wanglab/gogpt-training-data huggingface dataset:
Protein: p44-24 outer membrane protein (Q2GIH7)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MRSRSKLLLGSVMMSLAIVMAGNDVRAHDDVSALDTGGAGYFYIGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDNLAAALAKTSGKDIVQFANAVKITNSAIDGKICNRGKASGGSKGLSSSKAGSCDSIDKQSGSLEQSLTAALGDKGAEKWPKINNGTSDTTLNGNDTSSTPYTKDASATVAKDLVALNHDEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITPKLAYRLKAGLSYQLSPEISAFAGGFYHRVVGDGVYDDLPAQLQCKSQKQ
Protein: Probable D,D-dipeptide transport system permease protein DdpC (P77463)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Probable D,D-dipeptide transport ATP-binding protein DdpF
- Probable D,D-dipeptide transport system permease protein DdpB
- Probable D,D-dipeptide-binding periplasmic protein DdpA
- Oligopeptide transport ATP-binding protein OppD
- Dipeptide transport ATP-binding protein DppD
- Oligopeptide transport ATP-binding protein OppF
- Nickel import ATP-binding protein NikD
- Dipeptide transport ATP-binding protein DppF
- Putrescine export system ATP-binding protein SapD
Sequence:
MMLSEETSAVRPQKQTRFNGAKLVWMLKGSPLTVTSAVIIVLMLLMMIFSPWLATHDPNAIDLTARLLPPSAAHWFGTDEVGRDLFSRVLVGSQQSILAGLVVVAIAGMIGSLLGCLSGVLGGRADAIIMRIMDIMLSIPSLVLTMALAAALGPSLFNAMLAIAIVRIPFYVRLARGQALVVRQYTYVQAAKTFGASRWHLINWHILRNSLPPLIVQASLDIGSAILMAATLGFIGLGAQQPSAEWGAMVANGRNYVLDQWWYCAFPGAAILLTAVGFNLFGDGIRDLLDPKAGGKQS
Protein: Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial (Isocitric dehydrogenase subunit gamma) (NAD(+)-specific ICDH subunit gamma) (P51553)
Organism: Homo sapiens (Human)
Function: Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11256614}.
Interaction partners:
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Cytoplasmic aconitate hydratase
- Glutamate dehydrogenase 2, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MALKVATVAGSAAKAVLGPALLCRPWEVLGAHEVPSRNIFSEQTIPPSAKYGGRHTVTMIPGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIETNHNLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHESVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVAARYPQITFENMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYGHVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNENMHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA
Protein: Rab-like protein 3 (Q5HYI8)
Organism: Homo sapiens (Human)
Function: Required for KRAS signaling regulation and modulation of cell proliferation. Regulator of KRAS prenylation, and probably prenylation of other small GTPases. Required for lymphocyte development and function (By similarity). Not required for myeloid cell development (By similarity).
Interaction partners:
Sequence:
MASLDRVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYKEGTPEEKTYYIELWDVGGSVGSASSVKSTRAVFYNSVNGIIFVHDLTNKKSSQNLRRWSLEALNRDLVPTGVLVTNGDYDQEQFADNQIPLLVIGTKLDQIHETKRHEVLTRTAFLAEDFNPEEINLDCTNPRYLAAGSSNAVKLSRFFDKVIEKRYFLREGNQIPGFPDRKRFGAGTLKSLHYD
Protein: Histone H2B type 2-E (H2B-clustered histone 21) (Histone H2B-GL105) (Histone H2B.q) (H2B/q) (Q16778)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.3
- Histone H3.1t
- Histone H3.2
- Histone H3.1
- Histone H4
- Histone H2A type 2-C
- Histone H2A type 2-A
- Histone H2A.Z
- Histone H3-7
- Histone H4-like protein type G
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Alpha-2-HS-glycoprotein (59 kDa bone sialic acid-containing protein) (BSP) (Fetuin-A) (Glycoprotein PP63) (P24090)
Organism: Rattus norvegicus (Rat)
Function: Could inhibit both insulin-receptor tyrosine kinase activity and insulin-stimulated receptor autophosphorylation and, concomitantly, antagonize the mitogenic effect of the hormone in cultured rat hepatoma cells.
Subcellular location: Secreted.
