wanglab/gogpt-training-data huggingface dataset:
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A5YAI9)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MEERHVLFGKYEMGRLLGKGTFAKVYYGKELATGESVAVKVISKDQVKKKGMMEQIKREISVMRLVRHPNIVELKEVMATKKKIFFVMEHVRGGELFAKVYKGKLKEHVARKYFQQLISAVDFCHSRGVSHRDLKPENLLLDEKEDLKISDFGLSALPEQLLNDGLLHTQCGTPAYVAPEVLRKKGYDGSRADIWSCGVVLYVLLAGFLPFQDENMMKMYRKVFKAEFEFPTWFSTESKRLISKLLVADPEKRITIPAIMRDPWFRKEFTRPLAFSIQEPIDDDESAPSKSAKLSSPKFFNAFEFISSMSSGFDLSGLFEDKRKSGTMFTSRCSASAIMSKVEAVAKGLNFRVGKAKDFKMRLQGSSEGRKGRLFVTAEVFEVAPEVAVVEFSKSAGDTLEYAKFCEEDVRPALKDIVWTWQGDSFNEAEEHEKQVQQDTAEPNTL
Protein: Enkurin domain-containing protein 1 (Q7TSV9)
Organism: Mus musculus (Mouse)
Function: Microtubule-binding protein which regulates microtubule organization and stability (By similarity). Promotes the stability of astral microtubules and facilitates the proper orientation of the mitotic spindle (By similarity). This allows the oriented division of basal keratinocytes and contributes to epidermal stratification. Required for the assembly of both primary and motile cilia. Destabilizes the interaction between CCP110 and CEP97 by competing with CEP97 for binding to CCP110 which promotes the removal of CCP110 and CEP97 from the mother centriole and allows the initiation of ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:35301795}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:35301795}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:35301795}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9H0I2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9H0I2}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9H0I2}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9H0I2}. Note=Localized at the centrosome and accumulates at the parental centrioles during centriole duplication in cycling cells (By similarity). In ciliated cells, detected at the basal body of the cilium (By similarity). Localizes to the centrosome during interphase, to the primary cilium at G0, to the spindle poles during mitosis and to the centrosomes and central spindle during telophase and cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q9H0I2}.
Interaction partners:
- FIGNL1-interacting regulator of recombination and mitosis
Sequence:
MCEGPSRISGPIPPDPTLCPDYYRRPASAQGRLEGNALKLDLLTSGRDLDSSPPRGPRIRPEAREILERGQRGVGDVLLQLGCISLGSGVSPKRKNPKDHEKENLRRIKEIQRRFQDQERSREQGQPKPLKALWRSPKYDNVESRVKARMKELGPTSVTEPAHFLRAHSRCGPGLPPSRASSPQLALPGPQAKGPGLGVDFISRNALAAKRAPRRHSRSLQVLAQVQEQQRQAQERYNATQKGHVPHYLLERRDLWRKEAEARQRSQPDPSMPPGHTLMPENQRLETLNNLLQSQSQLLRELVLLPAGADSLRAQGHRAELDRKLVQIEEAIKIFSRPKVFVKMDT
Protein: Nuclear envelope phosphatase-regulatory subunit 1 (Transmembrane protein 188) (H3BUT5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.
