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Q9H582

- ZN644_HUMAN

UniProt

Q9H582 - ZN644_HUMAN

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Protein

Zinc finger protein 644

Gene

ZNF644

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

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri410 – 43223C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri448 – 47023C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri496 – 51823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri525 – 54824C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri586 – 60924C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 98725C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1038 – 106023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
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 644
Alternative name(s):
Zinc finger motif enhancer-binding protein 2
Short name:
Zep-2
Gene namesi
Name:ZNF644
Synonyms:KIAA1221, ZEP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29222. ZNF644.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Myopia 21, autosomal dominant (MYP21) [MIM:614167]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti587 – 5871I → V in MYP21. 1 Publication
Corresponds to variant rs146936371 [ dbSNP | Ensembl ].
VAR_066389
Natural varianti672 – 6721S → G in MYP21. 1 Publication
VAR_066390
Natural varianti680 – 6801R → G in MYP21. 1 Publication
VAR_066391
Natural varianti699 – 6991C → Y in MYP21. 1 Publication
VAR_066392

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614167. phenotype.
PharmGKBiPA134984168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13271327Zinc finger protein 644PRO_0000047698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei1000 – 10001Phosphoserine4 Publications
Modified residuei1189 – 11891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H582.
PaxDbiQ9H582.
PRIDEiQ9H582.

PTM databases

PhosphoSiteiQ9H582.

Expressioni

Tissue specificityi

Expressed in liver, placenta, retina and retinal pigment epithelium.1 Publication

Gene expression databases

BgeeiQ9H582.
CleanExiHS_ZNF644.
ExpressionAtlasiQ9H582. baseline and differential.
GenevestigatoriQ9H582.

Organism-specific databases

HPAiHPA057795.

Interactioni

Protein-protein interaction databases

BioGridi123913. 11 interactions.
IntActiQ9H582. 2 interactions.
MINTiMINT-4658204.
STRINGi9606.ENSP00000337008.

Structurei

3D structure databases

ProteinModelPortaliQ9H582.
SMRiQ9H582. Positions 398-434, 443-472, 488-551, 580-615.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri410 – 43223C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri448 – 47023C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri496 – 51823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri525 – 54824C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri586 – 60924C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri963 – 98725C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1038 – 106023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG262560.
GeneTreeiENSGT00530000063587.
HOVERGENiHBG058603.
InParanoidiQ9H582.
OMAiECNFMAV.
OrthoDBiEOG747PH4.
PhylomeDBiQ9H582.
TreeFamiTF333705.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 8 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H582-1) [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
MRSFLQQDVN KTKSRLNVLN GLANNMDDLK INTDITGAKE ELLDDNNFIS
60 70 80 90 100
DKESGVHKPK DCQTSFQKNN TLTLPEELSK DKSENALSGG QSSLFIHAGA
110 120 130 140 150
PTVSSENFIL PKGAAVNGPV SHSSLTKTSN MNKGSVSLTT GQPVDQPTTE
160 170 180 190 200
SCSTLKVAAD LQLSTPQKAS QHQVLFLLSD VAHAKNPTHS NKKLPTSASV
210 220 230 240 250
GCDIQNSVGS NIKSDGTLIN QVEVGEDGED LLVKDDCVNT VTGISSGTDG
260 270 280 290 300
FRSENDTNWD PQKEFIQFLM TNEETVDKAP PHSKIGLEKK RKRKMDVSKI
310 320 330 340 350
TRYTEDCFSD SNCVPNKSKM QEVDFLEQNE ELQAVDSQKY ALSKVKPEST
360 370 380 390 400
DEDLESVDAF QHLIYNPDKC GEESSPVHTS TFLSNTLKKK CEESDSESPA
410 420 430 440 450
TFSTEEPSFY PCTKCNVNFR EKKHLHRHMM YHLDGNSHFR HLNVPRPYAC
460 470 480 490 500
RECGRTFRDR NSLLKHMIIH QERRQKLMEE IRELKELQDE GRSARLQCPQ
510 520 530 540 550
CVFGTNCPKT FVQHAKTHEK DKRYYCCEEC NFMAVTENEL ECHRGIAHGA
560 570 580 590 600
VVKCPMVTSD IAQRKTQKKT FMKDSVVGSS KKSATYICKM CPFTTSAKSV
610 620 630 640 650
LKKHTEYLHS SSCVDSFGSP LGLDKRKNDI LEEPVDSDST KTLTKQQSTT
660 670 680 690 700
FPKNSALKQD VKRTFGSTSQ SSSFSKIHKR PHRIQKARKS IAQSGVNMCN
710 720 730 740 750
QNSSPHKNVT IKSSVDQKPK YFHQAAKEKS NAKANSHYLY RHKYENYRMI
760 770 780 790 800
KKSGESYPVH FKKEEASSLN SLHLFSSSSN SHNNFISDPH KPDAKRPESF
810 820 830 840 850
KDHRRVAVKR VIKESKKESS VGGEDLDSYP DFLHKMTVVV LQKLNSAEKK
860 870 880 890 900
DSYETEDESS WDNVELGDYT TQAIEDETYS DINQEHVNLF PLFKSKVEGQ
910 920 930 940 950
EPGENATLSY DQNDGFYFEY YEDTGSNNFL HEIHDPQHLE TADASLSKHS
960 970 980 990 1000
SVFHWTDLSL EKKSCPYCPA TFETGVGLSN HVRGHLHRAG LSYEARHVVS
1010 1020 1030 1040 1050
PEQIATSDKM QHFKRTGTGT PVKRVRKAIE KSETTSEHTC QLCGGWFDTK
1060 1070 1080 1090 1100
IGLSNHVRGH LKRLGKTKWD AHKSPICVLN EMMQNEEKYE KILKALNSRR
1110 1120 1130 1140 1150
IIPRPFVAQK LASSDDFISQ NVIPLEAYRN GLKTEALSVS ASEEEGLNFL
1160 1170 1180 1190 1200
NEYDETKPEL PSGKKNQSLT LIELLKNKRM GEERNSAISP QKIHNQTARK
1210 1220 1230 1240 1250
RFVQKCVLPL NEDSPLMYQP QKMDLTMHSA LDCKQKKSRS RSGSKKKMLT
1260 1270 1280 1290 1300
LPHGADEVYI LRCRFCGLVF RGPLSVQEDW IKHLQRHIVN ANLPRTGAGM
1310 1320
VEVTSLLKKP ASITETSFSL LMAEAAS
Length:1,327
Mass (Da):149,565
Last modified:December 7, 2004 - v2
Checksum:i53CE36BE21FC5056
GO
Isoform 2 (identifier: Q9H582-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1230-1232: ALD → GLI
     1233-1327: Missing.

