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Protein

DENN domain-containing protein 4C

Gene

DENND4C

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

Functioni

Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin.1 Publication

GO - Molecular functioni

  • Rab guanyl-nucleotide exchange factor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
DENN domain-containing protein 4C
Gene namesi
Name:DENND4C
Synonyms:C9orf55, C9orf55B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:26079. DENND4C.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134939495.

Polymorphism and mutation databases

DMDMi158937337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16731673DENN domain-containing protein 4CPRO_0000089697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei505 – 5051PhosphoserineCombined sources
Modified residuei729 – 7291PhosphoserineCombined sources
Modified residuei732 – 7321PhosphoserineCombined sources
Modified residuei737 – 7371PhosphoserineCombined sources
Modified residuei739 – 7391PhosphothreonineCombined sources
Modified residuei753 – 7531PhosphoserineCombined sources
Modified residuei767 – 7671PhosphoserineCombined sources
Modified residuei810 – 8101PhosphoserineCombined sources
Modified residuei863 – 8631PhosphoserineCombined sources
Modified residuei890 – 8901PhosphoserineCombined sources
Modified residuei948 – 9481PhosphoserineCombined sources
Modified residuei989 – 9891PhosphoserineCombined sources
Modified residuei1008 – 10081PhosphoserineCombined sources
Modified residuei1016 – 10161PhosphoserineBy similarity
Modified residuei1042 – 10421PhosphoserineCombined sources
Modified residuei1089 – 10891PhosphoserineCombined sources
Modified residuei1110 – 11101PhosphoserineCombined sources
Modified residuei1387 – 13871PhosphoserineCombined sources
Modified residuei1391 – 13911PhosphoserineCombined sources
Modified residuei1404 – 14041PhosphoserineBy similarity
Modified residuei1563 – 15631PhosphoserineCombined sources
Isoform 2 (identifier: Q5VZ89-2)
Modified residuei144 – 1441PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in response to insulin.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5VZ89.
MaxQBiQ5VZ89.
PaxDbiQ5VZ89.
PRIDEiQ5VZ89.

PTM databases

iPTMnetiQ5VZ89.
PhosphoSiteiQ5VZ89.

Expressioni

Gene expression databases

BgeeiQ5VZ89.
CleanExiHS_DENND4C.

Organism-specific databases

HPAiHPA014917.
HPA015096.

Interactioni

Protein-protein interaction databases

BioGridi120799. 10 interactions.
IntActiQ5VZ89. 9 interactions.
STRINGi9606.ENSP00000369802.

Structurei

3D structure databases

ProteinModelPortaliQ5VZ89.
SMRiQ5VZ89. Positions 5-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4040UDENNAdd
BLAST
Domaini72 – 256185DENNPROSITE-ProRule annotationAdd
BLAST
Domaini322 – 39675dDENNPROSITE-ProRule annotationAdd
BLAST
Repeati585 – 61935PPRAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1199 – 12035Poly-Ser

Sequence similaritiesi

Contains 1 dDENN domain.PROSITE-ProRule annotation
Contains 1 DENN domain.PROSITE-ProRule annotation
Contains 1 uDENN domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2127. Eukaryota.
ENOG410XQMX. LUCA.
HOVERGENiHBG058313.
InParanoidiQ5VZ89.
OrthoDBiEOG790FZV.
PhylomeDBiQ5VZ89.
TreeFamiTF313237.

