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Q8NFC6

- BD1L1_HUMAN

UniProt

Q8NFC6 - BD1L1_HUMAN

Protein

Biorientation of chromosomes in cell division protein 1-like 1

Gene

BOD1L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (02 Oct 2007)
      Previous versions | rss
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    Functioni

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi2872 – 288413A.T hookAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biorientation of chromosomes in cell division protein 1-like 1
    Alternative name(s):
    Protein FAM44A
    Gene namesi
    Name:BOD1L1
    Synonyms:BOD1L, FAM44A, KIAA1327
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:31792. BOD1L1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: HPA

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164716652.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 30513051Biorientation of chromosomes in cell division protein 1-like 1PRO_0000187027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei266 – 2661Phosphoserine2 Publications
    Modified residuei473 – 4731N6-acetyllysine1 Publication
    Modified residuei482 – 4821Phosphoserine4 Publications
    Modified residuei484 – 4841Phosphoserine4 Publications
    Modified residuei635 – 6351Phosphoserine1 Publication
    Modified residuei1145 – 11451Phosphoserine1 Publication
    Modified residuei1354 – 13541Phosphothreonine2 Publications
    Modified residuei1531 – 15311Phosphoserine3 Publications
    Modified residuei1710 – 17101Phosphoserine1 Publication
    Modified residuei2501 – 25011Phosphoserine1 Publication
    Modified residuei2779 – 27791Phosphoserine1 Publication
    Modified residuei2780 – 27801Phosphoserine1 Publication
    Modified residuei2905 – 29051Phosphoserine1 Publication
    Modified residuei2907 – 29071Phosphoserine1 Publication
    Modified residuei2954 – 29541Phosphoserine1 Publication
    Modified residuei2956 – 29561Phosphothreonine1 Publication
    Modified residuei2958 – 29581Phosphoserine1 Publication
    Modified residuei2964 – 29641Phosphoserine1 Publication
    Modified residuei2973 – 29731Phosphoserine1 Publication
    Cross-linki2981 – 2981Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki2982 – 2982Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei2986 – 29861Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8NFC6.
    PaxDbiQ8NFC6.
    PRIDEiQ8NFC6.

    PTM databases

    PhosphoSiteiQ8NFC6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8NFC6.
    BgeeiQ8NFC6.
    CleanExiHS_FAM44A.
    GenevestigatoriQ8NFC6.

    Organism-specific databases

    HPAiHPA036943.
    HPA037362.
    HPA041290.

    Interactioni

    Protein-protein interaction databases

    BioGridi129238. 3 interactions.
    IntActiQ8NFC6. 1 interaction.
    STRINGi9606.ENSP00000040738.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NFC6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 3632Pro-richAdd
    BLAST
    Compositional biasi315 – 1046732Lys-richAdd
    BLAST
    Compositional biasi2760 – 27656Poly-Glu
    Compositional biasi2988 – 299710Poly-Glu

    Sequence similaritiesi

    Belongs to the BOD1 family.Curated
    Contains 1 A.T hook DNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000112474.
    InParanoidiQ8NFC6.
    OMAiTCTGAEG.
    OrthoDBiEOG7X3QQD.
    PhylomeDBiQ8NFC6.
    TreeFamiTF335808.

