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Q9UBU7

- DBF4A_HUMAN

UniProt

Q9UBU7 - DBF4A_HUMAN

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Protein

Protein DBF4 homolog A

Gene

DBF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri289 – 33749DBF4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. enzyme activator activity Source: ProtInc
  2. nucleic acid binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA replication Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. mitotic cell cycle Source: Reactome
  4. positive regulation of catalytic activity Source: GOC
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DBF4 homolog A
Alternative name(s):
Activator of S phase kinase
Chiffon homolog A
DBF4-type zinc finger-containing protein 1
Gene namesi
Name:DBF4
Synonyms:ASK, DBF4A, ZDBF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:17364. DBF4.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 674674Protein DBF4 homolog APRO_0000234061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731Phosphothreonine1 Publication
Modified residuei345 – 3451Phosphothreonine1 Publication
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei359 – 3591Phosphoserine2 Publications
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei508 – 5081Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UBU7.
PaxDbiQ9UBU7.
PRIDEiQ9UBU7.

PTM databases

PhosphoSiteiQ9UBU7.

Expressioni

Tissue specificityi

Highly expressed in testis and thymus. Expressed also in most cancer cells lines.1 Publication

Inductioni

Induced in G1 phase at low level, increased during G1-S phase and remain high during S and G2-M phase.2 Publications

Gene expression databases

BgeeiQ9UBU7.
CleanExiHS_DBF4.
ExpressionAtlasiQ9UBU7. baseline and differential.
GenevestigatoriQ9UBU7.

Organism-specific databases

HPAiHPA051589.

Interactioni

Subunit structurei

Forms a complex with CDC7. Note that CDC7 forms distinct complex either with DBF4A or DBF4B. Such complexes are stable upon replication stress. Interacts with MEN1, MCM2, ORC2, ORC4 and ORC6.4 Publications

Protein-protein interaction databases

BioGridi116129. 18 interactions.
DIPiDIP-31205N.
IntActiQ9UBU7. 3 interactions.
MINTiMINT-2842143.
STRINGi9606.ENSP00000265728.

Structurei

Secondary structure

1
674
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi217 – 2259Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi244 – 2463Combined sources
Turni297 – 3004Combined sources
Helixi306 – 3116Combined sources
Helixi313 – 3197Combined sources
Helixi322 – 3243Combined sources
Helixi325 – 3317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4F99X-ray2.33B210-350[»]
4F9AX-ray2.17B/D210-350[»]
4F9BX-ray2.50B/D210-350[»]
4F9CX-ray2.08B210-350[»]
ProteinModelPortaliQ9UBU7.
SMRiQ9UBU7. Positions 214-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 12889BRCT 1Add
BLAST
Domaini154 – 17926BRCT 2Add
BLAST

Sequence similaritiesi

Contains 2 BRCT domains.Curated
Contains 1 DBF4-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri289 – 33749DBF4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG314450.
GeneTreeiENSGT00530000063909.
HOVERGENiHBG063274.
InParanoidiQ9UBU7.
KOiK06629.
OMAiDIWEEEN.
OrthoDBiEOG7BGHK5.
PhylomeDBiQ9UBU7.
TreeFamiTF332790.

