wanglab/gogpt-training-data huggingface dataset:
Protein: Syntaxin-binding protein 1 (N-Sec1) (Protein unc-18 homolog 1) (Unc18-1) (Protein unc-18 homolog A) (Unc-18A) (p67) (P61763)
Organism: Bos taurus (Bovine)
Function: Participates in the regulation of synaptic vesicle docking and fusion through interaction with GTP-binding proteins (By similarity). Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61764}. Membrane; Peripheral membrane protein.
Interaction partners:
- Syntaxin-1A
- Syntaxin-1B
- Vesicle-associated membrane protein 2
- Amyloid beta precursor protein binding family A member 1.
- Synaptosomal-associated protein 25
- Syntaxin-3
- Syntaxin 2
- Regulating synaptic membrane exocytosis 1
- Synaptotagmin-1
- Ras-related protein Rab-3A
Sequence:
MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS
Protein: Uncharacterized protein C23H3.12c (O13942)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRIIALPLPNQRVFLHCYPSEYLAKKVTIHDKIINRIYKYWDSWSASKSYTKQKVVSLGNRILHATPYEENFLRAIAPVKKLNDTELHQTLYIEHPPNLESSTILAELNRSKQLQKTHTNYLIGNIIGLPLTIPFILIPLIPNIPGFYLCYRAYCNFRAIQGSIQLARVMSIENIQMQESEKLEKALKLFTNGDATPLNALIGHPDFVDRYKRAVAQEQRKSKIIK
Protein: TSC22 domain family protein 4 (TSC22-related-inducible leucine zipper protein 2) (Q9Y3Q8)
Organism: Homo sapiens (Human)
Function: Binds DNA and acts as a transcriptional repressor. Involved in the regulation of systematic glucose homeostasis and insulin sensitivity, via transcriptional repression of downstream insulin signaling targets such as OBP2A/LCN13 (By similarity). Acts as a negative regulator of lipogenic gene expression in hepatocytes and thereby mediates the control of very low-density lipoprotein release. May play a role in neurite elongation and survival (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9EQN3}. Cytoplasm {ECO:0000250|UniProtKB:Q9EQN3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9EQN3}. Synapse {ECO:0000250|UniProtKB:Q9EQN3}. Note=Localizes away from the nucleus to neurite processes and synaptic termini as cerebellar granular neurons differentiate (By similarity). Accumulates in the cytoplasm of differentiated Purkinje cells (By similarity). Localized to both the cytoplasm and nucleus in immature cerebellar granular neurons and atrophic Purkinje cells (By similarity). {ECO:0000250|UniProtKB:Q9EQN3}.
Interaction partners:
- Sperm acrosome developmental regulator
- Nuclear receptor-binding protein
- Nuclear receptor-binding protein 2
- TSC22 domain family protein 1
- TSC22 domain family protein 2
- LIM/homeobox protein Lhx4
- TSC22 domain family protein 3
Sequence:
MSGGKKKSSFQITSVTTDYEGPGSPGASDPPTPQPPTGPPPRLPNGEPSPDPGGKGTPRNGSPPPGAPSSRFRVVKLPHGLGEPYRRGRWTCVDVYERDLEPHSFGGLLEGIRGASGGAGGRSLDSRLELASLGLGAPTPPSGLSQGPTSWLRPPPTSPGPQARSFTGGLGQLVVPSKAKAEKPPLSASSPQQRPPEPETGESAGTSRAATPLPSLRVEAEAGGSGARTPPLSRRKAVDMRLRMELGAPEEMGQVPPLDSRPSSPALYFTHDASLVHKSPDPFGAVAAQKFSLAHSMLAISGHLDSDDDSGSGSLVGIDNKIEQAMDLVKSHLMFAVREEVEVLKEQIRELAERNAALEQENGLLRALASPEQLAQLPSSGVPRLGPPAPNGPSV
Protein: Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1) (Q9C0D5)
Organism: Homo sapiens (Human)
Function: May be a scaffold component in the postsynaptic density.
Subcellular location: Postsynaptic density {ECO:0000250}.
