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Protein

Protein zwilch homolog

Gene

ZWILCH

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

Functioni

Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:15824131).1 Publication

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic cell cycle checkpoint Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein zwilch homolog
Short name:
hZwilch
Gene namesi
Name:ZWILCH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:25468. ZWILCH.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • kinetochore Source: MGI
  • RZZ complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670465.

Polymorphism and mutation databases

BioMutaiZWILCH.
DMDMi166228729.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Protein zwilch homologPRO_0000314800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H900.
MaxQBiQ9H900.
PaxDbiQ9H900.
PeptideAtlasiQ9H900.
PRIDEiQ9H900.

PTM databases

iPTMnetiQ9H900.
PhosphoSiteiQ9H900.

Expressioni

Gene expression databases

BgeeiQ9H900.
CleanExiHS_ZWILCH.
ExpressionAtlasiQ9H900. baseline and differential.
GenevisibleiQ9H900. HS.

Organism-specific databases

HPAiHPA039386.

Interactioni

Subunit structurei

Component of the RZZ complex composed of KNTC1/ROD, ZW10 and ZWILCH; in the complex interacts directly with KNTC1/ROD.3 Publications

Protein-protein interaction databases

BioGridi120376. 11 interactions.
DIPiDIP-36478N.
IntActiQ9H900. 2 interactions.
MINTiMINT-4989376.
STRINGi9606.ENSP00000311429.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54Combined sources
Helixi8 – 2316Combined sources
Beta strandi32 – 4312Combined sources
Helixi50 – 534Combined sources
Beta strandi61 – 666Combined sources
Helixi103 – 11715Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi148 – 15811Combined sources
Beta strandi161 – 17616Combined sources
Helixi182 – 19312Combined sources
Beta strandi199 – 20911Combined sources
Beta strandi224 – 2329Combined sources
Beta strandi245 – 2528Combined sources
Helixi267 – 28115Combined sources
Helixi295 – 30713Combined sources
Helixi348 – 35710Combined sources
Helixi363 – 37816Combined sources
Helixi393 – 40210Combined sources
Helixi415 – 43824Combined sources
Helixi444 – 4518Combined sources
Beta strandi453 – 4553Combined sources
Helixi457 – 47721Combined sources
Turni478 – 4803Combined sources
Helixi485 – 50117Combined sources
Beta strandi510 – 5134Combined sources
Helixi517 – 5226Combined sources
Turni523 – 5253Combined sources
Beta strandi529 – 5368Combined sources
Beta strandi542 – 55110Combined sources
Beta strandi578 – 58912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IF8X-ray2.55A1-334[»]
B335-591[»]
ProteinModelPortaliQ9H900.
SMRiQ9H900. Positions 1-309, 339-590.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H900.

Family & Domainsi

Sequence similaritiesi

Belongs to the ZWILCH family.Curated

Phylogenomic databases

eggNOGiKOG4803. Eukaryota.
ENOG410Y8MB. LUCA.
GeneTreeiENSGT00390000013696.
HOGENOMiHOG000155813.
HOVERGENiHBG108779.
InParanoidiQ9H900.
KOiK11579.
OMAiNPLDEQH.
OrthoDBiEOG75J0MR.
PhylomeDBiQ9H900.
TreeFamiTF324453.