Interaction partners:
Sequence:
MLLIVVSVCTATGAWNWLIDPETQKVSFFTSLWNHPFFTISCITLIGLFFAGIHKRVVAPSIIAARCRTVLAEYNMSCDDTGKLILKPRPHVQ
Protein: DUF3349 domain-containing protein (O53292)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTKTFSHPHFFRSVLRWLQVGYPEGVPGPDRVALLSLLRSTPLTEEQIGEVVRHFTENGSPAVADRVIDRDEIAEFISEVTHHDAGPENIQRVAGILAAAGWPLAGVDVGESESGSDRAPASQG
Protein: Putative oxidoreductase C6G10.06 (EC 1.-.-.-) (O14252)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Putative oxidoreductase that negatively regulates the retrieval of cargo from late endosomes to the Golgi.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSATSREGNKTKIGIVGGGIIGICTAFYLTEEQEYKKGELDIFIFESKEIAGGSSGIDSAILTKLCQNEIIQPLSTLALKLYEGLDKKFDGKKNWEYRTANSWFCKMKWDNTNVAKVPDTLQWLQRERMQKCSSIGSGNDFAMINPKLFCQFMAKEIEKRGVKFIFGSVKEVSKHHITYVPKQEAEDTIIKAQVHKTLVSAGPWTGYLLPFTGIAGLCIPIIHLSVGNFPVGDSIVVCCLNTMGNLNICKTTEIFSKNREQLIFMGTPKFHLLPKDSNRCFFNPFEIIELKEMTDLVLSENTKSNYLDASFKFLPTSRITGIPIISTTKSGVFVAAGHANWGITQAPATGLCMAEMLLGKEKTSINTDPFHLNLGE
Protein: Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (V9HWJ5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDAEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKSPGVLAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLFAKEVAPVPKIH
Protein: UGT protein (A3FMH4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MEKQQKSSHVVLVMVTFQGHITPMLQLASILHSKGFSITIVHPELNSPNPSNHPKFTFISIPDKLTESQLSDKDAASPVWSLNKNCAAPLQQCLEKILHSLHHIAAVIYDTLMYCAQTITEDLGLLGIVLRTGSATTMLFYPAFSQLDEERIDFVHEIKSPELQALQLKRLRALLSQNATKAMTEVRVAFANVLKRSSAIIVNSMEFLELEALSKVKQYFPAPIITIGPLHKLARAICSSLLTEDDKCISWLNKQAPKSVIYVSFASIVNIDK
Protein: At3g10405 (Vacuolar acid trehalase) (A0JQ78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSISSLGSAISKPTSSSSSYTYLGSSSRIFGLVTSSLLWTKSKSHHTNTKLKKQKLCVRNSAQEIPKTLEEDSKFVPLDPQDPRFGPPVLLLLGLQLHEAQKIQELLKELDGEFMEIVFCTDDMIKRSLWEAVTTKQPDLKRVKIAESLPRICFLSGLTGEEMMMFIDAFPETGLEPVVFAAMVPNSADKPIFELTEEIMGDHELLTGSSSS
Protein: Sperm-associated microtubule inner protein 4 (Q8N865)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25074808}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:E1B9R1}. Note=Localizes to the A-tubules of DMTs. {ECO:0000250|UniProtKB:E1B9R1}.
Interaction partners:
- Leucine-rich colipase-like protein 1
Sequence:
MEVIHGRPYCCRELEGADILSNTFYSNELHNPLQTVTRPTASEDRYQELRESLQQCRLPWGAEREYGGIIPISLPEDHRPKYEPPRVMGKGHQHYGFGGETWPRKLPVEQFYYLTQNKKSDVYGNDSLIPKPPNSTVGEICLPYPIEHPYHTHICRGAMFPTFTSPEDLYTGIKARTQQPFPPTVPTKAYDSTVLKTRGNPYRYELIDIPMDSKKKALTWPGQGVYYDFPRGVEKNKPVFYPKPPKTFAPNTSLNSWDPICSAKEANIQRNLERSHWLTSYTHDFTGLGPMDPLELDDYHEKMVAELTRKIGFDPEPQEKFHPVFKPPRPLEGRIARLIQNRRSLEAIVQQRPRSCPDCTPRVLCNFHTFVPSSKEMVALSDNIPAGVTHKNQDIEEKIIEEQSLLSTYELPSCYPTKDLTSIYDIKPFPKITDTKKTEDLYWRQQSLKTQPTPYCKPDHWIHYENLKSPLRDQYNMCPDPVSLSKPSVLQNKQDTEAFTLEHFLSKPEEELFLNMENNEETRPVLGWIPRAGVTKPQTNLLELKNSFSKTGAQKRFHKSILEDHKDLRDNEHSGMKHQFYGHNSYYFYN
Protein: Lumican (Q6IQQ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MFALGSILLAGLLSLSLAQYDYYDEYYIPSAPLEGVSSPSCAQECECPINFPTAMYCNERNLKFIPIVPTGIKYLYLQNNFIEEIKAGVFDNATDLRWLVLDNNNITSDKIQAGTIDKLGSLEKLLFSHNKLTKPPGSLSKSLDELKLIGNKLTSFPANTLAGMENLTTVHLSKNKLTTESLTGAFKGLKSLILLDVSENKLKKLPSGVPASLLMLYADNNDIDSIPNGYLAKLPLLQYLRISHNKLVDSGVPAGVFNVSSLLELDLSFNKLKTIPEINESLEHLYLQVNEINKFELTNICRFSSPVNYSRLRTLRLDGNNITHSSMPDDTANCLRQASEIIFE
Protein: 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-OHD-1 alpha-hydroxylase) (25-hydroxyvitamin D(3) 1-alpha-hydroxylase) (VD3 1A hydroxylase) (Calcidiol 1-monooxygenase) (Cytochrome P450 subfamily XXVIIB polypeptide 1) (Cytochrome P450C1 alpha) (Cytochrome P450VD1-alpha) (Cytochrome p450 27B1) (O15528)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1alpha-position to form the hormonally active form of vitamin D3, 1alpha,25-dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR). Has 1alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway. Converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3, an active ligand of VDR. Also active on 25-hydroxyvitamin D2. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin.