Family and domain databases

Gene3Di3.40.50.10190. 2 hits.
InterProiIPR001357. BRCT_dom.
IPR006572. Znf_DBF.
[Graphical view]
PfamiPF07535. zf-DBF. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
SM00586. ZnF_DBF. 1 hit.
[Graphical view]
PROSITEiPS51265. ZF_DBF4. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBU7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNSGAMRIHS KGHFQGGIQV KNEKNRPSLK SLKTDNRPEK SKCKPLWGKV
60 70 80 90 100
FYLDLPSVTI SEKLQKDIKD LGGRVEEFLS KDISYLISNK KEAKFAQTLG
110 120 130 140 150
RISPVPSPES AYTAETTSPH PSHDGSSFKS PDTVCLSRGK LLVEKAIKDH
160 170 180 190 200
DFIPSNSILS NALSWGVKIL HIDDIRYYIE QKKKELYLLK KSSTSVRDGG
210 220 230 240 250
KRVGSGAQKT RTGRLKKPFV KVEDMSQLYR PFYLQLTNMP FINYSIQKPC
260 270 280 290 300
SPFDVDKPSS MQKQTQVKLR IQTDGDKYGG TSIQLQLKEK KKKGYCECCL
310 320 330 340 350
QKYEDLETHL LSEQHRNFAQ SNQYQVVDDI VSKLVFDFVE YEKDTPKKKR
360 370 380 390 400
IKYSVGSLSP VSASVLKKTE QKEKVELQHI SQKDCQEDDT TVKEQNFLYK
410 420 430 440 450
ETQETEKKLL FISEPIPHPS NELRGLNEKM SNKCSMLSTA EDDIRQNFTQ
460 470 480 490 500
LPLHKNKQEC ILDISEHTLS ENDLEELRVD HYKCNIQASV HVSDFSTDNS
510 520 530 540 550
GSQPKQKSDT VLFPAKDLKE KDLHSIFTHD SGLITINSSQ EHLTVQAKAP
560 570 580 590 600
FHTPPEEPNE CDFKNMDSLP SGKIHRKVKI ILGRNRKENL EPNAEFDKRT
610 620 630 640 650
EFITQEENRI CSSPVQSLLD LFQTSEEKSE FLGFTSYTEK SGICNVLDIW
660 670
EEENSDNLLT AFFSSPSTST FTGF
Length:674
Mass (Da):76,858
Last modified:May 1, 2000 - v1
Checksum:i353FEB7E85507E5C
GO
Isoform 2 (identifier: Q9UBU7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-234: LYRPFYL → SPAVHLM
     235-674: Missing.

Show »
Length:234
Mass (Da):26,124
Checksum:i50357B9FCF8472BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti581 – 5811I → L in EAL24170. (PubMed:12690205)Curated
Sequence conflicti584 – 5841R → Q in EAL24170. (PubMed:12690205)Curated
Sequence conflicti619 – 6191L → P in EAL24170. (PubMed:12690205)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121Y → N.
Corresponds to variant rs1476703 [ dbSNP | Ensembl ].
VAR_052970
Natural varianti575 – 5751H → R.
Corresponds to variant rs2041049 [ dbSNP | Ensembl ].
VAR_052971

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei228 – 2347LYRPFYL → SPAVHLM in isoform 2. 1 PublicationVSP_018203
Alternative sequencei235 – 674440Missing in isoform 2. 1 PublicationVSP_018204Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028069 mRNA. Translation: BAA78326.1.
AB028070 mRNA. Translation: BAA78327.1.
AF160249 mRNA. Translation: AAD41911.1.
AF160876 mRNA. Translation: AAD45357.1.
AK292569 mRNA. Translation: BAF85258.1.
AC003083 Genomic DNA. Translation: AAS07442.1.
AC005164 Genomic DNA. Translation: AAS07418.1.
CH236949 Genomic DNA. Translation: EAL24170.1.
CH471091 Genomic DNA. Translation: EAW76930.1.
BC036045 mRNA. Translation: AAH36045.1.
BC047693 mRNA. Translation: AAH47693.1.
CCDSiCCDS5611.1. [Q9UBU7-1]
PIRiT02633.
RefSeqiNP_006707.1. NM_006716.3. [Q9UBU7-1]
UniGeneiHs.485380.

Genome annotation databases

EnsembliENST00000265728; ENSP00000265728; ENSG00000006634. [Q9UBU7-1]
ENST00000413643; ENSP00000414083; ENSG00000006634. [Q9UBU7-2]
GeneIDi10926.
KEGGihsa:10926.
UCSCiuc003ujf.1. human. [Q9UBU7-1]

