wanglab/gogpt-training-data huggingface dataset:
Protein: Endoplasmin (EC 3.6.4.-) (94 kDa glucose-regulated protein) (GRP-94) (Endoplasmic reticulum resident protein 99) (ERp99) (Heat shock protein 90 kDa beta member 1) (Polymorphic tumor rejection antigen 1) (Tumor rejection antigen gp96) (P08113)
Organism: Mus musculus (Mouse)
Function: Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD) (By similarity). Has ATPase activity. May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:20865800}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome {ECO:0000250|UniProtKB:P14625}.
Interaction partners:
- Protein disulfide-isomerase A4
- Endoplasmic reticulum chaperone BiP
- Calreticulin
- Hypoxia up-regulated protein 1
- DnaJ homolog subfamily B member 11
- Protein disulfide-isomerase A6
- Prolow-density lipoprotein receptor-related protein 1
- Calreticulin
- Protein disulfide-isomerase A3
- Protein disulfide-isomerase
Sequence:
MRVLWVLGLCCVLLTFGFVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVRKYSQFINFPIYVWSSKTETVEEPLEEDEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADEKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHSTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREATEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVMDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPEAQVEEEPEEEPEDTSEDAEDSEQDEGEEMDAGTEEEEEETEKESTEKDEL
Protein: Kinetoplastid kinetochore protein 18 (Q38FF3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTCVKELLQLPTDEVRACVFPLSDVEVTLVLCELGKLLQRWLYATRYKLVSSFEVFLHLFVHVADREPKRIANAFLGSCKEGQHLSLLADVCETLFSPSRISLLAEVDVELFLTFLKFLCDIPVLKDRLGNVLVKILLEFLSAAVERDGDYRQPRACASVLITLTRGSKANKDRMKVECDRLGETLEKTTDVYLRLQCVELLFRLHVHDGTILATSSLCGLLKRGVPKLPNDEHLLTNMLVLLESYDADREVPRILQFTTILVEVDSIQVCGPTKIYFSLSMLVIMMPGYTGDNITIPYEHIRSMKLTRERKLGLRLHVVPPQLSGIMSFEALKDTLTVSLTQATVDAFRASGIRDWVAARKNFAPLGSAREVRDTSTKLYALSVPETEKRGNTEGYNAGEGRAAKRDELGMPFLEIKEEGHPSGGGRGNGDMGMFHDLNEVATSKVTRMRQDCRRELQSVFHFAEEEIEKMRRTNASERDAFNTSLKEDLIMIRRVGAQVKAKTAECVESLNQELTETQALGELLRDELGKLQDSLTSALHSSEEAEVGHLIELKTLVDAEMKSIKDKLMRLVSLAGPFRTLGNHTLQREPVAGAST
Protein: Cytochrome bo(3) ubiquinol oxidase subunit 1 (cyt bo(3) subunit 1) (EC 7.1.1.3) (Cytochrome b562-o complex subunit I) (Cytochrome o ubiquinol oxidase subunit 1) (Cytochrome o subunit 1) (Oxidase bo(3) subunit 1) (Ubiquinol oxidase chain A) (Ubiquinol oxidase polypeptide I) (Ubiquinol oxidase subunit 1) (P0ABI8)
Organism: Escherichia coli (strain K12)
Function: Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction; ubiquinol-8 is the natural substrate for E.coli. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron and generating a proton motive force. All the redox centers of this enzyme complex are located within the largest subunit, subunit I. Protons are probably pumped via D- and K- channels found in this subunit.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:6365921}; Multi-pass membrane protein {ECO:0000269|PubMed:6365921}.
