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Q96S55

- WRIP1_HUMAN

UniProt

Q96S55 - WRIP1_HUMAN

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Protein

ATPase WRNIP1

Gene

WRNIP1

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

Functioni

Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri17 – 4024UBZ-typeAdd
BLAST
Nucleotide bindingi268 – 2758ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. DNA binding Source: InterPro
  4. identical protein binding Source: IntAct
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA replication Source: UniProtKB-KW
  3. DNA synthesis involved in DNA repair Source: UniProtKB
  4. regulation of DNA-dependent DNA replication initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA replication

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase WRNIP1 (EC:3.6.1.3)
Alternative name(s):
Werner helicase-interacting protein 1
Gene namesi
Name:WRNIP1Imported
Synonyms:WHIPImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20876. WRNIP1.

Subcellular locationi

Nucleus By similarity
Note: Colocalizes with WRN in granular structures in the nucleus.By similarity

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134982239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665ATPase WRNIP1PRO_0000084785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphoserine2 Publications
Cross-linki81 – 81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei85 – 851Phosphothreonine2 Publications
Modified residuei91 – 911Phosphoserine2 Publications
Modified residuei92 – 921Phosphoserine2 Publications
Modified residuei116 – 1161Phosphothreonine1 Publication
Cross-linki141 – 141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei153 – 1531Phosphoserine2 Publications
Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki301 – 301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki310 – 310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki316 – 316Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki322 – 322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki335 – 335Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki482 – 482Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei534 – 5341Phosphotyrosine1 Publication
Modified residuei562 – 5621Phosphotyrosine1 Publication
Cross-linki627 – 627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei633 – 6331N6-acetyllysine; alternate1 Publication
Cross-linki633 – 633Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki636 – 636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Sumoylated with SUMO1 and SUMO2/3.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96S55.
PaxDbiQ96S55.
PRIDEiQ96S55.

PTM databases

PhosphoSiteiQ96S55.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ96S55.
CleanExiHS_WRNIP1.
GenevestigatoriQ96S55.

Organism-specific databases

HPAiHPA031752.
HPA031753.

Interactioni

Subunit structurei

Homooligomer; most likely an octamer. Interacts with POLD1, POLD2 and POLD4. Interacts with the N-terminal domain of WRN. Interacts (via UBZ-type zinc finger) with polyubiquitin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2513471,EBI-2513471
DDX58O957862EBI-2513471,EBI-995350
POLD1P283402EBI-2513471,EBI-716569
POLD2P490052EBI-2513471,EBI-372354
POLD4Q9HCU82EBI-2513471,EBI-864968
TOLLIPQ9H0E22EBI-2513471,EBI-74615

Protein-protein interaction databases

BioGridi121227. 25 interactions.
IntActiQ96S55. 15 interactions.
MINTiMINT-3058154.
STRINGi9606.ENSP00000370150.

Structurei

Secondary structure

1
665
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Turni21 – 233Combined sources
Beta strandi26 – 283Combined sources
Helixi29 – 313Combined sources
Helixi32 – 398Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VHSX-ray1.90A/B17-40[»]
3VHTX-ray2.40B9-46[»]
ProteinModelPortaliQ96S55.
SMRiQ96S55. Positions 12-46, 225-660.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Sequence Analysis
Contains 1 UBZ-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri17 – 4024UBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG2256.
GeneTreeiENSGT00390000008538.
HOVERGENiHBG062192.
InParanoidiQ96S55.
KOiK07478.
OMAiPGHWDAD.
OrthoDBiEOG744T8W.
PhylomeDBiQ96S55.
TreeFamiTF324547.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR021886. MgsA_C.
IPR027417. P-loop_NTPase.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF12002. MgsA_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q96S55-1) [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
MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP
60 70 80 90 100
AAGSHRAGER AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD
110 120 130 140 150
DGGETESRES YDAPPTPSGA RLIPDFPVAR SSSPGRKGSG KRPAAAAAAG
160 170 180 190 200
SASPRSWDEA EAQEEEEAVG DGDGDGDADA DGEDDPGHWD ADAAEAATAF
210 220 230 240 250
GASGGGRPHP RALAAEEIRQ MLQGKPLADT MRPDTLQDYF GQSKAVGQDT
260 270 280 290 300
LLRSLLETNE IPSLILWGPP GCGKTTLAHI IASNSKKHSI RFVTLSATNA
310 320 330 340 350
KTNDVRDVIK QAQNEKSFFK RKTILFIDEI HRFNKSQQDT FLPHVECGTI
360 370 380 390 400
TLIGATTENP SFQVNAALLS RCRVIVLEKL PVEAMVTILM RAINSLGIHV
410 420 430 440 450
LDSSRPTDPL SHSSNSSSEP AMFIEDKAVD TLAYLSDGDA RAGLNGLQLA
460 470 480 490 500
VLARLSSRKM FCKKSGQSYS PSRVLITEND VKEGLQRSHI LYDRAGEEHY
510 520 530 540 550
NCISALHKSM RGSDQNASLY WLARMLEGGE DPLYVARRLV RFASEDIGLA
560 570 580 590 600
DPSALTQAVA AYQGCHFIGM PECEVLLAQC VVYFARAPKS IEVYSAYNNV
610 620 630 640 650
KACLRNHQGP LPPVPLHLRN APTRLMKDLG YGKGYKYNPM YSEPVDQEYL
660
PEELRGVDFF KQRRC
Length:665
Mass (Da):72,133
Last modified:August 16, 2005 - v2
Checksum:iDE43D8E59C4B29E8
GO
Isoform 21 Publication (identifier: Q96S55-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     338-362: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:640
Mass (Da):69,459
Checksum:i83117E6CEFDE7688
GO
Isoform 31 Publication (identifier: Q96S55-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-220: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:445
Mass (Da):49,570
Checksum:iBDED370A47C0D894
GO
Isoform 41 Publication (identifier: Q96S55-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-384: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:281
Mass (Da):31,339
Checksum:i1099DF56AA75F54A
GO

