wanglab/gogpt-training-data huggingface dataset:
Protein: Opticin (Oculoglycan) (Q920A0)
Organism: Mus musculus (Mouse)
Function: Inhibits angiogenesis in the vitreous humor of the eye, and therefore represses neovascularization. Binds collagen fibrils (By similarity). May be involved in collagen fiber organization via regulation of other members of the small leucine-rich repeat proteoglycan superfamily.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P58874}.
Interaction partners:
- Collagenase 3
- Matrilysin
- 72 kDa type IV collagenase
- Somatotropin
- Amelogenin, X isoform
Sequence:
MKFLAFLSLLSLVLQKAETASLLGEREREEQSPEEGDTYASLYVGNHTLSIEDYNEVIDLSNYEELADYGDQIPEAKISNLTLPTRTSPTSTVAQKTLSPNLTMAVPTTTGLLNSQSSHGLPTCLVCVCLGSSVYCDDADLENIPPLPQMTTYLYARFNHISHIQAGDFKGLTKLRRIDLSGNSISSIHNDALRLLPALQDLILPENQLAALPVLPSGIEFLDVRLNRLQSSGIQPEAFVALKKLQFLYLANNMLDSIPGPLPLSLRSLHLQNNMIETMESDTFCDTGEHRHERRQLEDIRLDGNPINLSLFPEAYFCLPRLPVGHFT
Protein: Cysteine desulfuration protein SufE (P76194)
Organism: Escherichia coli (strain K12)
Function: Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process. Together with the SufBCD complex, it thereby enhances up to 50-fold, the cysteine desulfurase activity of SufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of SufS.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Iron-sulfur cluster assembly protein SufB
- Cysteine desulfurase
- Iron-sulfur cluster assembly protein SufD
- Probable ATP-dependent transporter SufC
- Cysteine desulfurase CsdA
- Iron-sulfur cluster assembly protein SufA
Sequence:
MALLPDKEKLLRNFLRCANWEEKYLYIIELGQRLPELRDEDRSPQNSIQGCQSQVWIVMRQNAQGIIELQGDSDAAIVKGLIAVVFILYDQMTPQDIVNFDVRPWFEKMALTQHLTPSRSQGLEAMIRAIRAKAAALS
Protein: Aquaporin-1 (AQP-1) (Aquaporin-CHIP) (Channel-like integral membrane protein of 28 kDa) (Urine water channel) (P29972)
Organism: Homo sapiens (Human)
Function: Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23219802}; Multi-pass membrane protein {ECO:0000269|PubMed:7507481}.
Interaction partners:
- Ammonium transporter Rh type A
- Band 3 anion transport protein
- Glycophorin-A
- Ankyrin-1
- Blood group Rh
- Protein 4.2
- Aquaporin-11
- Putative aquaporin-12A
- Aquaporin-9
- Aquaporin-7
Sequence:
MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK
Protein: Pyridoxal 5'-phosphate synthase subunit PDX1.1 (AtPDX1.1) (AtPDX1;2) (PLP synthase subunit PDX1.1) (EC 4.3.3.6) (HEVER-like protein) (O80448)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16157873}.
Interaction partners:
- Probable pyridoxal 5'-phosphate synthase subunit PDX2
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Pyridoxal kinase
- Pyridoxal 5'-phosphate synthase subunit PDX1.3
- Pyridoxal 5'-phosphate synthase-like subunit PDX1.2
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 2
- Inorganic pyrophosphatase 1
- Inorganic pyrophosphatase 2
- Thiamine phosphate phosphatase-like protein
- RNA polymerase II degradation factor-like protein
Sequence:
MAGTGVVAVYGEGAMTETKQKSPFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPEMIKEIKNAVTIPVMAKARIGHFVEAQILEAIGVDYVDESEVLTLADEDNHINKHNFKIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVNGAIRLLRSMDDDEVFTYAKKIAAPYDLVVQTKELGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGVFKSGDPVKRAKAIVQAVTNYRDAAVLAEVSCGLGEAMVGLNLDDKVERFASRSE
Protein: Homeobox protein EMX1 (Empty spiracles homolog 1) (Empty spiracles-like protein 1) (Q04741)
Organism: Homo sapiens (Human)
Function: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:20887964}. Cytoplasm {ECO:0000269|PubMed:20887964}. Note=Might be shuttling between the nucleus and the cytoplasm.
