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Q9UBU7 (DBF4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein DBF4 homolog A
Alternative name(s):
Activator of S phase kinase
Chiffon homolog A
DBF4-type zinc finger-containing protein 1
Gene names
Name:DBF4
Synonyms:ASK, DBF4A, ZDBF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.11

Subunit structure

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. Ref.1 Ref.2 Ref.9 Ref.11

Subcellular location

Nucleus Ref.1.

Tissue specificity

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

Induction

Induced in G1 phase at low level, increased during G1-S phase and remain high during S and G2-M phase. Ref.1 Ref.2

Sequence similarities

Contains 2 BRCT domains.

Contains 1 DBF4-type zinc finger.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UBU7-1)

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.
Isoform 2 (identifier: Q9UBU7-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 674674Protein DBF4 homolog A
PRO_0000234061

Regions

Domain40 – 12889BRCT 1
Domain154 – 17926BRCT 2
Zinc finger289 – 33749DBF4-type

Amino acid modifications

Modified residue2731Phosphothreonine Ref.15
Modified residue3451Phosphothreonine Ref.15
Modified residue3541Phosphoserine Ref.14
Modified residue3591Phosphoserine Ref.14 Ref.16
Modified residue3811Phosphoserine Ref.15
Modified residue4131Phosphoserine Ref.15
Modified residue5081Phosphoserine Ref.17 Ref.18

Natural variations

Alternative sequence228 – 2347LYRPFYL → SPAVHLM in isoform 2.
VSP_018203
Alternative sequence235 – 674440Missing in isoform 2.
VSP_018204
Natural variant1121Y → N.
Corresponds to variant rs1476703 [ dbSNP | Ensembl ].
VAR_052970
Natural variant5751H → R.
Corresponds to variant rs2041049 [ dbSNP | Ensembl ].
VAR_052971

Experimental info

Sequence conflict5811I → L in EAL24170. Ref.6
Sequence conflict5841R → Q in EAL24170. Ref.6
Sequence conflict6191L → P in EAL24170. Ref.6

Secondary structure

1 .................. 674
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 353FEB7E85507E5C

FASTA67476,858
        10         20         30         40         50         60 
MNSGAMRIHS KGHFQGGIQV KNEKNRPSLK SLKTDNRPEK SKCKPLWGKV FYLDLPSVTI 

        70         80         90        100        110        120 
SEKLQKDIKD LGGRVEEFLS KDISYLISNK KEAKFAQTLG RISPVPSPES AYTAETTSPH 

       130        140        150        160        170        180 
PSHDGSSFKS PDTVCLSRGK LLVEKAIKDH DFIPSNSILS NALSWGVKIL HIDDIRYYIE 

       190        200        210        220        230        240 
QKKKELYLLK KSSTSVRDGG KRVGSGAQKT RTGRLKKPFV KVEDMSQLYR PFYLQLTNMP 

       250        260        270        280        290        300 
FINYSIQKPC SPFDVDKPSS MQKQTQVKLR IQTDGDKYGG TSIQLQLKEK KKKGYCECCL 

       310        320        330        340        350        360 
QKYEDLETHL LSEQHRNFAQ SNQYQVVDDI VSKLVFDFVE YEKDTPKKKR IKYSVGSLSP 

       370        380        390        400        410        420 
VSASVLKKTE QKEKVELQHI SQKDCQEDDT TVKEQNFLYK ETQETEKKLL FISEPIPHPS 

       430        440        450        460        470        480 
NELRGLNEKM SNKCSMLSTA EDDIRQNFTQ LPLHKNKQEC ILDISEHTLS ENDLEELRVD 

       490        500        510        520        530        540 
HYKCNIQASV HVSDFSTDNS GSQPKQKSDT VLFPAKDLKE KDLHSIFTHD SGLITINSSQ 

       550        560        570        580        590        600 
EHLTVQAKAP FHTPPEEPNE CDFKNMDSLP SGKIHRKVKI ILGRNRKENL EPNAEFDKRT 

       610        620        630        640        650        660 
EFITQEENRI CSSPVQSLLD LFQTSEEKSE FLGFTSYTEK SGICNVLDIW EEENSDNLLT 

       670 
AFFSSPSTST FTGF

« Hide

Isoform 2 [UniParc].

Checksum: 50357B9FCF8472BC
Show »

FASTA23426,124

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-359, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; THR-345; SER-381 AND SER-413, MASS SPECTROMETRY.
[16]"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, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[17]"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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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-508, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00170805.
IPI00744939.
PIRT02633.
RefSeqNP_006707.1. NM_006716.3.
UniGeneHs.485380.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F99X-ray2.33B210-350[»]
4F9AX-ray2.17B/D210-350[»]
4F9BX-ray2.50B/D210-350[»]
4F9CX-ray2.08B210-350[»]
ProteinModelPortalQ9UBU7.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31205N.
IntActQ9UBU7. 2 interactions.
MINTMINT-2842143.
STRING9606.ENSP00000265728.

PTM databases

PhosphoSiteQ9UBU7.

Polymorphism databases

DMDM74753231.

Proteomic databases

PaxDbQ9UBU7.
PRIDEQ9UBU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265728; ENSP00000265728; ENSG00000006634.
ENST00000413643; ENSP00000414083; ENSG00000006634.
GeneID10926.
KEGGhsa:10926.
UCSCuc003ujf.1. human.

Organism-specific databases

CTD10926.
GeneCardsGC07P087505.
HGNCHGNC:17364. DBF4.
MIM604281. gene.
neXtProtNX_Q9UBU7.
PharmGKBPA142672016.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314450.
HOVERGENHBG063274.
InParanoidQ9UBU7.
KOK06629.
OMAFTSYTEN.
OrthoDBEOG4894NR.
PhylomeDBQ9UBU7.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ9UBU7.
BgeeQ9UBU7.
CleanExHS_DBF4.
GenevestigatorQ9UBU7.
GermOnlineENSG00000006634. Homo sapiens.

Family and domain databases

InterProIPR001357. BRCT_dom.
IPR006572. Znf_DBF.
[Graphical view]
PfamPF07535. zf-DBF. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
SM00586. ZnF_DBF. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. False negative.
PS51265. ZF_DBF4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9UBU7.
ChEMBLCHEMBL4483.
GenomeRNAi10926.
NextBio41507.
SOURCESearch...

Entry information

Entry nameDBF4A_HUMAN
AccessionPrimary (citable) accession number: Q9UBU7
Secondary accession number(s): A4D1D8 expand/collapse secondary AC list , A8K954, O75226, Q75MS6, Q75N01, Q9Y2M6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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