Sequence cautioni

The sequence AAF80563.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15383.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti144 – 1441A → V in BAB60709. (PubMed:11301316)Curated
Sequence conflicti170 – 1734Missing in BAD92960. 1 PublicationCurated
Sequence conflicti265 – 2651I → N in BAB60709. (PubMed:11301316)Curated
Sequence conflicti377 – 3771L → F in BAB15383. (PubMed:14702039)Curated
Sequence conflicti499 – 4991H → Y in BAD97313. 1 PublicationCurated
Sequence conflicti545 – 5451E → G in BAB15383. (PubMed:14702039)Curated
Sequence conflicti568 – 5681I → M in BAB60709. (PubMed:11301316)Curated
Sequence conflicti576 – 5761L → F in BAB60709. (PubMed:11301316)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 384384Missing in isoform 4. 1 PublicationVSP_051782Add
BLAST
Alternative sequencei1 – 220220Missing in isoform 3. 1 PublicationVSP_051781Add
BLAST
Alternative sequencei338 – 36225Missing in isoform 2. 3 PublicationsVSP_051783Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB056152 mRNA. Translation: BAB60709.1.
AK026179 mRNA. Translation: BAB15383.1. Different initiation.
AK315471 mRNA. Translation: BAG37857.1.
AB209723 mRNA. Translation: BAD92960.1.
AK223593 mRNA. Translation: BAD97313.1.
AL139092 Genomic DNA. Translation: CAH73663.1.
AL139092 Genomic DNA. Translation: CAH73664.1.
AL139092 Genomic DNA. Translation: CAH73665.1.
AL139092 Genomic DNA. Translation: CAH73666.1.
CH471087 Genomic DNA. Translation: EAW55087.1.
BC018923 mRNA. Translation: AAH18923.1.
AF218313 mRNA. Translation: AAF80563.1. Different initiation.
CCDSiCCDS4475.1. [Q96S55-1]
CCDS4476.1. [Q96S55-2]
RefSeqiNP_064520.2. NM_020135.2. [Q96S55-1]
NP_569079.1. NM_130395.2. [Q96S55-2]
UniGeneiHs.236828.

Genome annotation databases

EnsembliENST00000380764; ENSP00000370141; ENSG00000124535. [Q96S55-4]
ENST00000380769; ENSP00000370146; ENSG00000124535. [Q96S55-3]
ENST00000380771; ENSP00000370148; ENSG00000124535. [Q96S55-2]
ENST00000380773; ENSP00000370150; ENSG00000124535. [Q96S55-1]
ENST00000618555; ENSP00000477551; ENSG00000124535. [Q96S55-1]
GeneIDi56897.
KEGGihsa:56897.
UCSCiuc003mtz.3. human. [Q96S55-1]
uc003mua.3. human. [Q96S55-2]