Interaction partners:
- T-box brain protein 1
- Forkhead box protein G1
- Neurogenic differentiation factor 6
Sequence:
MCLAGCTPRKAAAPGRGALPRARLPRTAPAAATMFQPAAKRGFTIESLVAKDGGTGGGTGGGGAGSHLLAAAASEEPLRPTALNYPHPSAAEAAFVSGFPAAAAAGAGRSLYGGPELVFPEAMNHPALTVHPAHQLGASPLQPPHSFFGAQHRDPLHFYPWVLRNRFFGHRFQASDVPQDGLLLHGPFARKPKRIRTAFSPSQLLRLERAFEKNHYVVGAERKQLAGSLSLSETQVKVWFQNRRTKYKRQKLEEEGPESEQKKKGSHHINRWRIATKQANGEDIDVTSND
Protein: Vomeronasal type-1 receptor 50 (Pheromone receptor VN2) (Vomeronasal receptor 2) (Vomeronasal type-1 receptor A5) (Vomeronasal type-1 receptor B1) (Q9EP51)
Organism: Mus musculus (Mouse)
Function: Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSKANLLHTDNNMKITLFSEVSVGISANSILFVVHLCKLLHENKPKPIDLYIAFFSITQLMLLITMGLIAVDMFMPWGRWDSTTCQSLIYLHRLLRGLTFCATCLLNVLWTITLSPRSSCLTKFKHKSPHHISGAFLFFCVLYMSFSSHLLVSIIATFNSTSDNFLYVTQSCSILPVSYSRTSILSTMMTMREAFLIGLMALSSGYVVVLLWRHKKQARHLHSTSLSSKASPEQRATSTIMLLMGFFVVLYILDTVIFQARLKFKDVSTFFCVKIIISHSYATFSPFVFICNDKYMIKFVTSMCGRIVNV
Protein: Beta-amyrin 28-monooxygenase (EC 1.14.14.126) (Beta-amyrin 28-oxidase) (Cytochrome P450 716A15) (VvCYP716A15) (F6H9N6)
Organism: Vitis vinifera (Grape)
Function: Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolic acid. Catalyzes the carboxylation of alpha-amyrin and lupeol at the C-28 position to form ursolic acid and betulinic acid respectively. May be involved in saponin biosynthesis in fruit skin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEVFFLSLLLIFVLSVSIGLHLLFYKHRSHFTGPNLPPGKIGWPMVGESLEFLSTGWKGHPEKFIFDRISKYSSEVFKTSLLGEPAAVFAGAAGNKFLFSNENKLVHAWWPSSVDKVFPSSTQTSSKEEAKKMRKLLPQFFKPEALQRYIGIMDHIAQRHFADSWDNRDEVIVFPLAKRFTFWLACRLFMSIEDPAHVAKFEKPFHVLASGLITVPIDLPGTPFHRAIKASNFIRKELRAIIKQRKIDLAEGKASQNQDILSHMLLATDEDGCHMNEMEIADKILGLLIGGHDTASAAITFLIKYMAELPHIYEKVYEEQMEIANSKAPGELLNWDDVQKMRYSWNVACEVMRLAPPLQGAFREAITDFVFNGFSIPKGWKLYWSANSTHKSPECFPQPENFDPTRFEGDGPAPYTFVPFGGGPRMCPGKEYARLEILVFMHNVVKRFKWDKLLPDEKIIVDPMPMPAKGLPVRLHPRKP
Protein: Mitogen-activated protein kinase kinase kinase 11 (EC 2.7.11.25) (Mixed lineage kinase 3) (Q66HA1)
Organism: Rattus norvegicus (Rat)
Function: Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Location is cell cycle dependent. {ECO:0000250}.
