Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc finger protein 185

Gene

ZNF185

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

Functioni

May be involved in the regulation of cellular proliferation and/or differentiation.

GO - Molecular functioni

  • zinc ion binding Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 185
Alternative name(s):
LIM domain protein ZNF185
P1-A
Gene namesi
Name:ZNF185
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12976. ZNF185.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • Cell junctionfocal adhesion 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37558.

Polymorphism and mutation databases

BioMutaiZNF185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 689689Zinc finger protein 185PRO_0000075911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei153 – 1531PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO15231.
MaxQBiO15231.
PRIDEiO15231.

PTM databases

iPTMnetiO15231.

Expressioni

Tissue specificityi

Expressed in placenta, pancreas and kidney. Also expressed in prostate, testis, ovary and blood.

Gene expression databases

BgeeiO15231.
CleanExiHS_ZNF185.
ExpressionAtlasiO15231. baseline and differential.
GenevisibleiO15231. HS.

Organism-specific databases

HPAiHPA000400.
HPA016438.

Interactioni

Protein-protein interaction databases

BioGridi113525. 2 interactions.
IntActiO15231. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO15231.
SMRiO15231. Positions 627-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini627 – 68963LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi159 – 1657Poly-Glu

Sequence similaritiesi

Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain

Phylogenomic databases

GeneTreeiENSGT00530000063872.
HOGENOMiHOG000232182.
HOVERGENiHBG071794.
InParanoidiO15231.
OMAiEQPHVYI.
OrthoDBiEOG72C52Z.
PhylomeDBiO15231.
TreeFamiTF335114.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR001781. Znf_LIM.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15231-1) [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
MSISALGGRT KGKPLPPGEE ERNNVLKQMK VRTTLKGDKS WITKQDESEG
60 70 80 90 100
RTIELPSGRS RATSFSSAGE VPKPRPPSTR APTGYIIRGV FTKPIDSSSQ
110 120 130 140 150
PQQQFPKANG TPKSAASLVR TANAGPPRPS SSGYKMTTED YKKLAPYNIR
160 170 180 190 200
RSSTSGDTEE EEEEEVVPFS SDEQKRRSEA ASGVLRRTAP REHSYVLSAA
210 220 230 240 250
KKSTGPTQET QAPFIAKRVE VVEEDGPSEK SQDPPALARS TPGSNSADGG
260 270 280 290 300
RTKASRAIWI ECLPSMPSPA GSQELSSRGE EIVRLQILTP RAGLRLVAPD
310 320 330 340 350
VEGMRSSPGN KDKEAPCSRE LQRDLAGEEA FRAPNTDAAR SSAQLSDGNV
360 370 380 390 400
GSGATGSRPE GLAAVDIGSE RGSSSATSVS AVPADRKSNS TAAQEDAKAD
410 420 430 440 450
PKGALADYEG KDVATRVGEA WQERPGAPRG GQGDPAVPAQ QPADPSTPER
460 470 480 490 500
QSSPSGSEQL VRRESCGSSV LTDFEGKDVA TKVGEAWQDR PGAPRGGQGD
510 520 530 540 550
PAVPTQQPAD PSTPEQQNSP SGSEQFVRRE SCTSRVRSPS SCMVTVTVTA
560 570 580 590 600
TSEQPHIYIP APASELDSSS TTKGILFVKE YVNASEVSSG KPVSARYSNV
610 620 630 640 650
SSIEDSFAME KKPPCGSTPY SERTTGGICT YCNREIRDCP KITLEHLGIC
660 670 680
CHEYCFKCGI CSKPMGDLLD QIFIHRDTIH CGKCYEKLF
Length:689
Mass (Da):73,525
Last modified:October 5, 2010 - v3
Checksum:i0CCA739701FE1423
GO
Isoform 2 (identifier: O15231-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: Missing.
     141-144: YKKL → MQRQ
     205-205: G → GS
     246-275: Missing.
     305-372: Missing.

Note: No experimental confirmation available.
Show »
Length:452
Mass (Da):48,621
Checksum:i9B4871D31EEEE57C
GO
Isoform 3 (identifier: O15231-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-205: G → GS

Show »
Length:690
Mass (Da):73,613
Checksum:i7E7AFDCFF902FE68
GO
Isoform 4 (identifier: O15231-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-304: Missing.