Interaction partners:
- Protoheme IX farnesyltransferase
- Cytochrome bo
- Cytochrome bo
- Cytochrome bo
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit E
- Succinate dehydrogenase flavoprotein subunit
Sequence:
MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN
Protein: Uncharacterized protein At4g28440 (O49453)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nucleic acid-binding, OB-fold-like protein
- Expressed protein
- F5O8.30 protein
- F11M21.26 protein
- Replication protein A 70 kDa DNA-binding subunit A
- Replication protein A 70 kDa DNA-binding subunit C
- Replication protein A 70 kDa DNA-binding subunit B
- Replication protein A 70 kDa DNA-binding subunit D
- Chloroplastic import inner membrane translocase subunit HP30-2
- Expressed protein
Sequence:
MATTGTAAVATGTSTVKRKPVFVKVEQLKPGTTGHTLTVKVIEANIVVPVTRKTRPASSLSRPSQPSRIVECLIGDETGCILFTARNDQVDLMKPGATVILRNSRIDMFKGTMRLGVDKWGRIEATGAASFTVKEDNNLSLVEYELINVGGDQ
Protein: Uncharacterized protein (O53315)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Protein-glutamine gamma-glutamyltransferase-like C-terminal domain-containing protein
- Probable methanol dehydrogenase transcriptional regulatory protein MoxR3
- Possible integral membrane protein
- Possible conserved secreted protein
Sequence:
MKRLIALGIFLIVGIELLALILHDRRLVLAGSGLALALVLLNVRRMLGNRDELTAAPDSDDLGEGLRRWLSNTETTIRWSESTRADWDRHLRPMLARRFEIATGHRQAKDPVAFAATGRMLFGDELWEWVNPNNVTHTGDRQPGPGRAALEEILQKLEQV
Protein: Potassium voltage-gated channel subfamily E member 3 (MinK-related peptide 2) (MiRP2) (Minimum potassium ion channel-related peptide 2) (Potassium channel subunit beta MiRP2) (Q9JJV7)
Organism: Rattus norvegicus (Rat)
Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Associated with KCNC4/Kv3.4 is proposed to form the subthreshold voltage-gated potassium channel in skeletal muscle and to establish the resting membrane potential (RMP) in muscle cells (By similarity). Associated with KCNQ1/KCLQT1 may form the intestinal cAMP-stimulated potassium channel involved in chloride secretion that produces a current with nearly instantaneous activation with a linear current-voltage relationship.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:14679187}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:12954870}. Perikaryon {ECO:0000250|UniProtKB:Q9Y6H6}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Y6H6}. Membrane raft {ECO:0000250|UniProtKB:Q9Y6H6}. Note=Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal neurons. {ECO:0000250|UniProtKB:Q9Y6H6}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily E member 2
- Intermediate conductance calcium-activated potassium channel protein 4
- Inward rectifier potassium channel 13
- Potassium voltage-gated channel subfamily E member 1
- Potassium two pore domain channel subfamily K member 5
- Potassium voltage-gated channel subfamily E regulatory subunit 4
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Potassium voltage-gated channel subfamily E regulatory subunit 5
- A-kinase anchoring protein 9
Sequence:
METSNGTETWYKSLHAVLKALNTTLHSHLLCRPGPGPGSGTGPDNQTEDHRASLPGRNDNSYMYILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNRVSMI
Protein: Uncharacterized protein (O45690)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTRPHQPRIDLNHGFLRFIRRNQVDRDEYNRVHEERKSEIRERIGSSDSSQDGEEKAQSNVYVPPHLRRQKKENEEKFSALKASRSQSQSDTGSEEGEGASGGGEASCPIQQKQKAFDENVRRQVRRRIERTHPTVDDICIVLANYSLQEAASKNSENSNEDLFELVLTLKSGEQKTIGVPRNTQAARLAKSLSREHHFSDSQCRNLRIFIEEQLELRFAREKSTATSSDASIPGSPTSSSESSIIEFSA
Protein: PRA1 family protein F1 (AtPRA1.F1) (Q9FZ63)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- MATH domain and coiled-coil domain-containing protein At3g58220
- Protein PAL OF QUIRKY
- AT4G01090 protein
- Ras-related protein RABD2b
