wanglab/gogpt-training-data huggingface dataset:
Protein: Light-independent protochlorophyllide reductase subunit B (DPOR subunit B) (LI-POR subunit B) (EC 1.3.7.7) (P26163)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
Interaction partners:
- Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
- 2-vinyl bacteriochlorophyllide hydratase
- Light-independent protochlorophyllide reductase subunit N
- Bacteriochlorophyll synthase 33 kDa chain
- Magnesium-chelatase subunit H
- Chlorophyllide reductase 35.5 kDa chain
- Chlorophyllide reductase 52.5 kDa chain
- Magnesium protoporphyrin IX methyltransferase
- Chlorophyllide reductase subunit Z
- Photosynthetic reaction center, H subunit
Sequence:
MKLTLWTYEGPPHVGAMRVATAMKDLQLVLHGPQGDTYADLLFTMIERRNARPPVSFSTFEASHMGTDTAILLKDALAAAHARYKPQAMAVALTCTAELLQDDPNGISRALNLPVPVVPLELPSYSRKENYGADETFRALVRALAVPMERTPEVTCNLLGATALGFRHRDDVAEVTKLLATMGIKVNVCAPLGASPDDLRKLGQAHFNVLMYPETGESAARHLERACKQPFTKIVPIGVGATRDFLAEVSKITGLPVVTDESTLRQPWWSASVDSTYLTGKRVFIFGDGTHVIAAARIAAKEVGFEVVGMGCYNREMARPLRTAAAEYGLEALITDDYLEVEKAIEAAAPELILGTQMERNIAKKLGLPCAVISAPVHVQDFPARYAPQMGFEGANVLFDTWVHPLVMGLEEHLLTMFREDFEFHDAAGASHHGGKAVAREESPVAPADLAPAATSDTPAAPSPVVVTQASGEIRWMPEAERELRKIPFFVRGKAKRNTELYAAHKGVCDITVETLYEAKAHYAR
Protein: ATP-dependent Clp protease adapter protein CLPS1, chloroplastic (Q9SX29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Small adapter protein that modulate the activity of CLPC (By similarity). Involved in plastid biogenesis in particular when chloroplast protein synthesis capacity is a limiting factor. Probably involved in substrate selection for plastid Clp protease system. Recruitment to ClpC chaperones is facilitated by CLPF thus forming a binary adapter for selective substrate recognition and delivery to plastid Clp protease system (CLPC).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:23898032}.
Interaction partners:
- ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
- ATP-dependent Clp protease ATP-binding subunit CLPT2
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 3, chloroplastic
- Chaperone protein ClpC1, chloroplastic
- Chaperone protein ClpD, chloroplastic
- Chaperone protein ClpC2, chloroplastic
- Chloroplastic ATP-dependent Clp protease proteolytic subunit 1
- ATP-dependent Clp protease proteolytic subunit 6, chloroplastic
- ATP-dependent Clp protease proteolytic subunit 5, chloroplastic
Sequence:
METAICGRLALAPSSLFNSKSGDKHLVSKGPCVNRSILMTLSTSAALGKGGGVLDKPIIEKTTPGRESEFDLRKSKKIAPPYRVILHNDNFNKREYVVQVLMKVIPGMTVDNAVNIMQEAHINGLAVVIVCAQADAEQHCMQLRGNGLLSSVEPDGGGC
Protein: Putative increased recombination centers protein 14 (Q08522)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized protein YOR055W
- Putative uncharacterized protein YCL046W
- Uncharacterized protein IRC9
- Uncharacterized protein IRC4
- Increased recombination centers protein 19
- Putative uncharacterized protein YLR232W
- Putative regulator of rDNA transcription protein 16
Sequence:
MVVNPLTKIGLTSQDSHSMGTFAALKIFFTDLEISGPIPSPSMNETVYLPVEGLGLPVYLPIEGCFTVAKNLLEVFLKKVFLNIIKKYYNCCSFPICILLSTKVIQVQKKCIQ
Protein: Signal transducing adapter molecule 2 (STAM-2) (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) (O93436)
Organism: Gallus gallus (Chicken)
Function: Involved in intracellular signal transduction mediated by EGF. As a protein associated with focal adhesions and actin filaments, it may play a role in EGF receptor-stimulated cytoskeletal reorganization. The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9694904, ECO:0000269|PubMed:9801161}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Hepatocyte growth factor-regulated tyrosine kinase substrate.