Interaction partners:
- Albumin
- Prothrombin
- Toll-like receptor 4
- Matrix Gla protein
- Fibrinogen alpha chain
- Vitamin D-binding protein
- Plasminogen
- Alpha-1-antiproteinase
- Protein AMBP
- Beta-2-glycoprotein 1
Sequence:
MKSLVLLLCFAQLWSCQSAPQGAGLGFRELACDDPETEHVALIAVDYLNKHLLQGFRQILNQIDKVKVWSRRPFGEVYELEIDTLETTCHALDPTPLANCSVRQQAEHAVEGDCDFHILKQDGQFRVLHAQCHSTPDSAEDVRKFCPRCPILIRFNDTNVVHTVKTALAAFNAQNNGTYFKLVEISRAQNVPFPVSTLVEFVIAATDCTGQEVTDPAKCNLLAEKQYGFCKATLIHRLGGEEVSVACKLFQTQPQPANANPAGPAPTVGQAAPVAPPAGPPESVVVGPVAVPLGLPDHRTHHDLRHAFSPVASVESASGEVLHSPKVGQPGDAGAAGPVAPLCPGRVRYFKI
Protein: Stripe, isoform B (Stripe, isoform E) (Q8IN91)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIMEGLETLVAPTHHAFLLTETAAAAHFNVLSFDTCLFKTSTAAQSSGSPSTATYLSPAQFGGSHHGGASTSSNSLNSSSTASSSSTSSSLLHYTTASAAAAAAAAAAASANNSVLRARNQTATPTQGGSPGHVAVQPSATASSGRSSASHLSLLNTSGQHSPTSSAVEQVEAHKQLIEALPGDLNTPVTTSSDIPSFFGPTTVVEPPPITGSIESEDLSLEPQVISVASPVLSHCSPLKEERSTPPALAIVKEESSNNSCNMYPQHNNNNNNNNNTTSSSTTTTSKQTTSESNTECVGSPGNHTQSHQQQQQQLQHNNTSSSNSNCHHSHQQQQQQQQQQHMSSPQQQYQQHQILHQQQQLPNHHHHHHHHHHHHSQLQQLQQQQQQQQQQQQHQQQPLHQQQQLQHQQQQQHHQQHYQQHAIQHQQSQQQASKISYRGIFTTTGNAMNAAAAAAAAAAQQQHQQQQQHQQQLPSPQLGVLAGPMSPPSNSLGNSWGLPSPDKTMFQPPLFSLPAHYATMQQQQQQQQQQQQQQQQQQAAGAAPSPYDDGRAAAAAAAQHAELLGLTMDCTPLLLKQPPPSYAGASAGFPGLGDLHSSHEQQLQQQQYVRSQPKYQWLDSPADYAQQQQQVQQVQQQQQQQQTLVLPGPTSSASSSNAALGVLIPKQENYPDMQPSSNGTGYSGGSGGSSAAAAAAAAAAAAAVQLAEYSPSTSKGHEILSQVYQQSTVPLKLVPVKPRKYPNRPSKTPVHERPYACPVENCDRRFSRSDELTRHIRIHTGQKPFQCRICMRSFSRSDHLTTHIRTHTGEKPFSCDICGRKFARSDEKKRHAKVHLKQRIKKEKVRGEQQQQQQQQQQQQQQQQQQQLQQQQEQHHLSLQQHQQYQQHHLLHSADLAIVTSSASM
Protein: Uncharacterized protein 3 (P86737)
Organism: Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone)
Subcellular location: Secreted {ECO:0000269|PubMed:21050442}.
Interaction partners:
Sequence:
MVPVARASLFTLACLLVSVCAQNFPGPPPGAVLRGPFPPARPSLTNRVHPPTSAAGMQLMRRMAVSEAVLSSDYTKRMTALDAIQNIPCVFRNPVLKYLLMDYMDMKPLPLPGSVQSQMSPATQSMILTDRGRRLQAGKLLNSRCVQSHDRLGALMYDIAEVPMAASAL
Protein: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) (O13917)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenylate kinase
- Adenine deaminase
- Thymidylate kinase
- Dihydrofolate reductase
- Probable deoxyuridine 5'-triphosphate nucleotidohydrolase
- Uncharacterized mitochondrial carrier C8C9.12c
- Pterin-4-alpha-carbinolamine dehydratase
- Adenylosuccinate synthetase
Sequence:
MDPVRLYYSYNDIHKMCAQQAEKILETFRPDVIIAIGGGGFIPARILRTFLKKKGSKNIPIQAIGLSLYEELVSDSPEEVPGLEVKRTQWLDFSTLGMVDLVGKNILIVDEVDDTRTTLHYALRELQRDVAEQAKKLNREGEKTTFGIFVVHNKVKPKNAQLDKEILDKYYFTGCNTPDCWIMYPWEAQDIEEHDSHVAKMGDLKP
Protein: Tubulin alpha-1 chain (EC 3.6.5.-) (P11139)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-5 chain
- Tubulin beta-4 chain
- Tubulin beta-6 chain
- Tubulin beta-8 chain
- Tubulin beta-9 chain
- Tubulin beta-1 chain
- Tubulin beta-7 chain
- Tubulin beta-2 chain