Family and domain databases

InterProiIPR005112. dDENN_dom.
IPR001194. DENN_dom.
IPR005113. uDENN_dom.
[Graphical view]
PfamiPF03455. dDENN. 1 hit.
PF02141. DENN. 1 hit.
[Graphical view]
SMARTiSM00801. dDENN. 1 hit.
SM00799. DENN. 1 hit.
[Graphical view]
PROSITEiPS50947. DDENN. 1 hit.
PS50211. DENN. 1 hit.
PS50946. UDENN. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VZ89-1) [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
MGATIECWDP ETKYPLPVFS TFVLTGSSAK KVYGAAIQFY EPYSRELLSE
60 70 80 90 100
KQLMHLGLLT PVERKMVSKS INTNKCICLL SHWPFFEAFR KFLMFIYKLS
110 120 130 140 150
VSGPHPLPIE KHISHFMQNI PFPSPQRPRI LVQLSVHDAL ILSQPVSTPL
160 170 180 190 200
PLSGANFSTL LMNLGPENCA TLLLFVLLES KILLHSLRPA VLTGVAEAVV
210 220 230 240 250
AMIFPFQWQC PYIPLCPLSL AAVLSAPLPF IVGVDSRYFD LHDPPQDVVC
260 270 280 290 300
IDLDTNMLYV SDEKKNMNWK QLPKKPCKNL LSTLKKLYPQ LSSVHQKTQE
310 320 330 340 350
GSAIDMTPIE ADFSWQKKMT QLEMEIQEAF LRFMASILKG YRTYLRPITE
360 370 380 390 400
APSNKATAAD SLFDRQGFLK SRDRAYAKFY TLLSKTQIFI RFIEECSFVS
410 420 430 440 450
DKDTGLAFFD DCIEKLFPDK GTEKTDKVDF DSAEDTRLIE LDDSQKSEHT
460 470 480 490 500
VFIMPPEPPP DDGKDLSPKY SYKYFPRLDL KLFDRPQELK LCFSRHPTGN
510 520 530 540 550
SITKSPPLMA KRTKQEIKTA HKLAKRCYTN PPQWAKCLFS HCYSLWFICL
560 570 580 590 600
PAYVRVSHPK VRALQQAYDV LIKMRKTDVD PLDEVCYRVV MQLCGLWGHP
610 620 630 640 650
VLAVRVLFEM KTARIKPNAI TYGYYNKVVL ESPWPSSTRS GIFLWTKVRN
660 670 680 690 700
VVRGLAQFRQ PLKKTVQRSQ VSSISGGQSD QGYGSKDELI KDDAEIHVPE
710 720 730 740 750
EQAARELITK TKMQTEEVCD ASAIVAKHSQ PSPEPHSPTE PPAWGSSIVK
760 770 780 790 800
VPSGIFDVNS RKSSTGSISN VLFSTQDPVE DAVFGEATNL KKNGDRGEKR
810 820 830 840 850
QKHFPERSCS FSSESRAGML LKKSSLDSNS SEMAIMMGAD AKILTAALTC
860 870 880 890 900
PKTSLLHIAR THSFENVSCH LPDSRTCMSE STWNPEHRSS PVPEMLEESQ
910 920 930 940 950
ELLEPVVDDV PKTTATVDTY ESLLSDSNSN QSRDLKTVSK DLRNKRSSLY
960 970 980 990 1000
GIAKVVQRED VETGLDPLSL LATECTGGKT PDSEDKLFSP VIARNLADEI
1010 1020 1030 1040 1050
ESYMNLKSPL GSKSSSMELH REENRESGMT TAFIHALERR SSLPLDHGSP
1060 1070 1080 1090 1100
AQENPESEKS SPAVSRSKTF TGRFKQQTPS RTHKERSTSL SALVRSSPHG
1110 1120 1130 1140 1150
SLGSVVNSLS GLKLDNILSG PKIDVLKSGM KQAATVASKM WVAVASAYSY
1160 1170 1180 1190 1200
SDDEEETNRD YSFPAGLEDH ILGENISPNT SISGLVPSEL TQSNTSLGSS
1210 1220 1230 1240 1250
SSSGDVGKLH YPTGEVPFPR GMKGQDFEKS DHGSSQNTSM SSIYQNCAME
1260 1270 1280 1290 1300
VLMSSCSQCR ACGALVYDEE IMAGWTADDS NLNTACPFCK SNFLPLLNIE
1310 1320 1330 1340 1350
FKDLRGSASF FLKPSTSGDS LQSGSIPLAN ESLEHKPVSS LAEPDLINFM
1360 1370 1380 1390 1400
DFPKHNQIIT EETGSAVEPS DEIKRASGDV QTMKISSVPN SLSKRNVSLT
1410 1420 1430 1440 1450
RSHSVGGPLQ NIDFTQRPFH GISTVSLPNS LQEVVDPLGK RPNPPPVSVP
1460 1470 1480 1490 1500
YLSPLVLRKE LESLLENEGD QVIHTSSFIN QHPIIFWNLV WYFRRLDLPS
1510 1520 1530 1540 1550
NLPGLILTSE HCNEGVQLPL SSLSQDSKLV YIQLLWDNIN LHQEPREPLY
1560 1570 1580 1590 1600
VSWRNFNSEK KSSLLSEEQQ ETSTLVETIR QSIQHNNVLK PINLLSQQMK
1610 1620 1630 1640 1650
PGMKRQRSLY REILFLSLVS LGRENIDIEA FDNEYGIAYN SLSSEILERL
1660 1670
QKIDAPPSAS VEWCRKCFGA PLI
Length:1,673
Mass (Da):186,857
Last modified:August 21, 2007 - v2
Checksum:iEC6A7115E22A7B02
GO
Isoform 2 (identifier: Q5VZ89-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-573: Missing.
     675-675: S → SALQNVTGGSDGDTVSHGSVDSSNDANNGEHTVFVRDLIRLESIDNHSST
     764-766: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:1,146
Mass (Da):126,244
Checksum:i6E1B04E6EB21C576
GO
Isoform 3 (identifier: Q5VZ89-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-573: Missing.
     574-818: Missing.
     1608-1609: SL → GI
     1610-1673: Missing.