- Signal transducing adaptor molecule.
- Ubiquitin specific peptidase 8
- Ubiquitin-ribosomal protein eS31 fusion protein
- Tumor susceptibility 101
- Ubiquitin-ribosomal protein eL40 fusion protein
- Histone H2A deubiquitinase MYSM1
- Polyubiquitin-B
- Vacuolar protein sorting 36 homolog.
- Vacuolar protein sorting 25 homolog.
Sequence:
MPLSASNPFEQDVEKATNEHNNSEDWGLIMDICDKVGSTPNGAKDCLKAIMRRVNHKVPHVALQALTLLGACVSNCGRIFHLEVCSRDFATEARGIINKAHGKVSEKLKTLMVEWSEEFQKDPQCSLISATIKSLKEEGVTFPAAGSQATTNAAKNGSSLSKNKEDEDIRKAIELSLQEQKQQQMETKSLYPSAEIQQTNQNLRKVRALYDFEAVEDNELTFKSGEIIFVLDDSDTDWWKGENHRGVGLFPSNFVTSDLNVEPEAATVDNSCVPEDATEEIKKAEPEAVYIDEDKMDKTLQVLQSIDPTDLNLDTDLLDSEVICQQMGPMIDEKLEEIDRKHSELSELNVKVLEALELYNKLMNETPMYSAYSKLHHPAQYPPTSSGVSVQSYPVQPPSGNYMIQGVHQVTVSQGYGLGPDQMGQLRSLPQNINSSDCNLYTKSNRQRMCHMKAITTWQRFSKHTSER
Protein: NAD-dependent protein deacylase Sir2 (EC 2.3.1.286) (Regulatory protein SIR2 homolog) (A0R2N3)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}.
Interaction partners:
- Glutamine-dependent NAD
- Probable nicotinate-nucleotide adenylyltransferase
- NAD kinase
- nicotinamidase
- Soluble pyridine nucleotide transhydrogenase
- NAD
- Pyrimidine-specific ribonucleoside hydrolase RihA
- Purine nucleoside phosphorylase
- proton-translocating NAD
- NAD
Sequence:
MQVTVLSGAGISAESGVPTFRDAETGLWAQVDPYEISSTDGWQRNPEKVWAWYLWRHYMMARVAPNEAHRTVAAWEDHLDVRVVTQNIDDLHERAGSTNVYHLHGSLFEFRCDACGSAFEGNLPEMPEPVETIDPPVCPCSGLIRPSVVWFGEPLPDAAWNRSVLAVSSADVVIVVGTSSIVYPAAGLPEAALAAGKPVIEVNPERTPLSDSATVSLRETASEALPTLLQRLPELLNRSA
Protein: Signal recognition particle subunit SRP72 (Signal recognition particle 72 kDa protein homolog) (P38688)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds signal recognition particle RNA (7SL RNA) in presence of SRP68 (By similarity). Can bind 7SL RNA with low affinity (By similarity). The SRP complex possibly participates in the elongation arrest function.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O76094}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11352936}. Nucleus, nucleolus {ECO:0000269|PubMed:11352936}. Note=Transiently localizes to the nucleolus during biogenesis of the SRP. The SRP-RNC complex is bound to the endoplasmic reticulum membrane due to the interaction of the SRP with the membrane SRP-receptor (SRP101-SRP102). {ECO:0000269|PubMed:11352936}.