Interaction partners:
- Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3
- Alpha-internexin
- Disks large homolog 4
- Disks large homolog 1
- Disks large-associated protein 1
Sequence:
MLKAVLKKSREGGKGGKKEAGSDFGPETSPVLHLDHSADSPVSSLPTAEDTYRVSLAKGVSMSLPSSPLLPRQSHLVQSRVNKKSPGPVRKPKYVESPRVPGDAVIMPFREVAKPTEPDEHEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITIEDKNETMCTALSQGISPCSTLTSSTASPSTDSPCSTLNSCVSKTAANKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNKDGNLRLGVQKGVLHDRRADNCSPVAEEETTGSAESTLPKAESSAGDGPVPYSQGSSSLIMPRPNSVAATSSTKLEDLSYLDGQRNAPLRTSIRLPWHNTAGGRAQEVKARFAPYKPQDILLKPLLFEVPSITTDSVFVGRDWLFHQIEENLRNTELAENRGAVVVGNVGFGKTAIISKLVALSCHGSRMRQIASNSPGSSPKTSDPTQDLHFTPLLSPSSSTSASSTAKTPLGSISAENQRPREDAVKYLASKVVAYHYCQADNTYTCLVPEFVHSIAALLCRSHQLAAYRDLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTNLRNEQKIPEEEYIILIDGLNEAEFHKPDYGDTLSSFITKIISKFPAWLKLIVTVRANFQEIISALPFVKLSLDDFPDNKDIHSDLHAYVQHRVHSSQDILSNISLNGKADATLIGKVSSHLVLRSLGSYLYLKLTLDLFQRGHLVIKSASYKVVPVSLSELYLLQCNMKFMTQSAFERALPILNVALASLHPMTDEQIFQAINAGHIQGEQGWEDFQQRMDALSCFLIKRRDKTRMFCHPSFREWLVWRADGENTAFLCEPRNGHALLAFMFSRQEGKLNRQQTMELGHHILKAHIFKGLSKKTGISSSHLQALWIGYSTEGLSAALASLRNLYTPNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLLLEFGACLDGTSENGMTALCYAAAAGHMKLVCLLTKKGVRVDHLDKKGQCALVHSALRGHGDILQYLLTCEWSPGPPQPGTLRKSHALQQALTAAASMGHSSVVQCLLGMEKEHEVEVNGTDTLWGETALTAAAGRGKLEVCELLLGHGAAVSRTNRRGVPPLFCAARQGHWQIVRLLLERGCDVNLSDKQGRTPLMVAACEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAAIDQTDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTSVVVALLRKGAKLGNAAWAMATSKPDILIILLQKLMEEGNVMYKKGKMKEAAQRYQYALRKFPREGFGEDMRPFNELRVSLYLNLSRCRRKTNDFGMAEEFASKALELKPKSYEAFYARARAKRNSRQFVAALADLQEAVKLCPTNQEVKRLLARVEEECKQLQRSQQQKQQGPLPAPLNDSENEEDTPTPGLSDHFHSEETEEEETSPQEESVSPTPRSQPSSSVPSSYIRNLQEGLQSKGRPVSPQSRAGIGKSLREPVAQPGLLLQPSKQAQIVKTSQHLGSGQSAVRNGSMKVQISSQNPPPSPMPGRIAATPAGSRTQHLEGTGTFTTRAGCGHFGDRLGPSQNVRLQCGENGPAHPLPSKTKTTERLLSHSSVAVDAAPPNQGGLATCSDVRHPASLTSSGSSGSPSSSIKMSSSTSSLTSSSSFSDGFKVQGPDTRIKDKVVTHVQSGTAEHRPRNTPFMGIMDKTARFQQQSNPPSRSWHCPAPEGLLTNTSSAAGLQSANTEKPSLMQVGGYNNQAKTCSVSTLSASVHNGAQVKELEESKCQIPVHSQENRITKTVSHLYQESISKQQPHISNEAHRSHLTAAKPKRSFIESNV
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (p67) (p67eIF2) (Peptidase M) (O08663)
Organism: Mus musculus (Mouse)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm. Note=About 30% of expressed METAP2 associates with polysomes. {ECO:0000255|HAMAP-Rule:MF_03175}.
