wanglab/gogpt-training-data huggingface dataset:
Protein: Tehao (Q58SL6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FCLGLSPQCTCAAEGNVVRFHCPDEYAMLLEVSEPGASLYMSYYASTXLQWLPXFNIXSLVKIXFDAXIFWXEXXLSDLLKTLGVQTVKTIIFRDRTLETVVTRDVLNSGNGYMETSQPENITTWHFGSVPGLKKFKFFSHVPELQESIFHGFDTLRDLHLSVNVTTLPGNMLSTVNGTLKTLTIESPGIVSFGNPLLRELQQLRNLSLALIHPFHERDKQLQPHFFGSMTNLEEVRLASATSSVNRSMFKGTNKLQLIKMNGNDDLMELPGEIFLDQVNLKTLDLSCNAIVTLHEDVFKGLGNLTLLDLSKNRLTNLS
Protein: Plasma membrane ATPase proteolipid 2 (P40975)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane.
Interaction partners:
- Plasma membrane ATPase proteolipid 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4
- Plasma membrane proteolipid 3
- Putative uncharacterized protein YDR193W
- Plasma membrane ATPase 1
- Small ribosomal subunit protein uS14B
- Probable transport protein YPL264C
- Small ribosomal subunit protein eS32A
Sequence:
MLMSTLPGGVILVFILVGLACIAIISTIIYRKWQARQRGLQRF
Protein: UNC5C-like protein (Protein unc-5 homolog C-like) (ZU5 and death domain-containing protein) (Q8IV45)
Organism: Homo sapiens (Human)
Function: Inhibits NF-kappa-B-dependent transcription by impairing NF-kappa-B binding to its targets.
Subcellular location: Membrane {ECO:0000305}; Single-pass type III membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:14769797}.
Interaction partners:
- Adhesion G protein-coupled receptor L2
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
Sequence:
MCPQESSFQPSQFLLLVGVPVASVLLLAQCLRWHCPRRLLGACWTLNGQEEPVSQPTPQLENEVSRQHLPATLPEMVAFYQELHTPTQGQTMVRQLMHKLLVFSAREVDHRGGCLMLQDTGISLLIPPGAVAVGRQERVSLILVWDLSDAPSLSQAQGLVSPVVACGPHGASFLKPCTLTFKHCAEQPSHARTYSSNTTLLDAKVWRPLGRPGAHASRDECRIHLSHFSLYTCVLEAPVGREARKWLQLAVFCSPLVPGQSHLQLRIYFLNNTPCALQWALTNEQPHGGRLRGPCQLFDFNGARGDQCLKLTYISEGWENVDDSSCQLVPHLHIWHGKCPFRSFCFRRKAADENEDCSALTNEIIVTMHTFQDGLETKYMEILRFQASEEESWAAPPPVSQPPPCNRLPPELFEQLRMLLEPNSITGNDWRRLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTVMERLDCASAIQNYLSGTHGGSPGPERGGARDNQGLELDEKL
Protein: DNA/RNA-binding protein ALBA2 (PfAlba2) (Q8IDN4)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000269|PubMed:22167473}. Chromosome, telomere {ECO:0000269|PubMed:22167473}. Cytoplasm {ECO:0000269|PubMed:22167473}. Note=Localizes to the nucleus in the ring stages and expands to punctate loci in the cytoplasm during the trophozoite and schizont stages. {ECO:0000269|PubMed:22167473}.
Interaction partners:
- Ribonuclease P/MRP protein subunit RPP1, putative
- Ribonuclease P protein subunit RPR2, putative
- Ribonuclease P protein subunit p29, putative
- H/ACA ribonucleoprotein complex subunit 2
Sequence:
MPGSTKSDTKLENEIRISYKSDALDYVYKAIVLFETYDEIILSGVGKAISSVVNVAEMVKRRAKGLHQFTKLYEKEHVIKREDNSGLKKNAKNEDKKSGDEEEEEEEEEEDEENNKNKEANNRTVEFITTVPCMKIILSKNEDKIDKNEIGYQKPLDEKEVNVMTPEQILKEKSYRRRYRRGGRGGDRFRSYRRNYYETSMWNNRRYEKRN
Protein: Major capsid protein 2 (MCP2) (Q70LC7)
Organism: Acidianus filamentous virus 1 (isolate United States/Yellowstone) (AFV-1)
Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 900 nm in length and 24 nm in width (Probable). Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form (Probable). Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues (Probable). This certainly protects the viral DNA under conditions such as the extreme desiccation of its host (Probable).