Interaction partners:
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP14
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SEC65
- Signal recognition particle subunit SRP21
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle receptor subunit beta
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL30
Sequence:
MAKDNLTNLLSQLNIQLSQDEHSQVEQTCVKLLDSGCENPADVFRRCLVAVIQQDKYQKALHYLKKFKHIDDKYGRKFALEKLYIFYKLNMPDEFNTLYTAIITDDLDTVLKKDIESLRGILHVRAQYCYKNGLYQEAFKIYQHLASHNEKDQDSQIELSCNERVPLSVATELMNRSPLVTPMDESSYDLLFNESFIMASVGKYDKAIELLEKALQGATNEGYQNDINTIKLQLSFVLQMVGKTAQSKEILKGLLQELKADSPFSLICQNNLNAFVDFSKYNTNFNLLLRELNVEKLNTFNLQTFTHEQWSNIQRNVLFLRLFNNVKIHSQESLLSRTFDKYSKLVDNVTLESYKTQAKKLYHHTTKTILSGTDGSTIGILLLTIQLLIIEKEWENAIRIGELFLNESWKSSFEKFNDSQAIVCYILFELYKIKGRNNSKSVLLKKLGSVRVQLSGKIQENIPFWKHVGFELLSMGNAKESKALLREISNFSKGDADVLVDRVVSSDSLDIAQGIDLVRDIDIDKLIQLGVKPLESSAKRSKNTAVSKVQKRKVLELKKKRKIKRLEKFLQGRDTSKLPDPERWLPLRDRSTYRPKKKQQGAKQTQGGAMNKKSEQALDISKKGKPTVNKKPKNKKKGRK
Protein: EMSY transcriptional repressor, BRCA2 interacting (H0YET8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
QPSQPQRTLLQHVAQSQTATQTSVVVKSIPASSPGAITHIMQQALSSHTAFTKHSEELGTEEGEVEEMDTLDPQTGLFYRSALTQSQSAKQQKLSQPPLEQTQLQVKTLQCFQTKQKQTIHLQADQLQHKLPQMPQLSIRHQKLTPLQQEQAQPKPDVQHTQHPMVAKDRQLPTLMAQPPQTVVQVLAVKTTQQLPKLQQAPNQPKIYVQPQTPQSQMSLPASSEKQTASQAIPQYAIPCHSSSNVVVEPSGLLELNNFTSQQLDDEETAMEQDIDSSTEDGTEPSPSQSSAERS
Protein: Indole-3-acetic acid-amido synthetase GH3.8 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 8) (OsGH3-8) (OsMGH3) (Q0D4Z6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excessive free auxin. Produces more IAA-Asp levels than IAA-Ala levels in vitro. May participate in the activation of disease resistance by preventing the accumulation of free IAA, which reduces the expression of a group of auxin-responsive genes encoding expansins that control cell wall loosening and expansion. Contributes to late events in stamen and carpel differentiation, and influences floret fertility.