    Family and domain databases

    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR026955. Bod1_like.
    [Graphical view]
    PANTHERiPTHR31532. PTHR31532. 1 hit.
    SMARTiSM00384. AT_hook. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8NFC6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATNPQPQPP PPAPPPPPPQ PQPQPPPPPP GPGAGPGAGG AGGAGAGAGD     50
    PQLVAMIVNH LKSQGLFDQF RRDCLADVDT KPAYQNLRQR VDNFVANHLA 100
    THTWSPHLNK NQLRNNIRQQ VLKSGMLESG IDRIISQVVD PKINHTFRPQ 150
    VEKAVHEFLA TLNHKEEGSG NTAPDDEKPD TSLITQGVPT PGPSANVAND 200
    AMSILETITS LNQEASAARA STETSNAKTS ERASKKLPSQ PTTDTSTDKE 250
    RTSEDMADKE KSTADSGGEG LETAPKSEEF SDLPCPVEEI KNYTKEHNNL 300
    ILLNKDVQQE SSEQKNKSTD KGEKKPDSNE KGERKKEKKE KTEKKFDHSK 350
    KSEDTQKVKD EKQAKEKEVE SLKLPSEKNS NKAKTVEGTK EDFSLIDSDV 400
    DGLTDITVSS VHTSDLSSFE EDTEEEVVTS DSMEEGEITS DDEEKNKQNK 450
    TKTQTSDSSE GKTKSVRHAY VHKPYLYSKY YSDSDDELTV EQRRQSIAKE 500
    KEERLLRRQI NREKLEEKRK QKAEKTKSSK TKGQGRSSVD LEESSTKSLE 550
    PKAARIKEVL KERKVLEKKV ALSKKRKKDS RNVEENSKKK QQYEEDSKET 600
    LKTSEHCEKE KISSSKELKH VHAKSEPSKP ARRLSESLHV VDENKNESKL 650
    EREHKRRTST PVIMEGVQEE TDTRDVKRQV ERSEICTEEP QKQKSTLKNE 700
    KHLKKDDSET PHLKSLLKKE VKSSKEKPER EKTPSEDKLS VKHKYKGDCM 750
    HKTGDETELH SSEKGLKVEE NIQKQSQQTK LSSDDKTERK SKHRNERKLS 800
    VLGKDGKPVS EYIIKTDENV RKENNKKERR LSAEKTKAEH KSRRSSDSKI 850
    QKDSLGSKQH GITLQRRSES YSEDKCDMDS TNMDSNLKPE EVVHKEKRRT 900
    KSLLEEKLVL KSKSKTQGKQ VKVVETELQE GATKQATTPK PDKEKNTEEN 950
    DSEKQRKSKV EDKPFEETGV EPVLETASSS AHSTQKDSSH RAKLPLAKEK 1000
    YKSDKDSTST RLERKLSDGH KSRSLKHSSK DIKKKDENKS DDKDGKEVDS 1050
    SHEKARGNSS LMEKKLSRRL CENRRGSLSQ EMAKGEEKLA ANTLSTPSGS 1100
    SLQRPKKSGD MTLIPEQEPM EIDSEPGVEN VFEVSKTQDN RNNNSQQDID 1150
    SENMKQKTSA TVQKDELRTC TADSKATAPA YKPGRGTGVN SNSEKHADHR 1200
    STLTKKMHIQ SAVSKMNPGE KEPIHRGTTE VNIDSETVHR MLLSAPSEND 1250
    RVQKNLKNTA AEEHVAQGDA TLEHSTNLDS SPSLSSVTVV PLRESYDPDV 1300
    IPLFDKRTVL EGSTASTSPA DHSALPNQSL TVRESEVLKT SDSKEGGEGF 1350
    TVDTPAKASI TSKRHIPEAH QATLLDGKQG KVIMPLGSKL TGVIVENENI 1400
    TKEGGLVDMA KKENDLNAEP NLKQTIKATV ENGKKDGIAV DHVVGLNTEK 1450
    YAETVKLKHK RSPGKVKDIS IDVERRNENS EVDTSAGSGS APSVLHQRNG 1500
    QTEDVATGPR RAEKTSVATS TEGKDKDVTL SPVKAGPATT TSSETRQSEV 1550
    ALPCTSIEAD EGLIIGTHSR NNPLHVGAEA SECTVFAAAE EGGAVVTEGF 1600
    AESETFLTST KEGESGECAV AESEDRAADL LAVHAVKIEA NVNSVVTEEK 1650
    DDAVTSAGSE EKCDGSLSRD SEIVEGTITF ISEVESDGAV TSAGTEIRAG 1700
    SISSEEVDGS QGNMMRMGPK KETEGTVTCT GAEGRSDNFV ICSVTGAGPR 1750
    EERMVTGAGV VLGDNDAPPG TSASQEGDGS VNDGTEGESA VTSTGITEDG 1800
    EGPASCTGSE DSSEGFAISS ESEENGESAM DSTVAKEGTN VPLVAAGPCD 1850
    DEGIVTSTGA KEEDEEGEDV VTSTGRGNEI GHASTCTGLG EESEGVLICE 1900
    SAEGDSQIGT VVEHVEAEAG AAIMNANENN VDSMSGTEKG SKDTDICSSA 1950
    KGIVESSVTS AVSGKDEVTP VPGGCEGPMT SAASDQSDSQ LEKVEDTTIS 2000
    TGLVGGSYDV LVSGEVPECE VAHTSPSEKE DEDIITSVEN EECDGLMATT 2050
    ASGDITNQNS LAGGKNQGKV LIISTSTTND YTPQVSAITD VEGGLSDALR 2100
    TEENMEGTRV TTEEFEAPMP SAVSGDDSQL TASRSEEKDE CAMISTSIGE 2150
    EFELPISSAT TIKCAESLQP VAAAVEERAT GPVLISTADF EGPMPSAPPE 2200
    AESPLASTSK EEKDECALIS TSIAEECEAS VSGVVVESEN ERAGTVMEEK 2250
    DGSGIISTSS VEDCEGPVSS AVPQEEGDPS VTPAEEMGDT AMISTSTSEG 2300
    CEAVMIGAVL QDEDRLTITR VEDLSDAAII STSTAECMPI SASIDRHEEN 2350
    QLTADNPEGN GDLSATEVSK HKVPMPSLIA ENNCRCPGPV RGGKEPGPVL 2400
    AVSTEEGHNG PSVHKPSAGQ GHPSAVCAEK EEKHGKECPE IGPFAGRGQK 2450
    ESTLHLINAE EKNVLLNSLQ KEDKSPETGT AGGSSTASYS AGRGLEGNAN 2500
    SPAHLRGPEQ TSGQTAKDPS VSIRYLAAVN TGAIKADDMP PVQGTVAEHS 2550
    FLPAEQQGSE DNLKTSTTKC ITGQESKIAP SHTMIPPATY SVALLAPKCE 2600
    QDLTIKNDYS GKWTDQASAE KTGDDNSTRK SFPEEGDIMV TVSSEENVCD 2650
    IGNEESPLNV LGGLKLKANL KMEAYVPSEE EKNGEILAPP ESLCGGKPSG 2700
    IAELQREPLL VNESLNVENS GFRTNEEIHS ESYNKGEISS GRKDNAEAIS 2750
    GHSVEADPKE VEEEERHMPK RKRKQHYLSS EDEPDDNPDV LDSRIETAQR 2800
    QCPETEPHDT KEENSRDLEE LPKTSSETNS TTSRVMEEKD EYSSSETTGE 2850
    KPEQNDDDTI KSQEEDQPII IKRKRGRPRK YPVETTLKMK DDSKTDTGIV 2900
    TVEQSPSSSK LKVMQTDESN KETANLQERS ISNDDGEEKI VTSVRRRGRK 2950
    PKRSLTVSDD AESSEPERKR QKSVSDPVED KKEQESDEEE EEEEEDEPSG 3000
    ATTRSTTRSE AQRSKTQLSP SIKRKREVSP PGARTRGQQR VEEAPVKKAK 3050
    R 3051
    Length:3,051
    Mass (Da):330,466
    Last modified:October 2, 2007 - v2
    Checksum:i44AD19BDDFDCE560
    GO