Interaction partners:
- Methionine aminopeptidase 1
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL14
- Sphingolipid delta
- Sphingolipid delta
- Small ribosomal subunit protein uS17
- sphingolipid 4-desaturase
- Small ribosomal subunit protein uS19
Sequence:
MAGVEQAASFGGHLNGDLDPDDREEGTSSTAEEAAKKKRRKKKKGKGAVSAVQQELDKESGALVDEVAKQLESQALEEKERDDDDEDGDGDADGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Protein: LexA repressor (EC 3.4.21.88) (A1B3Z0)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA repair protein RecN
- DNA polymerase IV
- DNA repair protein RadA
- DNA mismatch repair protein MutL
- UvrABC system protein A
- Heat-inducible transcription repressor HrcA
- Crossover junction endodeoxyribonuclease RuvC
- Indole-3-glycerol phosphate synthase
- Cyclic pyranopterin monophosphate synthase
Sequence:
MLTRKQIQLLEFIQARMARDGVPPSFDEMKLALDLRSKSGIHRLVTALEERGFIRRLPHRARALEIVRLPESLSKGPGFQPRVIEGTMPDRPAPLPRGAMEVSVSAIELPVMGRIAAGVPIEAISEISHHIAVPTTMLSGQDRHYALEVRGDSMIEAGINDGDVVVIREQNAAESGDIVVALVDGYEATLKRYRRKGNMIALEAANPAYETRVLPEDKVRIQGRLVGLIRSY
Protein: Eukaryotic translation initiation factor 3 subunit K (eIF3k) (Eukaryotic translation initiation factor 3 subunit 12) (eIF-3 p25) (Q9DBZ5)
Organism: Mus musculus (Mouse)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03010}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MAMFEQMRANVGKLLKGIDRYNPENLATLERYVETQAKENAYDLEANLAVLKLYQFNPAFFQTTVTAQILLKALTNLPHTDFTLCKCMIDQAHQEERPIRQILYLGDLLETCHFQAFWQALDENMDLLEGITGFEDSVRKFICHVVGITYQHIDRWLLAEMLGDLTDNQLKVWMSKYGWSADESGQVFICSQEESIKPKNIVEKIDFDSVSSIMASSQ
Protein: V-type proton ATPase subunit e 2 (V-ATPase subunit e 2) (Vacuolar proton pump subunit e 2) (Q91XE7)
Organism: Mus musculus (Mouse)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q5EB76}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5EB76}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit H
- V-type proton ATPase subunit F
- V-type proton ATPase 16 kDa proteolipid subunit c
- Renin receptor
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit G 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit G 2
Sequence:
MTAHSFALPVIIFTTFWGLIGIAGPWFVPKGPNRGVIITMLVATAVCCYLFWLIAILAQLNPLFGPQLKNETIWYVRFLWE
Protein: Uncharacterized protein (Q581B5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSVDHPGMLKHLLSENARLKALAAQPEHERILQDVLLTQLQRFFSDARQSVEDTVDKTSTPCSERSERREGAAGEESGVQRFSALVETLCILGTQNEELQRHMSDMQTKTVAALNEKVEALESERGSLKRRVEELEREVAAKGTTNTADEELTPPLMAELRSLRTSEELLRQQLQNVHERGEAAVAESEKLAKDGIRATMLLPRLLESVEEVRGALKLVESERDVLRLQLQELKERQSVQHTLCEAQLREQVALSQSSVQHLLSRISVLETREAQARDEVAACMQTIERQQGIIQNLQACQGVAVETLASKRRRLESEIFDNPDSVRRDLVTFWCEGREELEQLREEVQKLRSKVQQLKPLKEKLGQLERNRSAVATRIVDLADEVSRVREENQKLRVQYSGLEVERDYLRGSLAAVISQHMQEEELSSCCAAVREAAARSAASSVSAVVDPQVIQQTMRQARELQSEVAQLGKQKEKLHRCISLREKRLAALVAREAVQCPAAAAQEARPAVENGSVMHTVSWAEAHAVDVLSSLEEGVATESGLQRQGVLVAMQTRLDAAEREVAVCKQQLEASDTAREEAEARYSAARAELQATLSARETAMTEMHHTNTVLLQSVERLRSEQKQLRQSYYDLAAFTENLASALEVMLLFVQGETNLAASVGRLLLQHRSEICELTQQAADGWEMRRDDVQRVVESIDRMCEYVRQSTEQNQREQALNSVTHLRRLTDAVKQQEGRLKEMQKNFTEVCQKLGESLATRVAEAQQQAEGLWKKRLGMLQEERHRLQGQLKAEKDLLSRMECLMIPGAMTQPTLTAAEATVAHAVINPGTDAPELPDQERNEVVDVINRLLAAVSQPATTEEDVPNPLLLPAGQCKRGGSGECEAELVEEEGQGGERGERDVLETVSGITKV