Subcellular location: Virion {ECO:0000269|PubMed:19934032}.
Interaction partners:
Sequence:
MVNKKYRQDSKDRYQYKQYIYRSIGGIVPPEMAETVTANQTAQWEAGFTPYHKLRLAIKEICKTDGIPNIKWGMYIAFGEKLLKSYLKMKAGSASSDMIAEYINNAISAFSSRTGISQETAQKIADFITSNY
Protein: Chymotrypsinogen B2 (EC 3.4.21.1) [Cleaved into: Chymotrypsin B2 chain A; Chymotrypsin B2 chain B; Chymotrypsin B2 chain C] (Q6GPI1)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Alpha-1-antichymotrypsin
- Alpha-1-antitrypsin
- Chymotrypsinogen B
- Carboxypeptidase A1
- Colipase
- Carboxypeptidase B
- Bile salt-activated lipase
- Serine protease inhibitor Kazal-type 1
- Alpha-2-macroglobulin
- Serine protease 1
Sequence:
MAFLWLLSCWALLGTTFGCGVPAIHPVLSGLSRIVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNPKFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKKSWGRRITDVMICAGASGVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSRTCSTTTPAVYARVAKLIPWVQKILAAN
Protein: Alginate biosynthesis transcriptional regulatory protein AlgB (P23747)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system AlgB/KinB involved in regulation of alginate biosynthesis genes. Positive regulator of the alginate biosynthetic gene AlgD.
Interaction partners:
- histidine kinase
- RNA polymerase sigma-H factor
- GDP-mannose 6-dehydrogenase
- Transcription factor AmrZ
- RNA polymerase sigma-54 factor
- Sigma factor AlgU negative regulatory protein
- AlgW protein
- Probable periplasmic serine endoprotease DegP-like
- Sigma factor AlgU regulatory protein MucB
- Positive regulator for alginate biosynthesis MucC
Sequence:
METTSEKQGRILLVDDESAILRTFRYCLEDEGYSVATASSAPQAEALLQRQVFDLCFLDLRLGEDNGLDVLAQMRVQAPWMRVVIVTAHSAVDTAVDAMQAGAVDYLVKPCSPDQLRLAAAKQLEVRQLTARLEALEDEVRRQGDGLESHSPAMAAVLETARQVAATDANILILGESGSGKGELARAIHTWSKRAKKPQVTINCPSLTAELMESELFGHSRGAFTGATESTLGRVSQADGGTLFLDEIGDFPLTLQPKLLRFIQDKEYERVGDPVTRRADVRILAATNRDLGAMVAQGQFREDLLYRLNVIVLNLPPLRERAEDILGLAERFLARFVKDYGRPARGFSEAAREAMRQYPWPGNVRELRNVIERASIICNQELVDVDHLGFSAAQSASSAPRIGESLSLEDLEKAHITAVMASSATLDQAAKTLGIDASTLYRKRKQYGL
Protein: Tachykinin-like peptide-I (P.nigriventer tachykinin peptides I) (PnTkP-I) (U29-ctenitoxin-Pn1a) (U29-CNTX-Pn1a) (P86298)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKD
Protein: Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) (Q9VIF3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03190}.
Interaction partners:
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Coenzyme Q8
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Decaprenyl diphosphate synthase subunit 2, isoform A
- AarF domain containing kinase 5, isoform A
- All trans-polyprenyl-diphosphate synthase PDSS1
- AarF domain-containing kinase 1
Sequence:
MMRNALLVSGKLRHLLSCSIGRNSTRSSSTAKSLDAGTQKEVRHHENHASEWWNQNGTMGALHALNEIRVPFIRDGIVSRGTVKPGYVNTTKVLLGQNILEVGCGGGLLTEHLARLGAQVAGIDLGEKLIEAAREHLKCSSPELASNVVYKIEPVDQHAKANCECYDAVIVSEVLEHVKDKVSLLEASVRSLKPGGSIFITTLNKTIPSWFGGVLLSEYVLNLVPRGTHHWDKMISPLDVQRILDTSKFISGFIFRLGYSLFSRSSAVNCQTVLVNGSTYDFWSNTWRWINNNQMCYALQAVKQAQREYN
Protein: GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (GTP-CH-I) (Protein punch) (P48596)
Organism: Drosophila melanogaster (Fruit fly)
Function: Isoform B is required for eye pigment production, Isoform C may be required for normal embryonic development and segment pattern formation.
