 1
- Calaxin
- Parkin coregulated gene protein
- Methyl-CpG-binding domain protein 1
- EF-hand domain-containing protein 1
- Tektin-1
- EF-hand domain-containing family member C2
- Piercer of microtubule wall 1 protein
Sequence:
MGVALTRSAQWTAAGHGAKTLEVTPLNEAIVKEIIMFVESFIYKYPQEANYVFVEPLEWKTNLDPSAFGSGYAVSGTTVKSEEADKNGEPLLYLSVPQIKIRSFGQLSRMLYIAKNMKLKEAQACIEANRNPVAKILGLDYNIISEKIGNSFVSNILDKITKDDDSESEIKMKIALQLKQLDLHLLNHSLKHISLEIRLNPGTVKNDIELLKQFSGKGKQTVLESIEYTSDYEFSNGCRAPPWRQIKGEICYVLVKPHDAETLCVTCSKEGVFLNGGKTDDEGQINYERKGEIYKDLVTLLKEKSAIFSENMSKQEIKFSEQPQKDQPNEAPKEEVAITHKASVTSRKSTQEKNRINLGRSQLTKRLEPSLNWRTSVSSKDRNTLRDTQVEKHGGKLEKSRSSVSPGRAQLIRKSVEKIEEIISDSSSESEEDEEQPDHRQEANADLPSEYWQIQKLVKYLKGGNQTATVIALCSMKDFNLAQETCQLAIRDVGGLEVLINLLETDEVKCKIGSLKILKEISHNPQIRRNIVDLGGLPVMVNILDSPHKSLKCLAAETIANVAKFRRARRVVRRHGGITKLVALLDCGKHSGEPAQSSLYETRDVEVARCGALALWSCSKSYANKEAIRKAGGIPLLARLLKTSHENMLIPVVGTLQECASEENYRAAIKAERIIENLVKNLNSENEQLQEHCAMAIYQCAEDEETRDLVRLHGGLKPLASLLNNTDNKERLAAVTGAIWKCSISKENVTKFREYKAIETLVGLLTDQPEEVLVNVVGALGECCQEHENRVIIRRCGGIQPLVNLLVGINQALLVNVTKAVGACAVEPESMMIIDRLDGVRLLWSLLKNPHPDVKASAAWALCPCIQNAKDAGEMVRSFVGGLELVVNLLKSDNKEVLASVCAVITNIAKDQENLAVITDHGVVPLLSKLANTNNDKLRRHLAETISRCCMWGRNRVAFGEHKAVAPLVRYLKSNDTNVHRATAQALYQLSEDADNCVTMHENGAVKLLLDMVGSPDEELQEAAAGCISNIRRLALAIEKARYS