Polymorphism databases

DMDMi73622085.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB056152 mRNA. Translation: BAB60709.1 .
AK026179 mRNA. Translation: BAB15383.1 . Different initiation.
AK315471 mRNA. Translation: BAG37857.1 .
AB209723 mRNA. Translation: BAD92960.1 .
AK223593 mRNA. Translation: BAD97313.1 .
AL139092 Genomic DNA. Translation: CAH73663.1 .
AL139092 Genomic DNA. Translation: CAH73664.1 .
AL139092 Genomic DNA. Translation: CAH73665.1 .
AL139092 Genomic DNA. Translation: CAH73666.1 .
CH471087 Genomic DNA. Translation: EAW55087.1 .
BC018923 mRNA. Translation: AAH18923.1 .
AF218313 mRNA. Translation: AAF80563.1 . Different initiation.
CCDSi CCDS4475.1. [Q96S55-1 ]
CCDS4476.1. [Q96S55-2 ]
RefSeqi NP_064520.2. NM_020135.2. [Q96S55-1 ]
NP_569079.1. NM_130395.2. [Q96S55-2 ]
UniGenei Hs.236828.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VHS X-ray 1.90 A/B 17-40 [» ]
3VHT X-ray 2.40 B 9-46 [» ]
ProteinModelPortali Q96S55.
SMRi Q96S55. Positions 12-46, 225-660.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121227. 25 interactions.
IntActi Q96S55. 15 interactions.
MINTi MINT-3058154.
STRINGi 9606.ENSP00000370150.

PTM databases

PhosphoSitei Q96S55.

Polymorphism databases

DMDMi 73622085.

Proteomic databases

MaxQBi Q96S55.
PaxDbi Q96S55.
PRIDEi Q96S55.

Protocols and materials databases

DNASUi 56897.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380764 ; ENSP00000370141 ; ENSG00000124535 . [Q96S55-4 ]
ENST00000380769 ; ENSP00000370146 ; ENSG00000124535 . [Q96S55-3 ]
ENST00000380771 ; ENSP00000370148 ; ENSG00000124535 . [Q96S55-2 ]
ENST00000380773 ; ENSP00000370150 ; ENSG00000124535 . [Q96S55-1 ]
ENST00000618555 ; ENSP00000477551 ; ENSG00000124535 . [Q96S55-1 ]
GeneIDi 56897.
KEGGi hsa:56897.
UCSCi uc003mtz.3. human. [Q96S55-1 ]
uc003mua.3. human. [Q96S55-2 ]

Organism-specific databases

CTDi 56897.
GeneCardsi GC06P002766.
H-InvDB HIX0005529.
HGNCi HGNC:20876. WRNIP1.
HPAi HPA031752.
HPA031753.
MIMi 608196. gene.
neXtProti NX_Q96S55.
PharmGKBi PA134982239.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2256.
GeneTreei ENSGT00390000008538.
HOVERGENi HBG062192.
InParanoidi Q96S55.
KOi K07478.
OMAi PGHWDAD.
OrthoDBi EOG744T8W.
PhylomeDBi Q96S55.
TreeFami TF324547.

Miscellaneous databases

GeneWikii WRNIP1.
GenomeRNAii 56897.
NextBioi 62333.
PROi Q96S55.
SOURCEi Search...

Gene expression databases

Bgeei Q96S55.
CleanExi HS_WRNIP1.
Genevestigatori Q96S55.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR021886. MgsA_C.
IPR027417. P-loop_NTPase.
IPR006642. Znf_Rad18_put.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
PF12002. MgsA_C. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view ]
SUPFAMi SSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel protein interacts with the Werner's syndrome gene product physically and functionally."
    Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F., Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.
    J. Biol. Chem. 276:20364-20369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-665 (ISOFORM 1).
    Tissue: Kidney epitheliumImported.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: BrainImported and KidneyImported.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: MuscleImported.
  7. "Characterization of RuvB homologs in human and mouse."
    Adamson A.W., Shannon M.E., Lamerdin J.E., Thelen M.P.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-665 (ISOFORM 1).
  8. "Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta."
    Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.
    Genes Cells 10:13-22(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH POLD1; POLD2 AND POLD4.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534 AND TYR-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain."
    Bish R.A., Myers M.P.
    J. Biol. Chem. 282:23184-23193(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, UBIQUITINATION AT LYS-81; LYS-141; LYS-225; LYS-301; LYS-310; LYS-316; LYS-322; LYS-335; LYS-482; LYS-627; LYS-633 AND LYS-636, DOMAIN UBZ-TYPE ZINC-FINGER.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-85; SER-91; SER-92 AND THR-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 THR-85; SER-91 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-75 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWRIP1_HUMAN
AccessioniPrimary (citable) accession number: Q96S55
Secondary accession number(s): B2RDB0
, Q53EP6, Q59ET8, Q5W0E2, Q5W0E4, Q8WV26, Q9H681, Q9NRJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: November 26, 2014
This is version 112 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3