Interaction partners:
- Reticulon-like protein
- Vacuolar protein sorting-associated protein VTA1 homolog
- CAP, isoform X
- 6-pyruvoyl tetrahydrobiopterin synthase
- Inosine triphosphate pyrophosphatase
- Molybdenum cofactor biosynthesis protein 1
- Trifunctional purine biosynthetic protein adenosine-3
- alkaline phosphatase
- alkaline phosphatase
- Alkaline phosphatase
Sequence:
MSFTRQLSEMSASELNDAIDDTNFPQAHILSRGRNNSVCSTSSTSGTSSLADRQQNQAEEATAIAGTPVEEVAPAPALVPLAGNQRPRLILKTNGSSPDSDGTQPKTPLTPRTSTTPGHEKCTFHHDLELDHKPPTREALLPDMARSYRLLLGGLGENPDRQGLIKTPERAAKAMLYFTKGYDQSLEDVLNGAVFDEDHDEMVVVKDIEMFSMCEHHLVPFYGKVSIGYLPCNKILGLSKLARIVEIFSRRLQVQERLTKQIAVAVTQAVQPAGVAVVVEGVHMCMVMRGVQKINSKTVTSTMLGVFRDDPKTREEFLNLVNSK
Protein: Lysosome-associated membrane glycoprotein 1 (LAMP-1) (Lysosome-associated membrane protein 1) (120 kDa lysosomal membrane glycoprotein) (CD107 antigen-like family member A) (LGP-120) (Lysosomal membrane glycoprotein A) (LGP-A) (P2B) (CD antigen CD107a) (P11438)
Organism: Mus musculus (Mouse)
Function: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, autophagy, and cholesterol homeostasis. Also plays an important role in NK-cells cytotoxicity. Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule (By similarity). In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content (By similarity). Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:23847195}; Single-pass type I membrane protein {ECO:0000255}. Cytolytic granule membrane {ECO:0000305|PubMed:32839608}; Single-pass type I membrane protein {ECO:0000255}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane (By similarity). Colocalizes with OSBPL1A at the late endosome (By similarity). {ECO:0000250|UniProtKB:P05300, ECO:0000250|UniProtKB:P11279}.
Interaction partners:
- Lysosome-associated membrane glycoprotein 2
- CD63 antigen
- Serine/threonine-protein kinase mTOR
- Cathepsin D
- GATOR1 complex protein NPRL2
- Regulatory-associated protein of mTOR
- Protein SEC13 homolog
- GATOR1 complex protein NPRL3
- GATOR1 complex protein DEPDC5
- KICSTOR complex protein kaptin
Sequence:
MAAPGARRPLLLLLLAGLAHGASALFEVKNNGTTCIMASFSASFLTTYETANGSQIVNISLPASAEVLKNGSSCGKENVSDPSLTITFGRGYLLTLNFTKNTTRYSVQHMYFTYNLSDTEHFPNAISKEIYTMDSTTDIKADINKAYRCVSDIRVYMKNVTVVLRDATIQAYLSSGNFSKEETHCTQDGPSPTTGPPSPSPPLVPTNPTVSKYNVTGNNGTCLLASMALQLNITYLKKDNKTVTRAFNISPNDTSSGSCGINLVTLKVENKNRALELQFGMNASSSLFFLQGVRLNMTLPDALVPTFSISNHSLKALQATVGNSYKCNTEEHIFVSKMLSLNVFSVQVQAFKVDSDRFGSVEECVQDGNNMLIPIAVGGALAGLVLIVLIAYLIGRKRSHAGYQTI
Protein: RE54693p (Q9VGC5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- RE22940p
- GH10201p
Sequence:
MSKLPCSYDAENKIWKGIPQNNPFKPETSLGRIIFKNMRNWPKNVCQISDSEGVEVTFGQALTWAIRIAQQLKSRGLDHKDIIGISARNTTYIMPTAVACFFHGTPFQSANPILEESTLKHLYNISKPKIIFTDADHYDKLYSATSAFKPEIILTTGTKDGVLSIQDLLAPTKTEFFYQPTPLKEGPSQTVAILTSSGTTGMPKAVCISNDILTQETVFVNGYDTIFISASLDWITGLWATIFSTVNGCTRIISSKPFAADYFVYLVSKYSITYALIPPEHCCSLLDCPTATPEKLGSLTKLNFGGGRMTQATVERVKKLAPNGVLNSSYGMTEVGFIVFNHGHLKLTAAGNPLPGIQVKIVDDDGNQLGVNQTGEIIVHNGFSWNGYFADPEATKAMQDEEGWFHTGDMGYFDEDDYLYMTDRKKEVLKWKGLQMWPAEVEAVIDELPEVKRVCVIGVYDETQGDVPGALVVREDNATLTAQQVIDHVAKRLPDIQKQLRAGVQFADEIPQNHNGKVVRRYARDLFVALSKKN
Protein: Lamin-B2 (P21619)
Organism: Mus musculus (Mouse)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Subcellular location: Nucleus lamina {ECO:0000269|PubMed:28241138}.
Interaction partners:
- Prelamin-A/C
- Delta
- Lamin-B1
- Caspase-6
- Granzyme B
- Emerin
- Barrier-to-autointegration factor
- SUN domain-containing protein 1
- Inner nuclear membrane protein Man1
- Lamina-associated polypeptide 2, isoforms alpha/zeta
Sequence:
MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADARRVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVAQGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEDLRSQHDEQVRLYRVELEQTYQAKLDNAKLLSDQNDKAAHAAREELKEARMRVESLSYQLLGLQKQASAAENHIHELEEALAGERDKFRKMLDAKEQEMTEVRDAMQQQLAEYQELLDIKLALDMEISAYRKLLEGEEERLKLSPSPSSRITISRATSSSSSSSGVGMSVGQGRGKRRRLETEDTSGSPSRASRVSSGSRLAQQTVATGVVNIDEVDPEGRFVRLKNSSDKDQSLGNWRIKRQVLEGEDIAYKFTPKYVLRAGQTVTVWAAGAGATHSPPSTLVWKSQTNWGPGESFRTALVSADGEEVAVKAAKHSSVQGRENGEEEEEEEAEFGEEDLFHQQGDPRTTSRGCRLM
Protein: Keratin, type I cytoskeletal 13 (Cytokeratin-13) (CK-13) (Keratin-13) (K13) (P13646)
Organism: Homo sapiens (Human)
Function: Type 1 keratin (Probable). Maintains postnatal tongue mucosal cell homeostasis and tissue organization in response to mechanical stress, potentially via regulation of the G1/S phase cyclins CCNE1 and CCNE2 (By similarity).
Interaction partners:
- Keratin, type II cytoskeletal 4
- Keratin, type II cytoskeletal 6A
- Small proline-rich protein 3
Sequence:
MSLRLQSSSASYGGGFGGGSCQLGGGRGVSTCSTRFVSGGSAGGYGGGVSCGFGGGAGSGFGGGYGGGLGGGYGGGLGGGFGGGFAGGFVDFGACDGGLLTGNEKITMQNLNDRLASYLEKVRALEEANADLEVKIRDWHLKQSPASPERDYSPYYKTIEELRDKILTATIENNRVILEIDNARLAADDFRLKYENELALRQSVEADINGLRRVLDELTLSKTDLEMQIESLNEELAYMKKNHEEEMKEFSNQVVGQVNVEMDATPGIDLTRVLAEMREQYEAMAERNRRDAEEWFHTKSAELNKEVSTNTAMIQTSKTEITELRRTLQGLEIELQSQLSMKAGLENTVAETECRYALQLQQIQGLISSIEAQLSELRSEMECQNQEYKMLLDIKTRLEQEIATYRSLLEGQDAKMIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVRRP
Protein: Putative syntaxin-131 (AtSYP131) (Q9SRV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vesicle trafficking protein that functions in the secretory pathway.
