wanglab/gogpt-training-data huggingface dataset:
Protein: Megakaryocyte-associated tyrosine-protein kinase (EC 2.7.10.2) (CSK homologous kinase) (CHK) (Hematopoietic consensus tyrosine-lacking kinase) (Protein kinase HYL) (Tyrosine-protein kinase CTK) (P42679)
Organism: Homo sapiens (Human)
Function: Could play a significant role in the signal transduction of hematopoietic cells. May regulate tyrosine kinase activity of SRC-family members in brain by specifically phosphorylating their C-terminal regulatory tyrosine residue which acts as a negative regulatory site. It may play an inhibitory role in the control of T-cell proliferation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9171348}. Membrane {ECO:0000269|PubMed:9171348}. Note=In platelets, 90% of MATK localizes to the membrane fraction, and translocates to the cytoskeleton upon thrombin stimulation.
Interaction partners:
- High affinity nerve growth factor receptor
- BDNF/NT-3 growth factors receptor
- NT-3 growth factor receptor
- Receptor tyrosine-protein kinase erbB-2
- Signaling lymphocytic activation molecule
- CD48 antigen
- Receptor-type tyrosine-protein phosphatase C
- Proteasome subunit alpha type-7
- Small ribosomal subunit protein uS9
- Tyrosine-protein phosphatase non-receptor type substrate 1
Sequence:
MAGRGSLVSWRAFHGCDSAEELPRVSPRFLRAWHPPPVSARMPTRRWAPGTQCITKCEHTRPKPGELAFRKGDVVTILEACENKSWYRVKHHTSGQEGLLAAGALREREALSADPKLSLMPWFHGKISGQEAVQQLQPPEDGLFLVRESARHPGDYVLCVSFGRDVIHYRVLHRDGHLTIDEAVFFCNLMDMVEHYSKDKGAICTKLVRPKRKHGTKSAEEELARAGWLLNLQHLTLGAQIGEGEFGAVLQGEYLGQKVAVKNIKCDVTAQAFLDETAVMTKMQHENLVRLLGVILHQGLYIVMEHVSKGNLVNFLRTRGRALVNTAQLLQFSLHVAEGMEYLESKKLVHRDLAARNILVSEDLVAKVSDFGLAKAERKGLDSSRLPVKWTAPEALKHGKFTSKSDVWSFGVLLWEVFSYGRAPYPKMSLKEVSEAVEKGYRMEPPEGCPGPVHVLMSSCWEAEPARRPPFRKLAEKLARELRSAGAPASVSGQDADGSTSPRSQEP
Protein: Cadaverine/lysine antiporter (P0AAE8)
Organism: Escherichia coli (strain K12)
Function: Under acidic conditions, in the presence of lysine, functions as a cadaverine:lysine antiporter that facilitates the excretion of cadaverine and the uptake of lysine. At neutral pH, also catalyzes the uptake of cadaverine via a proton symport mechanism, however the physiological relevance of this uptake activity is probably negligible because the expression of cadB is low at neutral pH. Cadaverine uptake activity is low at acidic pH.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16877381}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inducible lysine decarboxylase
- Transcriptional activator CadC
- Inducible ornithine decarboxylase
- Constitutive lysine decarboxylase
- Glutamate decarboxylase alpha
Sequence:
MSSAKKIGLFACTGVVAGNMMGSGIALLPANLASIGGIAIWGWIISIIGAMSLAYVYARLATKNPQQGGPIAYAGEISPAFGFQTGVLYYHANWIGNLAIGITAVSYLSTFFPVLNDPVPAGIACIAIVWVFTFVNMLGGTWVSRLTTIGLVLVLIPVVMTAIVGWHWFDAATYAANWNTADTTDGHAIIKSILLCLWAFVGVESAAVSTGMVKNPKRTVPLATMLGTGLAGIVYIAATQVLSGMYPSSVMAASGAPFAISASTILGNWAAPLVSAFTAFACLTSLGSWMMLVGQAGVRAANDGNFPKVYGEVDSNGIPKKGLLLAAVKMTALMILITLMNSAGGKASDLFGELTGIAVLLTMLPYFYSCVDLIRFEGVNIRNFVSLICSVLGCVFCFIALMGASSFELAGTFIVSLIILMFYARKMHERQSHSMDNHTASNAH
Protein: Xyloside xylosyltransferase 1 (EC 2.4.2.62) (UDP-xylose:alpha-xyloside alpha-1,3-xylosyltransferase) (Q3U4G3)
Organism: Mus musculus (Mouse)
Function: Alpha-1,3-xylosyltransferase, which elongates the O-linked xylose-glucose disaccharide attached to EGF-like repeats in the extracellular domain of target proteins by catalyzing the addition of the second xylose. Known targets include Notch proteins and coagulation factors, such as F9.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NBI6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NBI6}.