Interaction partners:
- Cell division control protein 42 homolog
- Dual specificity mitogen-activated protein kinase kinase 7
- C-Jun-amino-terminal kinase-interacting protein 2
- C-Jun-amino-terminal kinase-interacting protein 1
- Ras-related C3 botulinum toxin substrate 1
- C-Jun-amino-terminal kinase-interacting protein 3
- Mitogen-activated protein kinase kinase kinase kinase
- Glutamate receptor ionotropic, kainate 2
- Disks large homolog 4
- E3 ubiquitin-protein ligase SH3RF1
Sequence:
MEPLKNLFLKSPLGSWNGSGSGGGGGSGGVRPEGSPKATAAYANPVWTALFDYEPNGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIEGDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGAGDSPTFPRFRAIQLEPAESGQTWGRQSPRRLDDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSPEPEEPRRSGPTERGNSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGLSRERGESPTAPPPAQMASPCPPDLPSTPLIHLSQATPDARGPLTPAPLLLDLGVSSGQPSAKSPRREETRGRTVSPPPGISRSAPGTPGTPRSPPLGLISRPRPSPLRNRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFRGGSQDCRTQTKDVGAQAPWAPEAGP
Protein: Sphingosine 1-phosphate receptor 5 (S1P receptor 5) (S1P5) (Endothelial differentiation G-protein-coupled receptor 8) (Nerve growth factor-regulated G-protein-coupled receptor 1) (NRG-1) (Sphingosine 1-phosphate receptor Edg-8) (S1P receptor Edg-8) (Q9JKM5)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/O)alpha and G(12) subclass of heteromeric G-proteins. Displays antiproliferative effects in transfected CHO-K1 and HEK293 cells.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- RCG53912, isoform CRA_a.
- Sphingosine kinase 1
- SPNS lysolipid transporter 2, sphingosine-1-phosphate
- Membrane-bound transcription factor site-1 protease
Sequence:
MESGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAAVCLAVCAFIVLENLAVLLVLGRHPRFHAPMFLLLGSLTLSDLLAGAAYATNILLSGPLTLRLSPALWFAREGGVFVALAASVLSLLAIALERHLTMARRGPAPAASRARTLAMAVAAWGLSLLLGLLPALGWNCLGRLEACSTVLPLYAKAYVLFCVLAFLGILAAICALYARIYCQVRANARRLRAGPGSRRATSSSRSRHTPRSLALLRTLSVVLLAFVACWGPLFLLLLLDVACPARACPVLLQADPFLGLAMANSLLNPIIYTFTNRDLRHALLRLLCCGRGPCNQDSSNSLQRSPSAVGPSGGGLRRCLPPTLDRSSSPSEHSCPQRDGMDTSCSTGSPGAATANRTLVPDATD
Protein: NAD(+) hydrolase SARM1 (NADase SARM1) (hSARM1) (EC 3.2.2.6) (NADP(+) hydrolase SARM1) (EC 3.2.2.-) (Sterile alpha and Armadillo repeat protein) (Sterile alpha and TIR motif-containing protein 1) (Sterile alpha motif domain-containing protein 2) (MyD88-5) (SAM domain-containing protein 2) (Tir-1 homolog) (HsTIR) (Q6SZW1)
Organism: Homo sapiens (Human)
Function: NAD(+) hydrolase, which plays a key role in axonal degeneration following injury by regulating NAD(+) metabolism. Acts as a negative regulator of MYD88- and TRIF-dependent toll-like receptor signaling pathway by promoting Wallerian degeneration, an injury-induced form of programmed subcellular death which involves degeneration of an axon distal to the injury site. Wallerian degeneration is triggered by NAD(+) depletion: in response to injury, SARM1 is activated and catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR), cyclic ADPR (cADPR) and nicotinamide; NAD(+) cleavage promoting cytoskeletal degradation and axon destruction. Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules. Can activate neuronal cell death in response to stress. Regulates dendritic arborization through the MAPK4-JNK pathway (By similarity). Involved in innate immune response: inhibits both TICAM1/TRIF- and MYD88-dependent activation of JUN/AP-1, TRIF-dependent activation of NF-kappa-B and IRF3, and the phosphorylation of MAPK14/p38.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20306472}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PDS3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6PDS3}. Synapse {ECO:0000250|UniProtKB:Q6PDS3}. Mitochondrion {ECO:0000269|PubMed:20306472, ECO:0000269|PubMed:22145856}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q6PDS3}.
