wanglab/gogpt-training-data huggingface dataset:
Protein: (3aS,4S,5R,7aS)-5-hydroxy-7a-methyl-1-oxo-octahydro-1H-indene-4-carboxyl-CoA dehydrogenase (5OH-HIC-CoA dehydrogenase) (EC 1.3.1.-) (P71847)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the final steps of cholesterol and steroid degradation. Probably catalyzes the introduction of a double bound into the C ring of 5OH-HIC-CoA, leading to the formation of (5R,7aS)-5-hydroxy-7a-methyl-1-oxo-3,5,6,7-tetrahydro-2H-indene-4-carboxyl-CoA (Probable).
Interaction partners:
- Cholesterol ring-cleaving hydrolase IpdA subunit
- (7aS)-7a-methyl-1,5-dioxo-2,3,5,6,7,7a-hexahydro-1H-indene-carboxyl-CoA hydrolase (HIEC-CoA hydrolase)
- Probable short-chain type dehydrogenase/reductase
- Cholesterol ring-cleaving hydrolase IpdB subunit
- Probable short-chain type dehydrogenase/reductase
- 
- Acyl-CoA dehydrogenase IpdE1
- Probable acyl-CoA dehydrogenase FadE32
- 3-[
- Probable acyl-CoA dehydrogenase FadE31
Sequence:
MRLRTPLTELIGIEHPVVQTGMGWVAGARLVSATANAGGLGILASATMTLDELAAAITKVKAVTDKPFGVNIRADAADAGDRVELMIREGVRVASFALAPKQQLIARLKEAGAVVIPSIGAAKHARKVAAWGADAMIVQGGEGGGHTGPVATTLLLPSVLDAVAGTGIPVIAAGGFFDGRGLAAALCYGAAGVAMGTRFLLTSDSTVPDAVKRRYLQAGLDGTVVTTRVDGMPHRVLRTELVEKLESGSRARGFAAALRNAGKFRRMSQMTWRSMIRDGLTMRHGKELTWSQVLMAANTPMLLKAGLVDGNTEAGVLASGQVAGILDDLPSCKELIESIVLDAITHLQTASALVE
Protein: Protein SSX4 (Cancer/testis antigen 5.4) (CT5.4) (O60224)
Organism: Homo sapiens (Human)
Function: Could act as a modulator of transcription.
Interaction partners:
- Protein SSXT
- Calcium-responsive transactivator
- Hypoxia-inducible factor 1-alpha
- Afadin- and alpha-actinin-binding protein
- SS18-like protein 2
Sequence:
MNGDDAFARRPRDDAQISEKLRKAFDDIAKYFSKKEWEKMKSSEKIVYVYMKLNYEVMTKLGFKVTLPPFMRSKRAADFHGNDFGNDRNHRNQVERPQMTFGSLQRIFPKIMPKKPAEEENGLKEVPEASGPQNDGKQLCPPGNPSTLEKINKTSGPKRGKHAWTHRLRERKQLVVYEEISDPEEDDE
Protein: HTLV-1 basic zipper factor (HBZ) (P0C746)
Organism: Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1)
Function: Contributes to the regulation of viral RNA transcription by interacting with host proteins involved in transcriptional activation such as ATF4, or CREB1, and by inhibiting their activity. Additionally, HBZ suppresses host NF-kappa-B-driven transcription mediated by host RELA as well as transcription of some classical NF-kappa-B target genes, including IL8, IL2RA, IRF4, VCAM1, and VEGFA.
Subcellular location: Host nucleus {ECO:0000269|PubMed:12438606}.
Interaction partners:
Sequence:
MVNFVSAGLFRCLPVSCPEDLLVEELVDGLLSLEEELKDKEEEEAVLDGLLSLEEESRGRLRRGPPGEKAPPRGETHRDRQRRAEEKRKRKKEREKEEEKQTAEYLKRKEEEKARRRRRAEKKAADVARRKQEEQERRERKWRQGAEKAKQHSARKEKMQELGIDGYTRQLEGEVESLEAERRKLLQEKEDLMGEVNYWQGRLEAMWLQ
Protein: DnaJ heat shock protein family (Hsp40) member B6 (E9PH18)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFGVADDDALAEERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGLKEGGKRKKQKQREESKKKKSTKGNH
Protein: Somatotropin (I6WN98)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFALLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFRTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: DNA-directed RNA polymerases I and III subunit RPAC2 (RNA polymerases I and III subunit AC2) (AC19) (DNA-directed RNA polymerase I subunit D) (RNA polymerase I 16 kDa subunit) (RPA16) (RPC16) (hRPA19) (P0DPB6)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104}. Nucleus, nucleolus {ECO:0000305|PubMed:34887565}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase I subunit RPA34
Sequence:
MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIMKNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKDYKDQKASRNESTF
Protein: Soluble inorganic pyrophosphatase 1, chloroplastic (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase 1) (PPase 1) (Q93Y52)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16313235}.