Interaction partners:
- Coagulation factor IX
- Protein O-glucosyltransferase 1
- GDP-fucose protein O-fucosyltransferase 1
Sequence:
MGLLRGGAACARAMARLGALRSHYCALLLAAALAVCAFYYLGSGRETFSSATKRLKEARAGAAAPTPPAPELARGSAAPASGAKAKSLEGGVVVPVDYHLLMMFTKAEHNAPLQAKARVALSSLLRLAKFEAHEVLNLHFVSEEASREVAKALLRELLPPAAGFKCKVIFHDVAVLTDKLFPVVEAMQKYFSAGSGTYYSDSIFFLSVAMHQIMPKEIPRIIQLDLDLKYKTNIRELFEEFDNFLPGAVIGIAREMQPVYRHTFWQFRHENPKTRVGDPPPEGLPGFNSGVMLLNLEAMRQSPLYSHLLEPSWVQQLADKYHFRGHLGDQDFFTMIGMEHPELFHVLDCTWNRQLCTWWRDHGYSDVFQAYFRCEGHVKIYHGNCNTPIPED
Protein: 4-hydroxyproline betaine 2-epimerase (Hyp-B 2-epimerase) (EC 5.1.1.22) ((4R)-4-hydroxyproline betaine 2-epimerase) (Q0FPQ4)
Organism: Salipiger bermudensis (strain DSM 26914 / JCM 13377 / KCTC 12554 / HTCC2601) (Pelagibaca bermudensis)
Function: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. To a lesser extent, can also catalyze the racemization of L-proline betaine.
Interaction partners:
- Possible dioxygenase reductase subunit
- Probable dienelactone hydrolase protein
Sequence:
MKIAEIQLFQHDLPVVNGPYRIASGDVWSLTTTIVKIIAEDGTIGWGETCPVGPTYAEAHAGGALAALEVLASGLAGAEALPLPLHTRMDSLLCGHNYAKSALDIAVHDLWGKRLGVPVHELLGGALTDSVSSYYSLGVMEPDEAARQALEKQREGYSRLQVKLGARPIEIDIEAIRKVWEAVRGTGIALAADGNRGWTTRDALRFSRECPDIPFVMEQPCNSFEDLEAIRPLCHHALYMDEDGTSLNTVITAAATSLVDGFGMKVSRIGGLQHMRAFRDFCAARNLPHTCDDAWGGDIVSAACTHIASTVLPRLMEGAWLAQPYVAEHYDAENGVRIEGGRIRVPQGPGLGLTIDPERFGPPLFSA
Protein: Cytochrome b6-f complex subunit 8 (Cytochrome b6-f complex subunit PetN) (Cytochrome b6-f complex subunit VIII) (Q6ENI5)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00395}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00395}.