Show »
Length:630
Mass (Da):67,281
Checksum:i63CC539EF52C25A5
GO
Isoform 5 (identifier: O15231-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.
     177-205: RSEAASGVLRRTAPREHSYVLSAAKKSTG → SS
     246-304: Missing.

Note: No experimental confirmation available.
Show »
Length:468
Mass (Da):49,972
Checksum:i530D1C7F62C34557
GO
Isoform 6 (identifier: O15231-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     372-372: G → GRLCAAASFASFLEDQDGHSANSQSCKPRPAAI

Show »
Length:721
Mass (Da):76,857
Checksum:i177A88C27289F3A6
GO
Isoform 7 (identifier: O15231-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     276-304: Missing.

Show »
Length:660
Mass (Da):70,380
Checksum:i373470CD29FE5785
GO
Isoform 8 (identifier: O15231-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     276-304: Missing.
     372-372: G → GRLCAAASFASFLEDQDGHSANSQSCKPRPAAI

Show »
Length:692
Mass (Da):73,711
Checksum:i38B94FB3CEF11C3E
GO
Isoform 9 (identifier: O15231-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-403: MSISALGGRT...QEDAKADPKG → MAARDELGLG...PEELAAPSPA

Note: No experimental confirmation available.
Show »
Length:327
Mass (Da):34,954
Checksum:iCCAF1D825E0F9C1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131K → E in ABF57661 (PubMed:16799630).Curated
Sequence conflicti132 – 1321S → F in ABF57661 (PubMed:16799630).Curated
Sequence conflicti150 – 1501R → G in ABF57661 (PubMed:16799630).Curated
Sequence conflicti236 – 2361A → V in BAH13507 (PubMed:14702039).Curated
Sequence conflicti257 – 2571A → T in ABF57661 (PubMed:16799630).Curated
Sequence conflicti326 – 3261A → S in BAH13507 (PubMed:14702039).Curated
Sequence conflicti406 – 4061A → D in ABF57661 (PubMed:16799630).Curated
Sequence conflicti408 – 4081Y → C in CAA70733 (PubMed:9268636).Curated
Sequence conflicti414 – 4141A → P in ABF57657 (PubMed:16799630).Curated
Sequence conflicti414 – 4141A → P in AAY54245 (PubMed:16799630).Curated
Sequence conflicti414 – 4141A → P in CAA70733 (PubMed:9268636).Curated
Sequence conflicti488 – 4881Q → H in ABF57660 (PubMed:16799630).Curated
Sequence conflicti492 – 4921G → R in CAA70733 (PubMed:9268636).Curated
Sequence conflicti517 – 5171Q → R in BAC04511 (PubMed:14702039).Curated
Sequence conflicti621 – 6211S → F in ABF57657 (PubMed:16799630).Curated
Sequence conflicti621 – 6211S → F in AAY54245 (PubMed:16799630).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 403403MSISA…ADPKG → MAARDELGLGGDSLEAMPVP AARGRPRITNGPEELAAPSP A in isoform 9. 1 PublicationVSP_054773Add
BLAST
Alternative sequencei1 – 140140Missing in isoform 2. 1 PublicationVSP_039898Add
BLAST
Alternative sequencei1 – 135135Missing in isoform 5. 1 PublicationVSP_045080Add
BLAST
Alternative sequencei141 – 1444YKKL → MQRQ in isoform 2. 1 PublicationVSP_039899
Alternative sequencei177 – 20529RSEAA…KKSTG → SS in isoform 5. 1 PublicationVSP_045081Add
BLAST
Alternative sequencei205 – 2051G → GS in isoform 2 and isoform 3. 2 PublicationsVSP_039900
Alternative sequencei246 – 30459Missing in isoform 4 and isoform 5. 2 PublicationsVSP_043405Add
BLAST
Alternative sequencei246 – 27530Missing in isoform 2. 1 PublicationVSP_039901Add
BLAST
Alternative sequencei276 – 30429Missing in isoform 7 and isoform 8. 1 PublicationVSP_047205Add
BLAST
Alternative sequencei305 – 37268Missing in isoform 2. 1 PublicationVSP_039902Add
BLAST
Alternative sequencei372 – 3721G → GRLCAAASFASFLEDQDGHS ANSQSCKPRPAAI in isoform 6 and isoform 8. 1 PublicationVSP_047206