Interaction partners:
Sequence:
MALAIRSSLRAAAMGRKAFRQAVPVRVAPAQRVRSVTTASAEITAYSVEEKGPKDSLEYRMFFKQGAKEVSCWHEIPLYAGDGHLHYICEIPKETSAKMEVATDEPRTPIKQDVKKGKLRFYPYNINWNYGMLPQTWEDPGHTDATLGAAGDNDPVDVVEIGAAAAKRGGVYKVKPVGVLAMIDDGELDWKVIAISADDPKAALCNDVEDVEKHFPGEIQKVLEWFRDYKIPDGKPANKFGYDNKCMNKEFTLNVIKETHEAYVKLKSGARANSEELSLI
Protein: Inosine-5'-monophosphate dehydrogenase 4 (IMP dehydrogenase 4) (IMPD 4) (IMPDH 4) (EC 1.1.1.205) (P50094)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase 3
- GMP synthase
- Inner kinetochore subunit NKP2
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase 2
- Bifunctional purine biosynthesis protein ADE16
- Bifunctional purine biosynthesis protein ADE17
- AMP deaminase
- Hypoxanthine-guanine phosphoribosyltransferase
- IMP-specific 5'-nucleotidase 1
Sequence:
MSAAPLDYKKALEHLKTYSSKDGLSVQELMDSTTRGGLTYNDFLVLPGLVNFPSSAVSLQTKLTKKITLNTPFVSSPMDTVTEADMAIYMALLGGIGFIHHNCTPKEQASMVKKVKMFENGFINSPIVISPTTTVGEVKVMKRKFGFSGFPVTEDGKCPGKLVGLVTSRDIQFLEDDSLVVSEVMTKNPVTGIKGITLKEGNEILKQTKKGKLLIVDDNGNLVSMLSRADLMKNQNYPLASKSATTKQLLCGAAIGTIEADKERLRLLVEAGLDVVILDSSQGNSVFQLNMIKWIKETFPDLEIIAGNVATREQAANLIAAGADGLRIGMGSGSICITQEVMACGRPQGTAVYNVCQFANQFGVPCMADGGVQNIGHITKALALGSSTVMMGGMLAGTTESPGEYFYKDGKRLKAYRGMGSIDAMQKTGNKGNASTSRYFSESDSVLVAQGVSGAVVDKGSIKKFIPYLYNGLQHSCQDIGCESLTSLKENVQNGEVRFEFRTASAQLEGGVHNLHSYEKRLYN
Protein: Cytokinesis protein 2 (Homolog of CDC15 protein 1) (Q05080)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Throughout most of the cell cycle it forms a double ring that coincides with the septins. After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Mediates cytoskeletal rearrangements required for cytokinesis. In conjunction with the medial actin ring exhibits contraction-like action.
Subcellular location: Cytoplasm, cytoskeleton. Bud neck.
Interaction partners:
- Cytokinesis protein 3
- Ras GTPase-activating-like protein IQG1
- Ingression protein 1
- Myosin-1
- Chitin synthase 2
- Myosin light chain 1
- BNI1-related protein 1
- RHO GTPase-activating protein RGD1
- High osmolarity signaling protein SHO1
- Cell division control protein 15
Sequence:
MSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETENKRKLASIDKYEKPLPSPEVTMATQFRNSTPVIRNETKVVANPTLSLRSSPVQLQSNVDDSVLRQKPDKPRPIVGEEQLKPDEDSKNPDEKGLMVHKRNQSLSSPSESSSSNPTDFSHIKKRQSMESMTTSVSSMANSIDDSQRFAKSWNSSNRKRKSMSHLQVPSSASSRSDDGGRTPNSAHNLNEDDYNTRRDTSTSTILFKPPVAVRGTSRGHTHRQSMIMQDSSNPIEDALYEMERIQSSSKPGTKTGNIMDERGVVRDRGITVTLPIVTSEGFPVIEYAKAMYPLIGNEAPGLANFHKGDYLLITEIVNKDWYKGEVYDNDRIDRNHRIGLIPYNFIQLLHQGL
Protein: U15-myrmicitoxin-Tb1b (U15-MYRTX-Tb1b) (A0A6M3Z4L2)
Organism: Tetramorium bicarinatum (Tramp ant)
Subcellular location: Secreted {ECO:0000269|PubMed:30149710}.