Show »
Length:791
Mass (Da):86,970
Checksum:i76BF2D89AD747D32
GO
Isoform 4 (identifier: Q5VZ89-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-573: Missing.
     574-818: Missing.
     819-1003: Missing.

Note: No experimental confirmation available.
Show »
Length:670
Mass (Da):73,931
Checksum:iAA59FEFF544AC1A3
GO
Isoform 5 (identifier: Q5VZ89-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1370-1387: SDEIKRASGDVQTMKISS → RYQRVQRPLYVVINGVPL
     1388-1609: Missing.
     1610-1673: Missing.

Show »
Length:1,387
Mass (Da):154,479
Checksum:iDFA5CF2CC37C4D7C
GO
Isoform 6 (identifier: Q5VZ89-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1608-1673: Missing.

Note: No experimental confirmation available.
Show »
Length:1,607
Mass (Da):179,409
Checksum:iB03ED897D7F51D85
GO

Sequence cautioni

The sequence BAA91294.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91478.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA92039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15221.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH10466.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAM21141.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti447 – 4471S → G in BAC86313 (PubMed:14702039).Curated
Sequence conflicti668 – 6758RSQVSSIS → CKSAFFLT in CAH10466 (PubMed:17974005).Curated
Sequence conflicti1061 – 10611S → P in BAA91294 (PubMed:14702039).Curated
Sequence conflicti1420 – 14201H → R in BAA91478 (PubMed:14702039).Curated
Sequence conflicti1533 – 15331Q → H in BAA92039 (PubMed:14702039).Curated
Sequence conflicti1626 – 16261I → V in CAH10466 (PubMed:17974005).Curated
Sequence conflicti1632 – 16321D → G in CAH10466 (PubMed:17974005).Curated
Sequence conflicti1657 – 16571P → A in CAD39177 (PubMed:17974005).Curated
Sequence conflicti1661 – 16611V → A in CAH10466 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti991 – 9911V → G.
Corresponds to variant rs34267952 [ dbSNP | Ensembl ].
VAR_061640
Natural varianti1030 – 10301T → A.
Corresponds to variant rs17818730 [ dbSNP | Ensembl ].
VAR_022891
Natural varianti1107 – 11071N → H.
Corresponds to variant rs6475322 [ dbSNP | Ensembl ].
VAR_022892

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 573573Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_027377Add
BLAST
Alternative sequencei574 – 818245Missing in isoform 3 and isoform 4. 1 PublicationVSP_027378Add
BLAST
Alternative sequencei675 – 6751S → SALQNVTGGSDGDTVSHGSV DSSNDANNGEHTVFVRDLIR LESIDNHSST in isoform 2. CuratedVSP_027379
Alternative sequencei764 – 7663Missing in isoform 2. CuratedVSP_027380
Alternative sequencei819 – 1003185Missing in isoform 4. CuratedVSP_027381Add
BLAST
Alternative sequencei1370 – 138718SDEIK…MKISS → RYQRVQRPLYVVINGVPL in isoform 5. 1 PublicationVSP_027382Add
BLAST
Alternative sequencei1388 – 1609222Missing in isoform 5. 1 PublicationVSP_027383Add
BLAST
Alternative sequencei1608 – 167366Missing in isoform 6. 1 PublicationVSP_027385Add
BLAST
Alternative sequencei1608 – 16092SL → GI in isoform 3. 1 PublicationVSP_027384
Alternative sequencei1610 – 167364Missing in isoform 3 and isoform 5. 1 PublicationVSP_027386Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161909, AL391834 Genomic DNA. Translation: CAH70581.2.
AL391834 Genomic DNA. Translation: CAM21138.1.
AL391834 Genomic DNA. Translation: CAM21139.1.
AL391834 Genomic DNA. Translation: CAM21140.1.
AL391834 Genomic DNA. Translation: CAM21141.1. Different initiation.
AL391834, AL161909 Genomic DNA. Translation: CAM21148.1.
AK000627 mRNA. Translation: BAA91294.1. Different initiation.
AK001046 mRNA. Translation: BAA91478.1. Different initiation.
AK002020 mRNA. Translation: BAA92039.1. Different initiation.
AK025705 mRNA. Translation: BAB15221.1. Different initiation.
AK125842 mRNA. Translation: BAC86313.1.
AL834521 mRNA. Translation: CAD39177.1.
CR627367 mRNA. Translation: CAH10466.1. Different initiation.
RefSeqiNP_060395.5. NM_017925.6.
UniGeneiHs.249591.