- Potassium transporter 13
- At4g01410 hydroxyproline-rich glycoprotein family)
- Protein kinase superfamily protein
- PRA1 family protein A2
- PRA1 family protein A3
- PRA1 family protein H
Sequence:
MTTYGTNQKSSNDLAPKLEYITRGINQHKRSGLATRRPWKQMLDLGSFNFPRKLATVITRIRANTVYFQTNYTIVVLFSVFLSLIWNPFSLLVLLALLGAWLFLYFLRDEPLTVFDREIDHRIVLIIMSVITLSILFLTDAKLNIAVAIVAGALAVLSHAAVRKTEDLFQTDEETSLLNP
Protein: Selenoprotein F (15 kDa selenoprotein) (Q9ERR7)
Organism: Mus musculus (Mouse)
Function: May be involved in redox reactions associated with the formation of disulfide bonds (By similarity). May contribute to the quality control of protein folding in the endoplasmic reticulum. May regulate protein folding by enhancing the catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}. Note=The association with UGGT1/UGCGL1 is essential for its retention in the endoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- UDP-glucose:glycoprotein glucosyltransferase 1
- UDP-glucose:glycoprotein glucosyltransferase 1
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein K
- Selenoprotein S
- Selenoprotein M
- Selenoprotein N
- Protein adenylyltransferase SelO, mitochondrial
- Ethanolaminephosphotransferase 1
- Selenoprotein H
Sequence:
MAAGQGGWLRPALGLRLLLATAFQAVSALGAEFASEACRELGFSSNLLCSSCDLLGQFNLLPLDPVCRGCCQEEAQFETKKLYAGAILEVCGUKLGRFPQVQAFVRSDKPKLFRGLQIKYVRGSDPVLKLLDDNGNIAEELSILKWNTDSVEEFLSEKLERI
Protein: Recombining-binding protein suppressor of hairless (D6R946)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDHTEGSPAEEPPAHAPSPGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNAD
Protein: Small ribosomal subunit protein uS14z/uS14y/uS14x (40S ribosomal protein S29) (Q680P8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS24z
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein uS17z
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS8z
- Small ribosomal subunit protein uS9x
- Small ribosomal subunit protein eS19y
- Small ribosomal subunit protein eS17z
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS10x
Sequence:
MGHSNVWNSHPKKYGPGSRLCRVCGNSHGLIRKYGLNCCRQCFRSNAKEIGFIKYR
Protein: Folate receptor beta (FR-beta) (Folate receptor 2) (Folate-binding protein 2) (Q05685)
Organism: Mus musculus (Mouse)
Function: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH. Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Folate receptor alpha
- Sperm-egg fusion protein Juno
- Izumo sperm-egg fusion protein 1
- Glutamate carboxypeptidase 2
- Reduced folate transporter
- Proton-coupled folate transporter
Sequence:
MAWKQTPLLLLVYMVTTGSGRDRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCSVNTSQELHKADSRLYFNWDHCGKMEPACKSHFIQDSCLYECSPNLGPWIQQVDQSWRKERFLDVPLCKEDCHQWWEACRTSFTCKRDWHKGWDWSSGINKCPNTAPCHTFEYYFPTPASLCEGLWSHSYKVSNYSRGSGRCIQMWFDSTQGNPNEDVVKFYASFMTSGTVPHAAVLLVPSLAPVLSLWLPG
Protein: CCAAT/enhancer-binding protein (E5Q8C6)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005879}.
Interaction partners:
- CCAAT/enhancer-binding protein gamma
- Mitogen-activated protein kinase.
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase.
- Activating transcription factor 4.
- [histone H3]-lysine
- Peroxisome proliferator-activated receptor gamma
- Mitogen-activated protein kinase
- DNA damage-inducible transcript 3 protein
- Forkhead box protein O1
Sequence:
MQRLVAWDPACLPLPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKAAEYGYVSLGRLGAAKNALHPGCFAPLHPPPPPPPPQPAELKAEPGFEPADCKRKEEAGAPGGGAAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPAACYAGAAPAPSQVKSKTKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC
Protein: D-alanyl carrier protein (DCP) (D-alanine--poly(phosphoribitol) ligase subunit 2) (P63957)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00565}.