Interaction partners:
- Probable indole-3-acetic acid-amido synthetase GH3.13
- Probable indole-3-acetic acid-amido synthetase GH3.11
Sequence:
MAVMTDVSTTGTALRTPAAGAVKEGDVEKLRFIDEMTTNVDAVQERVLGEILGRNAGTEYLTKCGLDGATDRAAFRAKVPVVSYDDLQPYIQRIANGDRSPILSTHPVSEFLTSSGTSAGERKLMPTIMDELDRRQLLYSLLMPVMNLYVPGLDKGKGLYFLFVKSETKTPGGLTARPVLTSYYKSDHFKNRPYDPYHNYTSPTAAILCADAFQSMYAQMVCGLCQRNDVLRLGAVFASGLLRAIRFLQLNWEQLADDIESGELTPRVTDPSVREAVAAILLPDPELAKLIRAECSKGDWAGIITRVWPNTKYLDVIVTGAMAQYIPTLEFYSGGLPMACTMYASSECYFGLNLRPMCDPSEVSYTIMPNMGYFEFLPVDETGAASGDATQLVDLARVEVGREYELVITTYAGLNRYRVGDVLRVTGFHNAAPQFRFVRRKNVLLSIESDKTDEAELQRAVERASALLRPHGASVVEYTSQACTKRIPGHYVIYWELLTKGAGATVVDADTLGRCCLEMEEALNTVYRQSRVADGSIGPLEIRVVRPGTFEELMDYAISRGASINQYKVPRCVTFPPIVELLDSRVVSSHFSPALPHWTPARRSE
Protein: Uncharacterized aarF domain-containing protein kinase 2 (EC 2.7.11.-) (Q7Z695)
Organism: Homo sapiens (Human)
Function: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:33988507}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Atypical kinase COQ8A, mitochondrial
- Atypical kinase COQ8B, mitochondrial
Sequence:
MVAPWRVSVRVCLSHLRCFELRQGLSLLRPSECPRDARLCWLLLGTLPKVVSLCGDVGEGAPDVLSRRRVRCSGAAGAGPAESLPRAGPLGGVFLHLRLWLRAGALLVKFFPLLLLYPLTYLAPSVSTLWLHLLLKATETSGPTYIKLGQWASTRRDLFSEAFCAQFSKLHVRVTPHPWTHTERFLRQAFGDDWGSILSFENREPVGSGCVAQVYKAYANTAFLETDSVQRLGRASCLPPFSHTGAVGGLRELFGYLGNGRKPPENLADQSFLERLLLPKADLVGSNAGVSRAQVPGHQPEATNLISVAVKVLHPGLLAQVHMDLLLMKIGSRVLGVLPGIKWLSLPEIVEEFEKLMVQQIDLRYEAQNLEHFQVNFRNVKAVKFPTPLRPFVTREVLVETYEESVPVSSYQQAGIPVDLKRKIARLGINMLLKMIFVDNFVHADLHPGNILVQGANGLSSSQEAQLQQADICDTLVVAVPSSLCPLRLVLLDAGIVAELQAPDLRNFRAVFMAVVMGQGQRVAELILHHARASECRDVEGFKTEMAMLVTQARKNTITLEKLHVSSLLSSVFKLLMTHKVKLESNFASIVFAIMVLEGLGRSLDPKLDILEAARPFLLTGPVCPP
Protein: Chaperone protein DNAJ, putative (Q57VY8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFTYSTFLRSVSVGQACRLMGFAAPPIERRVLRRRYVELVKKHHPDNNGPESSAEVMANITAAYKTLQCLAGKQKEAMKGNNVDRSDTPSTGGGGREEMEAVAASFVVPGTPLSMANWDLPWQRGKTTTQKRKQEKDEQQLREGSTSLFEYVALARALEKRRGAQAERIAAALRSSEGSHGFGSGYFEQLHLQQRRDSPWVVKRKPLFILVCAYYRLRLVSAWWRWLAGLRYVVMGR
Protein: (R)-mandelonitrile beta-glucosyltransferase (EC 2.4.1.354) (UDP-glycosyltransferase 85A19) (B2XBQ5)
Organism: Prunus dulcis (Almond) (Amygdalus dulcis)
Function: Involved in the biosynthesis of the cyanogenic glycoside (R)-prunasin, a precursor of (R)-amygdalin, which at high concentrations is associated with intense bitterness in kernels of almond. Stereo-selectively glucosylates (R)-mandelonitrile to produce (R)-prunasin.