Subcellular location: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- UPF0235 protein At5g63440
- VAMP-like protein YKT62
- Syntaxin-31
- Putative SNAP25 homologous protein SNAP30
- SNAP25 homologous protein SNAP33
- Vesicle-associated membrane protein 727
- 25.3 kDa vesicle transport protein SEC22-1
- VAMP-like protein YKT61
- Syntaxin-51
- Vesicle-associated membrane protein 724
Sequence:
MNDLLKGSLEFSRDRSNRSDIESGHGPGNSGDLGLSGFFKKVQEIEKQYEKLDKHLNKLQGAHEETKAVTKAPAMKSIKQRMERDVDEVGRISRFIKGKIEELDRENLENRTKPGCGKGTGVDRTRTATTIAVKKKFKDKISEFQTLRQNIQQEYREVVERRVFTVTGQRADEEAIDRLIETGDSEQIFQKAIREQGRGQIMDTLAEIQERHDAVRDLEKKLLDLQQVFLDMAVLVDAQGEMLDNIENMVSSAVDHVQSGNNQLTKAVKSQKSSRKWMCIAILILLIIIIITVISVLKPWTQKNGA
Protein: Protein NRT1/ PTR FAMILY 8.2 (AtNPF8.2) (Peptide transporter PTR5) (Q9LFB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Peptide transporter. Mediates the transport of di- and tripeptides. High affinity transporter. Involved in the uptake of peptides during pollen germination and tube growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18753286}; Multi-pass membrane protein {ECO:0000269|PubMed:18753286}.
Interaction partners:
- F-box/LRR-repeat protein 3
Sequence:
MEDDKDIYTKDGTLDIHKKPANKNKTGTWKACRFILGTECCERLAYYGMSTNLINYLEKQMNMENVSASKSVSNWSGTCYATPLIGAFIADAYLGRYWTIASFVVIYIAGMTLLTISASVPGLTPTCSGETCHATAGQTAITFIALYLIALGTGGIKPCVSSFGADQFDDTDEKEKESKSSFFNWFYFVINVGAMIASSVLVWIQMNVGWGWGLGVPTVAMAIAVVFFFAGSNFYRLQKPGGSPLTRMLQVIVASCRKSKVKIPEDESLLYENQDAESSIIGSRKLEHTKILTFFDKAAVETESDNKGAAKSSSWKLCTVTQVEELKALIRLLPIWATGIVFASVYSQMGTVFVLQGNTLDQHMGPNFKIPSASLSLFDTLSVLFWAPVYDKLIVPFARKYTGHERGFTQLQRIGIGLVISIFSMVSAGILEVARLNYVQTHNLYNEETIPMTIFWQVPQYFLVGCAEVFTFIGQLEFFYDQAPDAMRSLCSALSLTAIAFGNYLSTFLVTLVTKVTRSGGRPGWIAKNLNNGHLDYFFWLLAGLSFLNFLVYLWIAKWYTYKKTTGHAL
Protein: Uncharacterized oxidoreductase C28F2.05 (EC 1.-.-.-) (Q9USV2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKPFSPSQTNFEKEQLCFGVYQLKDCYQQVIEALSLGIRVIDSAITYRNEKECEQAIQDFCHQNVNIKREDITLITKIPDSLQGFERTWKAVEQSLRRTGRPKLDVVLIHSPKWPVRRIESWRALLQHQKEGRINKIGVSNYNIHHLEEIISLGLPLPAINQVEFSAFNNRPTFLSYCFNHGILVQAFSPLTRGYRLSDIRLLDLSLKYNKTPANILLRYCLQKGVSPIFKASSFVHIHENVKAEQFMLDPSDMDVMDTWDEEFVSKPTWNPIILP
Protein: Neurochondrin (M-Sema F-associating protein of 75 kDa) (Norbin) (Q9Z0E0)
Organism: Mus musculus (Mouse)
Function: Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling. Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35095}. Endosome membrane {ECO:0000250|UniProtKB:O35095}; Lipid-anchor {ECO:0000250|UniProtKB:O35095}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35095}. Postsynapse {ECO:0000250|UniProtKB:O35095}. Note=Localizes to somatic regions of neurons. Localization to endosome membrane requires palmitoylation. {ECO:0000250|UniProtKB:O35095}.
Interaction partners:
- General receptor for phosphoinositides 1-associated scaffold protein
- Metabotropic glutamate receptor 5
- FERM and PDZ domain-containing protein 4
Sequence:
MSCCDLAAAGQLGKAGIMASDCEPALNQAESRNPTLERYLGALREAKNDSEQFAALLLVTKAVKAGDIDAKTRRRIFDAVGFTFPNRLLTTKEAPDGCPDHVLRALGVALLACFCSDPELASHPQVLNKIPILSTFLTARGDPDDAARRSMIDDTYQCLTAVAGTPRGPRHLIAGGTVSALCQAYLGHGYGFDQALALLVGLLAAAETQCWKEAEPDLLAVLRGLSEDFQRAEDASKFELCQLLPLFLPPTTVPPECHRDLQAGLARILGSKLSSWQRNPALKLAARLAHACGSDWIPVGSSGSKFLALLVNLACVEVRLALEETGTEVKEDVVTACYALMELGIQECTRCEQSLLKEPQKVQLVSIMKEAIGAVIHYLLQVGPEKQKEPFVFASVRILGAWLAEETSSLRKEVCQLLPFLVRYAKTLYEEAEEASDISQQVANLAISPTTPGPSWPGDALRLLLPGWCHLTVEDGPREILIKEGAPSLLCKYFLQQWELTSPGHDTSVLPDSVEIGLQTCCHIFLNLVVTAPGLIKRDACFTSLMNTLMTSLPSLVQQQGRLLLAANVATLGLLMARLLSTSPALQGTPASRGFFAAAILFLSQSHVARATPGSDQAVLALSPDYEGIWADLQELWFLGMQAFTGCVPLLPWLAPAALRSRWPQELLQLLGSVSPNSVKPEMVAAYQGVLVELARANRLCREAMRLQAGEETASHYRMAALEQCLSEP
Protein: Inositol-3-phosphate synthase 1 (EC 5.5.1.4) (MIP synthase 1) (Myo-inositol 1-phosphate synthase 1) (PeMIPS 1) (C0HM53)
Organism: Populus euphratica (Euphrates poplar)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. May play a role in oxidative stress resistance and influences ascorbate levels.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29579299}. Nucleus {ECO:0000269|PubMed:29579299}.
Interaction partners:
Sequence:
MFIEKFKVESPNVKYTEDEIHSVYNYETTELVHENKNGSYQWTVKPKTVQYEFKTDIHVPKLGVMLVGWGGNNGSTLTGGVIANREGISWATKDKVQQANYFGSLTQASSIRVGSFNGEEIYAPFKSLLPMVNPDDIVFGGWDISDMNLADAMARAKVFDFDLQKQLRPYMESMVPLPGIYDPDFIAANQDSRANNVIKGTKKEQVQQIIKDIREFKEKNKVDKVVVLWTANTERYSNIVVGLNDTMENLLAAVEKDESEISPSTLYALACIYENIPFINGSPQNTFVPGLVDLAIKRNSLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVSSNGILYEPGEHPDHVVVIKYVPYVGDSKRAMDEYTSEIFMGGKNTIVLHNTCEDSLLAAPIILDLVLLAELSTRIQLKGEAEGKFHSFHPVATILSYLTKAPLVPPGTPVVNALSKQRAMLENILRACVGLAPENNMILEYK
Protein: Citrate synthase, mitochondrial (EC 2.3.3.1) (Citrate (Si)-synthase) (O75390)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00889}.
Interaction partners:
- Cytoplasmic aconitate hydratase
- Aconitate hydratase, mitochondrial
- Malate dehydrogenase, mitochondrial
- ATP-citrate synthase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Fumarate hydratase, mitochondrial
- Pyruvate carboxylase, mitochondrial
Sequence:
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
Protein: Hypoxia-inducible factor 1-alpha (F1QNB9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Egl-9 family hypoxia-inducible factor 3.
- Hypoxia-inducible factor 1 subunit alpha,-like
- Hypoxia-inducible factor 1-alpha
- Cellular tumor antigen p53
- Catenin beta-1
- Aryl hydrocarbon receptor nuclear translocator.
