sde2

Replication stress response regulator SDE2

468 amino acids

Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression.

Belongs to the SDE2 family.

50.788 kDa

MASVWVRDALSSRLQLVRVAPGAAALDLLSQAGTAIPLTDFYITCNGHLADLEEKLQDGRTYSIVPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWIKKQADREAEKEQRRLERLQRKLAEPKHYFTDPEYHKQCHDMSERLEEAVIKGLQASSSSMASAESDDTRKRKKDMYSSKGTPGKKKCFWTGLEGLETSSSSDSASDSDLDESPCSSSSSSSDSKYYENIKERLQSPESQSSPEELGQGSSDGSHQMLEGHSSSDRSHQMLEGQASCSGSDQMLEGPSSSAGAQWQSSSKGTELVQESQSIPVESEQNMESQNSSDESKQTAFNNSGINVECENVTSPGSTGQDGQTPNDGVRPASPSIPISKQELQQPSNAETSPIDLLAFKTAAELEALGLEKLKLELGALALKCGGTLQERAARLFSVRGLPRDQIDPSLFAKPAKGKKK

sde2

Replication stress response regulator SDE2

467 amino acids

Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression.

Belongs to the SDE2 family.

51.381 kDa

MELFVISPDLKFNNLTVAPDSTVSDLIDHFTVKNGVSLTDFYVSSNGRLSRSNDLLQSGVVYRLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKEMAEWLKKQADREAEKEQRRLERIQRKLAEPKHYFTDTNYEQQCHDLSERLEDSVLKGMQASSSGLVQADEGPSLKRANPTDSKKKAKKKCYWTGMAGLEEMASSSEGSDDSDSEVSPSTSGASCSSGFPKPVVSAHKADPQEQPSSSSPAQRKHNQEELQKRDKEECTSEISSSSSSPAANNEKLNQEETNEISSSSSSPAPKPTEVNQQEMETEMECTAQISSSSSSPAEHSEEEVQQTAERVEKMAEEVQKTAEEVQKKTEESTAEISPSSSIPEEKSQVLSQVEDPLDLLSVSGPEQLEALGLERLKKELMERGMKCGGTLQERAARLFSVKGLTPDQIDPSLLAKPSKGKKK

sde2

Replication stress response regulator SDE2

454 amino acids

Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression.

Belongs to the SDE2 family.

49.363 kDa

MASVWVRDALSGRLQLVRVAPGAVALDLLYQEGTAIPLTDFYVKCNGHLADLEEKLQDGHTYSIEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWTKKQADREAEKEQRRLERLQRKLAEPKHYFTDPEYHKQCHDMSERLEEAVIKGLQASSSDVVSAESDDTRKRKKDMYASKGTSSKKKCFWTGLEGLEASSSSDSSSDSDLDESPCSSSSGSKHHEYIKERLGSPESSSSSDGLEEASSAGSHQMLKGQTSGSESDNILEGPSSSAGSLHVPQLQSSSKGTEHIQEPQTCPAESEQNTETPNISDGSEENPTTVTNSECKSVTSAANTGQNEQILDDGHKFASPTLLEPKSELQQSSNTEPSSIDLVAYKTVAELEALGLEKLKLELVALGLKCGGTLQERAARLFSVRGLARDQIDPSLFAKPAKAKKK

SDE2

Replication stress response regulator SDE2

451 amino acids

Involved in both DNA replication and cell cycle control (PubMed:27906959). Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner (PubMed:27906959). Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression (PubMed:27906959).

Belongs to the SDE2 family.

49.742 kDa

MAEAAALVWIRGPGFGCKAVRCASGRCTVRDFIHRHCQDQNVPVENFFVKCNGALINTSDTVQHGAVYSLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQKRLERLQRKLVEPKHCFTSPDYQQQCHEMAERLEDSVLKGMQAASSKMVSAEISENRKRQWPTKSQTDRGASAGKRRCFWLGMEGLETAEGSNSESSDDDSEEAPSTSGMGFHAPKIGSNGVEMAAKFPSGSQRARVVNTDHGSPEQLQIPVTDSGRHILEDSCAELGESKEHMESRMVTETEETQEKKAESKEPIEEEPTGAGLNKDKETEERTDGERVAEVAPEERENVAVAKLQESQPGNAVIDKETIDLLAFTSVAELELLGLEKLKCELMALGLKCGGTLQERAARLFSVRGLAKEQIDPALFAKPLKGKKK

SDE2

Replication stress response regulator SDE2

451 amino acids

Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression.

Belongs to the SDE2 family.