Interaction partners:
Sequence:
MSPVASKEKPHAVFVPFPAQGHINPMLQLAKLLNYKGFHITFVNTEFNHKRMLESQGSHALDGLPSFRFETIPDGLPPADADARRNLPLVCDSTSKTCLAPFEALLTKLNSSPDSPPVTCIVADGVTSFTLDAAEHFGIPEVLFWTTSACGLMGYVQYYRLIEKGLTPFKDAKDFANGYLDTEIDWIPGMKDVRLKDMPSFIRTTDPNDIMLHYMVSETERSKKASAIILNTFDALEQEVVDALSTLLPPIYSIGPLQLPYSEIPSEYNDLKAIGSNLWAENTECLNWLDTKEPNSVVYVNFGSTTVMTNEQLVEFSWGLANSKKPFLWIIRPGLVAGETAVVPPEFLEETKERGMLASWCPQEQVLLHSAIGGFLTHSGWNSTLEALCGGVPLICWPFFAEQQTNVRYSCTQWGIGIEIDGEVKRDYIDGLVRTLMDGEEGKKMRKKALEWKMLAEDATAPKGSSYLALENVVSKVLLSPRD
Protein: Membrane-associated progesterone receptor component 1 (mPR) (25-DX) (Acidic 25 kDa protein) (Ventral midline antigen) (VEMA) (P70580)
Organism: Rattus norvegicus (Rat)
Function: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins (By similarity). May be implicated in 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) immunotoxicity.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00264}; Extracellular side {ECO:0000250|UniProtKB:O55022}. Secreted {ECO:0000250|UniProtKB:O00264}.
Interaction partners:
- Sigma intracellular receptor 2
- SERPINE1 mRNA-binding protein 1
- Progesterone receptor
- Ferrochelatase
- Lanosterol 14-alpha demethylase
- Cytochrome b5
- Progestin and adipoQ receptor family member 7
- Progestin and adipoQ receptor family member 8
- Cytochrome b5 type B
- Sigma non-opioid intracellular receptor 1
Sequence:
MAAEDVVATGADPSELEGGGLLQEIFTSPLNLLLLGLCIFLLYKIVRGDQPGASGDNDDDEPPPLPRLKPRDFTPAELRRYDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLNDWDSQFTFKYHHVGKLLKEGEEPTVYSDDEEPKDEAARKSD
Protein: AT5g52010/MSG15_9 (C2H2-like zinc finger protein) (Dbj|BAA78737.1) (Q9FJ91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSLFCNSIETLYPKPFLSHKSHFFTFSNSKFQNPKFTSFPLRHQWRIESCLKSASSSEIDMVRNKEGIFAPKEKKVVVLWDLDNKPPRGPPYEAATALRKVAEKLGRVVEISAYANRHAFIHLPHWVVEERRERRNLDFMERKGEVTPIDPYICGVCGRKCKTNLDLKKHFKQLHERERQKKVNRMRSLKGKKRQKFKERYVSGNEKYNEAARSLLTPKVGYGLEAELRRAGVYVKTVEDKPQAADWAVKRQIQHSMTRGIDWLVLVSDDKDFSDMLRKAREADLGTLVVSDMDRALGRHADLWVPWSGVEKGEIGEKDLIPGKRPRFEEDEVGFGGNDELFSLSYDEDEKAEMTVESDGFGRFNVSAFSEDEWVEDEGDFVLSDSSDDDSDDELF
Protein: 14-3-3 protein 3 (14-3-3-3) (EhP3) (P42650)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Adapter protein which is required for phagocytosis and motility, probably by regulating actin cytoskeleton dynamics. During phagocytosis, plays a role in the initiation and/or formation of the phagocytic cup and is involved in the recruitment of the actin binding protein coactosin to the phagocytic cup.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31095644}. Cell projection, phagocytic cup {ECO:0000269|PubMed:31095644}. Note=During phagocytosis, recruited from the cytoplasm to the site of nucleation of the phagocytic cup and stays there for the subsequent steps until membrane closure and formation of the phagosome. {ECO:0000269|PubMed:31095644}.