Polymorphism databases

DMDMi74753231.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB028069 mRNA. Translation: BAA78326.1 .
AB028070 mRNA. Translation: BAA78327.1 .
AF160249 mRNA. Translation: AAD41911.1 .
AF160876 mRNA. Translation: AAD45357.1 .
AK292569 mRNA. Translation: BAF85258.1 .
AC003083 Genomic DNA. Translation: AAS07442.1 .
AC005164 Genomic DNA. Translation: AAS07418.1 .
CH236949 Genomic DNA. Translation: EAL24170.1 .
CH471091 Genomic DNA. Translation: EAW76930.1 .
BC036045 mRNA. Translation: AAH36045.1 .
BC047693 mRNA. Translation: AAH47693.1 .
CCDSi CCDS5611.1. [Q9UBU7-1 ]
PIRi T02633.
RefSeqi NP_006707.1. NM_006716.3. [Q9UBU7-1 ]
UniGenei Hs.485380.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4F99 X-ray 2.33 B 210-350 [» ]
4F9A X-ray 2.17 B/D 210-350 [» ]
4F9B X-ray 2.50 B/D 210-350 [» ]
4F9C X-ray 2.08 B 210-350 [» ]
ProteinModelPortali Q9UBU7.
SMRi Q9UBU7. Positions 214-342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116129. 18 interactions.
DIPi DIP-31205N.
IntActi Q9UBU7. 3 interactions.
MINTi MINT-2842143.
STRINGi 9606.ENSP00000265728.

Chemistry

BindingDBi Q9UBU7.
ChEMBLi CHEMBL2111377.

PTM databases

PhosphoSitei Q9UBU7.

Polymorphism databases

DMDMi 74753231.

Proteomic databases

MaxQBi Q9UBU7.
PaxDbi Q9UBU7.
PRIDEi Q9UBU7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265728 ; ENSP00000265728 ; ENSG00000006634 . [Q9UBU7-1 ]
ENST00000413643 ; ENSP00000414083 ; ENSG00000006634 . [Q9UBU7-2 ]
GeneIDi 10926.
KEGGi hsa:10926.
UCSCi uc003ujf.1. human. [Q9UBU7-1 ]

Organism-specific databases

CTDi 10926.
GeneCardsi GC07P087505.
HGNCi HGNC:17364. DBF4.
HPAi HPA051589.
MIMi 604281. gene.
neXtProti NX_Q9UBU7.
PharmGKBi PA142672016.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG314450.
GeneTreei ENSGT00530000063909.
HOVERGENi HBG063274.
InParanoidi Q9UBU7.
KOi K06629.
OMAi DIWEEEN.
OrthoDBi EOG7BGHK5.
PhylomeDBi Q9UBU7.
TreeFami TF332790.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.

Miscellaneous databases

GeneWikii DBF4.
GenomeRNAii 10926.
NextBioi 41507.
PROi Q9UBU7.
SOURCEi Search...

Gene expression databases

Bgeei Q9UBU7.
CleanExi HS_DBF4.
ExpressionAtlasi Q9UBU7. baseline and differential.
Genevestigatori Q9UBU7.

Family and domain databases

Gene3Di 3.40.50.10190. 2 hits.
InterProi IPR001357. BRCT_dom.
IPR006572. Znf_DBF.
[Graphical view ]
Pfami PF07535. zf-DBF. 1 hit.
[Graphical view ]
SMARTi SM00292. BRCT. 1 hit.
SM00586. ZnF_DBF. 1 hit.
[Graphical view ]
PROSITEi PS51265. ZF_DBF4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel growth- and cell cycle-regulated protein, ASK, activates human Cdc7-related kinase and is essential for G1/S transition in mammalian cells."
    Kumagai H., Sato N., Yamada M., Mahony D., Seghezzi W., Lees E., Arai K., Masai H.
    Mol. Cell. Biol. 19:5083-5095(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH CDC7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  2. "Mammalian Cdc7-Dbf4 protein kinase complex is essential for initiation of DNA replication."
    Jiang W., McDonald D., Hope T.J., Hunter T.
    EMBO J. 18:5703-5713(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC7, INDUCTION.
  3. "Use of a semi-automated yeast two-hybrid system to identify proteins that interact with the human Cdc7 protein."
    Hollingsworth R.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Testis.
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Brain and Testis.
  9. "Functional interaction between tumor suppressor menin and activator of S-phase kinase."
    Schnepp R.W., Hou Z., Wang H., Petersen C., Silva A., Masai H., Hua X.
    Cancer Res. 64:6791-6796(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEN1.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Cdc7 is an active kinase in human cancer cells undergoing replication stress."
    Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C., Santocanale C.
    J. Biol. Chem. 282:208-215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC7.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; THR-345; SER-381 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDBF4A_HUMAN
AccessioniPrimary (citable) accession number: Q9UBU7
Secondary accession number(s): A4D1D8
, A8K954, O75226, Q75MS6, Q75N01, Q9Y2M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 114 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3