Interaction partners:
Sequence:
MDIKSEVIEIIDELFMEDVSDMMDEDLFDAGVLDSMGTVELIVEIENRFDIRVPVTEFGRDDWNTANKIIAGIVELQNA
Protein: Actin alpha cardiac muscle 1 (Actin, alpha cardiac muscle 1) (Cardiac muscle alpha actin 1) (B6VNT8)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Transcription factor HapC (Eurofung) (Q5B5Z6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- HapE
- Transcriptional activator HAP2
- Histone-like transcription factor, putative
- BZIP domain-containing protein
- GATA-type transcription factor sreA
Sequence:
MSSTSPSKEPEVEQEPQSGEEHEQMDKEQDNQTQGQGEFEVKEQDRWLPIANVARIMKLALPENAKIAKEAKECMQECVSEFISFITSEASEKCQQEKRKTVNGEDILFAMTSLGFENYAEALKIYLSKYRETQSARGEHQNRPPSSGYAGGGPVGGAASGPSVVRAGGAAAGGAFPEASDNAGSIMNQGLDPSEQDASAYGYPPMVGQGHNGAGGESY
Protein: Transcription elongation factor A protein 2 (Testis-specific S-II) (Transcription elongation factor S-II protein 2) (Transcription elongation factor TFIIS.l) (Q15560)
Organism: Homo sapiens (Human)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
Subcellular location: Nucleus.
Interaction partners:
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- RNA polymerase-associated protein LEO1
- Transcription initiation factor IIB
- RNA polymerase-associated protein RTF1 homolog
- Parafibromin
- Elongin-A
- DNA-directed RNA polymerase II subunit RPB9
- RNA polymerase-associated protein CTR9 homolog
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MMGKEEEIARIARRLDKMVTKKSAEGAMDLLRELKAMPITLHLLQSTRVGMSVNALRKQSSDEEVIALAKSLIKSWKKLLDASDAKARERGRGMPLPTSSRDASEAPDPSRKRPELPRAPSTPRITTFPPVPVTCDAVRNKCREMLTAALQTDHDHVAIGADCERLSAQIEECIFRDVGNTDMKYKNRVRSRISNLKDAKNPDLRRNVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCGKCRKKNCTYTQVQTRSSDEPMTTFVVCNECGNRWKFC
Protein: Sperm equatorial segment protein 1 (Q9D5A0)
Organism: Mus musculus (Mouse)
Function: Involved in fertilization ability of sperm.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20375058}. Note=Small proacrosomal granules (during the Golgi phase), enlarged acrosomal vesicles (during the cap phase), acrosome (during the elongating phase), equatorial segment of the acrosome (during the maturation phase) (By similarity). After acrosome reaction localizes to the equatorial segment region in both noncapacitated and capacitated, acrosome-reacted sperm (PubMed:25761597). {ECO:0000250|UniProtKB:Q6UW49, ECO:0000269|PubMed:25761597}.