Subcellular location: Mitochondrion membrane.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Vitamin D 25-hydroxylase
- 1,25-dihydroxyvitamin D
- Parathyroid hormone
- Nuclear receptor coactivator 1
- Mediator of RNA polymerase II transcription subunit 1
- Fibroblast growth factor 23
- Vitamin D-binding protein
- Sodium-dependent phosphate transport protein 2A
- Nuclear receptor coactivator 3
Sequence:
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSRLHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCRQRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPPALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPHWLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFREELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPSATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPAQFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQPEPGAAPVRPKTRTVLVPERSINLQFLDR
Protein: Homeobox protein Hox-A1 (Early retinoic acid 1) (Homeobox protein Hox-1.6) (Homeoboxless protein ERA-1-399) (Homeotic protein ERA-1-993) (P09022)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor. Regulates multiple developmental processes including brainstem, inner and outer ear, abducens nerve and cardiovascular development and morphogenesis as well as cognition and behavior (By similarity). Also part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments (By similarity). Activates transcription in the presence of PBX1A and PKNOX1.
Subcellular location: Nucleus {ECO:0000269|PubMed:29465778}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 1
Sequence:
MNSFLEYPILGSGDSGTCSARAYPSDHGITTFQSCAVSANSCGGDDRFLVGRGVQISSPHHHHHHHHHHHPQTATYQTSGNLGISYSHSSCGPSYGAQNFSAPYGPYGLNQEADVSGGYPPCAPAVYSGNLSTPMVQHHHHHQGYAGGTVGSPQYIHHSYGQEQQTLALATYNNSLSPLHASHQEACRSPASETSSPAQTFDWMKVKRNPPKTGKVGEYGYVGQPNAVRTNFTTKQLTELEKEFHFNKYLTRARRVEIAASLQLNETQVKIWFQNRRMKQKKREKEGLLPISPATPPGSDEKTEESSEKSSPSPSAPSPASSTSDTLTTSH
Protein: Leucine-rich repeat-containing protein 41 (Protein Muf1) (Q15345)
Organism: Homo sapiens (Human)
Function: Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Cullin-5
- E3 ubiquitin-protein ligase RBX1
- Elongin-B
Sequence:
MAAPEAWRARSCWFCEVAAATTMEATSREAAPAKSSASGPNAPPALFELCGRAVSAHMGVLESGVWALPGPILQSILPLLNIYYLERIEETALKKGLSTQAIWRRLWDELMKTRPSSLESVTCWRAKFMEAFFSHVLRGTIDVSSDRRLCDQRFSPLLHSSRHVRQLTICNMLQGATELVAEPNRRVLETLASSLHTLKFRHLLFSDVAAQQSLRQLLHQLIHHGAVSQVSLYSWPVPESALFILILTMSAGFWQPGPGGPPCRLCGEASRGRAPSRDEGSLLLGSRRPRRDAAERCAAALMASRRKSEAKQMPRAAPATRVTRRSTQESLTAGGTDLKRELHPPATSHEAPGTKRSPSAPAATSSASSSTSSYKRAPASSAPQPKPLKRFKRAAGKKGARTRQGPGAESEDLYDFVFIVAGEKEDGEEMEIGEVACGALDGSDPSCLGLPALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWVSLESLTLSYNGLGSNIFRLLDSLRALSGQAGCRLRALHLSDLFSPLPILELTRAIVRALPLLRVLSIRVDHPSQRDNPGVPGNAGPPSHIIGDEEIPENCLEQLEMGFPRGAQPAPLLCSVLKASGSLQQLSLDSATFASPQDFGLVLQTLKEYNLALKRLSFHDMNLADCQSEVLFLLQNLTLQEITFSFCRLFEKRPAQFLPEMVAAMKGNSTLKGLRLPGNRLGNAGLLALADVFSEDSSSSLCQLDISSNCIKPDGLLEFAKRLERWGRGAFGHLRLFQNWLDQDAVTAREAIRRLRATCHVVSDSWDSSQAFADYVSTM