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FYA5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- RP41
- Large ribosomal subunit protein uL23
- 40S ribosomal protein S8
- Candida glabrata strain CBS138 chromosome A complete sequence
- Small ribosomal subunit protein eS21
- Candida glabrata strain CBS138 chromosome M complete sequence
- Small ribosomal subunit protein eS6
- 60S ribosomal protein L36
- L21
- 60S acidic ribosomal protein P0
Sequence:
MANLRTQKRLAASVIGAGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSRSRTREHALSKRNGRHTGYGKRKGTKEARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKEAKGNAFKHKRALVEHIIQAKADAQREKALSEQAEARRMKNRAARERRAQRVAEKREALLKESA
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.30) (NAD(+) ADP-ribosyltransferase) (ADPRT) (Poly[ADP-ribose] synthase) (Protein ADP-ribosyltransferase Parp) (EC 2.4.2.-) (P35875)
Organism: Drosophila melanogaster (Fruit fly)
Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (By similarity). Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of CG1218/HPF1 (By similarity). Following interaction with CG1218/HPF1, catalyzes serine ADP-ribosylation of target proteins; CG1218/HPF1 conferring serine specificity by completing the Parp active site (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:12183365, ECO:0000269|PubMed:17827147}. Chromosome {ECO:0000269|PubMed:17827147}. Nucleus, nucleolus {ECO:0000269|PubMed:12183365}. Note=Highly enriched in nucleoli, heterochromatic chromosomal regions, and diverse euchromatic sites in the cells of most embryonic and adult tissues (PubMed:12183365). Localizes in chromatin and nucleoplasm (PubMed:17827147). {ECO:0000269|PubMed:12183365, ECO:0000269|PubMed:17827147}.
Interaction partners:
- Poly
- AT03047p
- Caspase drICE
- ATP-dependent DNA helicase II subunit 2
- Histone PARylation factor 1-like
- Breast cancer type 2 susceptibility protein homolog
- FI04011p
- ATP-dependent DNA helicase 2 subunit 1
- DNA ligase 4
- Flap endonuclease 1
Sequence:
MDIELPYLAEYARTGRATCKGCKSTISKDTLRIAVMVQSAFHDAKVPNWFHKTCFFKNQRPSSVGDIQNIGNLRFADQKELTDLVENIQEVISAQLGKKRSKAFNLALKDFGIEYAKSSRSTCRGCEQKINKDLVRLRKTVYDTEVGMKYGGQPLWHHLECFAQLRSELGWFASGEDMPGFQSLADDDQAKVKNAIPPIKSEELPDTKRAKMELSDTNEEGEKKQRLKDQNDAYFRFRDDIKNKMKKKDIDILLKFNNQQPVTGDTEKLFDQTADLLTFGAIESCSECNSCQFIVNKSGYICNGNHSEWTKCNKLLKEPTRSACIVPKELKALYNFLNTVKEIPSTRIFNNFPPNKSTFSRSLLKTNKNNDVLVRPTIPRISPPLYNLKFSIIGLKNQHKELRKRIENLGGKFEVKISENTIAIISTELEIQKKSTRMKFAEELGIHIVPIEFLDFVEADTEGAIKYINSTCICSWGTDPKSRIPKETTKSLNSNSIYTKSMPVSRTFKVKDGLAVDPDSGLEDIAHVYVDSNNKYSVVLGLTDIQRNKNSYYKVQLLKADKKEKYWIFRSWGRIGTNIGNSKLEEFDTSESAKRNFKEIYADKTGNEYEQRDNFVKRTGRMYPIEIQYDDDQKLVKHESHFFTSKLEISVQNLIKLIFDIDSMNKTLMEFHIDMDKMPLGKLSAHQIQSAYRVVKEIYNVLECGSNTAKLIDATNRFYTLIPHNFGVQLPTLIETHQQIEDLRQMLDSLAEIEVAYSIIKSEDVSDACNPLDNHYAQIKTQLVALDKNSEEFSILSQYVKNTHASTHKSYDLKIVDVFKVSRQGEARRFKPFKKLHNRKLLWHGSRLTNFVGILSHGLRIAPPEAPPTGYMFGKGIYFADMVSKSANYCCTSQQNSTGLMLLSEVALGDMMECTSAKYINKLSNNKHSCFGRGRTMPDPTKSYIRSDGVEIPYGETITDEHLKSSLLYNEYIVYDVAQVNIQYLFRMEFKYSY
Protein: Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Q05028)
Organism: Rattus norvegicus (Rat)
Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity).