Interaction partners:
Sequence:
MKLVVLVALWLWPSSLLAYPTITVLPDEEQNLNHYVHILQNLIMSVPTKEQDLGKKLSSSRTVDSAEPRSLASKVLLTPGLVSAQDVTPESDVLIRPVDETTNSRTRGFTLRRRRTQSTAFWSIRPNNISVVLRTEEPFIEKEPEPELESSRLPTEPEPELEPEPEPVAESRQMSEPEEELVTSTTPNKELTGTSRISSMATQPANTQATRITVTVKTTSTMDVSTDSEDVPQLSGQSEIPSAEDLPGRHSLNTRHEDILKKISNINAEIQQGLLGGNNSPEFKEFIKASREHLKRSLALAAAAEHKLEQMYGSNVFPEGRTSDPDNDMEMIINMLYNSRSKLSDYFNIKRVPSELREKASVVNAELRKILCVDQVEMQSLIKKLLSNNMKILNILNVP
Protein: Fas-binding factor 1 C-terminal domain-containing protein (Q586A8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSLKGAPSLQRQPTKQFSFDVLDEFYEGEDAYVQSDFDGEEVESKKKEEKKKEKSKKKKKKKDKKEKKSKSKEEKSTNKKGGKDTKETISTASVSAASGTESGGKAKTSDDYDYTYDDDSFDKYSEDFDDEIPVAPPSASSSGGSDPPSSGRQPARKELFSEEAAKAAKEQYEQQMRQMQEEQERREKALQRQQEELRAQMEEFKRLQEEKQREMEIEARAMRNTVGGAPAIGFPTGATGMEAKTGLPQEEQPVANIESQRRRQRERERAVHLRRLEQEEAARTLFQRLAQDVREVFHELNLSVVAAERERLLKDERYRKEREVRDRREELERREWLQKEVKEREERFWAAMEDREERFRTLIDAKIAKDDEEREARRKRDLEDREERAKNERELRDEITRMESQRRDREDAGIRERDQKFLQTQLDDMKRRYENQLEEARRQLELARAHSEEMHRTELAAMEKRYAESSAHSDRLHMQHVESFEAHTKNAAELQKIVEVLHKDMEKATQMNEAVTDERLEVLRQKERLINEQKALVDSVLEEIKYTKGEMEKERARIASLYAKFDIGLSNFTREAAEERRRCQESQAHYETLREQLEKDRRLMLHEVSQERKLFEQQYEEFMAKKLHAMAELQEERMAISRERTEAAMLRERRNNDEAELLKSLRAQEEAYAAKVDAMEEDRVAIGEMRREQKRLCDEIAAEREALRQERKSFEEEKVELLRRFEDLQRYAMESSATNERLRKEVARQSAEVVVREPPAKRIEPHVDPSELNSATSRLQMDLSRQRAMLQRISHT
Protein: Coiled-coil domain-containing 78 (Coiled-coil domain-containing protein 78 isoform X1) (E7F7G2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Multicilin
- Myotubularin-related protein 14
- Myotubularin 1.
- Ryanodine receptor 1a
- Basal body-orientation factor 1
Sequence:
MEDSSKQSSINQLHEQIRLLTDENVQLHERNKQLVSKLDSAQNKLGQQAASKSDLSVKLVQCEEDKLKISKDLVDVQIEANKMREQYEAEIFELKNMVLCHEGTASSLQAERDRLRQEVSAASTRLEISERNEHDLAEEFTVVKRNFLSLRDAYERERTQSEELSSELLALARTHDTLLQERERTHRHTLELERVRALLSRASQNRVKPEEFEQSKSTLGENGVQNKLREELEKLRKSYEEQQRRLEDKVVAMGREQQENKRAIQNTRLQLSQQSTTLILSQQQLKEAENEVSKLQNHLKELNREYRARLKHYIQDITECVSAAGNVDLGQKLKGFVESMLEEMKTSYRSREEQLTKAVRTYRKRIQGLSNAHQQLLIAYRMQREQILALPEHALDAGPPEAQFSPAGPELSGETEREIHRLREDKARLESQLKLAREQMAVLSESSQKTELTQEAWADVKRQIREITNSTQEAQERERIQLLTRATVAEEQLCELKEYVDNHLGRYKLEIIRLRRLLTSQEGRSNSARVNNPRPLHQTLKHSSNEI
Protein: D-xylose-proton symporter-like 1 (Q8L6Z8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Chloroplastic import inner membrane translocase subunit HP30-1
Sequence:
MGFDPENQSISSVGQVVGDSSSGGITAEKEPLLKENHSPENYSVLAAIPPFLFPALGALLFGYEIGATSCAIMSLKSPTLSGISWYDLSSVDVGIITSGSLYGALIGSIVAFSVADIIGRRKELILAAFLYLVGAIVTVVAPVFSILIIGRVTYGMGIGLTMHAAPMYIAETAPSQIRGRMISLKEFSTVLGMVGGYGIGSLWITVISGWRYMYATILPFPVIMGTGMCWLPASPRWLLLRALQGQGNGENLQQAAIRSLCRLRGSVIADSAAEQVNEILAELSLVGEDKEATFGELFRGKCLKALTIAGGLVLFQQITGQPSVLYYAPSILQTAGFSAAADATRISILLGLLKLVMTGVSVIVIDRVGRRPLLLCGVSGMVISLFLLGSYYMFYKNVPAVAVAALLLYVGCYQLSFGPIGWLMISEIFPLKLRGRGISLAVLVNFGANALVTFAFSPLKELLGAGILFCAFGVICVVSLFFIYYIVPETKGLTLEEIEAKCL
Protein: Protein Wiz (Widely-interspaced zinc finger-containing protein) (O88286)
Organism: Mus musculus (Mouse)
Function: May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization.
