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Protein

Nuclear-interacting partner of ALK

Gene

ZC3HC1

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

Functioni

Essential component of an SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry. May have an antiapoptotic role in NPM-ALK-mediated signaling events.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 fingeri102 – 15655C3HC-typeAdd
BLAST

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SIGNORiQ86WB0.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear-interacting partner of ALK
Alternative name(s):
Nuclear-interacting partner of anaplastic lymphoma kinase
Short name:
hNIPA
Zinc finger C3HC-type protein 1
Gene namesi
Name:ZC3HC1
Synonyms:NIPA
ORF Names:HSPC216
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:29913. ZC3HC1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051Y → F: Does not strongly affect phosphorylation status; when associated with F-137. 1 Publication
Mutagenesisi137 – 1371Y → F: Does not strongly affect phosphorylation status; when associated with F-105. 1 Publication
Mutagenesisi170 – 1712LP → FM: Abolishes interaction with SKP1. 1 Publication
Mutagenesisi354 – 3541S → A: Strongly reduces phosphorylation and induces the formation of a constitutive SCF(NIPA) E3 complex that degrades CCNB1 at G2/M phase and delays mitotic entry. 2 Publications
Mutagenesisi398 – 4014RKAK → AAAA: Induces a complete cytoplasmic redistribution. 1 Publication
Mutagenesisi399 – 3991K → P: Induces a partial cytoplasmic redistribution. 1 Publication

Organism-specific databases

PharmGKBiPA134931869.

Polymorphism and mutation databases

BioMutaiZC3HC1.
DMDMi73921220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 502501Nuclear-interacting partner of ALKPRO_0000096849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei28 – 281PhosphothreonineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei84 – 841PhosphothreonineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei329 – 3291PhosphoserineCombined sources
Modified residuei333 – 3331PhosphothreonineCombined sources
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei354 – 3541PhosphoserineCombined sources1 Publication
Modified residuei359 – 3591PhosphoserineCombined sources
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei381 – 3811PhosphoserineCombined sources
Modified residuei384 – 3841PhosphothreonineCombined sources
Modified residuei387 – 3871PhosphothreonineCombined sources
Modified residuei395 – 3951PhosphoserineCombined sources
Modified residuei407 – 4071PhosphoserineCombined sources
Modified residuei483 – 4831PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Phosphorylated on Ser residues at G2/M phase, but not during S and G0 phases. May also be weakly phosphorylated on Tyr residues. Ser-354 phosphorylation, a major site during the course of cell-cycle-dedendent phosphorylation, results in its dissociation from the SCF(NIPA) complex, thereby preventing CCNB1 degradation leading to mitotic entry.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ86WB0.
MaxQBiQ86WB0.
PaxDbiQ86WB0.
PeptideAtlasiQ86WB0.
PRIDEiQ86WB0.

PTM databases

iPTMnetiQ86WB0.
PhosphoSiteiQ86WB0.
SwissPalmiQ86WB0.

Expressioni

Tissue specificityi

Widely expressed. Highly expressed in heart, skeletal muscle and testis. Expressed in brain, placenta, lung, kidney, liver, pancreas, spleen, thymus, prostate, ovary small intestine and colon. Weakly or not expressed in leukocytes.1 Publication

Developmental stagei

Weakly expressed in G0/G1 phases, abundant during S and G2/M phases, and strongly decreases thereafter.1 Publication

Gene expression databases

BgeeiQ86WB0.
CleanExiHS_ZC3HC1.
ExpressionAtlasiQ86WB0. baseline and differential.
GenevisibleiQ86WB0. HS.

Organism-specific databases

HPAiHPA019089.
HPA024023.

Interactioni

Subunit structurei

Interacts with the NPM-ALK fusion protein in a tyrosine phosphorylation-dependent manner. Interacts with SKP1. Component of a SCF(NIPA) E3 complex with SKP1, RBX1 and CUL1 when not phosphorylated on Ser-354. Interacts with CCNB1.2 Publications

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119592. 34 interactions.
IntActiQ86WB0. 4 interactions.
MINTiMINT-4539594.
STRINGi9606.ENSP00000351052.

Structurei

3D structure databases

ProteinModelPortaliQ86WB0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni170 – 21041F-box-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi396 – 4027Nuclear localization signal1 Publication

Domaini

The F-box-like region is required for the interaction with SKP1.1 Publication

Sequence similaritiesi

Contains 1 C3HC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri102 – 15655C3HC-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4765. Eukaryota.
ENOG410ZQX4. LUCA.
GeneTreeiENSGT00390000006086.
HOVERGENiHBG082030.
InParanoidiQ86WB0.
OMAiYSLKWAG.
OrthoDBiEOG7TXKGG.
PhylomeDBiQ86WB0.
TreeFamiTF314674.