Interaction partners:
Sequence:
MKIVKLITIFAMIATLMVTVTNGEAVFLTPDQIKAMIKRHG
Protein: Prolactin (PRL) (P01240)
Organism: Ovis aries (Sheep)
Function: Prolactin acts primarily on the mammary gland by promoting lactation, mammogenesis, mitogenesis and osmoregulation.
Subcellular location: Secreted.
Interaction partners:
- Prolactin receptor
- Growth hormone receptor
- Tyrosine-protein kinase
- Pro-opiomelanocortin
- Oxytocin-neurophysin 1
- Uncharacterized protein
- Progonadoliberin-1
- Somatotropin
- Leptin receptor
- Signal transducer and activator of transcription 5A
Sequence:
MDSKGSAQKGSRLLLLLVVSNLLLCQGVVSTPVCPNGPGNCQVSLRDLFDRAVMVSHYIHNLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGVPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARHSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC
Protein: Uteroglobin (Club cell phospholipid-binding protein) (CCPBP) (Club cells 10 kDa secretory protein) (CC10) (Secretoglobin family 1A member 1) (Urinary protein 1) (UP-1) (UP1) (Urine protein 1) (P11684)
Organism: Homo sapiens (Human)
Function: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2.
Subcellular location: Secreted.
Interaction partners:
- Surfactant protein C
- Secretoglobin family 3A member 2
- Pulmonary surfactant-associated protein B
- Plexin-B1
- Secretoglobin family 3A member 1
- Pulmonary surfactant-associated protein D
- Pulmonary surfactant-associated protein A1
- Aquaporin-5
- Forkhead box protein J1
- Rod outer segment membrane protein 1
Sequence:
MKLAVTLTLVTLALCCSSASAEICPSFQRVIETLLMDTPSSYEAAMELFSPDQDMREAGAQLKKLVDTLPQKPRESIIKLMEKIAQSSLCN
Protein: Arachidonate 12-lipoxygenase, 12R-type (12R-LOX) (12R-lipoxygenase) (EC 1.13.11.-) (Epidermis-type lipoxygenase 12) (Epidermis-type lipoxygenase 2) (e-LOX 2) (O70582)
Organism: Mus musculus (Mouse)
Function: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. Does not convert arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
Interaction partners:
- Cytosolic phospholipase A2
- Cytosolic phospholipase A2 zeta
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Cytosolic phospholipase A2 epsilon
- Cytosolic phospholipase A2 beta
- Cytosolic phospholipase A2 gamma
- Polyunsaturated fatty acid
- Cytosolic phospholipase A2 delta
- Polyunsaturated fatty acid lipoxygenase ALOX15
Sequence:
MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKDPWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIPSYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIKNIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRILDGIPTVELNGQQQHHCAPMCLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLLESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLCIPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLGRESSGFPTCLRTIPELIEYVTMVMYTCSARHAAVNSGQLEYTSWMPNFPSSMRNPPMQTKGLTTLQTYMDTLPDVKTTCIVLLVLWTLCREPDDRRPLGHFPDIHFVEEGPRRSIEAFRQNLNQISHNIRQRNKCLTLPYYYLDPVLIENSISI
Protein: Phosphoglucomutase, cytoplasmic 1 (PGM 1) (EC 5.4.2.2) (Glucose phosphomutase 1) (P93804)
Organism: Zea mays (Maize)
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Subcellular location: Cytoplasm {ECO:0000303|PubMed:9662542}.