Protein: Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK) (Q99661)
Organism: Homo sapiens (Human)
Function: In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21820309, ECO:0000269|PubMed:23891108}. Nucleus {ECO:0000250|UniProtKB:P70096}. Chromosome, centromere {ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:17485487}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:17485487, ECO:0000269|PubMed:23891108}. Note=Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MAPRE1 (By similarity). Association with microtubule plus ends is also mediated by interaction with KIF18B. Centromeric localization requires the presence of BUB1 and SGO2. {ECO:0000250|UniProtKB:P70096, ECO:0000269|PubMed:17485487, ECO:0000269|PubMed:21820309}.
Interaction partners:
- Targeting protein for Xklp2
- Aurora kinase B
- Cell division cycle protein 20 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Serine/threonine-protein kinase PLK1
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Centromere-associated protein E
- Histone H3-like centromeric protein A
- Centromere protein F
- Kinesin-like protein KIF18B
Sequence:
MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKEIDFDDVAAINPELLQLLPLHPKDNLPLQENVTIQKQKRRSVNSKIPAPKESLRSRSTRMSTVSELRITAQENDMEVELPAAANSRKQFSVPPAPTRPSCPAVAEIPLRMVSEEMEEQVHSIRGSSSANPVNSVRRKSCLVKEVEKMKNKREEKKAQNSEMRMKRAQEYDSSFPNWEFARMIKEFRATLECHPLTMTDPIEEHRICVCVRKRPLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKAQNASKGIYAMASRDVFLLKNQPCYRKLGLEVYVTFFEIYNGKLFDLLNKKAKLRVLEDGKQQVQVVGLQEHLVNSADDVIKMIDMGSACRTSGQTFANSNSSRSHACFQIILRAKGRMHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIATISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQLIQMETEEMEACSNGALIPGNLSKEEEELSSQMSSFNEAMTQIRELEEKAMEELKEIIQQGPDWLELSEMTEQPDYDLETFVNKAESALAQQAKHFSALRDVIKALRLAMQLEEQASRQISSKKRPQ
Protein: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (DHBPS) (EC 4.1.99.12) (P0A7J0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Subcellular location: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Riboflavin synthase
- Riboflavin biosynthesis protein RibD
- 6,7-dimethyl-8-ribityllumazine synthase
- GTP cyclohydrolase-2
- Transcription elongation factor GreA
Sequence:
MNQTLLSSFGTPFERVENALAALREGRGVMVLDDEDRENEGDMIFPAETMTVEQMALTIRHGSGIVCLCITEDRRKQLDLPMMVENNTSAYGTGFTVTIEAAEGVTTGVSAADRITTVRAAIADGAKPSDLNRPGHVFPLRAQAGGVLTRGGHTEATIDLMTLAGFKPAGVLCELTNDDGTMARAPECIEFANKHNMALVTIEDLVAYRQAHERKAS
Protein: PTS system N-acetylmuramic acid-specific EIIBC component (EIIBC-MurNAc) [Includes: N-acetylmuramic acid-specific phosphotransferase enzyme IIB component (EC 2.7.1.192) (PTS system N-acetylmuramic acid-specific EIIB component); N-acetylmuramic acid permease IIC component (PTS system N-acetylmuramic acid-specific EIIC component)] (P77272)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is responsible for growth on MurNAc as the sole source of carbon and energy. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426}.