Show »
Length:1,232
Mass (Da):139,012
Checksum:i50D719F07AF12CBA
GO
Isoform 3 (identifier: Q9H582-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1222: Missing.
     1223-1229: MDLTMHS → MLIRQNL

Show »
Length:105
Mass (Da):11,724
Checksum:i237D95A0CC5CAD1D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti296 – 2961D → M in BAD32777. 1 PublicationCurated
Sequence conflicti1125 – 11251L → P in BAD32777. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035593
Natural varianti556 – 5561M → V.
Corresponds to variant rs17131242 [ dbSNP | Ensembl ].
VAR_052885
Natural varianti587 – 5871I → V in MYP21. 1 Publication
Corresponds to variant rs146936371 [ dbSNP | Ensembl ].
VAR_066389
Natural varianti672 – 6721S → G in MYP21. 1 Publication
VAR_066390
Natural varianti680 – 6801R → G in MYP21. 1 Publication
VAR_066391
Natural varianti699 – 6991C → Y in MYP21. 1 Publication
VAR_066392
Natural varianti794 – 7941A → V.
Corresponds to variant rs10922938 [ dbSNP | Ensembl ].
VAR_052886

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 12221222Missing in isoform 3. 2 PublicationsVSP_015855Add
BLAST
Alternative sequencei1223 – 12297MDLTMHS → MLIRQNL in isoform 3. 2 PublicationsVSP_015856
Alternative sequencei1230 – 12323ALD → GLI in isoform 2. 1 PublicationVSP_012158
Alternative sequencei1233 – 132795Missing in isoform 2. 1 PublicationVSP_012159Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019255 mRNA. Translation: BAD32777.1.
AK291520 mRNA. Translation: BAF84209.1.
AL136109 Genomic DNA. Translation: CAI23362.1.
AL136109 Genomic DNA. Translation: CAI23363.1.
CH471097 Genomic DNA. Translation: EAW73118.1.
BC050656 mRNA. Translation: AAH50656.1.
BC063683 mRNA. Translation: AAH63683.2.
BC110841 mRNA. Translation: AAI10842.1.
BC132776 mRNA. Translation: AAI32777.1.
BC132778 mRNA. Translation: AAI32779.1.
AB033047 mRNA. Translation: BAA86535.1.
CCDSiCCDS731.1. [Q9H582-1]
CCDS732.1. [Q9H582-3]
RefSeqiNP_057704.2. NM_016620.3. [Q9H582-3]
NP_115562.3. NM_032186.4. [Q9H582-3]
NP_958357.1. NM_201269.2. [Q9H582-1]
XP_005271318.1. XM_005271261.2. [Q9H582-1]
XP_006711010.1. XM_006710947.1. [Q9H582-3]
XP_006711011.1. XM_006710948.1. [Q9H582-3]
UniGeneiHs.173001.
Hs.745048.