Subcellular location: Secreted {ECO:0000250}. Note=Released by platelets upon wounding. {ECO:0000250}.
Interaction partners:
- Platelet-derived growth factor receptor beta
- Platelet-derived growth factor receptor alpha
- Platelet-derived growth factor subunit A
- Platelet-derived growth factor C
- Platelet-derived growth factor D
- Pro-epidermal growth factor
- Insulin-like growth factor 1
- Receptor protein-tyrosine kinase
- Protransforming growth factor alpha
- Insulin-1
Sequence:
LPLCCYLRLVSAEGDPIPEELYEMLSDHSIRSFDDLQRLLHRDSVDEDGAELDLNMTRAHSGVESESSSRGRRSLGSLAAAEPAVIAECKTRTEVFQISRNLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRASQVQMRPVQVRKIEIVRKKPVFKKATVTLEDHLACKCETVVTPRPVTRSPGTSREHRAKTPQTRVTVRTVRIRRPPKGKHRKFKHTHDKK
Protein: ATP synthase F(0) complex subunit B1, mitochondrial (ATP synthase peripheral stalk-membrane subunit B1) (ATP synthase proton-transporting mitochondrial F(0) complex subunit B1) (ATP synthase subunit B1) (ATPase subunit B1) (Q20053)
Organism: Caenorhabditis elegans
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the subunits of the catalytic subcomplexes relative to the rotary elements (Probable). Plays a role in germline development.
Subcellular location: Mitochondrion {ECO:0000255|RuleBase:RU368017, ECO:0000269|PubMed:17223323}. Mitochondrion inner membrane {ECO:0000255|RuleBase:RU368017}.
Interaction partners:
- Probable ATP synthase subunit g 1, mitochondrial
- F-ATPase gamma subunit
- ATP synthase subunit d
- Probable ATP synthase subunit g 2, mitochondrial
- Oligomycin sensitivity conferral protein
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ATP synthase-coupling factor 6
- ATP synthase F
- ATP synthase c subunit
Sequence:
MSLSRLSSPQTFSRVFIVARGAATGHAVAPSSDNSIGYFEKIAYRFKGIPLPTETEAPKSMFDACNKEWSAPELLPSVPKDFKEHPDRDLTNYPYPSRPMYPPKTRLLMMPDSWFTAFQKVTGTSGPYLFFGGLFAFLVNKELWVFEEQGHMTVGWILFYLLVSRTAGYKIDAGLYKDYQERVGFFKGLIQEDLKEAVDFRKTSAAQTASFAALKEGMPTSLKDSMQLQLEAAYRKNVQTISNEIKRRIEYLKETEETKARFERDQLLKLINDSVEKQVSQKDFQEKFLQNAIQQLKGIAV
Protein: Histidine rich calcium binding protein (A0A8I5ZZ96)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGFQEPWLYSCLLWATVAILLVPPVVTQELRGTGLGLGNWNNNAGIPGSSEDLSTEYGHHIHSHGAYQGEKDRHHREEDEDFSREYGHQVQDHRYPGHEVGEENVSEEVFRGHVRQLHGHHKPNSEDLGDSAESHFPRQQSHNREEEDGVVSGEDHRHIPRHDHHGNEEEDDDGEEEERVGVMENSDDKHQAHGHHSHSKERDGLHHAHSHRHQGHHDEDDDDEDGVSTEGEHQAHRYQDHDEEDDDDSDEESHAHRLQGQEDENDDEDGDSSENGHQTQDHQGHKEQDDDDDEEEEEEEEEEEEEEEEEEEEEEDDDDDSTEHRHRHQTQGHRKGKDEDESDEDDHVTRHGRRGHEDEDDDDDDDDDDDDDNDGGSTENVHQAHRHRGHEHEDDGDDSEEDYHHVPSHGHQSHQNEEEEDEAVSTEHWHQSPRHAHHDLGRENQEEATVKYSRHVASHRPQGHSAEEDSLEDSTNEVPGHHHHRVSRDGDEDISTEFGHKAPRHRLQDQDEWTRQGHGKSVQEDIGHQPLQPTGPGSGESRKEDDHSSQEGDEDLKQRQEAHSEEEEEEEEGHGLPMSLEDEEEEEKDKKESKGDRAAVSAPLSHHRKHDDDDDGDGDDDDDDNDDDDEILEENLLPFTIIPNPLAGREVAREGSSEEESREVTGQQDAQEYENYQPGSLCGYCSFCNRCSECESCHCDEENMGEHCDQCQHCQFCYLCPLVCDTLCTPGSYVDYFSSSVYQ
Protein: Adenosylhomocysteinase (EC 3.13.2.1) (Q803T5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Betaine--homocysteine S-methyltransferase 1
- Cystathionine beta-synthase
- Cystathionine beta-synthase
- Zgc:172121.