Interaction partners:
- N-acetylmuramic acid 6-phosphate etherase
- PTS system glucose-specific EIIA component
- HTH-type transcriptional regulator MurR
- PTS system N-acetylglucosamine-specific EIICBA component
- Phosphocarrier protein HPr
- Putative D-alanyl-D-alanine carboxypeptidase
- Anhydromuropeptide permease
- Cryptic beta-glucoside bgl operon antiterminator
- Beta-hexosaminidase
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
Sequence:
MAKEISSELLNTILTRVGGPGNIASCGNCMTRLRLGVHDSSLVDPNIKTLEGVKGVILTSDQVQVVFGPGKAHRAAKAMSELLGEAPVQDAAEIAAQNKRQLKAKQTSGVQQFLAKFATIFTPLIPGFIAAGLLLGIATLIATVMHVPADAQGTLPDALNFMKVFSKGLFTFLVILVGYNAAQAFGGTGVNGAIIAALFLLGYNPAATTGYYAGFHDFFGLPIDPRGNIIGVLIAAWACARIEGMVRRFMPDDLDMLLTSLITLLITATLAYLIIMPLGGWLFEGMSWLFMHLNSNPFGCAVLAGLFLIAVVFGVHQGFIPVYLALMDSQGFNSLFPILSMAGAGQVGAALALYWRAQPHSALRSQVRGAIIPGLLGVGEPLIYGVTLPRMKPFVTACLGGAAGGLFIGLIAWWGLPMGLNSAFGPSGLVALPLMTSAQGILPAMAVYAGGILVAWVCGFIFTTLFGCRNVNLD
Protein: Delta-aminolevulinic acid dehydratase (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) (O42768)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Interaction partners:
- Porphobilinogen deaminase
- 5-aminolevulinate synthase, mitochondrial
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Inorganic pyrophosphatase
- Uroporphyrinogen decarboxylase
- Acetylornithine aminotransferase, mitochondrial
- Protoporphyrinogen oxidase
Sequence:
MHTADFLDIEPTEISSILSGGYNHPLLREWQSERQLKKNMLIFPLFISDIPDEATPIDSLPNIKRFGINKLVDYVKPLVEKGLRSVILFGVPLKEGTKDPVGTAADDPEGPVIQAIKLLRKEFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRIAAVAVNYAKAGAHCVAPSDMIDGRIKDIKKGLISAGLAHKTFVLSYAAKFSGNLYGPFRDAACSSPSNGDRKCYQLPQAGRGLARRALARDKNEGADGIIVKPSTFYLDIMRDASEICEDLPICAYHVSGEYAMLHAAAEKGIVDLKSIAFESHEGFLRAGARLIISYFTPEFLDWLSN
Protein: Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) (DOPA decarboxylase) (Q7SZR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tyrosine 3-monooxygenase
- Tryptophan hydroxylase 1
- Dopamine beta-hydroxylase
- Tryptophan hydroxylase 2
- Tyrosine hydroxylase 2.
- Tryptophan hydroxylase 1b.
- Serotonin N-acetyltransferase
- Phenylalanine hydroxylase.
- Catechol O-methyltransferase A
- Catechol O-methyltransferase B
Sequence:
MDAAEFRRRGREMVDYVADYIENIEKRQVYPDVEPGYLRSLIPEEAPEEPESYEDVVKDIERVIMPGVTHWHSPYFYAYFPTAHSYPAMLADILCGAIGCIGFSWAASPACTELETVMLDWLGKMLKLPEDFLAGTKGKGGGVIQSTASEATLITLLAARSKIVRLIQADHPDRSETDIISKLVAYSSDQAHSSVERAGLIGGVRMKKIPTDSKFSVRGDALERILKEDKAAGLIPFFFCATLGTTASCAFDCITELGPICNAEKMWMHIDAAYAGSAFICPEFRPLLNGIEFADSFNFNPHKWLLINFDCSAMWVKKRADIIGAFKMEPLYLKHDHQESGLVTDYRHWQIPLGRRFRSLKMWFVFRMYGLKALQAYIRKHVGLAKEFEAFVRADQRFEISADVVMGLVCFRLKGPNELSENLLKRINSARKIHLVPCHLAGLFVLRFAVCARATESRHVQEAWCHIRQLASELLQELLH
Protein: Estrogen receptor 2b (B8JJL3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