Subcellular location: Nucleus {ECO:0000269|PubMed:16702210}.
Interaction partners:
- Histone-lysine N-methyltransferase EHMT2
- Histone-lysine N-methyltransferase EHMT1
Sequence:
MEGLLAGGLAAPDHPRGPAPREDIESGAEAAEGEGDIFPSSHYLPITKEGPRDILDGRSGISDGQPHPGLSEALPRATSATHRISSCYWDGDSLDFQPGSPPPHLLGPFPASLDVQGSWEHPMVQEAREGTPSEQRFKDSVIVRTMKPYAKLKGSRKFLHHQGEVKFLEKYSPSHHKFDWLQDTDEQGPLKDTGLHLDLPAQPPTVTSFRRVIVPVDNTPKTLDMEVMGTREDLEDFGQVAQPSEWGLHTSASEVATQTWTVNSEASVERLQPLLSPVQTGPYLCELLQEVAGGVDSNEEEEEEPAVFPCIECSIYFKHKEHLLEHMSQHRRAPGQEPPADLAPLACSECGWAFTEPTALEQHWQLHQASREKIIEEIQKLKQFPGDEGREARLQCSKCVFGTNSSRAFMQHAKLHVRGSLPSRQATEPFRGGSPVLDVSTLVYPSYGDSSGLNTCVHCGFTAPSKSLLREHTRLVHAHHAHWEEVGEAFEDLTSQPCTSQDAYTHSPDTATVDYFSKSEPLLASVWQENPSGYDPDLAFGPDYQQPGMRNFPLLNSGQQSLGKLAFPSPMASASYSIQRNRNKSTVHLQRMEDKSHLWSEEEEEEDEDVVLTSERDFTPENGAFPPLAIPSLIPQPALELKQTFQDALQAVDASETQQQQLQGMVPIVLMAKLRPQVIAATTRASPQLPPEEPELRSTHPLDFLLLDAPLGGSLGLNTLLEGDPAMALKHEERKCPYCPDRFHYGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTISPINILQELLATSAAELPPSPLGREPGGPPRSFLTSRRPRLPLTMPFPPTWAEDPGPIYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAPLGLTPSLTKKSNSPKEFLAGAARPGLLTLAKPMDAPAVNKAIKSPPGFSAKGLTHPSSSPLLKKAPLTLAGSPTPKNPEDKSPQLSLSPRPTSPKAQWPQSEDEGPLNLTSGPEPTRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGHLHPPGPSPKALAKVLSTGGPGSSLEARSPSDLHISPLTKKLPPPPGSPLGHSPTASPPPTARKMFSGLATPSLPKKLKPEHMRVEIKREMLPGTLHGEPHPSEGPWGTPREDMAPLNLSARAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKLCLIKKEPPAGDLAPALTEDGSPTAAPGALHSPLPLSPLASRPGKPGAGPTQVPRELSLSPITGSKPSAASYLGPVATKRPLQEDRFLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPPLGLAPGGLSLVGRSAGGEPGLEAGRAADSGERPLATSPPGTVKSEEHQRQNINKFERRQARPSDASAARGGEEVNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEEPQAPQAQTAAVEAP