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Protein

E3 ubiquitin-protein ligase ZNF645

Gene

ZNF645

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

Functioni

E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. May operate on tyrosine-phosphorylated SRC substrates.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 9741RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri112 – 13827C2H2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase ZNF645 (EC:6.3.2.-)
Alternative name(s):
Zinc finger protein 645
Gene namesi
Name:ZNF645
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:26371. ZNF645.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Localized over the postacrosomal perinuclear theca region and the entire length of sperm tail.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134934025.

Polymorphism and mutation databases

BioMutaiZNF645.
DMDMi74759980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425E3 ubiquitin-protein ligase ZNF645PRO_0000056316Add
BLAST

Proteomic databases

PaxDbiQ8N7E2.
PRIDEiQ8N7E2.

PTM databases

iPTMnetiQ8N7E2.
PhosphoSiteiQ8N7E2.

Expressioni

Tissue specificityi

Exclusively expressed in testis and sperm, including spermatocytes, round and elongated spermatids, and Leydig cells.1 Publication

Gene expression databases

BgeeiQ8N7E2.
CleanExiHS_ZNF645.
GenevisibleiQ8N7E2. HS.

Organism-specific databases

HPAiHPA005845.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi127688. 6 interactions.
STRINGi9606.ENSP00000323348.

Structurei

3D structure databases

ProteinModelPortaliQ8N7E2.
SMRiQ8N7E2. Positions 54-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 15459HYB domainAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi254 – 34390Pro-richAdd
BLAST

Domaini

The HYB domain forms a phosphotyrosine-binding pocket upon dimerization, and mediates as well the recognition of its flanking acidic amino acids.By similarity

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri57 – 9741RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri112 – 13827C2H2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2932. Eukaryota.
ENOG410XQ6S. LUCA.
GeneTreeiENSGT00510000047522.
HOGENOMiHOG000082498.
HOVERGENiHBG057723.
InParanoidiQ8N7E2.
KOiK15714.
OMAiPQFTENQ.
OrthoDBiEOG7GN2NX.
PhylomeDBiQ8N7E2.
TreeFamiTF332910.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N7E2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKMPAGEQE CEYNKEGKYY SKGVKLVRKK KKIPGYRWGD IKINIIGEKD
60 70 80 90 100
DLPIHFCDKC DLPIKIYGRI IPCKHAFCYH CANLYDKVGY KVCPRCRYPV
110 120 130 140 150
LRIEAHKRGS VFMCSIVQQC KRTYLSQKSL QAHIKRRHKR ARKQVTSASL
160 170 180 190 200
EKVRPHIAPP QTEISDIPKR LQDRDHLSYI PPEQHTMVSL PSVQHMLQEQ
210 220 230 240 250
HNQPHKDIQA PPPELSLSLP FPIQWETVSI FTRKHGNLTV DHIQNNSDSG
260 270 280 290 300
AKKPTPPDYY PECQSQPAVS SPHHIIPQKQ HYAPPPSPSS PVNHQMPYPP
310 320 330 340 350
QDVVTPNSVR SQVPALTTTY DPSSGYIIVK VPPDMNSPPL RAPQSQNGNP
360 370 380 390 400
SASEFASHHY NLNILPQFTE NQETLSPQFT QTDAMDHRRW PAWKRLSPCP
410 420
PTRSPPPSTL HGRSHHSHQR RHRRY
Length:425
Mass (Da):48,785
Last modified:October 1, 2002 - v1
Checksum:i873C2802514CD9E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671P → L in ADI56589 (PubMed:20657603).Curated
Sequence conflicti411 – 4111H → Q in ADI56589 (PubMed:20657603).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti166 – 1661D → E.2 Publications
Corresponds to variant rs5951426 [ dbSNP | Ensembl ].
VAR_030340
Natural varianti287 – 2871S → F.
Corresponds to variant rs12860105 [ dbSNP | Ensembl ].
VAR_030341

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ355336 mRNA. Translation: ADI56589.1.
AK098601 mRNA. Translation: BAC05348.1.
BX293560 Genomic DNA. Translation: CAI40652.1.
BC074910 mRNA. Translation: AAH74910.1.
BC126190 mRNA. Translation: AAI26191.1.
BC126192 mRNA. Translation: AAI26193.1.
CCDSiCCDS14205.1.
RefSeqiNP_689790.1. NM_152577.3.
UniGeneiHs.132485.

Genome annotation databases

EnsembliENST00000323684; ENSP00000323348; ENSG00000175809.
GeneIDi158506.
KEGGihsa:158506.
UCSCiuc004dai.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ355336 mRNA. Translation: ADI56589.1.
AK098601 mRNA. Translation: BAC05348.1.
BX293560 Genomic DNA. Translation: CAI40652.1.
BC074910 mRNA. Translation: AAH74910.1.
BC126190 mRNA. Translation: AAI26191.1.
BC126192 mRNA. Translation: AAI26193.1.
CCDSiCCDS14205.1.
RefSeqiNP_689790.1. NM_152577.3.
UniGeneiHs.132485.

3D structure databases

ProteinModelPortaliQ8N7E2.
SMRiQ8N7E2. Positions 54-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127688. 6 interactions.
STRINGi9606.ENSP00000323348.

PTM databases

iPTMnetiQ8N7E2.
PhosphoSiteiQ8N7E2.

Polymorphism and mutation databases

BioMutaiZNF645.
DMDMi74759980.

Proteomic databases

PaxDbiQ8N7E2.
PRIDEiQ8N7E2.

Protocols and materials databases

DNASUi158506.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323684; ENSP00000323348; ENSG00000175809.
GeneIDi158506.
KEGGihsa:158506.
UCSCiuc004dai.3. human.

Organism-specific databases

CTDi158506.
GeneCardsiZNF645.
HGNCiHGNC:26371. ZNF645.
HPAiHPA005845.
neXtProtiNX_Q8N7E2.
PharmGKBiPA134934025.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2932. Eukaryota.
ENOG410XQ6S. LUCA.
GeneTreeiENSGT00510000047522.
HOGENOMiHOG000082498.
HOVERGENiHBG057723.
InParanoidiQ8N7E2.
KOiK15714.
OMAiPQFTENQ.
OrthoDBiEOG7GN2NX.
PhylomeDBiQ8N7E2.
TreeFamiTF332910.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii158506.
PROiQ8N7E2.

Gene expression databases

BgeeiQ8N7E2.
CleanExiHS_ZNF645.
GenevisibleiQ8N7E2. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR007087. Znf_C2H2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human RING finger protein ZNF645 is a novel testis-specific E3 ubiquitin ligase."
    Liu Y.Q., Bai G., Zhang H., Su D., Tao D.C., Yang Y., Ma Y.X., Zhang S.Z.
    Asian J. Androl. 12:658-666(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT GLU-166.
    Tissue: Testis.
  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].
    Tissue: Testis.
  3. "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].
  4. "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], VARIANT GLU-166.
  5. Cited for: FUNCTION, DOMAIN HYB.

Entry informationi

Entry nameiZN645_HUMAN
AccessioniPrimary (citable) accession number: Q8N7E2
Secondary accession number(s): A0AV29
, A0AV31, E3SBK4, Q6DJY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 103 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 X
    Human chromosome X: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.