- Estrogen receptor
- Aromatase
- Prostaglandin E synthase 3
- Vitellogenin 1
- G-protein coupled estrogen receptor 1
- Palmitoyltransferase ZDHHC7
- type I protein arginine methyltransferase
- Striatin
Sequence:
MSSSPGPAPVLDSSKADRGASPALLPRLYASPLGMDNQTVCIPSPYVEACQDYSPPHGGEFNHGALTLYSPVSSAVLGFHRPPVSESLVPLSPTILWPPHSLHCPPPLAYSETRSHSAWEEAKTHTLSQSSSVLSHTKLLGQQLEGDNGLNPSASIVGKGDTHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKSRRKSCQACRLRKCYEVGMMKCGVRRERCSYRGARHRRNPQIRDSSGGVVGLRGQSQQHLEFPLSPSQHLFPSGGRAEGRGLNYSPEQLVSCILEAEPPQIYLREPVKKPYTEASMMMSLTSLADKELVLMISWAKKIPGFVELTLSDQVHLLECCWLDILMLGLMWRSVDHPGKLIFTPDLKLNREEGNCVEGIMEIFDMLLATTSRFRELKLQREEYVCLKAMILLNSNNCSSLPQTPEDVESRGKVLNLLDSVTDALVWIISRTGLSSQQQSIRLAHLLMLLSHIRHLSNKGIEHLSNMKRKNVVLLYDLLLEMLDANTSQSSRMLEDRQQSPENLHTSRPQPDLKDSDQETPHSPRAEETVNKTLHSSLLREDMDTN
Protein: Secretogranin-2 (Chromogranin-C) (Secretogranin II) (SgII) [Cleaved into: Secretoneurin (SN); Manserin] (Q03517)
Organism: Mus musculus (Mouse)
Function: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules.
Subcellular location: Secreted. Note=Neuroendocrine and endocrine secretory granules.
Interaction partners:
- Secretogranin-1
- Chromogranin-A
- Secretogranin-3
- Carboxypeptidase E
- Neuroendocrine protein 7B2
- ProSAAS
- Neurosecretory protein VGF
Sequence:
MAGAKAYRLGAVLLLIHLIFLISGAEAASFQRNQLLQKEPDLRLENVQKFPSPEMIRALEYIEKLRQQAHREESSPDYNPYQGVSVPLQLKENGEESHLAESSRDALSEDEWMRIILEALRQAENEPPSAPKENKPYALNLEKNFPVDTPDDYETQQWPERKLKHMRFPLMYEENSRENPFKRTNEIVEEQYTPQSLATLESVFQELGKLTGPSNQKRERVDEEQKLYTDDEDDVYKTNNIAYEDVVGGEDWSPIEEKIETQTQEEVRDSKENTEKNEQINEEMKRSGQLGLPDEENRRESKDQLSEDASKVITYLRRLVNAVGSGRSQSGPNGDRAARLLQKPLDSQSIYQLIEISRNLQIPPEDLIEMLKAGEKPNGLVEPEQDLELAVDLDDIPEADLDRPDMFQSKMLSKGGYPKAPGRGMVEALPDGLSVEDILNVLGMENVVNQKSPYFPNQYSQDKALMRLPYGPGKSRANQIPKVAWIPDVESRQAPYENLNDQELGEYLARMLVKYPELLNTNQLKRVPSPVSSEDDLQEEEQLEQAIKEHLGPGSSQEMERLAKVSKRIPVGSLKNEDTPNRQYLDEDMLLKVLEYLNQEQAEQGREHLAKRAMENM
Protein: Enriched in surface-labeled proteome protein 9 (Q38DP0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGDVRPSLLLIVFASAFITMLNGAVSDQPFAMDGFVTMKVEVVASSASKPDATKLSNLMISGNINSSYPLKVSWLTLGGGAVDVYTESGYAVVGVDGHCKVNKHPGNNSEVILWDSLRAILAANNYTVNQTDLLDRGLDLVSYSLPLNLKIPSEYGGSGSVETYSVEYYVLNTWTVNHDEVDEFPVKLLLKSAKGEQILFTFFDFSKDTLNMSSFEFPESCTKLNDKAGNHSAGEDDGNNQLDGKFMPRLPPEFSAYIQVIAPEEKRTWTVSEQFSESKKFSRSTVVTSVPNSGGQVAVYDWYTLGKYQISYFREQRKVGSTLKSPLSKDLRDYLFKDFDVCRKAHLGINVTARTSSALMLNSVDAVPVYIGTQKVRGINCKVWAATVSGIRVRWYWTEKQVNAFENTTEGGHHLLLRMIVEGIGTSPYFAHHPFVAQENLLPSQYHKRACAWLNPVDPTCRGGHRRFKYIYDVFSFVDFLDREAELPDSCMSFRAPSVSLPSGLNDTLSSTRVLVFLFLFSITSATMGGFVTWCFMSSRIRRLKVDFINAGRNIVARQS
Protein: Flagellar calcium-binding protein TB-24 (Q57UL6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}.