Family and domain databases

InterProiIPR013909. NIPA/Rsm1.
IPR012935. Znf_C3HC-like.
[Graphical view]
PfamiPF08600. Rsm1. 1 hit.
PF07967. zf-C3HC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86WB0-1) [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
MAAPCEGQAF AVGVEKNWGA VVRSPEGTPQ KIRQLIDEGI APEEGGVDAK
60 70 80 90 100
DTSATSQSVN GSPQAEQPSL ESTSKEAFFS RVETFSSLKW AGKPFELSPL
110 120 130 140 150
VCAKYGWVTV ECDMLKCSSC QAFLCASLQP AFDFDRYKQR CAELKKALCT
160 170 180 190 200
AHEKFCFWPD SPSPDRFGML PLDEPAILVS EFLDRFQSLC HLDLQLPSLR
210 220 230 240 250
PEDLKTMCLT EDKISLLLHL LEDELDHRTD ERKTTIKLGS DIQVHVTACI
260 270 280 290 300
LSVCGWACSS SLESMQLSLI TCSQCMRKVG LWGFQQIESS MTDLDASFGL
310 320 330 340 350
TSSPIPGLEG RPERLPLVPE SPRRMMTRSQ DATFSPGSEQ AEKSPGPIVS
360 370 380 390 400
RTRSWDSSSP VDRPEPEAAS PTTRTRPVTR SMGTGDTPGL EVPSSPLRKA
410 420 430 440 450
KRARLCSSSS SDTSSRSFFD PTSQHRDWCP WVNITLGKES RENGGTEPDA
460 470 480 490 500
SAPAEPGWKA VLTILLAHKQ SSQPAETDSM SLSEKSRKVF RIFRQWESLC

SC
Length:502
Mass (Da):55,262
Last modified:June 1, 2003 - v1
Checksum:iD5DEDF9E30070586
GO
Isoform 2 (identifier: Q86WB0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MAAPCEGQAF...IAPEEGGVDA → MRGLPRKREAWTQPHPLEALYESLRVLE

Note: No experimental confirmation available.
Show »
Length:481
Mass (Da):53,559
Checksum:iB0EF4F07386A8554
GO
Isoform 3 (identifier: Q86WB0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     341-411: Missing.

Note: No experimental confirmation available.
Show »
Length:431
Mass (Da):47,771
Checksum:iEC1DCB8077C127C7
GO

Sequence cautioni

The sequence AAF36136.1 differs from that shown. Reason: Frameshift at positions 93, 187 and 220. Curated
The sequence AAH28917.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAS07546.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAS07547.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791V → I in BAB14024 (PubMed:14702039).Curated
Sequence conflicti278 – 2781K → R in AAF36136 (PubMed:11042152).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti271 – 2711T → A.1 Publication
Corresponds to variant rs1464890 [ dbSNP | Ensembl ].
VAR_023312
Natural varianti363 – 3631R → H.1 Publication
Corresponds to variant rs11556924 [ dbSNP | Ensembl ].
VAR_023313

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949MAAPC…GGVDA → MRGLPRKREAWTQPHPLEAL YESLRVLE in isoform 2. 1 PublicationVSP_015217Add
BLAST
Alternative sequencei341 – 41171Missing in isoform 3. 1 PublicationVSP_015218Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ537494 mRNA. Translation: CAD61161.1.
AF151050 mRNA. Translation: AAF36136.1. Frameshift.
AK001317 mRNA. Translation: BAA91619.1.
AK022373 mRNA. Translation: BAB14024.1.
AC073320 Genomic DNA. Translation: AAS07546.1. Sequence problems.
AC073320 Genomic DNA. Translation: AAS07547.1. Sequence problems.
AC087071 Genomic DNA. No translation available.
BC011551 mRNA. Translation: AAH11551.1.
BC028917 mRNA. Translation: AAH28917.1. Different initiation.
CCDSiCCDS34753.1. [Q86WB0-1]
CCDS64767.1. [Q86WB0-2]
CCDS75659.1. [Q86WB0-3]
RefSeqiNP_001269119.1. NM_001282190.1. [Q86WB0-2]
NP_001269120.1. NM_001282191.1. [Q86WB0-3]
NP_057562.3. NM_016478.4. [Q86WB0-1]
UniGeneiHs.194157.

Genome annotation databases

EnsembliENST00000311873; ENSP00000309301; ENSG00000091732. [Q86WB0-2]
ENST00000358303; ENSP00000351052; ENSG00000091732. [Q86WB0-1]
ENST00000360708; ENSP00000353933; ENSG00000091732. [Q86WB0-3]
GeneIDi51530.
KEGGihsa:51530.
UCSCiuc003vpi.4. human. [Q86WB0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ537494 mRNA. Translation: CAD61161.1.
AF151050 mRNA. Translation: AAF36136.1. Frameshift.
AK001317 mRNA. Translation: BAA91619.1.
AK022373 mRNA. Translation: BAB14024.1.
AC073320 Genomic DNA. Translation: AAS07546.1. Sequence problems.
AC073320 Genomic DNA. Translation: AAS07547.1. Sequence problems.
AC087071 Genomic DNA. No translation available.
BC011551 mRNA. Translation: AAH11551.1.
BC028917 mRNA. Translation: AAH28917.1. Different initiation.
CCDSiCCDS34753.1. [Q86WB0-1]
CCDS64767.1. [Q86WB0-2]
CCDS75659.1. [Q86WB0-3]
RefSeqiNP_001269119.1. NM_001282190.1. [Q86WB0-2]
NP_001269120.1. NM_001282191.1. [Q86WB0-3]
NP_057562.3. NM_016478.4. [Q86WB0-1]
UniGeneiHs.194157.