Interaction partners:
Sequence:
MAESREDCVFLSKLAEQSERYDEMVQYMKQVAALNTELSVEERNLLSVAYKNVIGSRRASWRIITSLEQKEQAKGNDKHVEIIKGYRAKIEDELAKYCDDVLKVIKENLLPNASTSESKVFYKKMEGDYYRYYAEFTVDEKRQEVADKSLAAYTEATEISNADLAPTHPIRLGLALNFSVFYYEIMNDADKACQLAKQAFDDSIAKLDEVPESSYKDSTLIMQLLRDNLTLWTSDTADEE
Protein: AhpC (Q5FZJ0)
Organism: Helicobacter pylori (Campylobacter pylori)
Interaction partners:
Sequence:
MLVTKLAPDFKAPAVLGNNEVDEHFELSKNLGKNGAILFFWPKDFTFVCPTEIIAFDKRVKDFHEKGFNVIGVSIDSEQVHFAWKNTPVEKGGIGQVSFPVVADITKSISRDYDVLFEEAIALRGAFLIDKNMKVRHAVINDLPLGRNADEMLRMVDALLHFEEHGEVCPAGWRKGDKGMKATHQGVAEYLKENSIKL
Protein: Midkine and pleiotrophin 1, isoform A (Midkine and pleiotrophin 1, isoform B) (Midkine and pleiotrophin 1, isoform C) (RH10518p) (Q9W0S5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tyrosine-protein phosphatase 99A
Sequence:
MRINCNALFLASLVTWSGVMCSTVLGTTEGQETPLALPVAEQTQPTTAIQGEVWEEDDHEVLIRNERGTKSDGLSCRYGKNPWTECDTKTNTRSRTLTLKKGDPACDQTRTIQKKCKKACRYEKGSWSECATGQMTRADKLKASSDPSCEATRVIKKNCKPGKSKDKSAKEQRKNKDKAARKGRV
Protein: COP9/Signalosome and eIF3 complex-shared subunit 1 (COP9 signalosome complex subunit 7) (Signalosome subunit 7) (Eukaryotic translation initiation factor 3 subunit M) (eIF3m) (Q94261)
Organism: Caenorhabditis elegans
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-1 targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MADTRELPVFAYIDDVKQLQELRQYLNKHDSVKLDPNGPSETAQNMIEICSTLNVLPSWSQDVDLVLNSISSLIVVVPGEKCEPVVDSFIKNVAPQFYKGTGWASHAGIAVRVLSNLYKGYSNFHTVQEKIFKALVDMCAEARLIGELECNLETLQDRFNTWKTPVEGQREILRAVHRALLVDQRVDQAAKVMTALLGTYTEKDAAAARDDAMECVRTAVVDPKSFSFDHLERLSAVKALKTSDPLMFTALELFISGTLKDYKEFVAKNPKFVTEHLKVDETILLKKIRLLTLMSLAEEKNEISLDELAKQLDILADETLEEFVIDAIQVNAISGKINEMARTLIVSSYQHRRFGTEQWVLLEKRLKVLIANLKQTHNNVHEVNQRIEAL
Protein: H-2 class II histocompatibility antigen, E-U alpha chain (P14439)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MATIGALLLRFFFIAVLMSSQKSWAIKEEHTIIQAEFYLLPDKRGEYMFDFDGDEIFHVDIEKSETIWRLEEFAKFASFEAQGALANIAVDKANLDVMKKRSNNTPDANVAPEVTVLSRSPVNLGEPNILVCFIDKFSPPVVNVTWLRNGQPVTEGVSETVFLPRDDHLFRKFHYLTFLPSTDDFYDCEVDHWGLEEPLRKHWEFEEKTLLPETKENVVCALGLFVGLVGIVVGIILIMKGIKKRNVVERRQGAL
Protein: Dead end protein homolog 1 (RNA-binding motif, single-stranded-interacting protein 4) (Q6VY05)
Organism: Mus musculus (Mouse)
Function: RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression (By similarity). Relieves miRNA repression in germline cells (By similarity). Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs (By similarity). Sequence-specific RNA-binding factor that binds specifically to U-rich regions (URRs) in the 3' untranslated region (3'-UTR) of several mRNAs (By similarity). Does not bind to miRNAs (By similarity). Isoform 1 may play a role during primordial germ cell (PGC) survival. However, does not seem to be essential for PGC migration.