Family and domain databases

InterProiIPR018630. RZZ-complex_zwilch.
[Graphical view]
PfamiPF09817. DUF2352. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9H900-1) [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
MWERLNCAAE DFYSRLLQKF NEEKKGIRKD PFLYEADVQV QLISKGQPNP
60 70 80 90 100
LKNILNENDI VFIVEKVPLE KEETSHIEEL QSEETAISDF STGENVGPLA
110 120 130 140 150
LPVGKARQLI GLYTMAHNPN MTHLKINLPV TALPPLWVRC DSSDPEGTCW
160 170 180 190 200
LGAELITTNN SITGIVLYVV SCKADKNYSV NLENLKNLHK KRHHLSTVTS
210 220 230 240 250
KGFAQYELFK SSALDDTITA SQTAIALDIS WSPVDEILQI PPLSSTATLN
260 270 280 290 300
IKVESGEPRG PLNHLYRELK FLLVLADGLR TGVTEWLEPL EAKSAVELVQ
310 320 330 340 350
EFLNDLNKLD GFGDSTKKDT EVETLKHDTA AVDRSVKRLF KVRSDLDFAE
360 370 380 390 400
QLWCKMSSSV ISYQDLVKCF TLIIQSLQRG DIQPWLHSGS NSLLSKLIHQ
410 420 430 440 450
SYHGTMDTVS LSGTIPVQML LEIGLDKLKK DYISFFIGQE LASLNHLEYF
460 470 480 490 500
IAPSVDIQEQ VYRVQKLHHI LEILVSCMPF IKSQHELLFS LTQICIKYYK
510 520 530 540 550
QNPLDEQHIF QLPVRPTAVK NLYQSEKPQK WRVEIYSGQK KIKTVWQLSD
560 570 580 590
SSPIDHLNFH KPDFSELTLN GSLEERIFFT NMVTCSQVHF K
Length:591
Mass (Da):67,214
Last modified:January 15, 2008 - v2
Checksum:i522ECA229D2C0AE9
GO
Isoform 2 (identifier: Q9H900-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.

Show »
Length:477
Mass (Da):54,224
Checksum:i0443A2B101C275C1
GO

Sequence cautioni

The sequence AK000898 differs from that shown. Reason: Frameshift at position 248. Curated
The sequence AK000898 differs from that shown. Reason: Erroneous termination at position 366. Translated as Leu.Curated
The sequence BAB55133.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391Q → R in CAE45821 (PubMed:17974005).Curated
Sequence conflicti537 – 5371S → R in BAB14446 (PubMed:14702039).Curated
Sequence conflicti555 – 5551D → G in AK000898 (PubMed:14702039).Curated
Sequence conflicti570 – 5701N → S in AK000898 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti344 – 3441S → G.
Corresponds to variant rs11071896 [ dbSNP | Ensembl ].
VAR_038055

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 114114Missing in isoform 2. 3 PublicationsVSP_030365Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000898 mRNA. No translation available.
AK023175 mRNA. Translation: BAB14446.1.
AK027468 mRNA. Translation: BAB55133.1. Different initiation.
AK122787 mRNA. Translation: BAG53730.1.
BX640701 mRNA. Translation: CAE45821.1.
CH471082 Genomic DNA. Translation: EAW77779.1.
BC036900 mRNA. Translation: AAH36900.1.
BC090041 mRNA. Translation: AAH90041.1.
CCDSiCCDS10219.1. [Q9H900-1]
CCDS73746.1. [Q9H900-2]
RefSeqiNP_001274750.1. NM_001287821.1. [Q9H900-2]
NP_001274751.1. NM_001287822.1. [Q9H900-2]
NP_001274752.1. NM_001287823.1. [Q9H900-2]
NP_060445.3. NM_017975.4. [Q9H900-1]
UniGeneiHs.21331.

Genome annotation databases

EnsembliENST00000307897; ENSP00000311429; ENSG00000174442. [Q9H900-1]
ENST00000446801; ENSP00000402217; ENSG00000174442. [Q9H900-2]
ENST00000535141; ENSP00000437749; ENSG00000174442. [Q9H900-2]
ENST00000565627; ENSP00000454737; ENSG00000174442. [Q9H900-2]
ENST00000613446; ENSP00000477955; ENSG00000174442. [Q9H900-2]
GeneIDi55055.
KEGGihsa:55055.
UCSCiuc002aqa.5. human. [Q9H900-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000898 mRNA. No translation available.
AK023175 mRNA. Translation: BAB14446.1.
AK027468 mRNA. Translation: BAB55133.1. Different initiation.
AK122787 mRNA. Translation: BAG53730.1.
BX640701 mRNA. Translation: CAE45821.1.
CH471082 Genomic DNA. Translation: EAW77779.1.
BC036900 mRNA. Translation: AAH36900.1.
BC090041 mRNA. Translation: AAH90041.1.
CCDSiCCDS10219.1. [Q9H900-1]
CCDS73746.1. [Q9H900-2]
RefSeqiNP_001274750.1. NM_001287821.1. [Q9H900-2]
NP_001274751.1. NM_001287822.1. [Q9H900-2]
NP_001274752.1. NM_001287823.1. [Q9H900-2]
NP_060445.3. NM_017975.4. [Q9H900-1]
UniGeneiHs.21331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IF8X-ray2.55A1-334[»]
B335-591[»]
ProteinModelPortaliQ9H900.
SMRiQ9H900. Positions 1-309, 339-590.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120376. 11 interactions.
DIPiDIP-36478N.
IntActiQ9H900. 2 interactions.
MINTiMINT-4989376.
STRINGi9606.ENSP00000311429.