Interaction partners:
Sequence:
MDIVSLAWAALMVVFTFSLSLVVWGRSGL
Protein: Shugoshin (Q08490)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a central role in chromosome cohesion during mitosis and meiosis divisions by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. Probably act by protecting REC8 and RAD21 from separase degradation during anaphase. Also acts as a spindle checkpoint component required for sensing tension between sister chromatids during mitosis, its degradation when they separate preventing cell cycle arrest and chromosome loss in anaphase, a time when sister chromatids are no longer under tension.
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:14752166, ECO:0000269|PubMed:15062096}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15062096}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15062096}. Note=Localizes to the centromere during S and M phases, dissociates at the onset of anaphase. Colocalizes with kinetochores. Associates with the spindle pole. {ECO:0000269|PubMed:15062096}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Separin
- Protein phosphatase PP2A regulatory subunit A
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Histone H3
- Meiotic recombination protein REC8
- Inner centromere protein SLI15
- Meiosis-specific protein SPO13
Sequence:
MPKRKIAPNKESSRRTVSHDDLTPQIQEFQNLMDLESQKVENIRQSYSRQNSLLAKDNSILKIKVNSLEKKISQLVQENVTLRSKTSISEAIYRERLSNQLQVIENGIIQRFDEIFYMFENVRKNENLPSSSLRTMLKRTSSRSRSCSLSSPTYSKSYTRLSNHENNLSHESSFNKDDGPDLEPKAKKRKSSRRQSMFVSTSLEPEDETGENEPMMENSSVEVPAESHESAQVEETIDALNPEEENSDSVSNFTNSIIEYSIPEENPTEPEHSSSKLEIFNDSTNMLSTVPSNPLPLPLPGPSATLPTTTSDASTVYPSSSSSTNSHPKTKIKHSMKPPRIELKKKVIDEVMPVSNMSSNSEISFTRTRRTRGKAVDYTLPSLRAKMRRPSEKLVDATTVIDIHDLQVSKRNRETSHKRKSLSQDSIPDEPQLREVVVSKDYGTPKGKKTEDEIHEDTAHLMTTSNNNSNNKNEKKLTSNNSPKKSSPLLDITNKSENKKKSTRTKKLFKNAIVNNLSDENSTTRPSKSSKGTSNNNNNYNNFDNNNSNINNVNNKSVSFRLNEDDLAVFDLFGNGKAVKHQPKTYRTKK
Protein: Benzoate 4-monooxygenase bphA (EC 1.14.14.92) (Benzoate-para-hydroxylase A) (BpH) (Cytochrome P450 monooxygenase cyp53A1) (P17549)
Organism: Aspergillus niger
Function: Cytochrome P450 monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway. Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH. 4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Ref.6). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Ref.6).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLALLLSPYGAYLGLALLVLYYLLPYLKRAHLRDIPAPGLAAFTNFWLLLQTRRGHRFVVVDNAHKKYGKLVRIAPRHTSIADDGAIQAVYGHGNGFLKSDFYDAFVSIHRGLFNTRDRAEHTRKRKTVSHTFSMKSIGQFEQYIHGNIELFVKQWNRMADTQRNPKTGFASLDALNWFNYLAFDIIGDLAFGAPFGMLDKGKDFAEMRKTPDSPPSYVQAVEVLNRRGEVSATLGCYPALKPFAKYLPDSFFRDGIQAVEDLAGIAVARVNERLRPEVMANNTRVDLLARLMEGKDSNGEKLGRAELTAEALTQLIAGSDTTSNTSCAILYWCMRTPGVIEKLHKALDEAIPQDVDVPTHAMVKDIPYLQWVIWETMRIHSTSAMGLPREIPAGNPPVTISGHTFYPGDVVSVPSYTIHRSKEIWGPDAEQFVPERWDPARLTPRQKAAFIPFSTGPRACVGRNVAEMELLVICGTVFRLFEFEMQQEGPMETREGFLRKPLGLQVGMKRRQPGSA
Protein: Linear primary-alkylsulfatase (EC 3.1.6.21) (Type III linear primary-alkylsulfatase) (P32717)
Organism: Escherichia coli (strain K12)
Function: Alkylsulfatase that cleaves the widely used detergent sodium dodecyl sulfate (SDS).