Interaction partners:
- Toll-like receptor 4
- TIR domain-containing adapter molecule 1
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 3
- Toll/interleukin-1 receptor domain-containing adapter protein
- TNF receptor-associated factor 6
- TIR domain-containing adapter molecule 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Interferon regulatory factor 3
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
Sequence:
MVLTLLLSAYKLCRFFAMSGPRPGAERLAVPGPDGGGGTGPWWAAGGRGPREVSPGAGTEVQDALERALPELQQALSALKQAGGARAVGAGLAEVFQLVEEAWLLPAVGREVAQGLCDAIRLDGGLDLLLRLLQAPELETRVQAARLLEQILVAENRDRVARIGLGVILNLAKEREPVELARSVAGILEHMFKHSEETCQRLVAAGGLDAVLYWCRRTDPALLRHCALALGNCALHGGQAVQRRMVEKRAAEWLFPLAFSKEDELLRLHACLAVAVLATNKEVEREVERSGTLALVEPLVASLDPGRFARCLVDASDTSQGRGPDDLQRLVPLLDSNRLEAQCIGAFYLCAEAAIKSLQGKTKVFSDIGAIQSLKRLVSYSTNGTKSALAKRALRLLGEEVPRPILPSVPSWKEAEVQTWLQQIGFSKYCESFREQQVDGDLLLRLTEEELQTDLGMKSGITRKRFFRELTELKTFANYSTCDRSNLADWLGSLDPRFRQYTYGLVSCGLDRSLLHRVSEQQLLEDCGIHLGVHRARILTAAREMLHSPLPCTGGKPSGDTPDVFISYRRNSGSQLASLLKVHLQLHGFSVFIDVEKLEAGKFEDKLIQSVMGARNFVLVLSPGALDKCMQDHDCKDWVHKEIVTALSCGKNIVPIIDGFEWPEPQVLPEDMQAVLTFNGIKWSHEYQEATIEKIIRFLQGRSSRDSSAGSDTSLEGAAPMGPT
Protein: Scarecrow-like protein 14 (AtSCL14) (GRAS family protein 2) (AtGRAS-2) (Q9XE58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18500650}.
Interaction partners:
- Transcription factor TGA2
- Protein PAT1 homolog
- Transcription factor TGA6
- Transcription factor TGA5
- Protein METHYLENE BLUE SENSITIVITY 1
- Haloacid dehalogenase-like hydrolase domain-containing protein At4g39970
- Glutaredoxin-C9
Sequence:
MGSYPDGFPGSMDELDFNKDFDLPPSSNQTLGLANGFYLDDLDFSSLDPPEAYPSQNNNNNNINNKAVAGDLLSSSSDDADFSDSVLKYISQVLMEEDMEEKPCMFHDALALQAAEKSLYEALGEKYPSSSSASSVDHPERLASDSPDGSCSGGAFSDYASTTTTTSSDSHWSVDGLENRPSWLHTPMPSNFVFQSTSRSNSVTGGGGGGNSAVYGSGFGDDLVSNMFKDDELAMQFKKGVEEASKFLPKSSQLFIDVDSYIPMNSGSKENGSEVFVKTEKKDETEHHHHHSYAPPPNRLTGKKSHWRDEDEDFVEERSNKQSAVYVEESELSEMFDKILVCGPGKPVCILNQNFPTESAKVVTAQSNGAKIRGKKSTSTSHSNDSKKETADLRTLLVLCAQAVSVDDRRTANEMLRQIREHSSPLGNGSERLAHYFANSLEARLAGTGTQIYTALSSKKTSAADMLKAYQTYMSVCPFKKAAIIFANHSMMRFTANANTIHIIDFGISYGFQWPALIHRLSLSRPGGSPKLRITGIELPQRGFRPAEGVQETGHRLARYCQRHNVPFEYNAIAQKWETIQVEDLKLRQGEYVVVNSLFRFRNLLDETVLVNSPRDAVLKLIRKINPNVFIPAILSGNYNAPFFVTRFREALFHYSAVFDMCDSKLAREDEMRLMYEKEFYGREIVNVVACEGTERVERPETYKQWQARLIRAGFRQLPLEKELMQNLKLKIENGYDKNFDVDQNGNWLLQGWKGRIVYASSLWVPSSS
Protein: L,D-transpeptidase 1 (LDT 1) (EC 2.3.2.-) (Ldt(Mt1)) (O53638)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems. Is thought to play a role in adaptation to the nonreplicative state of M.tuberculosis.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Probable hydrogen peroxide-inducible genes activator
Sequence:
MRRVVRYLSVVVAITLMLTAESVSIATAAVPPLQPIPGVASVSPANGAVVGVAHPVVVTFTTPVTDRRAVERSIRISTPHNTTGHFEWVASNVVRWVPHRYWPPHTRVSVGVQELTEGFETGDALIGVASISAHTFTVSRNGEVLRTMPASLGKPSRPTPIGSFHAMSKERTVVMDSRTIGIPLNSSDGYLLTAHYAVRVTWSGVYVHSAPWSVNSQGYANVSHGCINLSPDNAAWYFDAVTVGDPIEVVG
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial (H0YIV9)
Organism: Homo sapiens (Human)
Interaction partners:
- Glutamyl-tRNA
Sequence:
XSSGAHGEEGSARMWKTLTFFVALPGVAVSMLNVYLKSHHGEHERPEFIAYPHLRIRTKGSGRITAAVIEHLERLALVDFGSREAVARLEKAIAFADRLRAVDTDGVEPMESVLEDRCLYLRSDNVVEGNCADELLQNSHRVVEEYFVAPPGNISLPKLDEQEPFPHS
Protein: Inner kinetochore subunit mis17 (CENP-U homolog) (Constitutive centromere-associated network protein mis17) (Sim4 complex subunit mis17) (O94643)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore.