Genome annotation databases

EnsembliENST00000337393; ENSP00000337008; ENSG00000122482. [Q9H582-1]
ENST00000347275; ENSP00000340828; ENSG00000122482. [Q9H582-3]
ENST00000361321; ENSP00000354659; ENSG00000122482. [Q9H582-3]
ENST00000370440; ENSP00000359469; ENSG00000122482. [Q9H582-1]
GeneIDi84146.
KEGGihsa:84146.
UCSCiuc001dnv.3. human. [Q9H582-3]
uc001dnw.3. human. [Q9H582-1]

Polymorphism databases

DMDMi56404958.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019255 mRNA. Translation: BAD32777.1 .
AK291520 mRNA. Translation: BAF84209.1 .
AL136109 Genomic DNA. Translation: CAI23362.1 .
AL136109 Genomic DNA. Translation: CAI23363.1 .
CH471097 Genomic DNA. Translation: EAW73118.1 .
BC050656 mRNA. Translation: AAH50656.1 .
BC063683 mRNA. Translation: AAH63683.2 .
BC110841 mRNA. Translation: AAI10842.1 .
BC132776 mRNA. Translation: AAI32777.1 .
BC132778 mRNA. Translation: AAI32779.1 .
AB033047 mRNA. Translation: BAA86535.1 .
CCDSi CCDS731.1. [Q9H582-1 ]
CCDS732.1. [Q9H582-3 ]
RefSeqi NP_057704.2. NM_016620.3. [Q9H582-3 ]
NP_115562.3. NM_032186.4. [Q9H582-3 ]
NP_958357.1. NM_201269.2. [Q9H582-1 ]
XP_005271318.1. XM_005271261.2. [Q9H582-1 ]
XP_006711010.1. XM_006710947.1. [Q9H582-3 ]
XP_006711011.1. XM_006710948.1. [Q9H582-3 ]
UniGenei Hs.173001.
Hs.745048.

3D structure databases

ProteinModelPortali Q9H582.
SMRi Q9H582. Positions 398-434, 443-472, 488-551, 580-615.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123913. 11 interactions.
IntActi Q9H582. 2 interactions.
MINTi MINT-4658204.
STRINGi 9606.ENSP00000337008.

PTM databases

PhosphoSitei Q9H582.

Polymorphism databases

DMDMi 56404958.

Proteomic databases

MaxQBi Q9H582.
PaxDbi Q9H582.
PRIDEi Q9H582.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337393 ; ENSP00000337008 ; ENSG00000122482 . [Q9H582-1 ]
ENST00000347275 ; ENSP00000340828 ; ENSG00000122482 . [Q9H582-3 ]
ENST00000361321 ; ENSP00000354659 ; ENSG00000122482 . [Q9H582-3 ]
ENST00000370440 ; ENSP00000359469 ; ENSG00000122482 . [Q9H582-1 ]
GeneIDi 84146.
KEGGi hsa:84146.
UCSCi uc001dnv.3. human. [Q9H582-3 ]
uc001dnw.3. human. [Q9H582-1 ]

Organism-specific databases

CTDi 84146.
GeneCardsi GC01M091380.
HGNCi HGNC:29222. ZNF644.
HPAi HPA057795.
MIMi 614159. gene.
614167. phenotype.
neXtProti NX_Q9H582.
PharmGKBi PA134984168.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262560.
GeneTreei ENSGT00530000063587.
HOVERGENi HBG058603.
InParanoidi Q9H582.
OMAi ECNFMAV.
OrthoDBi EOG747PH4.
PhylomeDBi Q9H582.
TreeFami TF333705.

Miscellaneous databases

ChiTaRSi ZNF644. human.
GeneWikii ZNF644.
GenomeRNAii 84146.
NextBioi 73468.
PROi Q9H582.
SOURCEi Search...

Gene expression databases

Bgeei Q9H582.
CleanExi HS_ZNF644.
ExpressionAtlasi Q9H582. baseline and differential.
Genevestigatori Q9H582.

Family and domain databases

Gene3Di 3.30.160.60. 1 hit.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 8 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Zep-2: zinc finger motif enhancer binding protein-2."
    Fukamizu A.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  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).
    Tissue: Pericardium.
  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] (ISOFORMS 1 AND 3).
    Tissue: Duodenum, Eye and Skin.
  6. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-1327 (ISOFORM 1).
    Tissue: Brain.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-1000 AND SER-1189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-53.
  12. Cited for: VARIANTS MYP21 VAL-587; GLY-672; GLY-680 AND TYR-699, TISSUE SPECIFICITY.

Entry informationi

Entry nameiZN644_HUMAN
AccessioniPrimary (citable) accession number: Q9H582
Secondary accession number(s): A2RU71
, Q2TAM0, Q5TCC0, Q6BEP7, Q6P446, Q6PI06, Q7LG67, Q9ULJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: November 26, 2014
This is version 115 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 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

External Data

Dasty 3