- Kinesin-like protein KIN-8A
- Protein WVD2-like 2
Sequence:
MREIISIHIGQAGIQVGNSCWELYCLEHGIQPDGTMPSDSTVGACHDAFNTFFSETSSGQHVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTVGREIVDTCLERLRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDFGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVVVLLDNEAIYDICRRSLDIERPTYSNLNRLISQTISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISSAKAYHEQFSVPEITTSVFEPSNMMAKCDPRHGKYMACCLMYRGDVVPKDVNTAVAAIKAKRTIQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNNTAVAEVFSRIDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGGEGAEDDDEEGDEY
Protein: Beta-defensin 14 (BD-14) (mBD-14) (Defensin, beta 14) (Q7TNV9)
Organism: Mus musculus (Mouse)
Function: Has antibacterial activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-defensin 4
- Beta-defensin 1
- C-C chemokine receptor type 6
- Methyl-CpG-binding protein 2
Sequence:
MRLHYLLFVFLILFLVPAPGDAFLPKTLRKFFCRIRGGRCAVLNCLGKEEQIGRCSNSGRKCCRKKK
Protein: FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein) (O35601)
Organism: Mus musculus (Mouse)
Function: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2. Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2 (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15117}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000269|PubMed:21881001}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000269|PubMed:21881001}.
Interaction partners:
- Lymphocyte cytosolic protein 2
- Src kinase-associated phosphoprotein 1
- Linker for activation of T-cells family member 1
- GRB2-related adaptor protein 2
- Integrin alpha-4
- Integrin beta-1
- Src kinase-associated phosphoprotein 2
- Proto-oncogene vav
- Integrin alpha-5
- SH2/SH3 adapter protein Nck1
Sequence:
MAKFNTGSNPTEEAATSSRPFKVAGQSSPSGIQSRKNLFDNQGNASPPAGPSSMPKFGTTKPPLAAKPTYEEKPEKEPKPPFLKPTGGSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVVLRPPGNKLHNLNQESDLKTPGPKPGPAPPVPENELKPGFSKVAGAKSKFMPAAQDTDSKPRFPRHTFGQKPSLSTEDSQEENTSKNVPVQKGSPVQLGAKSKGAPFKPPKEDPEDKDHGAPSSPFPGVVLKPAASRGSPGLSKNFEEKKEDRKTDLAKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKNSATPKQKALPPLSVLGPPPPKPNRPPNVDLTRFRKADSANSATKSQTPYSTTSLPPPPPTHPASQPPLPASHPAHPPVPSLPPRNIKPPLDLKHPINDENQDGVMHSDGTGNLEEEQESEGETYEDIDSSKERDKKREKEEKKRLELERKEQKEREKKEQELKKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVEIDYDSLKRKKNSLNAVPPRLVEDDQDVYDDVAEQDAPNSHGQSGSGGMFPPPPTDDEIYDGIEEEDDDDGSVPQVDEKTNAWSWGILKMLKGKDDRKKSIREKPKVSESDNNEGSSLPSQHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGRAKTEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGARDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND
Protein: Hypersensitive-induced response protein 3 (AtHIR3) (Q9SRH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130, ECO:0000305|PubMed:17644812, ECO:0000305|Ref.7}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305|PubMed:17644812, ECO:0000305|Ref.7}.