49.821 kDa

MAEAAALVWIRGPGFGCKAVRCASARCTVRDFIHRHCQDQNVPVENFFVKCNGALIYTSDTVQHGAVYSLEPRLCGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQKRLERLQRKLVEPKHCFTSPDYQQQCHEMAERLEDSVLKGMQAASSKMVSAEISENRKRQWPTKSQTDREASAGKRRYFWLGMEGLETAEGSSSESSDDDSEEAPSTSGMGFHAPKIGGSGVEMAAKFPSGSQRARVVNTDPGSPEQLQIPVTDSGRHISEDSCAELGESKEHMESRMVTETEETQEKKAESREPIEEEPTGAGLNKDKETEERTDGERVAEVACEERENVAVAKLQESQPGNAVIDKETIDLLAFTSVAELELLGLEKLKCELMALGLKCGGTLQERAARLFSVRGLAKEQIDPALFAKPLKGKKK

Sde2

Replication stress response regulator SDE2

448 amino acids

Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression.

Belongs to the SDE2 family.

48.58 kDa

MAEAAVVAWVRGPGTVWKALPCASVGCSVRDVIYRHCQEQEVPVECFFVTCNGVLVNAGDKVQHGAVYSLEPRLRGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQRRLERLQRKLAEPAHCFTSPDYQRQCHEMAERLEDSVLKGMQAASSKMVSAEITETRKRPNKSKTDQETSAKKRKRKCFWLGMDGLEAAEGSSTGSSEDSSEDDSEDAPGTSEQSCCAREDGIDAVEVAADRPGSPRSSASGTHSESPEKLQCPVTEPGQGILENTGTEPGETSDKECNERKTVTDPEETPARKETESHEATEKDQKTGMSGGDRAAMVLSGEDRKSVPAANLEGNNSGDTALGLEAVDLSAFSSAAELESLGLERLKCELMVLGLKCGGTLQERAARLFSVRGLTKELIDPALFAKPSKGKKK

Sde2

Replication stress response regulator SDE2

448 amino acids

Involved in both DNA replication and cell cycle control. Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction with PCNA prevents monoubiquitination of the latter thereby inhibiting translesion DNA synthesis. The binding of SDE2 to PCNA also leads to processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is degraded by the DCX(DTL) complex in a cell cycle- and DNA damage dependent manner. Binding of SDE2 to PCNA is necessary to counteract damage due to ultraviolet light induced replication stress. The complete degradation of SDE2 is necessary to allow S-phase progression.

Belongs to the SDE2 family.

48.084 kDa

MAEAAVLAWVRGPGTAWKALPCASVGCSVRDVIYRHCEEQEIPVECFFVKCNGVLVAAGDKVCHGAVYSLEPRLRGGKGGFGSMLRALGAQIEKTTNREACRDLSGRRLRDVNHEKAMAEWVKQQAEREAEKEQRRLERLQRKLAEPAHCFASPDYQRQCHEMAERLEDSVLKGMQAASSKVVSAEVTETRKRPNRSKTDQGAGAKKKRCFWLGMEGLEAAEGSSTGSSDDSEDDDHEDAPGTSGPSCCARENGSDGGEVAADSPGSVQSSGSGTRSESPKELQNPMTEPGQGILENTGTEPGETSTREHNERKTVTVTETEETPARKETESPEPTEKGQETGVIGEDRAAMALSGEDRKSIPAATPEGSNSGDTALGVEALDLSAFSCAAELELLGLERLKCALMALGLKCGGTLQERAARLFSVRGLSKELIDPTLFAKPSKGKKK

sde2

Telomere maintenance protein SDE2

263 amino acids

Plays a role in the regulation of telomeric and centromeric silencing. Contributes to the prevention of abnormal telomere elongation. Required for chromosome segregation to daughter cells in mitosis and meiosis. May participate in the recruitment of the histone deacetylase silencing complex SHREC, which prevents transcription at telomeres.

Belongs to the SDE2 family.

29.251 kDa

MECKTVFLNGDFLKNSVNVNLNRLATVETLLRHVLGDSYETVLERAYLTHQSRIVHPDIQLCKLEGKSTSAHLNLTLCTRVLGGKGGFGSQLRAAGGRMSKKRNEQENQDSCRDLDGNRLGTIRQAKELSEYLAKKPAETRAKKEAKKQKLNKVLAADSSSSRFDDHEYLEDLEQSVSNVRDAFQNSLLYRRGSTSASSFSSGSNGATTDEPAEKEARNNNSSINSWSRRMQASESSNEAEGEDSESQTSKSLYEWDDPLYGL