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Protein

Zinc finger protein 687

Gene

ZNF687

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri533 – 55220C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri705 – 72723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri764 – 78724C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri792 – 81524C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri827 – 84923C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri858 – 88124C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 98624C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri993 – 101624C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1135 – 115824C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1200 – 122223C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 687
Gene namesi
Name:ZNF687
Synonyms:KIAA1441
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:29277. ZNF687.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670486.

Polymorphism and mutation databases

BioMutaiZNF687.
DMDMi74759771.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12371237Zinc finger protein 687PRO_0000234005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei148 – 1481PhosphothreonineCombined sources
Modified residuei251 – 2511PhosphoserineCombined sources
Modified residuei253 – 2531PhosphoserineCombined sources
Modified residuei266 – 2661PhosphoserineCombined sources
Modified residuei271 – 2711PhosphoserineCombined sources
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki336 – 336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei374 – 3741PhosphoserineCombined sources
Modified residuei433 – 4331PhosphoserineCombined sources
Modified residuei495 – 4951PhosphoserineCombined sources
Modified residuei1057 – 10571PhosphoserineCombined sources
Modified residuei1082 – 10821PhosphoserineCombined sources
Modified residuei1083 – 10831PhosphoserineCombined sources
Modified residuei1085 – 10851PhosphoserineCombined sources
Modified residuei1106 – 11061PhosphoserineCombined sources
Modified residuei1118 – 11181PhosphoserineCombined sources
Modified residuei1184 – 11841PhosphoserineBy similarity
Modified residuei1191 – 11911PhosphoserineCombined sources
Modified residuei1211 – 12111PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8N1G0.
MaxQBiQ8N1G0.
PaxDbiQ8N1G0.
PRIDEiQ8N1G0.

PTM databases

iPTMnetiQ8N1G0.
PhosphoSiteiQ8N1G0.

Expressioni

Gene expression databases

BgeeiQ8N1G0.
CleanExiHS_ZNF687.
ExpressionAtlasiQ8N1G0. baseline and differential.
GenevisibleiQ8N1G0. HS.

Organism-specific databases

HPAiHPA021193.
HPA053052.

Interactioni

Protein-protein interaction databases

BioGridi121643. 39 interactions.
IntActiQ8N1G0. 23 interactions.
STRINGi9606.ENSP00000319829.

Structurei

3D structure databases

ProteinModelPortaliQ8N1G0.
SMRiQ8N1G0. Positions 524-586, 673-876, 954-1057, 1128-1154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi130 – 305176Pro-richAdd
BLAST
Compositional biasi322 – 3254Poly-Ser
Compositional biasi922 – 9265Poly-Ser
Compositional biasi927 – 9304Poly-Glu
Compositional biasi955 – 9628Poly-Gly

Sequence similaritiesi

Contains 10 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri533 – 55220C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri705 – 72723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri764 – 78724C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri792 – 81524C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri827 – 84923C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri858 – 88124C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 98624C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri993 – 101624C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1135 – 115824C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1200 – 122223C2H2-type 10PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00530000063261.
HOGENOMiHOG000010306.
HOVERGENiHBG062228.
InParanoidiQ8N1G0.
OMAiFKQSPGH.
OrthoDBiEOG7H1JKM.
PhylomeDBiQ8N1G0.
TreeFamiTF329009.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF16622. zf-C2H2_11. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 14 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 8 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N1G0-1) [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
MGDMKTPDFD DLLAAFDIPD IDANEAIHSG PEENEGPGGP GKPEPGVGSE
60 70 80 90 100
SEDTAAASAG DGPGVPAQAS DHGLPPPDIS VVSVIVKNTV CPEQSEALAG
110 120 130 140 150
GSAGDGAQAA GVTKEGPVGP HRMQNGFGSP EPSLPGTPHS PAPPSGGTWK
160 170 180 190 200
EKGMEGKTPL DLFAHFGPEP GDHSDPLPPS APSPTREGAL TPPPFPSSFE
210 220 230 240 250
LAQENGPGMQ PPVSSPPLGA LKQESCSPHH PQVLAQQGSG SSPKATDIPA
260 270 280 290 300
SASPPPVAGV PFFKQSPGHQ SPLASPKVPV CQPLKEEDDD EGPVDKSSPG
310 320 330 340 350
SPQSPSSGAE AADEDSNDSP ASSSSRPLKV RIKTIKTSCG NITRTVTQVP
360 370 380 390 400
SDPDPPAPLA EGAFLAEASL LKLSPATPTS EGPKVVSVQL GDGTRLKGTV
410 420 430 440 450
LPVATIQNAS TAMLMAASVA RKAVVLPGGT ATSPKMIAKN VLGLVPQALP
460 470 480 490 500
KADGRAGLGT GGQKVNGASV VMVQPSKTAT GPSTGGGTVI SRTQSSLVEA
510 520 530 540 550
FNKILNSKNL LPAYRPNLSP PAEAGLALPP TGYRCLECGD AFSLEKSLAR
560 570 580 590 600
HYDRRSMRIE VTCNHCARRL VFFNKCSLLL HAREHKDKGL VMQCSHLVMR
610 620 630 640 650
PVALDQMVGQ PDITPLLPVA VPPVSGPLAL PALGKGEGAI TSSAITTVAA
660 670 680 690 700
EAPVLPLSTE PPAAPATSAY TCFRCLECKE QCRDKAGMAA HFQQLGPPAP
710 720 730 740 750
GATSNVCPTC PMMLPNRCSF SAHQRMHKNR PPHVCPECGG NFLQANFQTH
760 770 780 790 800
LREACLHVSR RVGYRCPSCS VVFGGVNSIK SHIQTSHCEV FHKCPICPMA
810 820 830 840 850
FKSGPSAHAH LYSQHPSFQT QQAKLIYKCA MCDTVFTHKP LLSSHFDQHL
860 870 880 890 900
LPQRVSVFKC PSCPLLFAQK RTMLEHLKNT HQSGRLEETA GKGAGGALLT
910 920 930 940 950
PKTEPEELAV SQGGAAPATE ESSSSSEEEE VPSSPEPPRP AKRPRRELGS
960 970 980 990 1000
KGLKGGGGGP GGWTCGLCHS WFPERDEYVA HMKKEHGKSV KKFPCRLCER
1010 1020 1030 1040 1050
SFCSAPSLRR HVRVNHEGIK RVYPCRYCTE GKRTFSSRLI LEKHVQVRHG
1060 1070 1080 1090 1100
LQLGAQSPGR GTTLARGSSA RAQGPGRKRR QSSDSCSEEP DSTTPPAKSP
1110 1120 1130 1140 1150
RGGPGSGGHG PLRYRSSSST EQSLMMGLRV EDGAQQCLDC GLCFASPGSL
1160 1170 1180 1190 1200
SRHRFISHKK RRGVGKASAL GLGDGEEEAP PSRSDPDGGD SPLPASGGPL
1210 1220 1230
TCKVCGKSCD SPLNLKTHFR THGMAFIRAR QGAVGDN
Length:1,237
Mass (Da):129,529
Last modified:October 1, 2002 - v1
Checksum:iD2DC99AA2AF44270
GO
Isoform 2 (identifier: Q8N1G0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1027-1103: YCTEGKRTFS...TPPAKSPRGG → SKGPGLRAVP...GARSETPPVF
     1104-1237: Missing.

Note: No experimental confirmation available.
Show »
Length:1,103
Mass (Da):115,571
Checksum:i3FDC8E46C8F47A9D
GO

Sequence cautioni

The sequence BAA92679.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14406.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAH18162.1 differs from that shown. Reason: Frameshift at position 1062. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3311R → W in CAH18162 (PubMed:17974005).Curated
Sequence conflicti439 – 4391K → E in BAB14406 (PubMed:14702039).Curated
Sequence conflicti515 – 5151R → G in BAB14406 (PubMed:14702039).Curated
Sequence conflicti639 – 6391A → V in CAH18162 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti259 – 2591G → E.
Corresponds to variant rs3748545 [ dbSNP | Ensembl ].
VAR_052894
Natural varianti344 – 3441R → T.
Corresponds to variant rs12045766 [ dbSNP | Ensembl ].
VAR_052895

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1027 – 110377YCTEG…SPRGG → SKGPGLRAVPLLPSCPLPFQ VLHRGKTHLQQPPDPRETCP GPARLAAWGPVPWPGDHLGS GFQCQSPGARSETPPVF in isoform 2. 1 PublicationVSP_018168Add
BLAST
Alternative sequencei1104 – 1237134Missing in isoform 2. 1 PublicationVSP_018169Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037862 mRNA. Translation: BAA92679.1. Different initiation.
CR749307 mRNA. Translation: CAH18162.1. Frameshift.
AL391069 Genomic DNA. Translation: CAH70322.1.
CH471121 Genomic DNA. Translation: EAW53452.1.
CH471121 Genomic DNA. Translation: EAW53453.1.
CH471121 Genomic DNA. Translation: EAW53454.1.
BC032463 mRNA. Translation: AAH32463.1.
AK023105 mRNA. Translation: BAB14406.1. Different initiation.
CCDSiCCDS992.1. [Q8N1G0-1]
RefSeqiNP_001291692.1. NM_001304763.1. [Q8N1G0-1]
NP_001291693.1. NM_001304764.1. [Q8N1G0-1]
NP_065883.1. NM_020832.2. [Q8N1G0-1]
XP_011508114.1. XM_011509812.1. [Q8N1G0-1]
XP_011508115.1. XM_011509813.1. [Q8N1G0-1]
UniGeneiHs.186756.
Hs.225083.

Genome annotation databases

EnsembliENST00000324048; ENSP00000319829; ENSG00000143373. [Q8N1G0-1]
ENST00000336715; ENSP00000336620; ENSG00000143373. [Q8N1G0-1]
GeneIDi57592.
KEGGihsa:57592.
UCSCiuc001exq.4. human. [Q8N1G0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037862 mRNA. Translation: BAA92679.1. Different initiation.
CR749307 mRNA. Translation: CAH18162.1. Frameshift.
AL391069 Genomic DNA. Translation: CAH70322.1.
CH471121 Genomic DNA. Translation: EAW53452.1.
CH471121 Genomic DNA. Translation: EAW53453.1.
CH471121 Genomic DNA. Translation: EAW53454.1.
BC032463 mRNA. Translation: AAH32463.1.
AK023105 mRNA. Translation: BAB14406.1. Different initiation.
CCDSiCCDS992.1. [Q8N1G0-1]
RefSeqiNP_001291692.1. NM_001304763.1. [Q8N1G0-1]
NP_001291693.1. NM_001304764.1. [Q8N1G0-1]
NP_065883.1. NM_020832.2. [Q8N1G0-1]
XP_011508114.1. XM_011509812.1. [Q8N1G0-1]
XP_011508115.1. XM_011509813.1. [Q8N1G0-1]
UniGeneiHs.186756.
Hs.225083.

3D structure databases

ProteinModelPortaliQ8N1G0.
SMRiQ8N1G0. Positions 524-586, 673-876, 954-1057, 1128-1154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121643. 39 interactions.
IntActiQ8N1G0. 23 interactions.
STRINGi9606.ENSP00000319829.

PTM databases

iPTMnetiQ8N1G0.
PhosphoSiteiQ8N1G0.

Polymorphism and mutation databases

BioMutaiZNF687.
DMDMi74759771.

Proteomic databases

EPDiQ8N1G0.
MaxQBiQ8N1G0.
PaxDbiQ8N1G0.
PRIDEiQ8N1G0.

Protocols and materials databases

DNASUi57592.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324048; ENSP00000319829; ENSG00000143373. [Q8N1G0-1]
ENST00000336715; ENSP00000336620; ENSG00000143373. [Q8N1G0-1]
GeneIDi57592.
KEGGihsa:57592.
UCSCiuc001exq.4. human. [Q8N1G0-1]

Organism-specific databases

CTDi57592.
GeneCardsiZNF687.
HGNCiHGNC:29277. ZNF687.
HPAiHPA021193.
HPA053052.
MIMi610568. gene.
neXtProtiNX_Q8N1G0.
PharmGKBiPA142670486.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00530000063261.
HOGENOMiHOG000010306.
HOVERGENiHBG062228.
InParanoidiQ8N1G0.
OMAiFKQSPGH.
OrthoDBiEOG7H1JKM.
PhylomeDBiQ8N1G0.
TreeFamiTF329009.

Miscellaneous databases

ChiTaRSiZNF687. human.
GeneWikiiZNF687.
GenomeRNAii57592.
PROiQ8N1G0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N1G0.
CleanExiHS_ZNF687.
ExpressionAtlasiQ8N1G0. baseline and differential.
GenevisibleiQ8N1G0. HS.

Family and domain databases

InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF16622. zf-C2H2_11. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 14 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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] (ISOFORM 1).
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "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 399-1237 (ISOFORM 2).
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-253; SER-266; SER-271; SER-433; SER-1082; SER-1083; SER-1085; SER-1191 AND SER-1211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-129; THR-148 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-253; SER-266; SER-1057; SER-1106 AND SER-1118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-140; SER-251; SER-253; SER-374; SER-433 AND SER-1057, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-253; SER-1057 AND SER-1191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285 AND LYS-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285 AND LYS-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285 AND LYS-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZN687_HUMAN
AccessioniPrimary (citable) accession number: Q8N1G0
Secondary accession number(s): D3DV17
, Q68DQ8, Q9H937, Q9P2A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 132 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.