Subcellular location: Periplasm {ECO:0000269|PubMed:25066955}.
Interaction partners:
- D-allose import ATP-binding protein AlsA
- D-allose transport system permease protein AlsC
- D-allulose-6-phosphate 3-epimerase
- D-allose-binding periplasmic protein
- D-allose kinase
- Uncharacterized protein YtcA
- Multidrug resistance protein MdtO
- Inner membrane protein YjeO
- Multidrug resistance outer membrane protein MdtP
- Multidrug resistance protein MdtN
Sequence:
MNNSRLFRLSRIVIALTAASGMMVNTANAKEEAKAATQYTQQVNQNYAKSLPFSDRQDFDDAQRGFIAPLLDEGILRDANGKVYYRADDYKFDINAAAPETVNPSLWRQSQINGISGLFKVTDKMYQVRGQDISNITFVEGEKGIIVIDPLVTPPAAKAALDLYFQHRPQKPIVAVIYTHSHTDHYGGVKGIISEADVKSGKVQVIAPAGFMDEAISENVLAGNIMSRRALYSYGLLLPHNAQGNVGNGLGVTLATGDPSIIAPTKTIVRTGEKMIIDGLEFDFLMTPGSEAPAEMHFYIPALKALCTAENATHTLHNFYTLRGAKTRDTSKWTEYLNETLDMWGNDAEVLFMPHTWPVWGNKHINDYIGKYRDTIKYIHDQTLHLANQGYTMNEIGDMIKLPPALANNWASRGYYGSVSHNARAVYNFYLGYYDGNPANLHPYGQVEMGKRYVQALGGSARVINLAQEANKQGDYRWSAELLKQVIAANPGDQVAKNLQANNFEQLGYQAESATWRGFYLTGAKELREGVHKFSHGTTGSPDTIRGMSVEMLFDFMAVRLDSAKAAGKNISLNFNMSNGDNLNLTLNDSVLNYRKTLQPQADASFYISREDLHAVLTGQAKMADLVKAKKAKIIGNGAKLEEIIACLDNFDLWVNIVTPN
Protein: STE20-related kinase adapter protein beta (STRAD beta) (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein homolog) (ILP-interacting protein homolog) (Polyploidy-associated protein kinase) (Pseudokinase ALS2CR2) (Q8K4T3)
Organism: Mus musculus (Mouse)
Function: Pseudokinase which, in complex with CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta), binds to and activates STK11/LKB1. Adopts a closed conformation typical of active protein kinases and binds STK11/LKB1 as a pseudosubstrate, promoting conformational change of STK11/LKB1 in an active conformation (By similarity).
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Calcium-binding protein 39
- Calcium-binding protein 39-like
- Serine/threonine-protein kinase STK11
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- STE20-related kinase adapter protein alpha
- Translocation protein SEC63 homolog
- Protein transport protein Sec61 subunit gamma
- DDB1- and CUL4-associated factor 12
- 5'-AMP-activated protein kinase subunit gamma-1
Sequence:
MSLLDCFCASRTRVESLRPEKQSETSIHQYLVDESAISRPPPSARASEVICSTDVSHYELQVEIGRGFDNLTSVHLARHTPTGTLVTVKITNLESCTEERLKALQRAVILSHFFQHPNITTYWTVFTVGSWLWVISPFMAYGSASQLLRTYFPDGMSETLIRNILFGAVQGLNYLHQNGCIHRSFKASHILISGDGLVTLSGLSHLHSLLKHGQRHRAVFDFPQFSTSVQPWLSPELLRQDLHGYNVKSDIYSVGITACELASGQVPFQDMHRTQMLLQKLKGPPYSPLDVSIFPQSDSRMRNSQSGVDSGIGESVLVSTGTHTVNSDRLHTPSTKTFSPAFFSLVQLCLQQDPEKRPSASSLLSHVFFKQMKEESQDSILPLLPPAYNRPSASLQPVSPWSELEFQFPDDKDPVWEF
Protein: Alpha-S2-casein-like A (Casein alpha S2-like A) (Gamma-casein) (PP22) (Q02862)
Organism: Mus musculus (Mouse)
Function: Important role in the capacity of milk to transport calcium phosphate.