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK095258 mRNA. Translation: BAC04511.1.
AY997296 mRNA. Translation: AAY54245.1.
DQ508022 mRNA. Translation: ABF57657.1.
DQ508023 mRNA. Translation: ABF57658.1.
DQ508024 mRNA. Translation: ABF57659.1.
DQ508025 mRNA. Translation: ABF57660.1.
DQ508026 mRNA. Translation: ABF57661.1.
Y09538 mRNA. Translation: CAA70733.1.
AK296967 mRNA. Translation: BAG59511.1.
AK301530 mRNA. Translation: BAH13507.1.
U82671 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72895.1.
CCDSiCCDS48184.1. [O15231-1]
CCDS55528.1. [O15231-3]
CCDS55529.1. [O15231-6]
CCDS55530.1. [O15231-8]
CCDS55531.1. [O15231-4]
CCDS55532.1. [O15231-5]
CCDS69832.1. [O15231-9]
RefSeqiNP_001171577.1. NM_001178106.1. [O15231-6]
NP_001171578.1. NM_001178107.1. [O15231-8]
NP_001171579.1. NM_001178108.1. [O15231-3]
NP_001171580.1. NM_001178109.1. [O15231-7]
NP_001171581.1. NM_001178110.1. [O15231-4]
NP_001171584.1. NM_001178113.1. [O15231-5]
NP_001171586.1. NM_001178115.1. [O15231-9]
NP_009081.2. NM_007150.3. [O15231-1]
XP_005274788.1. XM_005274731.2. [O15231-6]
XP_005274792.1. XM_005274735.2. [O15231-8]
XP_005274794.1. XM_005274737.2. [O15231-3]
XP_005274795.1. XM_005274738.2. [O15231-1]
XP_005274798.1. XM_005274741.2. [O15231-7]
XP_005274802.1. XM_005274745.2. [O15231-4]
UniGeneiHs.16622.

Genome annotation databases

EnsembliENST00000318504; ENSP00000312782; ENSG00000147394. [O15231-4]
ENST00000318529; ENSP00000313919; ENSG00000147394. [O15231-5]
ENST00000324823; ENSP00000325307; ENSG00000147394. [O15231-2]
ENST00000370268; ENSP00000359291; ENSG00000147394. [O15231-1]
ENST00000370270; ENSP00000359293; ENSG00000147394. [O15231-6]
ENST00000449285; ENSP00000395228; ENSG00000147394. [O15231-3]
ENST00000454925; ENSP00000392984; ENSG00000147394. [O15231-9]
ENST00000535861; ENSP00000440847; ENSG00000147394. [O15231-6]
ENST00000539731; ENSP00000444367; ENSG00000147394. [O15231-8]
GeneIDi7739.
KEGGihsa:7739.
UCSCiuc004fgw.5. human. [O15231-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK095258 mRNA. Translation: BAC04511.1.
AY997296 mRNA. Translation: AAY54245.1.
DQ508022 mRNA. Translation: ABF57657.1.
DQ508023 mRNA. Translation: ABF57658.1.
DQ508024 mRNA. Translation: ABF57659.1.
DQ508025 mRNA. Translation: ABF57660.1.
DQ508026 mRNA. Translation: ABF57661.1.
Y09538 mRNA. Translation: CAA70733.1.
AK296967 mRNA. Translation: BAG59511.1.
AK301530 mRNA. Translation: BAH13507.1.
U82671 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72895.1.
CCDSiCCDS48184.1. [O15231-1]
CCDS55528.1. [O15231-3]
CCDS55529.1. [O15231-6]
CCDS55530.1. [O15231-8]
CCDS55531.1. [O15231-4]
CCDS55532.1. [O15231-5]
CCDS69832.1. [O15231-9]
RefSeqiNP_001171577.1. NM_001178106.1. [O15231-6]
NP_001171578.1. NM_001178107.1. [O15231-8]
NP_001171579.1. NM_001178108.1. [O15231-3]
NP_001171580.1. NM_001178109.1. [O15231-7]
NP_001171581.1. NM_001178110.1. [O15231-4]
NP_001171584.1. NM_001178113.1. [O15231-5]
NP_001171586.1. NM_001178115.1. [O15231-9]
NP_009081.2. NM_007150.3. [O15231-1]
XP_005274788.1. XM_005274731.2. [O15231-6]
XP_005274792.1. XM_005274735.2. [O15231-8]
XP_005274794.1. XM_005274737.2. [O15231-3]
XP_005274795.1. XM_005274738.2. [O15231-1]
XP_005274798.1. XM_005274741.2. [O15231-7]
XP_005274802.1. XM_005274745.2. [O15231-4]
UniGeneiHs.16622.