3D structure databases

ProteinModelPortaliQ86WB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119592. 34 interactions.
IntActiQ86WB0. 4 interactions.
MINTiMINT-4539594.
STRINGi9606.ENSP00000351052.

PTM databases

iPTMnetiQ86WB0.
PhosphoSiteiQ86WB0.
SwissPalmiQ86WB0.

Polymorphism and mutation databases

BioMutaiZC3HC1.
DMDMi73921220.

Proteomic databases

EPDiQ86WB0.
MaxQBiQ86WB0.
PaxDbiQ86WB0.
PeptideAtlasiQ86WB0.
PRIDEiQ86WB0.

Protocols and materials databases

DNASUi51530.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311873; ENSP00000309301; ENSG00000091732. [Q86WB0-2]
ENST00000358303; ENSP00000351052; ENSG00000091732. [Q86WB0-1]
ENST00000360708; ENSP00000353933; ENSG00000091732. [Q86WB0-3]
GeneIDi51530.
KEGGihsa:51530.
UCSCiuc003vpi.4. human. [Q86WB0-1]

Organism-specific databases

CTDi51530.
GeneCardsiZC3HC1.
H-InvDBHIX0007070.
HGNCiHGNC:29913. ZC3HC1.
HPAiHPA019089.
HPA024023.
neXtProtiNX_Q86WB0.
PharmGKBiPA134931869.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4765. Eukaryota.
ENOG410ZQX4. LUCA.
GeneTreeiENSGT00390000006086.
HOVERGENiHBG082030.
InParanoidiQ86WB0.
OMAiYSLKWAG.
OrthoDBiEOG7TXKGG.
PhylomeDBiQ86WB0.
TreeFamiTF314674.

Enzyme and pathway databases

UniPathwayiUPA00143.
SIGNORiQ86WB0.

Miscellaneous databases

ChiTaRSiZC3HC1. human.
GeneWikiiZC3HC1.
GenomeRNAii51530.
PROiQ86WB0.

Gene expression databases

BgeeiQ86WB0.
CleanExiHS_ZC3HC1.
ExpressionAtlasiQ86WB0. baseline and differential.
GenevisibleiQ86WB0. HS.

Family and domain databases

InterProiIPR013909. NIPA/Rsm1.
IPR012935. Znf_C3HC-like.
[Graphical view]
PfamiPF08600. Rsm1. 1 hit.
PF07967. zf-C3HC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a nuclear interacting partner of anaplastic lymphoma kinase (NIPA)."
    Ouyang T., Bai R.-Y., Bassermann F., von Klitzing C., Klumpen S., Miething C., Morris S.W., Peschel C., Duyster J.
    J. Biol. Chem. 278:30028-30036(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH NPM-ALK FUSION PROTEIN, PHOSPHORYLATION AT SER-354, MUTAGENESIS OF TYR-105; TYR-137; SER-354; LYS-399 AND 398-ARG--LYS-401.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Umbilical cord blood.
  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 1 AND 2).
    Tissue: Mammary gland.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1), VARIANTS ALA-271 AND HIS-363.
    Tissue: Kidney and Mammary gland.
  6. "NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry."
    Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J.
    Cell 122:45-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, DOMAIN, INTERACTION WITH SKP1 AND CCNB1, IDENTIFICATION IN SCF(NIPA) COMPLEX WITH SKP1; CUL1 AND RBX1, MUTAGENESIS OF 170-LEU-PRO-171 AND SER-354.
  7. "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-24 AND THR-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; SER-335; SER-338; SER-344; SER-354; SER-370; THR-384; THR-387 AND SER-395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-62; SER-335; SER-338; SER-344; SER-354; SER-359; SER-370; THR-387 AND SER-395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-24; SER-321; SER-335 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-24; SER-62; SER-321; SER-329; SER-335; SER-344 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; THR-28; SER-58; SER-62; THR-84; SER-321; SER-329; SER-335; SER-344; SER-354; SER-381; THR-387; SER-395 AND SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-344; SER-354 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNIPA_HUMAN
AccessioniPrimary (citable) accession number: Q86WB0
Secondary accession number(s): A6NH66
, Q75MF3, Q75MF4, Q8N330, Q96F75, Q9HA34, Q9NVX4, Q9P0R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 121 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

Caution

Reported to contain a F-box domain (PubMed:16009132). Such domain is however not predicted by any detection method.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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.