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Q9NVM9

- ASUN_HUMAN

UniProt

Q9NVM9 - ASUN_HUMAN

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Protein

Protein asunder homolog

Gene

ASUN

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

Functioni

Crucial regulator of the mitotic cell cycle and development. At prophase, required for dynein anchoring to the nuclear envelope important for proper centrosome-nucleus coupling. At G2/M phase, may be required for proper spindle formation and execution of cytokinesis.2 Publications

GO - Biological processi

  1. centrosome localization Source: MGI
  2. mitotic nuclear division Source: UniProtKB-KW
  3. mitotic spindle organization Source: MGI
  4. protein localization to nuclear envelope Source: MGI
  5. regulation of fertilization Source: UniProtKB
  6. regulation of mitotic cell cycle Source: UniProtKB
  7. sperm motility Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Protein asunder homolog
Alternative name(s):
Cell cycle regulator Mat89Bb homolog
Germ cell tumor 1
Sarcoma antigen NY-SAR-95
Gene namesi
Name:ASUN
Synonyms:C12orf11, GCT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:20174. ASUN.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134892469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 706706Protein asunder homologPRO_0000089845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei626 – 6261Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NVM9.
PaxDbiQ9NVM9.
PeptideAtlasiQ9NVM9.
PRIDEiQ9NVM9.

PTM databases

PhosphoSiteiQ9NVM9.

Expressioni

Tissue specificityi

Widely expressed. Tends to be up-regulated in seminomas compared to normal testis.1 Publication

Gene expression databases

BgeeiQ9NVM9.
CleanExiHS_C12orf11.
ExpressionAtlasiQ9NVM9. baseline and differential.
GenevestigatoriQ9NVM9.

Organism-specific databases

HPAiHPA039543.

Interactioni

Subunit structurei

Interacts with PAFAH1B1; this interaction may be required for proper recruitment of dynein complexes to the nuclear envelope at prophase.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CBFBQ139512EBI-741429,EBI-718750

Protein-protein interaction databases

BioGridi120846. 14 interactions.
IntActiQ9NVM9. 4 interactions.
MINTiMINT-6782559.
STRINGi9606.ENSP00000261191.

Structurei

3D structure databases

ProteinModelPortaliQ9NVM9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili567 – 62256Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the asunder family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG301038.
GeneTreeiENSGT00390000002793.
HOGENOMiHOG000046389.
InParanoidiQ9NVM9.
OMAiNSVELHY.
OrthoDBiEOG7TF78D.
PhylomeDBiQ9NVM9.
TreeFamiTF105815.

Family and domain databases

InterProiIPR019355. Cell_cycle_regulator_Mat89Bb.
[Graphical view]
PfamiPF10221. DUF2151. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NVM9-1) [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
MKIFSESHKT VFVVDHCPYM AESCRQHVEF DMLVKNRTQG IIPLAPISKS
60 70 80 90 100
LWTCSVESSM EYCRIMYDIF PFKKLVNFIV SDSGAHVLNS WTQEDQNLQE
110 120 130 140 150
LMAALAAVGP PNPRADPECC SILHGLVAAV ETLCKITEYQ HEARTLLMEN
160 170 180 190 200
AERVGNRGRI ICITNAKSDS HVRMLEDCVQ ETIHEHNKLA ANSDHLMQIQ
210 220 230 240 250
KCELVLIHTY PVGEDSLVSD RSKKELSPVL TSEVHSVRAG RHLATKLNIL
260 270 280 290 300
VQQHFDLAST TITNIPMKEE QHANTSANYD VELLHHKDAH VDFLKSGDSH
310 320 330 340 350
LGGGSREGSF KETITLKWCT PRTNNIELHY CTGAYRISPV DVNSRPSSCL
360 370 380 390 400
TNFLLNGRSV LLEQPRKSGS KVISHMLSSH GGEIFLHVLS SSRSILEDPP
410 420 430 440 450
SISEGCGGRV TDYRITDFGE FMRENRLTPF LDPRYKIDGS LEVPLERAKD
460 470 480 490 500
QLEKHTRYWP MIISQTTIFN MQAVVPLASV IVKESLTEED VLNCQKTIYN
510 520 530 540 550
LVDMERKNDP LPISTVGTRG KGPKRDEQYR IMWNELETLV RAHINNSEKH
560 570 580 590 600
QRVLECLMAC RSKPPEEEER KKRGRKREDK EDKSEKAVKD YEQEKSWQDS
610 620 630 640 650
ERLKGILERG KEELAEAEII KDSPDSPEPP NKKPLVEMDE TPQVEKSKGP
660 670 680 690 700
VSLLSLWSNR INTANSRKHQ EFAGRLNSVN NRAELYQHLK EENGMETTEN

GKASRQ
Length:706
Mass (Da):80,225
Last modified:July 19, 2005 - v2
Checksum:i925C733184461EA6
GO
Isoform 2 (identifier: Q9NVM9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Note: No experimental confirmation available.