Interaction partners:
- Alpha-1,4 glucan phosphorylase
- Alpha-1,4 glucan phosphorylase
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-6-phosphate isomerase, cytosolic
- UTP--glucose-1-phosphate uridylyltransferase
- Phosphoacetylglucosamine mutase
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-6-phosphate isomerase
- BHLH transcription factor
Sequence:
MGLFTVTKKATTPFDGQKPGTSGLRKKVTVFQQPHYLQNFVQSTFNALPVDQVRGATIVVSGDGRYFSKDAVQIITKMAAANGVRRVWVGQNSLMSTPAVSAVIRERVGADGSKATGAFILTASHNPGGPKEDFGIKYNMGNGGPAPESVTDKIFSNTTTISEYLISEDLPDVDISVVGVTSFSGPEGPFDVDVFDSSVDYIKLMKTIFDFEAIKKLLTSPKFTFCYDALHGVAGAYAKHIFVEELGADESSLLNCVPKEDFGGGHPDPNLTYAKELVERMGLGKSSSNVEPPEFGAAADGDADRNMILGKRFFVTPSDSVAIIAANAVQSIPYFASGLKGVARSMPTSAALDVVAKNLNLKFFEVPTGWKFFGNLMDAGMCSICGEESFGTGSDHIREKDGIWAVLAWLSIIAFKNKDNLGGDKLVTVEDIVRQHWATYGRHYYTRYDYENVDAGAAKELMANLVSMQSSLSDVNKLVKEIRSDVSEVVAADEFEYKDPVDGSVSKHQGIRYLFGDGSRLVFRLSGTGSVGATIRVYIEQYERDSSKTGRDSQDALAPLVDVALKLSKMQEYTGRSAPTVIT
Protein: Metal regulatory transcription factor 1 (Metal-response transcription factor Mtf1) (Q8QGH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGENGPLSETAMLFEDEEEDVDKLGREEEDEDKMANFDKDGNMISGPSSSSGTVYDRTTVLIEQDPIRLDEEGEEDGMTFLPEGEGDEGSLAFMGDPDGMSQGYIHHTISPDQIQFIINPGSTPMPRNIEGATLTLHSECPETKQREVKRYQCLFEGCTRTYSTAGNLRTHQKTHRGEYTFVCNQQGCGKAFLTSYSLKIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESEGCTKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGEKPFFCPSDGCEKTFSSQYSLKSHIRGHDKGPSFTVSGHPLSEDANHSLCLSDLSLISTDSELQENHNSQGLDLNSVTPIRIFELMFQSPENSVSEDDPKPTESLAESFGLEPSPQSAPADASTHPAFPQPPPSTCSSSCSITAPAQDAQTPPTTQQAPPPAVSSSSQTSSFPSAPPSSSQPAEVSSPSAPSATQHYMMAQSVSSPSAASVSSVPAGTAEVTAAVTHTVPLAAPPTISIAPTLGLQPSLVMSDQNLQWILSSAASAQQNPEQQGPKVEKVFFTTAIPVGGNSGMIGY
Protein: proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (Q9VZY9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase
- isoleucine--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- Probable glutamine--tRNA ligase
- Alanine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase
- Probable arginine--tRNA ligase, mitochondrial
- leucine--tRNA ligase
Sequence:
MNKASRIFCPALITPKNAVVKQTEQLSRSQKLLTELGLVKSGSNGTYQIMPMAQRSVDKCIDLVQSNMQQAGGQKITLPILTPTGLWKKTGRLDGDISEFYMVRDRSGKQFLMSPTHEEAVTAMLATTSPISYRQLPLRLFQIGPKFRDELKTRFGLMRAKEFLMKDMYSFDVSEETAMETYTLVNAAYDRLFKQLEVPFVKVNAATGIMGGSVSHEYHYVSPVGEDNLLQCSSCGFAGNSEVVKAPASCPSCNSSDLKEVRGVEVAHTFLLGDKYSKPLGATFLNTTGKPQSLVMGCYGIGITRVIAAALEVLSSDHELRWPKLLAPYDVCLIGPKQGSKEQPEAEVIENELLLNVGEICGHQELLHDDRKELTIGKRLLEAKRLGHPLTIVVGAKSARLDSPKLEVHTSKGETYELDFSETLKLVAEHSQHKKSLERGCFQSETEESKSRSVGHQL