    Sequence cautioni

    The sequence BAB15299.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence CAB70705.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH16987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti337 – 3371E → K in AAH65546. (PubMed:15489334)Curated
    Sequence conflicti337 – 3371E → K in AAH87835. (PubMed:15489334)Curated
    Sequence conflicti498 – 5025AKEKE → GILWF in AAM94279. 1 PublicationCurated
    Sequence conflicti1417 – 14171N → S in BAB15299. (PubMed:14702039)Curated
    Sequence conflicti1438 – 14381I → V in BAB15299. (PubMed:14702039)Curated
    Sequence conflicti1740 – 17401V → M in BAB15299. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti246 – 2461S → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036124
    Natural varianti429 – 4291T → M.
    Corresponds to variant rs2035820 [ dbSNP | Ensembl ].
    VAR_035220
    Natural varianti650 – 6501L → I.
    Corresponds to variant rs1971278 [ dbSNP | Ensembl ].
    VAR_035221
    Natural varianti1369 – 13691A → G.
    Corresponds to variant rs17745712 [ dbSNP | Ensembl ].
    VAR_035222
    Natural varianti1448 – 14481T → A.
    Corresponds to variant rs17745676 [ dbSNP | Ensembl ].
    VAR_035223
    Natural varianti1515 – 15151T → A.
    Corresponds to variant rs16888885 [ dbSNP | Ensembl ].
    VAR_035224
    Natural varianti1645 – 16451V → I.
    Corresponds to variant rs17807493 [ dbSNP | Ensembl ].
    VAR_035225
    Natural varianti2361 – 23611G → S.
    Corresponds to variant rs3822227 [ dbSNP | Ensembl ].
    VAR_035226
    Natural varianti2396 – 23961P → L.1 Publication
    Corresponds to variant rs3733557 [ dbSNP | Ensembl ].
    VAR_035227
    Natural varianti2944 – 29441V → M.
    Corresponds to variant rs28538279 [ dbSNP | Ensembl ].
    VAR_061166