Subcellular location: Secreted.
Interaction partners:
- Alpha-S1-casein
- Beta-casein
- Alpha-S2-casein-like B
- Whey acidic protein
- Kappa-casein
Sequence:
MKFFIFACLVVVALAKHEIKDKSSSEESSASIYPGKSKLDNSVFFQTTKDSASSSSSEESSEEVSEKIVQSEEQKVNLNQQKKFKQFSQESSFSQCCTPLHQQQQSSVNQWPQPNAIHNTPTQESISTSVEEILKKIIDMIKYIQYQQVTIPQLPQALHPQIPVSYWYPSKDYTFPNAHYTRFY
Protein: NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (Q6DHI5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}. Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03160}.
Interaction partners:
- Glutamine-dependent NAD
- Nicotinamide phosphoribosyltransferase
- Nicotinamide phosphoribosyltransferase
- Nudix-type motif 12.
- Uncharacterized protein LOC393330
- NAD
- Nicotinamide nucleotide transhydrogenase 2.
- Uncharacterized protein.
- Ectonucleotide pyrophosphatase/phosphodiesterase 1
- Sirtuin 6
Sequence:
MIVRQLWCSRGSTSHLCAAVRLNWRSPKMTRPSSDLTAFREHFAKAKHIAIITGAGVSAESGVPTFRGPGGFWRKWQAQDLATPEAFSRDPSLVWEFYHYRREVMRSKMPNPAHLAIAECEARLGQQGRSVVIITQNIDELHHRAGSKHVYEIHGSLFKTRCMSCGEVKANHKSPICPALDGKGAPDPNTKEARIPVELLPRCERKSCNGLLRPHVVWFGETLDSDILTAVERELEKCDLCLVVGTSSIVYPAAMFAPQVASRGVPVAEFNMECTPATQRFKYHFEGPCGSTLPPALERHESEAV
Protein: D-lactate dehydrogenase [cytochrome] 1, mitochondrial (EC 1.1.2.4) (D-lactate ferricytochrome C oxidoreductase) (D-LCR) (P32891)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the stereospecific oxidation of D-lactate to pyruvate.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}.
Interaction partners:
- L-lactate dehydrogenase
- Hydroxyacylglutathione hydrolase, mitochondrial
- Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
- External NADH-ubiquinone oxidoreductase 2, mitochondrial
- External NADH-ubiquinone oxidoreductase 1, mitochondrial
- Pyruvate kinase 1
- Pyruvate kinase 2
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2
- NAD-dependent malic enzyme, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
Sequence:
MLWKRTCTRLIKPIAQPRGRLVRRSCYRYASTGTGSTDSSSQWLKYSVIASSATLFGYLFAKNLYSRETKEDLIEKLEMVKKIDPVNSTLKLSSLDSPDYLHDPVKIDKVVEDLKQVLGNKPENYSDAKSDLDAHSDTYFNTHHPSPEQRPRIILFPHTTEEVSKILKICHDNNMPVVPFSGGTSLEGHFLPTRIGDTITVDLSKFMNNVVKFDKLDLDITVQAGLPWEDLNDYLSDHGLMFGCDPGPGAQIGGCIANSCSGTNAYRYGTMKENIINMTIVLPDGTIVKTKKRPRKSSAGYNLNGLFVGSEGTLGIVTEATVKCHVKPKAETVAVVSFDTIKDAAACASNLTQSGIHLNAMELLDENMMKLINASESTDRCDWVEKPTMFFKIGGRSPNIVNALVDEVKAVAQLNHCNSFQFAKDDDEKLELWEARKVALWSVLDADKSKDKSAKIWTTDVAVPVSQFDKVIHETKKDMQASKLINAIVGHAGDGNFHAFIVYRTPEEHETCSQLVDRMVKRALNAEGTCTGEHGVGIGKREYLLEELGEAPVDLMRKIKLAIDPKRIMNPDKIFKTDPNEPANDYR
Protein: YEATS domain-containing protein (Q57ZF8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00376}.