Interaction partners:
- FAD/NAD
- Flotillin-like protein 3
- AT3g47210/F13I12_260
- Calcineurin-binding protein 1
- Filament-like protein
- Haloacid dehalogenase-like hydrolase
- Transmembrane protein, putative
- Plant intracellular Ras-group-related LRR protein 5
- C2 domain-containing protein At1g53590
- Endoglucanase 22
Sequence:
MGNLFCCVLVKQSDVAVKERFGKFQKVLNPGLQFVPWVIGDYVAGTLTLRLQQLDVQCETKTKDNVFVTVVASIQYRVLADKASDAFYRLSNPTTQIKAYVFDVIRACVPKLNLDDVFEQKNEIAKSVEEELDKAMTAYGYEILQTLIIDIEPDQQVKRAMNEINAAARMRVAASEKAEAEKIIQIKRAEGEAESKYLSGLGIARQRQAIVDGLRDSVLGFAGNVPGTSAKDVLDMVMMTQYFDTMRDIGATSKSSAVFIPHGPGAVSDVAAQIRNGLLQANNAS
Protein: Prostaglandin E synthase (EC 5.3.99.3) (Glutathione peroxidase PTGES) (EC 1.11.1.-) (Glutathione transferase PTGES) (EC 2.5.1.18) (Microsomal prostaglandin E synthase 1) (MPGES-1) (Q95L14)
Organism: Bos taurus (Bovine)
Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (By similarity). Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:O14684}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14684}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14684}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000250|UniProtKB:O14684}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Prostacyclin synthase
- Carbonyl reductase 1])
- Carbonyl reductase
- Prostamide/prostaglandin F synthase
Sequence:
MPPSGLELMNGQVLPAFLLCSALLVIKMYVVAVITGQVRLRKKAFANPEDAQRHGGLQYCRNDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVARMHFLVFFLGRMVHTVAYLGKLRAPTRSLAYTLAQLPCASMALQIVWEAARHL
Protein: Protein lsd90 (90kDa large and small daughter protein) (A9ZLL8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in the metabolism of very long-chain fatty acid-containing phospholipids (VLCFA-PL).
Subcellular location: Note=Localizes to small particle-like structures, that differ from either the mitochondria, the endoplasmic reticulum near the nucleus, or the peroxisomes. {ECO:0000269|PubMed:18079165}.
Interaction partners:
- Probable phosphoketolase
- Hydrogen peroxide stress regulator 1
- Transcription factor prr1
- Heat shock protein hsp9
- Zinc finger protein rsv2
- Extender of the chronological lifespan protein 1
Sequence:
MVGTINESMQNMKIGAKETAQSAKQGIKNAGQSSSKTARDVMGNPVPGSYTAGNTANDGDSSYASSKNLPGNADIGATSSERTAYAAPQRAAVDTSNVSPPSTQTGGYASKDTTSTYEGAQPLSSQSSRSSNYTNVKITATQNNVDALTGAPIRIVTTTNARIQPDEKTLQDLLEQRQVALREAREAEEELQRARQYNDRSTSEALELEARAKKAAQDAELASERAREAQSSIERSASLREKQAREEAERAATALREAELKHRLAQANADVDVANSKLDIALKNEAAWKAERESSLAHQKAVIDSARAELERARHEAAVADATYKKEHYEYNALVAELEERNDNTLRTASIREAEARNLEVHMEDTLKDARMRSRNATEQVEVVKREINSEIDVYRSSVEKTKAELASYQKGLPSQKEACDRELDDATRALQAAFQDRFNAAKLRVNQFDVDSRQQLAMLTKKVRDAEDAEEKYRISCHQREEEITRCATQAYDAVKAAEKRNETIAEAARAKENEAKDLYSKAESITQDLNAKRSHPPQPANLDYSSAIQRAQERLTLEESKLTDLRTAEPSQYVNDVEVARRALRDAQAEQSKVESEYNSVKGSKLYTTEPVHPHAVTTNEPTDVSTKSKSAAYHYPATTETVSSKAARSATTPAYVGGATKTPSTTKAVESTPSTLPTSASTNAAATTTTKKPKAAKSTAVRDDVSSASSDSDKGTTGLGKSESKSSRKERRSSTSSGHGLMNNVRHALGMSNK
Protein: Profilin-2 (Pollen allergen Zea m 12) (ZmPRO2) (allergen Zea m 12) (P35082)
Organism: Zea mays (Maize)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-depolymerizing factor 1
- Expansin-B10
- Expansin-B9
- Expansin-B11
- Uncharacterized protein.
- Rho GDP-dissociation inhibitor 1
- Rho GDP-dissociation inhibitor 1
- Actin-1
- Actin-1
- Actin-1
Sequence:
MSWQAYVDEHLMCEIEGHHLAAAAIVGHDGAAWAQSTAFPEFKTEDMANIMKDFDEPGHLAPTGLFLGPTKYMVIQGEPGAVIRGKKGSGGITVKKTGQALVVGIYDEPMTPGQCNMVVERLGDYLLEQGM
Protein: Katanin p60 ATPase-containing subunit A-like 1 (Katanin p60 subunit A-like 1) (EC 5.6.1.1) (p60 katanin-like 1) (Q9BW62)
Organism: Homo sapiens (Human)
Function: Regulates microtubule dynamics in Sertoli cells, a process that is essential for spermiogenesis and male fertility. Severs microtubules in an ATP-dependent manner, promoting rapid reorganization of cellular microtubule arrays (By similarity). Has microtubule-severing activity in vitro.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03024, ECO:0000269|PubMed:22654668}. Cytoplasm {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26929214}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Note=Colocalizes with microtubules throughout the basal and adluminal compartments of Sertoli cells (By similarity). Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis (PubMed:26929214). {ECO:0000250|UniProtKB:Q8K0T4, ECO:0000269|PubMed:26929214}.