- Cystathionine gamma-lyase
- Cystathionase
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine aminotransferase 1
- Si:ch73-97h19.2.
- Methionine synthase
Sequence:
MSEKLPFKVADISLAEWGRKAIEIAENEMPGLMKMRELYGQSKPLKGARIAGCLHMTLQTAVLIETLTALGAEVQWSSCNIFSTQDHAAAAIAKTGVPVYAWKGETDEEYVWCIEQTIYFKDGQPLNMILDDGGDLTNLVHQKYPKLLAGIKGISEETTTGVHNLYKMLKSGELKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCVQALRGFGARVIVTEIDPINALQAAMEGYEVTTMDEACKEGNIFVTTTGCEDILLGRHFEHMKDDSIVCNIGHFDCEIDMKWLNEHAAKKINIKPQVDRYRMKNGRHIIVLAEGRLVNLGCAMGHPSFVMSNSFTNQVLAQIELWKNNSKYPLGVYFLPKKLDEEVAAAHLDKLGVKLTKLTEKQAKYLGLPSEGPFKPDHYRY
Protein: ADP-ribosylation factor-like protein 5A (P51646)
Organism: Rattus norvegicus (Rat)
Function: Lacks ADP-ribosylation enhancing activity.
Interaction partners:
Sequence:
MGILFTRIWRLFNHQEHKVIIVGLDNAGKTTILYQFSMNEVVHTSPTIGSNVEEIVVNNTRFLMWDIGGQESLRSSWNTYYTNTEFVIVVVDSTDRERISVTREELYKMLAHEDLRKAGLLIFANKQDVKECMTVAEISQFLKLTSIKDHQWHIQACCALTGEGLCQGLEWMMSRLKIR
Protein: Isocitrate dehydrogenase [NAD] subunit, mitochondrial (Q91VA7)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU361266}.
Interaction partners:
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Aconitate hydratase, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Succinate--CoA ligase subunit alpha, mitochondrial
- Cytoplasmic aconitate hydratase
- 2-oxoglutarate dehydrogenase-like, mitochondrial
Sequence:
MAALSNVRWLTRAVLAARNSGAWRGLGTSTAHAASQSQAQDVRVEGAFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFKEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIYTPMEYKGELASYDMQLRRKLDLFANVVHVKSLPGYKTRHNNLDLVIIREQTEGEYSSLEHESAKGVIECLKIVTRTKSQRIAKFAFDYATKKGRSKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSATNMLRHLNLEYHSSMIADAVKKVIKAGKVRTRDMGGYSTTTDFIKSVIGHLHPHGG
Protein: Zinc finger protein 596 (Q8TC21)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPSPDSMTFEDIIVDFTQEEWALLDTSQRKLFQDVMLENISHLVSIGKQLCKSVVLSQLEQVEKLSTQRISLLQGREVGIKHQEIPFIQHIYQKGTSTISTMRSHTQEDPFLCNDLGEDFTQHIALTQNVITYMRTKHFVSKKFGKIFSDWLSFNQHKEIHTKCKSYGSHLFDYAFIQNSALRPHSVTHTREITLECRVCGKTFSKNSNLRRHEMIHTGEKPHGCHLCGKAFTHCSDLRKHERTHTGEKPYGCHLCGKAFSKSSNLRRHEMIHTREKAQICHLCGKAFTHCSDLRKHERTHLGDKPYGCLLCGKAFSKCSYLRQHERTHNGEKPYECHLCGKAFSHCSHLRQHERSHNGEKPHGCHLCGKAFTESSVLKRHERIHTGEKPYECHVCGKAFTESSDLRRHERTHTGEKPYECHLCGKAFNHSSVLRRHERTHTGEKPYECNICGKAFNRSYNFRLHRRVHTGEKPYVCPLCGKAFSKFFNLRQHERTHTKKAMNM