Show »
Length:605
Mass (Da):68,494
Checksum:i7D9017DE546CF1BD
GO

Sequence cautioni

The sequence AAO65180.1 differs from that shown. Reason: Frameshift at positions 414, 445, 483, 498 and 507.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291E → G in BAA91725. (PubMed:14702039)Curated
Sequence conflicti53 – 531T → P in BAA91725. (PubMed:14702039)Curated
Sequence conflicti75 – 751L → P in BAA91725. (PubMed:14702039)Curated
Sequence conflicti454 – 4541K → R in BAA91721. (PubMed:14702039)Curated
Sequence conflicti457 – 4571R → P in BAA91721. (PubMed:14702039)Curated
Sequence conflicti459 – 4591W → R in BAA91725. (PubMed:14702039)Curated
Sequence conflicti484 – 4841E → K in AAO65180. (PubMed:12601173)Curated
Sequence conflicti490 – 4901D → N in AAO65180. (PubMed:12601173)Curated
Sequence conflicti699 – 6991E → K in AAH03081. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661M → T.
Corresponds to variant rs2306852 [ dbSNP | Ensembl ].
VAR_050864
Natural varianti227 – 2271S → P in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035673

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 101101Missing in isoform 2. 1 PublicationVSP_056514Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK001492 mRNA. Translation: BAA91721.1.
AK001499 mRNA. Translation: BAA91725.1.
AK297948 mRNA. Translation: BAG60263.1.
AC024093 Genomic DNA. No translation available.
BC003081 mRNA. Translation: AAH03081.1.
BC008368 mRNA. Translation: AAH08368.1.
AY211927 mRNA. Translation: AAO65180.1. Frameshift.
AL137401 mRNA. Translation: CAB70726.1.
CCDSiCCDS8708.1. [Q9NVM9-1]
PIRiT46457.
RefSeqiNP_060634.2. NM_018164.2.
XP_006719169.1. XM_006719106.1.
UniGeneiHs.505077.

Genome annotation databases

EnsembliENST00000261191; ENSP00000261191; ENSG00000064102. [Q9NVM9-1]
GeneIDi55726.
KEGGihsa:55726.
UCSCiuc001rhk.4. human. [Q9NVM9-1]

Polymorphism databases

DMDMi71153010.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK001492 mRNA. Translation: BAA91721.1 .
AK001499 mRNA. Translation: BAA91725.1 .
AK297948 mRNA. Translation: BAG60263.1 .
AC024093 Genomic DNA. No translation available.
BC003081 mRNA. Translation: AAH03081.1 .
BC008368 mRNA. Translation: AAH08368.1 .
AY211927 mRNA. Translation: AAO65180.1 . Frameshift.
AL137401 mRNA. Translation: CAB70726.1 .
CCDSi CCDS8708.1. [Q9NVM9-1 ]
PIRi T46457.
RefSeqi NP_060634.2. NM_018164.2.
XP_006719169.1. XM_006719106.1.
UniGenei Hs.505077.

3D structure databases

ProteinModelPortali Q9NVM9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120846. 14 interactions.
IntActi Q9NVM9. 4 interactions.
MINTi MINT-6782559.
STRINGi 9606.ENSP00000261191.

PTM databases

PhosphoSitei Q9NVM9.

Polymorphism databases

DMDMi 71153010.

Proteomic databases

MaxQBi Q9NVM9.
PaxDbi Q9NVM9.
PeptideAtlasi Q9NVM9.
PRIDEi Q9NVM9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261191 ; ENSP00000261191 ; ENSG00000064102 . [Q9NVM9-1 ]
GeneIDi 55726.
KEGGi hsa:55726.
UCSCi uc001rhk.4. human. [Q9NVM9-1 ]

Organism-specific databases

CTDi 55726.
GeneCardsi GC12M027059.
H-InvDB HIX0010501.
HGNCi HGNC:20174. ASUN.
HPAi HPA039543.
MIMi 615079. gene.
neXtProti NX_Q9NVM9.
PharmGKBi PA134892469.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG301038.
GeneTreei ENSGT00390000002793.
HOGENOMi HOG000046389.
InParanoidi Q9NVM9.
OMAi NSVELHY.
OrthoDBi EOG7TF78D.
PhylomeDBi Q9NVM9.
TreeFami TF105815.

Miscellaneous databases

GeneWikii C12orf11.
GenomeRNAii 55726.
NextBioi 35473633.
SOURCEi Search...

Gene expression databases

Bgeei Q9NVM9.
CleanExi HS_C12orf11.
ExpressionAtlasi Q9NVM9. baseline and differential.
Genevestigatori Q9NVM9.

Family and domain databases

InterProi IPR019355. Cell_cycle_regulator_Mat89Bb.
[Graphical view ]
Pfami PF10221. DUF2151. 1 hit.
[Graphical view ]
ProtoNeti Search...

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).
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Eye and Lymph.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-513 (ISOFORM 1).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 568-706 (ISOFORM 1).
    Tissue: Testis.
  6. "Genomic and expression analysis of the 12p11-p12 amplicon using EST arrays identifies two novel amplified and overexpressed genes."
    Bourdon V., Naef F., Rao P.H., Reuter V., Mok S.C., Bosl G.J., Koul S., Murty V.V., Kucherlapati R.S., Chaganti R.S.
    Cancer Res. 62:6218-6223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Drosophila genome-scale screen for PAN GU kinase substrates identifies Mat89Bb as a cell cycle regulator."
    Lee L.A., Lee E., Anderson M.A., Vardy L., Tahinci E., Ali S.M., Kashevsky H., Benasutti M., Kirschner M.W., Orr-Weaver T.L.
    Dev. Cell 8:435-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Human Asunder promotes dynein recruitment and centrosomal tethering to the nucleus at mitotic entry."
    Jodoin J.N., Shboul M., Sitaram P., Zein-Sabatto H., Reversade B., Lee E., Lee L.A.
    Mol. Biol. Cell 23:4713-4724(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAFAH1B1, SUBCELLULAR LOCATION.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-227.

Entry informationi

Entry nameiASUN_HUMAN
AccessioniPrimary (citable) accession number: Q9NVM9
Secondary accession number(s): B4DNK1
, Q86WE2, Q96HM2, Q9BTX2, Q9NTB6, Q9NVM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: October 29, 2014
This is version 89 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

RNAi in HeLa cells results in a multinucleated phenotype.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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