Interaction partners:
- Katanin p80 WD40 repeat-containing subunit B1
- KATNB1-like protein 1
- Glycerol-3-phosphate dehydrogenase, mitochondrial
Sequence:
MNLAEICDNAKKGREYALLGNYDSSMVYYQGVMQQIQRHCQSVRDPAIKGKWQQVRQELLEEYEQVKSIVSTLESFKIDKPPDFPVSCQDEPFRDPAVWPPPVPAEHRAPPQIRRPNREVRPLRKEMAGVGARGPVGRAHPISKSEKPSTSRDKDYRARGRDDKGRKNMQDGASDGEMPKFDGAGYDKDLVEALERDIVSRNPSIHWDDIADLEEAKKLLREAVVLPMWMPDFFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSDEHEASRRVKSELLIQMDGVGGALENDDPSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPTAKGRAELLKINLREVELDPDIQLEDIAEKIEGYSGADITNVCRDASLMAMRRRINGLSPEEIRALSKEELQMPVTKGDFELALKKIAKSVSAADLEKYEKWMVEFGSA
Protein: ATP synthase subunit beta (EC 7.1.2.2) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta) (P0ABB4)
Organism: Escherichia coli (strain K12)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Subcellular location: Cell inner membrane; Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit b
- ATP synthase subunit delta
- ATP synthase gamma chain
- ATP synthase subunit alpha
- ATP synthase subunit a
- ATP synthase epsilon chain
- ATP synthase subunit c
- DNA-directed RNA polymerase subunit beta
- Elongation factor G
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL
Protein: Voltage-dependent L-type calcium channel subunit beta-1 (CAB1) (Calcium channel voltage-dependent subunit beta 1) (Q8R3Z5)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of L-type calcium channels. Regulates the activity of L-type calcium channels that contain CACNA1A as pore-forming subunit (By similarity). Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit and increases the presence of the channel complex at the cell membrane. Required for functional expression L-type calcium channels that contain CACNA1D as pore-forming subunit. Regulates the activity of L-type calcium channels that contain CACNA1B as pore-forming subunit (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P19517}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side {ECO:0000250|UniProtKB:P19517}. Cell membrane {ECO:0000305|PubMed:21831364}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}.
Interaction partners:
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent L-type calcium channel subunit alpha-1D
Sequence:
MVQKSGMSRGPYPPSQEIPMEVFDPSPQGKYSKRKGRFKRSDGSTSSDTTSNSFVRQGSAESYTSRPSDSDVSLEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVPVQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQTLRQNRLSSSKSGDNSSSSLGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLAEVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRGKSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSSTPPNPLLNRTMATAALAASPAPVSNLQGPYLASGDQPLDRATGEHASVHEYPGELGQPPGLYPSNHPLGRAGTLRALSRQDTFDADTPGSRNSAYTEPGDSCVDMETDPSEGPGPGDPAGGGTPPARQGSWEDEEDYEEEMTDNRNRGRNKARYCAEGGGPVLGRNKNELEGWGQGVYTR
Protein: Splicing factor U2AF 35 kDa subunit (Q9U2U0)
Organism: Caenorhabditis elegans
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Probable splicing factor, arginine/serine-rich 4
- Probable splicing factor, arginine/serine-rich 2
- Uncharacterized protein.
- Branchpoint-bridging protein
- Probable splicing factor, arginine/serine-rich 3
- Splicing factor 3B subunit 1 domain-containing protein
- Probable splicing factor, arginine/serine-rich 6
- Probable splicing factor, arginine/serine-rich 5
- Small nuclear ribonucleoprotein Sm D3
Sequence:
MSYGDGLSGAEYLASIYGTEKDKVNCSFFFKTGACRHGDKCSRAHHTPTFSPTVVLKNFYHNPVVDVRQADAFDKVGKRNDQEQRYFDDFYEEVFVEMERKYGEVEEINVCENIGEHMVGNVYVKFMKEEDAEKAKNDLNNRWFNGQPIYAELCPVTDFRESRCRQHEVTTCSKGGFCNFMHLKAISAELGDRLYGRRGRRADAAGHYPSQRGGSGGGGGGGGGGGYGSGGGWGGGGGGRDRDRGGWGGGGGGRGYGGGGGGGGYGYGGGGGGRRRSRSRDRRRY