3D structure databases

ProteinModelPortaliO15231.
SMRiO15231. Positions 627-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113525. 2 interactions.
IntActiO15231. 1 interaction.

PTM databases

iPTMnetiO15231.

Polymorphism and mutation databases

BioMutaiZNF185.

Proteomic databases

EPDiO15231.
MaxQBiO15231.
PRIDEiO15231.

Protocols and materials databases

DNASUi7739.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318504; ENSP00000312782; ENSG00000147394. [O15231-4]
ENST00000318529; ENSP00000313919; ENSG00000147394. [O15231-5]
ENST00000324823; ENSP00000325307; ENSG00000147394. [O15231-2]
ENST00000370268; ENSP00000359291; ENSG00000147394. [O15231-1]
ENST00000370270; ENSP00000359293; ENSG00000147394. [O15231-6]
ENST00000449285; ENSP00000395228; ENSG00000147394. [O15231-3]
ENST00000454925; ENSP00000392984; ENSG00000147394. [O15231-9]
ENST00000535861; ENSP00000440847; ENSG00000147394. [O15231-6]
ENST00000539731; ENSP00000444367; ENSG00000147394. [O15231-8]
GeneIDi7739.
KEGGihsa:7739.
UCSCiuc004fgw.5. human. [O15231-1]

Organism-specific databases

CTDi7739.
GeneCardsiZNF185.
HGNCiHGNC:12976. ZNF185.
HPAiHPA000400.
HPA016438.
MIMi300381. gene.
neXtProtiNX_O15231.
PharmGKBiPA37558.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063872.
HOGENOMiHOG000232182.
HOVERGENiHBG071794.
InParanoidiO15231.
OMAiEQPHVYI.
OrthoDBiEOG72C52Z.
PhylomeDBiO15231.
TreeFamiTF335114.

Miscellaneous databases

ChiTaRSiZNF185. human.
GenomeRNAii7739.
PROiO15231.
SOURCEiSearch...

Gene expression databases

BgeeiO15231.
CleanExiHS_ZNF185.
ExpressionAtlasiO15231. baseline and differential.
GenevisibleiO15231. HS.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR001781. Znf_LIM.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure of a novel LIM domain gene (ZNF185) in Xq28 and comparisons with the orthologous murine transcript."
    Heiss N.S., Gloeckner G., Baechner D., Kioschis P., Klauck S.M., Hinzmann B., Rosenthal A., Herman G.E., Poustka A.
    Genomics 43:329-338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Blood.
  2. "ZNF185, an actin-cytoskeleton-associated growth inhibitory LIM protein in prostate cancer."
    Zhang J.S., Gong A., Young C.Y.
    Oncogene 26:111-122(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4; 6; 7 AND 8), SUBCELLULAR LOCATION.
  3. "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] (ISOFORMS 3; 5 AND 9).
    Tissue: Synovium and Tongue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. "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].
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiZN185_HUMAN
AccessioniPrimary (citable) accession number: O15231
Secondary accession number(s): A4FTV3
, A6NME5, B4DLE9, B7Z771, B8K2L9, B8K2M0, B8K2M1, B8K2M2, E9PFR6, F5GXF7, F5GZL4, F8W8V7, H0Y4M8, O00345, Q8N1R8, Q9NSD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 5, 2010
Last modified: June 8, 2016
This is version 136 of the entry and version 3 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.