Subcellular location: Nucleus. Cytoplasm. Note=Perinuclear germ granules, also called germ plasm or chromatoid body (By similarity). Colocalizes in perinuclear sites with APOBEC3. {ECO:0000250}.
Interaction partners:
- Nanos homolog 3
- Deleted in azoospermia-like
- Tudor domain-containing protein 7
- Nanos homolog 1
- Nanos homolog 2
Sequence:
MQSKRECEQWCERVNPENKAALEAWVRETGIRLVQVNGQRKYGGPPPGWVGSPPPSGSEVYIGRLPQDVYEHQLIPLFQRVGRLYEFRLMMTFSGLNRGFAYARYSSRRGAQAAIATLHNHQLRPSCQLLVCRSTEKCELTVDGLPLSLNRRALLLALQPFGPCLQETLLLPSPGSAPSQIALLKFSTHRAAAMAKKALVEGQSRLCGEQVAVEWLKPDLKQHFRQQLAGPSLRFLRPDVSQLTQTREKLGSQGARAALQLLCQRMKLGSPVFLTKCLGTGPAGWHRFWYQVVIPGHPVPFSGLIWVVLASDWQDGHEVAKDAVSAQLLEALSEPRTSLWSPGAEAGTMVKQ
Protein: Dihydrofolate reductase (EC 1.5.1.3) (P07807)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Interaction partners:
- Thymidylate synthase
- Dihydrofolate synthetase
- Serine hydroxymethyltransferase, mitochondrial
- Folylpolyglutamate synthase
- Serine hydroxymethyltransferase, cytosolic
- Probable folylpolyglutamate synthase
- Aminomethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Phosphoribosylglycinamide formyltransferase
Sequence:
MAGGKIPIVGIVACLQPEMGIGFRGGLPWRLPSEMKYFRQVTSLTKDPNKKNALIMGRKTWESIPPKFRPLPNRMNVIISRSFKDDFVHDKERSIVQSNSLANAIMNLESNFKEHLERIYVIGGGEVYSQIFSITDHWLITKINPLDKNATPAMDTFLDAKKLEEVFSEQDPAQLKEFLPPKVELPETDCDQRYSLEEKGYCFEFTLYNRK
Protein: F-box/LRR-repeat protein 15 (F-box only protein 37) (Q9H469)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation and bone mass maintenance. Also mediates ubiquitination of SMURF2 and WWP2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21572392}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- TIMELESS-interacting protein
- E3 ubiquitin-protein ligase RBX1
- Protein timeless homolog
- Ubiquitin-like protein NEDD8
Sequence:
MEPPMEPSGGEQEPGAVRFLDLPWEDVLLPHVLNRVPLRQLLRLQRVSRAFRSLVQLHLAGLRRFDAAQVGPQIPRAALARLLRDAEGLQELALAPCHEWLSDEDLVPVLARNPQLRSVALGGCGQLSRRALGALAEGCPRLQRLSLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAQRRGAGLRSLSLAVNANVGDAAVQELARNCPELHHLDLTGCLRVGSDGVRTLAEYCPVLRSLRVRHCHHVAESSLSRLRKRGVDIDVEPPLHQALVLLQDMAGFAPFVNLQV
Protein: Tryparedoxin peroxidase (Q4QF80)
Organism: Leishmania major
Interaction partners:
- Trypanothione synthetase
- Trypanothione reductase
- Tryparedoxin
- Tryparedoxin
Sequence:
MSCGNAKINSPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFSFVCPTEVIAFSDSVSRFNELNCEVLACSIDSEYAHLQWTLQDRKKGGLGTMAIPMLADKTKSIARSYGVLEESQGVAYRGLFIIDPHGMLRQITVNDMPVGRSVEEVLRLLEAFQFVEKHGEVCPANWKKGAPTMKPEPNASVEGYFSKL