Interaction partners:
- RuvB-like helicase
- SNF2 DNA repair protein, putative
- RuvB-like helicase
- Transmembrane protein, conserved
- HIT-type domain-containing protein
Sequence:
MIHGNAAPISRAFTIHFKGELFRALIDCRTALTLRDLIAVAVPNPSGSNSSSTTTGDFSTDWVDNCICAFGGQRLSLDTLTESAPLVLDVSWSESARGGTRKRMRRDFISFKEEDRNLLPCKVSQEEIGYSGRKSGSKEIKNNIDDKYSVFDAKSGVVLSFDSSSRYGVEGKFSADDNNSNDNSCSSDDGEDDDCINSEGRTPCEDYDDRQYEAILPVVVGGVVRLVNMESRDKSHEWTVYVRGLFNESKYLADCIESVRFFLDASFTPSERLVTSPPFELTEVGWGEFIVKVSIQLRHYPRPIQIDLSSSSASPVTSGVVKSPSLLPLLPTSAETLSDVKVASAILSPSTADGPLIGLTNGPALSPLISVLSRHHYHGCASDSVGHTIVKKEEEEEGDDQCTKCDAKRNVFGSTEKAEEAGRRAQNNNCVNVLFNPNASVSSDVETLGTCSGVVVLSHLLRFSHRVKRLHCIPPLGRPYEPEEHVGYTLVQHPVVTEHYDEIVIPDAPLEIKKALASLPELLQNRVSSVKGVRAPTTQQQGNHRGSTTLHRDAVASIYAEDGVSCWKYIKHEELDDIALAEAYLDNLSTCPKSFFHVDSHVVEANQPLALPRPGRGRRKLMGAEIDLAALRAAKKGLTDAIGRMRREAVLRQAAHIYQQYT
Protein: SEC24 homolog D, COPII coat complex component (E9PDM8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
Sequence:
MCPFMQFIEGGRRYQCGFCNCVNDVPPFYFQHLDHIGRRLDHYEKPELSLGSYEYVATLDYCRKSKPPNPPAFIFMIDVSYSNIKNGLVKLICEELKTMLEKIPKEEQEETSAIRVGFITYNKVLHFFNVKSNLAQPQMMVVTDVGEVFVPLLDGFLVNYQESQSVIHNLLDQIPDMFADSNENETVFAPVIQAGMEALKAADCPGKLFIFHSSLPTAEAPGKLKNRDDKKLVNTDKEKILFQPQTNVYDSLAKDCVAHGCSVTLFLFPSQYVDVASLGLVPQLTGGTLYKYNNFQMHLDRQQFLNDLRNDIEKKIGFDAIMRVRTSTGFRATDFFGGILMNNTTDVEMAAIDCDKAVTVEFKHDDKLSEDSGALIQCAVLYTTISGQRRLRIHNLGLNCSSQLADLYKSCETDALINFFAKSAFKAVLHQPLKVIREILVNQTAHMLACYRKNCASPSAASQLILPDSMKVLPVYMNCLLKNCVLLSRPEISTDERAYQRQLVMTMGVADSQLFFYPQLLPIHTLDVKSTMLPAAVRCSESRLSEEGIFLLANGLHMFLWLGVSSPPELIQGIFNVPSFAHINTDMTLLPEVGNPYSQQLRMIMGIIQQKRPYSMKLTIVKQREQPEMVFRQFLVEDKGLYGGSSYVDFLCCVHKEICQLLN
Protein: pH-responsive protein 2 (pH-regulated protein 2) (O13318)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for apical cell growth and plays an essential role in morphogenesis. May be integral to the pathogenic ability of the organism (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Glucan 1,3-beta-glucosidase BGL2
- Cell surface GPI-anchored protein ECM33
- Ecm33p
- Crh-like protein UTR2
- Crh-like protein CRH11
- Cell surface mannoprotein MP65
Sequence:
MLLKSLFPSILAATSFVSSVAAEDLPAIEIVGNKFFYSNNGSQFYIKGIAYQQNNLDSNESFVDPLANPEHCKRDIPYLEAVDTNVIRVYALDTSQDHTECMQMLQDAGIYVIADLSQPDESINRDDPSWDLDLFERYTSVVDLFHNYTNILGFFAGNEVTNKKSNTDASAFVKAAIRDTKAYIKSKGYRSIPVGYSANDDSAIRVSLADYFACGDEDEAADFFGINMYEWCGDSSYKASGYESATNDYKNLGIPIFFSEYGCNEVRPRKFTEVATLFGDQMTPVWSGGIVYMYFEEENNYGLVSIKDNTVSTLKDYSYYSSEIKDIHPSSAKASAESASSISRTTCPTNTNNWEASTNLPPTPDKEVCECMSASLKCVVDDKVDSDDYSDLFSYICAKIDCDGINANGTTGEYGAYSPCHSKDKLSFVMNLYYEQNKESKSACDFGGSASLQSAKTASSCSAYLSSAGSSGLGTVSGTVRTDTSQSTSDSGSGSSSSSSSSSSSSSSGSSGSKSAASIVSVNLLTKIATIGISIVVGFGLITM
Protein: Angio associated migratory cell protein (C9JG97)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLSVPLTASRAPSSNPLPKADDLAQEMEDVDFEEEEEEEGNEEGWVLEPQEGVVGSMEGPDDSEVTFALHSASVFCVSLDPKTNTLAVTGGEDDKAFVWRLSDGELLFECAGHKDSVTCAGFSHDSTLVATGDMSGLLKVWQVDTKEEVWSFEAGDLEWMEWHPRAPVLLAGTADGNTWMWKVPNGDCKTFQGPNCPATCGRVLPDGKRAVVGYEDGTIRIWDLKQGSPIHVLKGTEGHQGPLTCVAANQDGSLILTGSVDCQAKLVSATTGKVVGVFRPETVASQPSLGEGEESESNSVESLGFCSVMPLAAVGYLDGTLAIYDLATQTLRHQCQHQSGIVQLLWEAGTAVVYTCSLDGIVRLWDARTGRLLTDYRGHTAEILDFALSKDASLVVTTSGDHKAKVFCVQRPDR
Protein: Voltage-dependent L-type calcium channel subunit beta-3 (CAB3) (Calcium channel voltage-dependent subunit beta 3) (P54287)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. Increases CACNA1B peak calcium current and shifts the voltage dependencies of channel activation and inactivation (By similarity). Increases CACNA1C peak calcium current and shifts the voltage dependencies of channel activation and inactivation.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:10666413}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent calcium channel subunit alpha-2/delta-2
Sequence:
MYDDSYVPGFEDSEAGSADSYTSRPSLDSDVSLEEDRESARREVESQAQQQLERAKHKPVAFAVRTNVSYCGVLDEECPVQGSGVNFEAKDFLHIKEKYSNDWWIGRLVKEGGDIAFIPSPQRLESIRLKQEQKARRSGNPSSLSDIGNRRSPPPSLAKQKQKQAEHVPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADLSLAKRSVLNNPGKRTIIERSSARSSIAEVQSEIERIFELAKSLQLVVLDADTINHPAQLAKTSLAPIIVFVKVSSPKVLQRLIRSRGKSQMKHLTVQMMAYDKLVQCPPESFDVILDENQLDDACEHLAEYLEVYWRATHHPAPGPGMLGPPSAIPGLQNQQLLGERGEEHSPLERDSLMPSDEASESSRQAWTGSSQRSSRHLEEDYADAYQDLYQPHRQHTSGLPSANGHDPQDRLLAQDSEHDHNDRNWQRNRPWPKDSY
Protein: 3-beta-hydroxylase (Tp8878) (EC 1.14.14.-) (Cytochrome P450 71CB1) (X2EW55)
Organism: Tanacetum parthenium (Feverfew) (Matricaria parthenium)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti-cancer drugs highly active against colon cancer cells. Catalyzes the conversion of costunolide and parthenolide to 3-beta-hydroxycostunolide and 3-beta-hydroxyparthenolide, respectively.