Genome annotation databases

EnsembliENST00000380432; ENSP00000369797; ENSG00000137145.
GeneIDi55667.
KEGGihsa:55667.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161909, AL391834 Genomic DNA. Translation: CAH70581.2.
AL391834 Genomic DNA. Translation: CAM21138.1.
AL391834 Genomic DNA. Translation: CAM21139.1.
AL391834 Genomic DNA. Translation: CAM21140.1.
AL391834 Genomic DNA. Translation: CAM21141.1. Different initiation.
AL391834, AL161909 Genomic DNA. Translation: CAM21148.1.
AK000627 mRNA. Translation: BAA91294.1. Different initiation.
AK001046 mRNA. Translation: BAA91478.1. Different initiation.
AK002020 mRNA. Translation: BAA92039.1. Different initiation.
AK025705 mRNA. Translation: BAB15221.1. Different initiation.
AK125842 mRNA. Translation: BAC86313.1.
AL834521 mRNA. Translation: CAD39177.1.
CR627367 mRNA. Translation: CAH10466.1. Different initiation.
RefSeqiNP_060395.5. NM_017925.6.
UniGeneiHs.249591.

3D structure databases

ProteinModelPortaliQ5VZ89.
SMRiQ5VZ89. Positions 5-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120799. 10 interactions.
IntActiQ5VZ89. 9 interactions.
STRINGi9606.ENSP00000369802.

PTM databases

iPTMnetiQ5VZ89.
PhosphoSiteiQ5VZ89.

Polymorphism and mutation databases

DMDMi158937337.

Proteomic databases

EPDiQ5VZ89.
MaxQBiQ5VZ89.
PaxDbiQ5VZ89.
PRIDEiQ5VZ89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380432; ENSP00000369797; ENSG00000137145.
GeneIDi55667.
KEGGihsa:55667.

Organism-specific databases

CTDi55667.
GeneCardsiDENND4C.
H-InvDBHIX0007946.
HGNCiHGNC:26079. DENND4C.
HPAiHPA014917.
HPA015096.
neXtProtiNX_Q5VZ89.
PharmGKBiPA134939495.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2127. Eukaryota.
ENOG410XQMX. LUCA.
HOVERGENiHBG058313.
InParanoidiQ5VZ89.
OrthoDBiEOG790FZV.
PhylomeDBiQ5VZ89.
TreeFamiTF313237.

Miscellaneous databases

ChiTaRSiDENND4C. human.
GenomeRNAii55667.
NextBioi60426.
PROiQ5VZ89.

Gene expression databases

BgeeiQ5VZ89.
CleanExiHS_DENND4C.

Family and domain databases

InterProiIPR005112. dDENN_dom.
IPR001194. DENN_dom.
IPR005113. uDENN_dom.
[Graphical view]
PfamiPF03455. dDENN. 1 hit.
PF02141. DENN. 1 hit.
[Graphical view]
SMARTiSM00801. dDENN. 1 hit.
SM00799. DENN. 1 hit.
[Graphical view]
PROSITEiPS50947. DDENN. 1 hit.
PS50211. DENN. 1 hit.
PS50946. UDENN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-1673 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1036-1673 (ISOFORM 5).
    Tissue: Embryo, Hepatoma, Placenta, Signet-ring cell carcinoma and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 668-1673 (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 978-1673 (ISOFORM 1).
    Tissue: Fetal kidney and Lymph node.
  4. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  5. "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.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-729; SER-732; SER-737; SER-753; SER-767; SER-810; SER-863; SER-890; SER-989; SER-1008; SER-1042; SER-1089; SER-1387 AND SER-1391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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].
  8. "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-737; SER-753; SER-1042 AND SER-1110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors."
    Yoshimura S., Gerondopoulos A., Linford A., Rigden D.J., Barr F.A.
    J. Cell Biol. 191:367-381(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS GUANYL-NUCLEOTIDE EXCHANGE FACTOR.
  10. "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-989 AND SER-1387, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729; SER-732; SER-737; THR-739; SER-753; SER-1042 AND SER-1563, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDEN4C_HUMAN
AccessioniPrimary (citable) accession number: Q5VZ89
Secondary accession number(s): A2A3R1
, A2A3R2, A2A3R3, A2A3R9, Q6AI48, Q6ZUB3, Q8NCY7, Q9H6N4, Q9NUT1, Q9NWA5, Q9NWT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: August 21, 2007
Last modified: May 11, 2016
This is version 111 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 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.