Interaction partners:
- Inner kinetochore subunit mis15
- Inner kinetochore subunit mis6
- Inner kinetochore subunit fta7
- Inner kinetochore subunit mal2
- Inner kinetochore subunit fta2
- Inner kinetochore subunit fta6
- Inner kinetochore subunit fta3
- Inner kinetochore subunit fta4
- Inner kinetochore subunit fta1
- Inner kinetochore subunit cnl2
Sequence:
MENNSHNVDERRAARMRGAERYKIQNVEFSLDQNLLANLESSTSSSTRSSPASNQQNLEIVSQSEAYHKISDLDDSTSIFSISDQENILERRISEEVVRENSVSSIENVSSSAVARETQSSANILVKDNHFFSHKQKKIQRESIPFHKRDNIETSDAYSSSILENSPPNKVQRLSSLDSSQDSFQEEHPGNVTGTTFSSQAPEERIASPISTSSPESLTNQSSSLQSSLQTSSMAPRNLLDQSTEKDIVVGASDELVRIELTKLSKEAGGSKTLNELDAVQQFFQEFIKENEPLEPYVVKVKNAFVEQVSIRLLELIDLLDANRILSTACKKAANEKLAVQRDLSKLREDRLSVQRKKIQLRNEYIKLSHQQNFLDDIDDFFSQCETVKNELENVTTTPNSTEAFSEINEYASALSKNYGLESQLVELQSLLTQFYQKFLS
Protein: Histone H3, putative (Q4GYX7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Histone H4
- Histone H4
- Histone H2A
- Histone H2A
- SET domain-containing protein
- ATP synthase subunit beta
- Histone H2B
- SET domain-containing protein
- Uncharacterized protein
- Histone H2B
Sequence:
MSRTKETARTKKTITSKKSKKASKGSDAASGVKTAQRRWRPGTVALREIRQFQRSTDLLLQKAPFQRLVREVSGAQKEGLRFQSSAILAAQEATESYIVSLLADTNRACIHSGRVTIQPKDIHLALCLRGERA
Protein: ATP synthase subunit d, mitochondrial (ATPase subunit d) (Q9FT52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit O, mitochondrial
- ATP synthase subunit 9
- ATP synthase subunit delta, chloroplastic
- ATPase, F1 complex, OSCP/delta subunit protein
- ATP synthase subunit beta-2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- ATP synthase subunit alpha
Sequence:
MSGAGKKIADVAFKASRTIDWDGMAKVLVTDEARREFSNLRRAFDEVNTQLQTKFSQEPEPIDWDYYRKGIGAGIVDKYKEAYDSIEIPKYVDKVTPEYKPKFDALLVELKEAEQKSLKESERLEKEIADVQEISKKLSTMTADEYFEKHPELKKKFDDEIRNDNWGY
Protein: Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase)] (Q89E26)
Organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)
Interaction partners:
- Pyrroline-5-carboxylate reductase
- Glutamate 5-kinase
- Gamma-glutamyl phosphate reductase
- Glutamate synthase large chain
- Blr3010 protein
- Blr7995 protein
- Glutamine synthetase
- Blr2084 protein
- Glutamine synthetase
- Bll1069 protein
Sequence:
MPNIPPPFTAPYAPDDAEIAARLLPASHLSPPQEARIHRTATRLIEAIRKRDDRLGGVEDMLREFALSTKEGLALMVLAEALLRVPDARTADQFIEDKLGEGDFIHHETKSTAFLVNASAWALGLSARVIQPGETPDGTIGRLVKRLGAPAVRTATRQAMRLMGNHFVLGETIEQALERGKPRSGQKTRYSFDMLGEGARTAADARRYFDAYASAIETIGKAAGNHALPDRPGISVKLSALHPRFEAISRARVMVELVPQLLDLAQRAKAHDLNFTVDAEEADRLELSLDVIAATLADPSLKGWDGFGLAIQAYQKRASAVIDYVDALARAHDRKLMVRLVKGAYWDTEIKRAQERGLDGYPVFTRKAMTDLNYVACASKLLALRPRIFPQFATHNALTVATVLEMAEGSSGFEFQRLHGMGEALYEQLAKDHADIAYRTYAPVGSHRDLLAYLVRRLLENGANSSFVAQAADYRVPVPALLQRPADAIVRPQAAAHPRIPLPCDLFAPERRNSRGVEFGARTALDQLLTDVKAETGDLKPIADATPDQAHAAVAAARAGFAGWSRTPAGIRAAALEQAAHLLESRSAHFIALLQREGGKTLDDALSELREAADFCRYYAAQGRKLFGSETAMPGPTGESNALTMRGRGVFVAISPWNFPLAIFLGQVTAALMAGNSVVAKPAEQTPRIAREAVALLHEAGIPKSALYLVTGDGRIGAALTAHPDIAGVVFTGSTEVARSINRALAAKDGPIVPLIAETGGINAMIADATALPEQVADDVVTSAFRSAGQRCSALRLLFVQEDVADRMIEMVAGAARELKIGDPSDVATHVGPVIDVEAKQRLDAHIARMKTEARLHFAGPAPEGCFVAPHIFELTEAGQLTEEVFGPILHVVRYRPENLERVLRAIERTGYGLTLGVHSRIDDSIEAIIDRVQVGNIYVNRNMIGAVVGVQPFGGNGLSGTGPKAGGPHYLARFATEQTVTINTAAAGGNAALLAGEE
Protein: Pyruvate kinase PKM (EC 2.7.1.40) (P00548)
Organism: Gallus gallus (Chicken)
Function: Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP.
Interaction partners:
- Alpha-enolase
- L-lactate dehydrogenase A chain
- Gamma-enolase
- L-lactate dehydrogenase B chain
- Enolase 4
- Glucose-6-phosphate isomerase
- Lipoyl-binding domain-containing protein.
- Pyruvate dehydrogenase E1 component subunit beta
- Malic enzyme.
- Malic enzyme
Sequence:
MSKHHDAGTAFIQTQQLHAAMADTFLEHMCRLDIDSEPTIARNTGIICTIGPASRSVDKLKEMIKSGMNVARLNFSHGTHEYHEGTIKNVREATESFASDPITYRPVAIALDTKGPEIRTGLIKGSGTAEVELKKGAALKVTLDNAFMENCDENVLWVDYKNLIKVIDVGSKIYVDDGLISLLVKEKGKDFVMTEVENGGMLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQNVDMVFASFIRKAADVHAVRKVLGEKGKHIKIISKIENHEGVRRFDEIMEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPIICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHAIAREAEAAMFHRQQFEEILRHSVHHREPADAMAAGAVEASFKCLAAALIVMTESGRSAHLVSRYRPRAPIIAVTRNDQTARQAHLYRGVFPVLCKQPAHDAWAEDVDLRVNLGMNVGKARGFFKTGDLVIVLTGWRPGSGYTNTMRVVPVP
Protein: Small ribosomal subunit protein eS4, X isoform (40S ribosomal protein S4) (SCR10) (Single copy abundant mRNA protein) (P62701)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
Interaction partners:
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein eL31
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL27
Sequence:
MARGPKKHLKRVAAPKHWMLDKLTGVFAPRPSTGPHKLRECLPLIIFLRNRLKYALTGDEVKKICMQRFIKIDGKVRTDITYPAGFMDVISIDKTGENFRLIYDTKGRFAVHRITPEEAKYKLCKVRKIFVGTKGIPHLVTHDARTIRYPDPLIKVNDTIQIDLETGKITDFIKFDTGNLCMVTGGANLGRIGVITNRERHPGSFDVVHVKDANGNSFATRLSNIFVIGKGNKPWISLPRGKGIRLTIAEERDKRLAAKQSSG