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MFSSFETLILSFVSLFFMMIFIHSKWISSYSKMAKNLPPSPFGLPIIGNLHQLGMTPYNSLRTLAHKYGSLMLIHLGSVPVIVASSAEAAQEIMKTHDQIFSTRPKMNIASIVSFDAKIVAFSPYGEHWRQSKSVYLLNLLSTKRVQSFRHVREDETNLMLDVIENSCGSEIDLSNMIMSLTNDVVCRIAYGRKYYEDWFKELMKEVMDVLGVFSVGNYVPSLSWIDRLSGLEGRAYKAAKQLDAFLEGVVKQHETKSNESMRDQDVVDILLETQREQASAGTPFHRDTLKALMQEMFIAGTDTTSTAIEWEISEVIKHPRVMKKLQQELDEIAQGRQRITEEDLEDTQHPYLEAILKESMRLHIPVPLLLPREATHDVKVMGYDIAAGTQVLINAWMIARDPTIWEDADEFKPERFLDTNIDYKGLNFELLPFGAGRRGCPGIQFAMSVNKLALANLVYKFDFKLPNGLRLEQLDMTDSTGITVRRKYPLLVIPTARF
Protein: 4-alpha-glucanotransferase (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (Q8DT30)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Interaction partners:
- Alpha-1,4 glucan phosphorylase
- Alpha-1,4 glucan phosphorylase
- Endonuclease/exonuclease/phosphatase domain-containing protein
- Pullulanase
- Glycogen synthase
- 1,4-alpha-glucan branching enzyme GlgB
- Phosphoglucomutase
- Sucrose phosphorylase
- Intracellular alpha-amylase
- Glycogen biosynthesis protein GlgD
Sequence:
MEKRASGILMHISSLPGKFGIGTFGQEAYDFVDFLKKTGQTYWQLLPLTTTSYGDSPYQSFSAVAGNVNFIDFKKLQEAGLLDEDDYNSVSFGEDEEIVDYALLFKVRRPILEKAVINFLADKTNLKKLALFEEKNETWLDDYAEFMAIKEHFGNKSLQEWGDKKAIRRDEERLVRYRHLLADEISYHKVTQYFFFEQWLALKAYANKNKIKIIGDMPIYVAKDSVEVWTMPELFKMDDDLQPLSVAGCPPDEFSDEGQLWGNPIYDWKKHRETGFAWWIYRIQESFKIYDILRIDHFKGFSDYWEIKGNSKTAKNGSWHPGPGIALFRAVQNVLGDMPIIAEDLGYVDDRARQLLKETGFPGMKILEFGFYDLSGRSVDIPHHYVQNSVAYIGTHDNDVVNGWYDRLTVEQEEFVDAYTNRKPIEPVNQAMLRLLFSTVSNTAILTMQDLLNKPASSRMNTPSTIGGNWQWRMRAKDLTQDKINFLSKLTKLYQRGNEENDTKNKTIQ