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q57YU1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit, putative
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor-like protein, putative
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
Sequence:
MNCREIIRKLLLNPAHNNAATRTAQGDNGDSNQRAYTRISRLAAFQSAQTQESTPKTNGTGRATTEGLTEAEVRWLVMESRALFMSQPMLVEIAAPVRICGDVHGQYTDLLRLFDLGGFPPDANYIFLGDYVDRGDQSLETICLLLAYKLSFPETFFLLRGNHECSSINRIYGFFDECKRRYSVRLWKQFTDTFNCMPVAGLVEGRILCMHGGLSPELTDLDQIRRILRPTDVPDSGLICDLLWSDPSTNMESNWSENDRGVSWTFSESVVKSFNKKFDLDLICRAHQVVDAGYEFFAARQLVTVFSAPNYCDEFDNAGAFMCVDENLMCSFVQIEPTRTLLRYFF
Protein: Seed allergenic protein RAG2 (Seed allergenic protein RA14) (allergen Ory s aA_TI) (Q01882)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Seed storage protein.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MASNKVVFSALLLIIVSVLAATATMADHHKDQVVYSLGERCQPGMGYPMYSLPRCRAVVKRQCVGHGAPGGAVDEQLRQDCCRQLAAVDDSWCRCSALNHMVGGIYRELGATDVGHPMAEVFPGCRRGDLERAAASLPAFCNVDIPNGTGGVCYWLGYPRTPRTGH
Protein: Transcription activator of gluconeogenesis ERT1 (A0A1D8PSC7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MKIKQENITNTTSINTSNVNDKPKPKRKKTSRACNHCHKAHMTCDSGRPCKRCIQRGLDSTCEDAPRKRKKYLQDVPNSSLMSNHSMNSSDNLDSNGVSPMQPTLSQPMPPVQESSLPTNIPNQSQVPSQSPNTASQKQLSYSPPLASTYSPNHKTYSATLFQHSATSPELMQTVPEYFPELYNQHYQPSANPNQKRRTNFLSTAADLEYSTLSNILQENFGHHTTSNEGTPNSHNFSPALSPHNMPTNNTNAPSTSTQLLTNDQQRQATSFNNHTKHNTPSPLNTSHTKLYEDARYPKCDETINQYFLGDTDSGKMVVFPDVLTAIENMKNNDPAVYLERNSKSALSFVMSIQHENNSNGGKEDQLFKEPEEIYEKVKKPFSYTPGYHSLIAYLRKRFTKPMLVKMAESMATYRPSFIACTNSLKEHDLIFMEQCFQRTLLTYDNYIKISGTPTIVWRRTGEVAYVGNEFCVLTGWPKEELIGKDKRKFIVELLDDKSVLQYFQVFSRIAFGDFLGATMTECTLLTPNPNVKIRTGCMWTLKRDVFGIPMMIVGNFLPIL
Protein: Papilin (Abnormal cell migration protein 6) (O76840)
Organism: Caenorhabditis elegans
Function: Involved in pharynx morphogenesis probably by remodeling the basement membrane.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:19297413}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Metalloprotease mig-17
- Fibulin-1
- Ig-like domain-containing protein
- Integrin alpha pat-2
Sequence:
MRLLLFSAALLLCSVPTWAFSLSSFFGSDVAQKPYLHPNSPPERDPASSRMKRQAYQVYVDGDVSVTVDKSGQKETGNWGPWVPENECSRSCGGGVQLEKRQCSGDCTGASVRYISCNLNACESGTDFRAEQCSKFNDEALDGNYHKWTPYKGKNKCELVCKPESGNFYYKWADKVVDGTKCDSKSNDICVDGECLPVGCDGKLGSSLKFDKCGKCDGDGSTCKTIEGRFDERNLSPGYHDIIKLPEGATNIKIQEARKSTNNLALKNGSDHFYLNGNGLIQVEKEVEVGGTIFVYDDAEPETLSAQGPLSEELTVALLFRKGSRDTAIKYEFSIPLEEEVDYMYKFDNWTPCSVSCGKGVQTRNLYCIDGKNKGRVEDDLCEENNATKPEFEKSCETVDCEAEWFTGDWESCSSTCGDQGQQYRVVYCHQVFANGRRVTVEDGNCTVERPPVKQTCNRFACPEWQAGPWSACSEKCGDAFQYRSVTCRSEKEGEEGKLLAADACPADEQEKFDTERTCNLGPCEGLTFVTGEWNLCTRCNDTEETREVTCKDSQGRAYPLEKCLVDNSTEIPTDTRSCATQPPCEYEWTVSEWSKCTTECGHGHKTRRVICAIHQNGGLEVVDEGHCQAEKPEGKTNCTNEEKCTGTWYTSSWSECTAECGGGSQDRVAVCLNYDKKPVPEWCDEAVKPSEKQDCNVDDCPTCVDSEFGCCPDNSTFATGEFNFGCSNCSETEFGCCADNVTVATGPNSKGCEEFVESPLNLEADVANADAEASGDAPELCSVTNENGEAVDVECATIAPITALLGDGELIGNDTDASNETIHCSKTEFGCCPDWYTAASGKGNEGCPSFTLGGCNETQFGCCHDDVTLARGANLEGCGEPSCAASLYGCCKDRKTIAFGPHYSGCERSSFPCELSDFGCCPDGETAALGKNGTGCGENCLTTKFGCCPDGKTTAKGSHNEGCGCEFAQYGCCPDGKSVAKGAGFYGCPESCAQSQFGCCPDGKTRARGENKEGCPCQYTRYGCCPDGETTALGPRNDGCDNCRYAKHGCCPDGETKALGPDGAGCPPTTTPPFLMGGTVAPHKIAACNQTQESGTVCGAGYKLAWHYDTTEGRCNQFWYGGCGGNDNNFASQDMCETICVEPPGKGRCYLPRVDGPLRCDQLQPRYYYDHSKKHCVAFWWRGCLGNANNFNSFEECSMFCKDVGPYDAPTTAAPPPPPQQNAQQYLPTPEVQQIEIQSAEQPQPQQPQQQQQQQQQQPQQPRQSMEDICRSRQDAGPCETYSDQWFYNAFSQECETFTYGGCGGNLNRFRSKDECEQRCFFVHGAQPSAARQEQAQPAAQPAQPAQPSNIVSPPQQSASPVVVPSNSKQRDACHLNVDQGRCKGAFDSWYYEVATGSCVTFKYTGCGGNANRFASKDQCESLCVKPASEAASAGIDGAAGINSVCDEAKDTGPCTNFVTKWYYNKADGTCNRFHYGGCQGTNNRFDNEQQCKAACQNHKDACQLPKVQGPCSGKHSYYYYNTASHQCETFTYGGCLGNTNRFATIEECQARCPKDDQTTTTSQPEELPSLPLVQEDPQPRPAFSLKQSFAHSRRRDAPFARSVSARHHTPDSEEERVDCYAVPDPGSCGDYRLVWHYSATSNSCRQFYYGGCAGNTNRFETRDKCETSCVAKIEERVESVSEASKSLEEVRLTDPRMDSHFGYHDPEVDQIEEEAEYVIVDTGALPELCMLPEQRGSCYDNILRWRFDSEKSQCVTFMYSGCNPNANHFTSQETCERACGKWRNVAVCELPAEHGDCQLAIPRWYHDPKTSQCQMMMWTGCGGNGNAFSSKADCESLCRVETLWSNNTDFCTLERSAGPCTDSISMWYFDSTHLDCKPFTYGGCRGNQNRFVSKEQCQQSCRPGDTKSEDICTLRPEPGPCRLGLEKYFYDPVIQSCHMFHYGGCEGNANRFDSELDCFRRCSSVKVEASESERVGQLTSASTPVIYIVNKTAIFVGNTFRIRCNSYGVLPITWYKNGGLLQFGSRITEENDDTLEIVDALTADAGVYTCIAGQDSTMSEGVEVVIKRLPGHRTTSRPMLTPSKNFSLGTPPTPSPSTVSTTPFRIYTPGSAPSDARVSRPTSNSCMDVGNASTCDLIVKNGLCGKKRYGTFCCHTCTRVHNFKF
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q4WGE9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSLFQLLYQAGARQEESHGLSRRLAYTEGGITYDIDPLPVAQHKGLIAVAVMATLSFIATLALICFITYRLVFWRSNYQRYIGYNQYIILIYNLVIADLQQSLAFLICIKWIAEDKIEASSAACFLQGFWLQIGDPASGLFVLAIAIHTFLLVAMGHKLSYRIFVLGVVGLWVFVAILVIIPLAAHGRFVFIPSGAWCWISEEYEAVRLWTHYIWIFLAEFGTVCLYAVMWFQLRAQIKQSAILGSNHTASLKRLRRVIGYMVIYPIAYIVLSLPLAAGRMATARGNTPSLAYFCVAGALITSSGLVDVLLYTLTRRNLILESEPSEDHSYNRFASSKNRRNDNHLTTITADPKHTRTDISVLRTRRGHDEEEDHVDSPTRDGSTDNIVQPGVELAPMGKVFQHTTIEITHEPAYPEAEGSDRSSKDSLQRPVKSHDNASRMWGR
Protein: Calcineurin subunit B (Calcineurin regulatory subunit) (Protein phosphatase 2B regulatory subunit) (A0A1D8PP58)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein phosphatase
- FK506-binding protein 1
- Transcriptional regulator CRZ1
- Calcium-channel protein CCH1
- Rcn1p
- Mlc2p
- Calcium-transporting ATPase
- Calmodulin
- Mid1p
Sequence:
MGANASILDGFIEDTNFSIEEIDRLRKRFMKLDKDGSGQIDKQEFLSIPGISSNPLATRLMDVFDKDGDGSIDFEEFITGLSAFSGKSDNLNKLRFAFNIYDIDRDGYIGNGELFIVMKMMVGKNLKDEELQQIVDKTLMEADLDGDGKLNFEEFKNAVNTDTIANTLTLNMF
Protein: Lysosomal alpha-glucosidase (EC 3.2.1.20) (Acid maltase) (Q6P7A9)
Organism: Rattus norvegicus (Rat)
Function: Essential for the degradation of glycogen in lysosomes. Has highest activity on alpha-1,4-linked glycosidic linkages, but can also hydrolyze alpha-1,6-linked glucans.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P10253}. Lysosome membrane {ECO:0000250|UniProtKB:P10253}.
Interaction partners:
- Alpha-amylase.
- Pancreatic alpha-amylase
- Alpha-galactosidase
- Cytosolic beta-glucosidase
- Hexokinase-3
- Hexokinase-2
- Glucosidase, alpha; neutral C
- Glycogenin-1
Sequence:
MNIRKPLCSNSVVGACTLVSLTTAVILGHLMLRELMLLPQDLHESSSGLWKTYRPHHQESYEPAPLHIQEHAEQLRAVPTQCDVTPNSRFDCAPDKGITQEQCEARGCCWVPAGQVLNGPVMGQPWCFFPPSYPSYRLENLSSTESGYTATLTRTSPTFFPKDVLTLQLEVLMETDSRLHFMIKDPTSKRYEVPLETPRVLSQAPSPLYSVEFSEEPFGVIVRRKLGGRVLLNTTVAPLFFADQFLQLSTSLPSQHIAGLGEHLSPLMLSTEWTRITLWNRDVAPSQGVNLYGSHPFYLALEDGGLAHGVFLLNSNAMDVVLQPSPALTWRSTGGILDVYVFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAIVRQVVENMTRTHFPLDVQWNDLDYMDARRDFTFNQDGFADFPDMVHELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPETLDWWQDMVSEFHAQVPFDGMWIDMNEPSNFIRGSQQGCPDNELENPPYVPGVVGGALQAATICASSHQFLSTHYNLHNLYGLTEAIASSRALVKTRGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEHLAYSVPEILQFNLLGVPLVGADICGFQGNTTEELCVRWTQLGAFYPFMRNHNDLNSLPQEPYRFSETAQQAMRKAFTLRYALLPYLYTLFHGAHVKGDTVARPLFLEFPEDPSTWSVDRQLLWGPALLITPVLEPGKTDVTGYFPKGMWYNLQMVPVETLGSLPSSSPASSFRSIVHSKGQWLTLEAPLDTINVHLRAGYIIPLQGPSLTTTESRKQPMALAVALTESGEASGELFWDDGESLGVLERGAYTLVTFSAKNNTIVNKLVHVTKEGGELQLREVTILGVTTAPTQVLSNGISVSNFTYSPDDKSLSIPVSLLMGERFQIDWS