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006445 Genomic DNA. No translation available.
    AF528529 mRNA. Translation: AAM94279.1.
    BC016987 mRNA. Translation: AAH16987.1. Different initiation.
    BC065546 mRNA. Translation: AAH65546.1.
    BC087835 mRNA. Translation: AAH87835.1.
    AK025965 mRNA. Translation: BAB15299.1. Different termination.
    AB037748 mRNA. Translation: BAA92565.2.
    AL137350 mRNA. Translation: CAB70705.1. Different termination.
    CCDSiCCDS3411.2.
    PIRiT46424.
    RefSeqiNP_683692.2. NM_148894.2.
    UniGeneiHs.744935.

    Genome annotation databases

    EnsembliENST00000040738; ENSP00000040738; ENSG00000038219.
    GeneIDi259282.
    KEGGihsa:259282.
    UCSCiuc003gmz.1. human.

    Polymorphism databases

    DMDMi158931124.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006445 Genomic DNA. No translation available.
    AF528529 mRNA. Translation: AAM94279.1 .
    BC016987 mRNA. Translation: AAH16987.1 . Different initiation.
    BC065546 mRNA. Translation: AAH65546.1 .
    BC087835 mRNA. Translation: AAH87835.1 .
    AK025965 mRNA. Translation: BAB15299.1 . Different termination.
    AB037748 mRNA. Translation: BAA92565.2 .
    AL137350 mRNA. Translation: CAB70705.1 . Different termination.
    CCDSi CCDS3411.2.
    PIRi T46424.
    RefSeqi NP_683692.2. NM_148894.2.
    UniGenei Hs.744935.

    3D structure databases

    ProteinModelPortali Q8NFC6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 129238. 3 interactions.
    IntActi Q8NFC6. 1 interaction.
    STRINGi 9606.ENSP00000040738.

    PTM databases

    PhosphoSitei Q8NFC6.

    Polymorphism databases

    DMDMi 158931124.

    Proteomic databases

    MaxQBi Q8NFC6.
    PaxDbi Q8NFC6.
    PRIDEi Q8NFC6.

    Protocols and materials databases

    DNASUi 259282.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000040738 ; ENSP00000040738 ; ENSG00000038219 .
    GeneIDi 259282.
    KEGGi hsa:259282.
    UCSCi uc003gmz.1. human.

    Organism-specific databases

    CTDi 259282.
    GeneCardsi GC04M013571.
    H-InvDB HIX0004103.
    HGNCi HGNC:31792. BOD1L1.
    HPAi HPA036943.
    HPA037362.
    HPA041290.
    neXtProti NX_Q8NFC6.
    PharmGKBi PA164716652.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000112474.
    InParanoidi Q8NFC6.
    OMAi TCTGAEG.
    OrthoDBi EOG7X3QQD.
    PhylomeDBi Q8NFC6.
    TreeFami TF335808.

    Miscellaneous databases

    ChiTaRSi BOD1L1. human.
    GenomeRNAii 259282.
    NextBioi 93097.
    PROi Q8NFC6.

    Gene expression databases

    ArrayExpressi Q8NFC6.
    Bgeei Q8NFC6.
    CleanExi HS_FAM44A.
    Genevestigatori Q8NFC6.

    Family and domain databases

    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR026955. Bod1_like.
    [Graphical view ]
    PANTHERi PTHR31532. PTHR31532. 1 hit.
    SMARTi SM00384. AT_hook. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Guo J.H., Yu L.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-502.
      Tissue: Ovary.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-338 AND 2649-3051.
      Tissue: Duodenum, Skin and Uterus.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1207-1861.
    5. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1248-3051, VARIANT LEU-2396.
      Tissue: Brain.
    6. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2444-2874.
      Tissue: Testis.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-2981 AND LYS-2982.
      Tissue: Mammary cancer.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145 AND SER-1710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-484; THR-1354; SER-1531; SER-2954 AND SER-2986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-482; SER-484; SER-2907; THR-2956; SER-2958 AND SER-2964, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-473, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-484; SER-635; SER-1531 AND SER-2501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-482; SER-484; SER-1531; SER-2779; SER-2780; SER-2905; SER-2973 AND SER-2986, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-246.

    Entry informationi

    Entry nameiBD1L1_HUMAN
    AccessioniPrimary (citable) accession number: Q8NFC6
    Secondary accession number(s): Q6P0M8
    , Q96AL1, Q9H6G0, Q9NTD6, Q9P2L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3