Interaction partners:
Sequence:
MGCSGSKNTTNSKDGAASKGGKDGKTTADRKVAWERIRCAIPRDKDAESKSRRIELFKQFDTNGTGKLGFREVLDGCYSVLKLDEFTTHLPDIVQRAFDKAKDLGNKVKGVGEEDLVEFLEFRLMLCYIYDIFELTVMFDTMDKDGSLLLELQEFKEALPKLKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCWAVTKKLQVCGDPDGEENGANEGN
Protein: RE56428p (Q7YU59)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MSPRSPLRISPFGVHILIAAVLFTLIQSSKQDCVWYGVCNTNDFSHSQNCPYNGTAKEMATDGLELLKKRCGFLLENSENKFCCDKNQVELLNKNVELAGNILDRCPSCMENLVRHICQFTCSPKQAEFMHVVATQKNKKGDEYISSVDLHISTEYINKTYKSCSQVSVPQTGQLAFDLMCGAYSASRCNPTKWFNFMGDATNPYVPFQITYIQHEPKSNSNNFTPLNVTTVPCNQAVSSKLPACSCSDCDLSCPQGPPEPPRPEPFKIVGLDAYFVIMAAVFLVGVLVFLMGSFLFTQGSSMDDNFQVDGNDVSDEMPYSENDSYFEKLGAHTETFLETFFTKWGTYFASNPGLTLIAGASLVVILGYGINFIEITTDPVKLWASPNSKSRLEREFFDTKFSPFYRLEQIIIKAVNLPQIVHNTSNGPYTFGPVFDREFLTKVLDLQEGIKEINANGTQLKDICYAPLSDDGSEIDVSQCVVQSIWGYFGDDRERLDDHDEDNGFNVTYLDALYDCISNPYLCLAPYGGPVDPAIALGGFLPPGDQLTGSTKFELANAIILTFLVKNHHNKTDLENALTWEKKFVEFMTNYTKNNMSQYMDIAFTSERSIEDELNRESQSDVLTILVSYLIMFMYIAISLGHVKEFKRVFIDSKITLGIGGVIIVLASVVSSVGVFGYIGLPATLIIVEVIPFLVLAVGVDNIFILVQTHQRDQRKPNETLEQQVGRILGKVGPSILLTSLSESFCFFLGGLSDMPAVRAFALYAGVALIIDFLLQITCFVSLFTLDTKRREENRMDICCFIKGKKPDSITSNEGLLYKFFSSVYVPFLMKKIVRASVMVIFFAWLCFSIAIAPRIDIGLDQELAMPQDSFVLHYFQSLDENLNIGPPVYFVLKGDLAYTNSSDQNLVCAGQYCNDDSVLTQIYLASRHSNQTYIARPASSWIDDYFDWAAAASSCCKYRKDSGDFCPHQDTSCLRCNITKNSLLRPEEKEFVKYLPFFLKDNPDDTCAKAGHAAYGGAVRYSNSHERLNIEASYFMAYHTILKSSADYFLALESARKISANITQMLQGRLMSNGVPMASALTVEVFPYSVFYVFYEQYLTMWSDTLQSMGISVLSIFVVTFVLMGFDVHSALVVVITITMIVVNLGGLMYYWNISLNAVSLVNLVMAVGISVEFCSHLVHSFATSKSVSQIDRAADSLSKMGSSIFSGITLTKFAGILVLAFAKSQIFQVFYFRMYLGIVVIGAAHGLIFLPVLLSYIGAPVSNARLRYHSQAAAEHETALAGIL