- Cullin 2
- Von Hippel-Lindau tumor suppressor.
- hypoxia-inducible factor-proline dioxygenase
- histone acetyltransferase
Sequence:
MEAVAPGKKRVSSERRKEKSRDAARCRRGKESEVFYELSRELPLPHSVTSNLDKASVMRLALSYLRLRKLLNSDVLEKETALDTQWNGSFLKALDGFLLVLSADGDIVYLSENVSKCLGLPQIELTGHSVFEFTHPCDHEELREMLAHRFGLSKKSKDQNTNRSFLLRMKCTLTSRGRTVNVKSASWKVLRCSGRIHTADGVEKEVCEEKNTCSTYLVLICESIPHPANIEAPLDSRTFLSRHTLDMRFTYCDERITELLGFDPEDVLQHSVYEYYHALDSDHMTKTHHSLFVKGQVCTGQYRLLAKAGGFVWAETQATVIYNSKNSQAQCVVCVNYILSGIEQPKQILSLQQTNSTKIKQEEHQEEVEVTMAELKEEEKEMDKEDEECVQPVVQHNSLKGETEALTVADPVLTLDINITDSAISVLTEIPLYNDVMLPSSDVLLPLSPLSPPCSSLNDDEASTGHLQHDQFPFQQSSDSSRSQVDLPVDSELCDQLKPDHVEKHFSMDIESKTQGVGLDLEMLAPYIPMDDDFQLRTVSPVRPMCSSPCSGLDLTPSSSTQTSPALSAATPDSLSCDPVQQKNKTTVQDHSREIIQDSDISYKCQTNPKLLKRKLETIPLSEAIRLGSVLQVVTDFPEKKVRKTDAPSSEGIRHATILLLPSNVASRLLSRSSEGGAIAMPLPQITHHDCEVNAPVIGRQHLLQGEELLCALDLVI
Protein: Universal stress protein B (P0A8S5)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Universal stress protein A
- Universal stress protein E
- Universal stress protein D
- Universal stress protein F
- Uncharacterized protein YcgB
- Uncharacterized protein YodD
- Universal stress protein UP12
- Uncharacterized protein YhfG
- Probable protein adenylyltransferase Fic
- DNA-binding transcriptional regulator BolA
Sequence:
MISTVALFWALCVVCIVNMARYFSSLRALLVVLRNCDPLLYQYVDGGGFFTSHGQPNKQVRLVWYIYAQRYRDHHDDEFIRRCERVRRQFILTSALCGLVVVSLIALMIWH
Protein: Rhino (Q49BK7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTSGMSKMDQKKGKNIKKTARKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIQSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPNWKFPEITKPFGVNRGLDLDEILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK
Protein: Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic (PPIase CYP38) (EC 5.2.1.8) (Rotamase CYP38) (Thylakoid lumen PPIase) (Q9SSA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the assembly and stabilization of PSII, but has no PPIases activity.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:11826309, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Oxygen-evolving enhancer protein 1-2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP20-2, chloroplastic
- PsbP-like protein 1, chloroplastic
- Thylakoid lumenal 17.4 kDa protein, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Photosystem II stability/assembly factor HCF136
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Protein disulfide-isomerase LQY1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP16-3, chloroplastic
Sequence:
MAAAFASLPTFSVVNSSRFPRRRIGFSCSKKPLEVRCSSGNTRYTKQRGAFTSLKECAISLALSVGLMVSVPSIALPPNAHAVANPVIPDVSVLISGPPIKDPEALLRYALPIDNKAIREVQKPLEDITDSLKIAGVKALDSVERNVRQASRTLQQGKSIIVAGFAESKKDHGNEMIEKLEAGMQDMLKIVEDRKRDAVAPKQKEILKYVGGIEEDMVDGFPYEVPEEYRNMPLLKGRASVDMKVKIKDNPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDGFVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGEKTPFYGSTLEELGLYKAQVVIPFNAFGTMAMAREEFENDSGSSQVFWLLKESELTPSNSNILDGRYAVFGYVTDNEDFLADLKVGDVIESIQVVSGLENLANPSYKIAG