PTM databases

iPTMnetiQ9H900.
PhosphoSiteiQ9H900.

Polymorphism and mutation databases

BioMutaiZWILCH.
DMDMi166228729.

Proteomic databases

EPDiQ9H900.
MaxQBiQ9H900.
PaxDbiQ9H900.
PeptideAtlasiQ9H900.
PRIDEiQ9H900.

Protocols and materials databases

DNASUi55055.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307897; ENSP00000311429; ENSG00000174442. [Q9H900-1]
ENST00000446801; ENSP00000402217; ENSG00000174442. [Q9H900-2]
ENST00000535141; ENSP00000437749; ENSG00000174442. [Q9H900-2]
ENST00000565627; ENSP00000454737; ENSG00000174442. [Q9H900-2]
ENST00000613446; ENSP00000477955; ENSG00000174442. [Q9H900-2]
GeneIDi55055.
KEGGihsa:55055.
UCSCiuc002aqa.5. human. [Q9H900-1]

Organism-specific databases

CTDi55055.
GeneCardsiZWILCH.
H-InvDBHIX0012366.
HGNCiHGNC:25468. ZWILCH.
HPAiHPA039386.
MIMi609984. gene.
neXtProtiNX_Q9H900.
PharmGKBiPA142670465.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4803. Eukaryota.
ENOG410Y8MB. LUCA.
GeneTreeiENSGT00390000013696.
HOGENOMiHOG000155813.
HOVERGENiHBG108779.
InParanoidiQ9H900.
KOiK11579.
OMAiNPLDEQH.
OrthoDBiEOG75J0MR.
PhylomeDBiQ9H900.
TreeFamiTF324453.

Enzyme and pathway databases

ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTraceiQ9H900.
GenomeRNAii55055.
PROiQ9H900.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H900.
CleanExiHS_ZWILCH.
ExpressionAtlasiQ9H900. baseline and differential.
GenevisibleiQ9H900. HS.

Family and domain databases

InterProiIPR018630. RZZ-complex_zwilch.
[Graphical view]
PfamiPF09817. DUF2352. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 1 AND 2).
    Tissue: Teratocarcinoma and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Prostate.
  3. 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] (ISOFORM 2).
    Tissue: Uterus.
  5. "Zwilch, a new component of the ZW10/ROD complex required for kinetochore functions."
    Williams B.C., Li Z., Liu S., Williams E.V., Leung G., Yen T.J., Goldberg M.L.
    Mol. Biol. Cell 14:1379-1391(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KNTC1 AND ZW10.
  6. Cited for: ASSOCIATION WITH COLORECTAL CANCER.
  7. "ZW10 links mitotic checkpoint signaling to the structural kinetochore."
    Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III, Tagaya M., Cleveland D.W.
    J. Cell Biol. 169:49-60(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RZZ COMPLEX.
  8. "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-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery."
    Civril F., Wehenkel A., Giorgi F.M., Santaguida S., Di Fonzo A., Grigorean G., Ciccarelli F.D., Musacchio A.
    Structure 18:616-626(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), INTERACTION WITH KNTC1, IDENTIFICATION IN THE RRZ COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiZWILC_HUMAN
AccessioniPrimary (citable) accession number: Q9H900
Secondary accession number(s): B3KVB8
, Q6N049, Q8N404, Q96SY7, Q9NWG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 6, 2016
This is version 106 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

Miscellaneous

ZWILCH gene is deleted in a patient suffering from colorectal cancer with chromosomal instability.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.